bio 2.0.4 → 2.0.5

Sign up to get free protection for your applications and to get access to all the features.
@@ -530,22 +530,43 @@ class UniProtKB < EMBLDB
530
530
  # http://br.expasy.org/sprot/userman.html#OH_line
531
531
  def oh
532
532
  unless @data['OH']
533
- @data['OH'] = fetch('OH').split("\. ").map {|x|
534
- if x =~ /NCBI_TaxID=(\d+);/
535
- taxid = $1
536
- else
537
- raise ArgumentError, ["Error: Invalid OH line format (#{self.entry_id}):",
538
- $!, "\n", get('OH'), "\n"].join
539
-
540
- end
541
- if x =~ /NCBI_TaxID=\d+; (.+)/
542
- host_name = $1
543
- host_name.sub!(/\.$/, '')
544
- else
545
- host_name = nil
533
+ oh = []
534
+ a = fetch('OH').split(/(NCBI\_TaxID\=)(\d+)(\;)/)
535
+ t = catch :error do
536
+ taxid = nil
537
+ host_name = nil
538
+ while x = a.shift
539
+ x = x.to_s.strip
540
+ case x
541
+ when ''
542
+ next
543
+ when 'NCBI_TaxID='
544
+ if taxid then
545
+ oh.push({'NCBI_TaxID' => taxid, 'HostName' => host_name})
546
+ taxid = nil
547
+ host_name = nil
548
+ end
549
+ taxid = a.shift
550
+ throw :error, :missing_semicolon if a.shift != ';'
551
+ else
552
+ throw :error, :missing_taxid if host_name
553
+ host_name = x
554
+ host_name.sub!(/\.\z/, '')
555
+ end
556
+ end #while x...
557
+ if taxid then
558
+ oh.push({'NCBI_TaxID' => taxid, 'HostName' => host_name})
559
+ elsif host_name then
560
+ throw :error, :missing_taxid_last
546
561
  end
547
- {'NCBI_TaxID' => taxid, 'HostName' => host_name}
548
- }
562
+ nil
563
+ end #t = catch...
564
+ if t then
565
+ raise ArgumentError,
566
+ ["Error: Invalid OH line format (#{self.entry_id}):",
567
+ $!, "\n", get('OH'), "\n"].join
568
+ end
569
+ @data['OH'] = oh
549
570
  end
550
571
  @data['OH']
551
572
  end
@@ -922,6 +943,7 @@ class UniProtKB < EMBLDB
922
943
 
923
944
 
924
945
  def cc_alternative_products(data)
946
+ return nil unless data
925
947
  ap = data.join('')
926
948
  return ap unless ap
927
949
 
@@ -960,6 +982,7 @@ class UniProtKB < EMBLDB
960
982
 
961
983
 
962
984
  def cc_biophysiochemical_properties(data)
985
+ return nil unless data
963
986
  data = data[0]
964
987
 
965
988
  hash = {'Absorption' => {},
@@ -995,6 +1018,7 @@ class UniProtKB < EMBLDB
995
1018
 
996
1019
 
997
1020
  def cc_caution(data)
1021
+ return nil unless data
998
1022
  data.join('')
999
1023
  end
1000
1024
  private :cc_caution
@@ -1004,6 +1028,7 @@ class UniProtKB < EMBLDB
1004
1028
  #
1005
1029
  # CC P46527:CDKN1B; NbExp=1; IntAct=EBI-359815, EBI-519280;
1006
1030
  def cc_interaction(data)
1031
+ return nil unless data
1007
1032
  str = data.join('')
1008
1033
  it = str.scan(/(.+?); NbExp=(.+?); IntAct=(.+?);/)
1009
1034
  it.map {|ent|
@@ -1059,6 +1084,7 @@ class UniProtKB < EMBLDB
1059
1084
 
1060
1085
 
1061
1086
  def cc_pathway(data)
1087
+ return nil unless data
1062
1088
  data.map {|x| x.sub(/\.$/, '') }.map {|x|
1063
1089
  x.split(/; | and |: /)
1064
1090
  }[0]
@@ -1067,6 +1093,7 @@ class UniProtKB < EMBLDB
1067
1093
 
1068
1094
 
1069
1095
  def cc_rna_editing(data)
1096
+ return nil unless data
1070
1097
  data = data.join('')
1071
1098
  entry = {'Modified_positions' => [], 'Note' => ""}
1072
1099
  if data =~ /Modified_positions=(.+?)(\.|;)/
@@ -1083,6 +1110,7 @@ class UniProtKB < EMBLDB
1083
1110
 
1084
1111
 
1085
1112
  def cc_subcellular_location(data)
1113
+ return nil unless data
1086
1114
  data.map {|x|
1087
1115
  x.split('. ').map {|y|
1088
1116
  y.split('; ').map {|z|
@@ -1101,6 +1129,7 @@ class UniProtKB < EMBLDB
1101
1129
  #++
1102
1130
 
1103
1131
  def cc_web_resource(data)
1132
+ return nil unless data
1104
1133
  data.map {|x|
1105
1134
  entry = {'Name' => nil, 'Note' => nil, 'URL' => nil}
1106
1135
  x.split(';').each do |y|
@@ -1235,10 +1264,14 @@ class UniProtKB < EMBLDB
1235
1264
  begin
1236
1265
  ftlines.each do |line|
1237
1266
  if /^FT +([^\s]+) +(([^\s]+)\:)?([\<\?]?[0-9]+|\?)(?:\.\.([\>\?]?[0-9]+|\?))?\s*$/ =~ line
1238
- cur_ft = [$1.to_s, # Feature Name
1239
- "#{$2}#{$4}", # From
1240
- $5.to_s, # To
1241
- [] # Qualifiers
1267
+ f_name = $1.to_s
1268
+ f_from = "#{$2}#{$4}"
1269
+ f_to = $5.to_s
1270
+ f_to = f_from if f_to.empty?
1271
+ cur_ft = [f_name, # Feature Name
1272
+ f_from, # From
1273
+ f_to, # To
1274
+ [] # Qualifiers
1242
1275
  ]
1243
1276
  table.push cur_ft
1244
1277
  cont = false
data/lib/bio/version.rb CHANGED
@@ -10,7 +10,7 @@
10
10
  module Bio
11
11
 
12
12
  # BioRuby version (Array containing Integer)
13
- BIORUBY_VERSION = [2, 0, 4].extend(Comparable).freeze
13
+ BIORUBY_VERSION = [2, 0, 5].extend(Comparable).freeze
14
14
 
15
15
  # Extra version specifier (String or nil).
16
16
  # Existance of the value indicates development version.
@@ -0,0 +1,127 @@
1
+ ID 1A_AMVLE Reviewed; 1126 AA.
2
+ AC P03589;
3
+ DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
4
+ DT 21-JUL-1986, sequence version 1.
5
+ DT 22-FEB-2023, entry version 78.
6
+ DE RecName: Full=Replication protein 1a;
7
+ DE Includes:
8
+ DE RecName: Full=ATP-dependent helicase;
9
+ DE EC=3.6.4.-;
10
+ DE Includes:
11
+ DE RecName: Full=Methyltransferase;
12
+ DE EC=2.1.1.-;
13
+ GN ORFNames=ORF1a;
14
+ OS Alfalfa mosaic virus (strain 425 / isolate Leiden).
15
+ OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
16
+ OC Martellivirales; Bromoviridae; Alfamovirus.
17
+ OX NCBI_TaxID=12322;
18
+ OH NCBI_TaxID=4045; Apium graveolens (Celery).
19
+ OH NCBI_TaxID=83862; Astragalus glycyphyllos (Wild liquorice).
20
+ OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
21
+ OH NCBI_TaxID=41386; Caryopteris incana.
22
+ OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
23
+ OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
24
+ OH NCBI_TaxID=35936; Lablab purpureus (Hyacinth bean) (Dolichos lablab).
25
+ OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
26
+ OH NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
27
+ OH NCBI_TaxID=3869; Lupinus.
28
+ OH NCBI_TaxID=145753; Malva parviflora (Little mallow) (Cheeseweed mallow).
29
+ OH NCBI_TaxID=3879; Medicago sativa (Alfalfa).
30
+ OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
31
+ OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
32
+ OH NCBI_TaxID=23113; Philadelphus.
33
+ OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
34
+ OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
35
+ OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
36
+ OH NCBI_TaxID=157662; Teramnus repens.
37
+ OH NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
38
+ OH NCBI_TaxID=85293; Viburnum opulus (High-bush cranberry).
39
+ OH NCBI_TaxID=3916; Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
40
+ OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
41
+ RN [1]
42
+ RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
43
+ RX PubMed=6298738; DOI=10.1093/nar/11.5.1253;
44
+ RA Cornelissen B.J.C., Brederode F.T., Moormann R.J.M., Bol J.F.;
45
+ RT "Complete nucleotide sequence of alfalfa mosaic virus RNA 1.";
46
+ RL Nucleic Acids Res. 11:1253-1265(1983).
47
+ CC -!- FUNCTION: Involved in the virus replication. Contains a helicase domain
48
+ CC and a methyltransferase domain. The methyltransferase domain is
49
+ CC probably involved in viral RNA capping. Involved in the formation of ER
50
+ CC membrane spherular invaginations in which RNA replication complexes
51
+ CC form (By similarity). {ECO:0000250}.
52
+ CC -!- SUBUNIT: Interacts with RNA-directed RNA polymerase 2a. {ECO:0000250}.
53
+ CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
54
+ CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
55
+ CC -!- SIMILARITY: Belongs to the bromoviridae replication protein 1a family.
56
+ CC {ECO:0000305}.
57
+ CC ---------------------------------------------------------------------------
58
+ CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
59
+ CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
60
+ CC ---------------------------------------------------------------------------
61
+ DR EMBL; L00163; AAA46289.1; -; Genomic_RNA.
62
+ DR PIR; A04197; WMFM12.
63
+ DR RefSeq; NP_041192.1; NC_001495.1.
64
+ DR SMR; P03589; -.
65
+ DR GeneID; 962667; -.
66
+ DR KEGG; vg:962667; -.
67
+ DR Proteomes; UP000000358; Genome.
68
+ DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
69
+ DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
70
+ DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
71
+ DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
72
+ DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
73
+ DR GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
74
+ DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
75
+ DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
76
+ DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
77
+ DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
78
+ DR InterPro; IPR002588; Alphavirus-like_MT_dom.
79
+ DR InterPro; IPR027417; P-loop_NTPase.
80
+ DR Pfam; PF01443; Viral_helicase1; 1.
81
+ DR Pfam; PF01660; Vmethyltransf; 1.
82
+ DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
83
+ DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
84
+ DR PROSITE; PS51657; PSRV_HELICASE; 1.
85
+ PE 3: Inferred from homology;
86
+ KW ATP-binding; Helicase; Host endoplasmic reticulum; Host membrane;
87
+ KW Hydrolase; Membrane; Methyltransferase; Nucleotide-binding;
88
+ KW Reference proteome; Transferase.
89
+ FT CHAIN 1..1126
90
+ FT /note="Replication protein 1a"
91
+ FT /id="PRO_0000083254"
92
+ FT DOMAIN 90..278
93
+ FT /note="Alphavirus-like MT"
94
+ FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
95
+ FT DOMAIN 806..963
96
+ FT /note="(+)RNA virus helicase ATP-binding"
97
+ FT DOMAIN 964..1125
98
+ FT /note="(+)RNA virus helicase C-terminal"
99
+ FT REGION 69..406
100
+ FT /note="Methyltransferase"
101
+ FT REGION 834..1094
102
+ FT /note="ATP-dependent helicase"
103
+ FT BINDING 838..845
104
+ FT /ligand="ATP"
105
+ FT /ligand_id="ChEBI:CHEBI:30616"
106
+ FT /evidence="ECO:0000255"
107
+ SQ SEQUENCE 1126 AA; 125828 MW; BF5A8019B47D4CBF CRC64;
108
+ MNADAQSTDA SLSMREPLSH ASIQEMLRRV VEKQAADDTT AIGKVFSEAG RAYAQDALPS
109
+ DKGEVLKISF SLDATQQNIL RANFPGRRTV FSNSSSSSHC FAAAHRLLET DFVYRCFGNT
110
+ VDSIIDLGGN FVSHMKVKRH NVHCCCPILD ARDGARLTER ILSLKSYVRK HPEIVGEADY
111
+ CMDTFQKCSR RADYAFAIHS TSDLDVGELA CSLDQKGVMK FICTMMVDAD MLIHNEGEIP
112
+ NFNVRWEIDR KKDLIHFDFI DEPNLGYSHR FSLLKHYLTY NAVDLGHAAY RIERKQDFGG
113
+ VMVIDLTYSL GFVPKMPHSN GRSCAWYNRV KGQMVVHTVN EGYYHHSYQT AVRRKVLVDK
114
+ KVLTRVTEVA FRQFRPNADA HSAIQSIATM LSSSTNHTII GGVTLISGKP LSPDDYIPVA
115
+ TTIYYRVKKL YNAIPEMLSL LDKGERLSTD AVLKGSEGPM WYSGPTFLSA LDKVNVPGDF
116
+ VAKALLSLPK RDLKSLFSRS ATSHSERTPV RDESPIRCTD GVFYPIRMLL KCLGSDKFES
117
+ VTITDPRSNT ETTVDLYQSF QKKIETVFSF ILGKIDGPSP LISDPVYFQS LEDVYYAEWH
118
+ QGNAIDASNY ARTLLDDIRK QKEESLKAKA KEVEDAQKLN RAILQVHAYL EAHPDGGKIE
119
+ GLGLSSQFIA KIPELAIPTP KPLPEFEKNA ETGEILRINP HSDAILEAID YLKSTSANSI
120
+ ITLNKLGDHC QWTTKGLDVV WAGDDKRRAF IPKKNTWVGP TARSYPLAKY ERAMSKDGYV
121
+ TLRWDGEVLD ANCVRSLSQY EIVFVDQSCV FASAEAIIPS LEKALGLEAH FSVTIVDGVA
122
+ GCGKTTNIKQ IARSSGRDVD LILTSNRSSA DELKETIDCS PLTKLHYIRT CDSYLMSASA
123
+ VKAQRLIFDE CFLQHAGLVY AAATLAGCSE VIGFGDTEQI PFVSRNPSFV FRHHKLTGKV
124
+ ERKLITWRSP ADATYCLEKY FYKNKKPVKT NSRVLRSIEV VPINSPVSVE RNTNALYLCH
125
+ TQAEKAVLKA QTHLKGCDNI FTTHEAQGKT FDNVYFCRLT RTSTSLATGR DPINGPCNGL
126
+ VALSRHKKTF KYFTIAHDSD DVIYNACRDA GNTDDSILAR SYNHNF
127
+ //
@@ -0,0 +1,232 @@
1
+ ID 5HT1B_RABIT Reviewed; 390 AA.
2
+ AC P49144;
3
+ DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
4
+ DT 01-FEB-1996, sequence version 1.
5
+ DT 22-FEB-2023, entry version 127.
6
+ DE RecName: Full=5-hydroxytryptamine receptor 1B;
7
+ DE Short=5-HT-1B;
8
+ DE Short=5-HT1B;
9
+ DE AltName: Full=Serotonin 1D beta receptor;
10
+ DE Short=5-HT-1D-beta;
11
+ DE AltName: Full=Serotonin receptor 1B;
12
+ GN Name=HTR1B;
13
+ OS Oryctolagus cuniculus (Rabbit).
14
+ OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
15
+ OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
16
+ OX NCBI_TaxID=9986;
17
+ RN [1]
18
+ RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
19
+ RC TISSUE=Liver;
20
+ RX PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3;
21
+ RA Harwood G.S., Lockyer M., Giles H., Fairweather N.;
22
+ RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D beta
23
+ RT receptors.";
24
+ RL FEBS Lett. 377:73-76(1995).
25
+ RN [2]
26
+ RP NUCLEOTIDE SEQUENCE.
27
+ RC STRAIN=New Zealand white; TISSUE=Saphenous vein;
28
+ RA Wurch T., Cathala C., Palmer C., Valentin J.P., John G., Colpaert F.C.,
29
+ RA Pauwels P.J.;
30
+ RT "Molecular cloning and identification of a rabbit saphenous vein 5-HT 1DB
31
+ RT receptor gene.";
32
+ RL Neurosci. Res. Commun. 18:155-162(1996).
33
+ RN [3]
34
+ RP NUCLEOTIDE SEQUENCE.
35
+ RC STRAIN=New Zealand white;
36
+ RX PubMed=8878052; DOI=10.1007/bf00171053;
37
+ RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., Branchek T.A.,
38
+ RA Cohen M.L.;
39
+ RT "Differences in ligand binding profiles between cloned rabbit and human 5-
40
+ RT HT1D alpha and 5-HT1D beta receptors: ketanserin and methiothepin
41
+ RT distinguish rabbit 5-HT1D receptor subtypes.";
42
+ RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996).
43
+ CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
44
+ CC (serotonin). Also functions as a receptor for various alkaloids and
45
+ CC psychoactive substances. Ligand binding causes a conformation change
46
+ CC that triggers signaling via guanine nucleotide-binding proteins (G
47
+ CC proteins) and modulates the activity of down-stream effectors, such as
48
+ CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
49
+ CC Arrestin family members inhibit signaling via G proteins and mediate
50
+ CC activation of alternative signaling pathways. Regulates the release of
51
+ CC 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and
52
+ CC thereby affects neural activity, nociceptive processing, pain
53
+ CC perception, mood and behavior. Besides, plays a role in
54
+ CC vasoconstriction of cerebral arteries.
55
+ CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
56
+ CC {ECO:0000250}.
57
+ CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
58
+ CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
59
+ CC transmembrane helices. {ECO:0000250}.
60
+ CC -!- PTM: Phosphorylated. {ECO:0000250}.
61
+ CC -!- PTM: Palmitoylated. {ECO:0000250}.
62
+ CC -!- MISCELLANEOUS: A residue in the 7th transmembrane region ('Thr-355' in
63
+ CC human, 'Asn-351' in mouse and rat) is important for species-specific
64
+ CC sensitivity to various agonists. {ECO:0000250}.
65
+ CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
66
+ CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
67
+ CC ---------------------------------------------------------------------------
68
+ CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
69
+ CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
70
+ CC ---------------------------------------------------------------------------
71
+ DR EMBL; Z50163; CAA90531.1; -; Genomic_DNA.
72
+ DR EMBL; X89731; CAA61883.1; -; mRNA.
73
+ DR EMBL; U60826; AAB58467.1; -; Genomic_DNA.
74
+ DR PIR; S58126; S58126.
75
+ DR PIR; S68422; S68422.
76
+ DR RefSeq; NP_001076259.1; NM_001082790.1.
77
+ DR AlphaFoldDB; P49144; -.
78
+ DR SMR; P49144; -.
79
+ DR STRING; 9986.ENSOCUP00000016295; -.
80
+ DR BindingDB; P49144; -.
81
+ DR ChEMBL; CHEMBL5717; -.
82
+ DR GlyCosmos; P49144; 2 sites, No reported glycans.
83
+ DR GeneID; 100009594; -.
84
+ DR KEGG; ocu:100009594; -.
85
+ DR CTD; 3351; -.
86
+ DR eggNOG; KOG3656; Eukaryota.
87
+ DR InParanoid; P49144; -.
88
+ DR OrthoDB; 2999405at2759; -.
89
+ DR TreeFam; TF316350; -.
90
+ DR PRO; PR:P49144; -.
91
+ DR Proteomes; UP000001811; Unplaced.
92
+ DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
93
+ DR GO; GO:0045202; C:synapse; IEA:GOC.
94
+ DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
95
+ DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
96
+ DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
97
+ DR GO; GO:0046849; P:bone remodeling; IEA:InterPro.
98
+ DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
99
+ DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
100
+ DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
101
+ DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
102
+ DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
103
+ DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
104
+ DR CDD; cd15333; 7tmA_5-HT1B_1D; 1.
105
+ DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
106
+ DR InterPro; IPR002147; 5HT1B_rcpt.
107
+ DR InterPro; IPR002231; 5HT_rcpt.
108
+ DR InterPro; IPR000276; GPCR_Rhodpsn.
109
+ DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
110
+ DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
111
+ DR PANTHER; PTHR24248:SF66; OCTOPAMINE RECEPTOR BETA-3R; 1.
112
+ DR Pfam; PF00001; 7tm_1; 1.
113
+ DR PRINTS; PR00513; 5HT1BRECEPTR.
114
+ DR PRINTS; PR01101; 5HTRECEPTOR.
115
+ DR PRINTS; PR00237; GPCRRHODOPSN.
116
+ DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
117
+ DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
118
+ DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
119
+ DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
120
+ PE 2: Evidence at transcript level;
121
+ KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
122
+ KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
123
+ KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
124
+ FT CHAIN 1..390
125
+ FT /note="5-hydroxytryptamine receptor 1B"
126
+ FT /id="PRO_0000068920"
127
+ FT TOPO_DOM 1..49
128
+ FT /note="Extracellular"
129
+ FT /evidence="ECO:0000250"
130
+ FT TRANSMEM 50..75
131
+ FT /note="Helical; Name=1"
132
+ FT /evidence="ECO:0000250"
133
+ FT TOPO_DOM 76..84
134
+ FT /note="Cytoplasmic"
135
+ FT /evidence="ECO:0000250"
136
+ FT TRANSMEM 85..110
137
+ FT /note="Helical; Name=2"
138
+ FT /evidence="ECO:0000250"
139
+ FT TOPO_DOM 111..123
140
+ FT /note="Extracellular"
141
+ FT /evidence="ECO:0000250"
142
+ FT TRANSMEM 124..145
143
+ FT /note="Helical; Name=3"
144
+ FT /evidence="ECO:0000250"
145
+ FT TOPO_DOM 146..165
146
+ FT /note="Cytoplasmic"
147
+ FT /evidence="ECO:0000250"
148
+ FT TRANSMEM 166..187
149
+ FT /note="Helical; Name=4"
150
+ FT /evidence="ECO:0000250"
151
+ FT TOPO_DOM 188..205
152
+ FT /note="Extracellular"
153
+ FT /evidence="ECO:0000250"
154
+ FT TRANSMEM 206..228
155
+ FT /note="Helical; Name=5"
156
+ FT /evidence="ECO:0000250"
157
+ FT TOPO_DOM 229..315
158
+ FT /note="Cytoplasmic"
159
+ FT /evidence="ECO:0000250"
160
+ FT TRANSMEM 316..336
161
+ FT /note="Helical; Name=6"
162
+ FT /evidence="ECO:0000250"
163
+ FT TOPO_DOM 337..349
164
+ FT /note="Extracellular"
165
+ FT /evidence="ECO:0000250"
166
+ FT TRANSMEM 350..371
167
+ FT /note="Helical; Name=7"
168
+ FT /evidence="ECO:0000250"
169
+ FT TOPO_DOM 372..390
170
+ FT /note="Cytoplasmic"
171
+ FT /evidence="ECO:0000250"
172
+ FT REGION 260..282
173
+ FT /note="Disordered"
174
+ FT /evidence="ECO:0000256|SAM:MobiDB-lite"
175
+ FT MOTIF 146..148
176
+ FT /note="DRY motif; important for ligand-induced conformation
177
+ FT changes and signaling"
178
+ FT /evidence="ECO:0000250"
179
+ FT MOTIF 365..369
180
+ FT /note="NPxxY motif; important for ligand-induced
181
+ FT conformation changes and signaling"
182
+ FT /evidence="ECO:0000250"
183
+ FT BINDING 129
184
+ FT /ligand="ergotamine"
185
+ FT /ligand_id="ChEBI:CHEBI:190463"
186
+ FT /ligand_note="agonist"
187
+ FT /evidence="ECO:0000250|UniProtKB:P28222"
188
+ FT BINDING 134
189
+ FT /ligand="ergotamine"
190
+ FT /ligand_id="ChEBI:CHEBI:190463"
191
+ FT /ligand_note="agonist"
192
+ FT /evidence="ECO:0000250|UniProtKB:P28222"
193
+ FT BINDING 201
194
+ FT /ligand="ergotamine"
195
+ FT /ligand_id="ChEBI:CHEBI:190463"
196
+ FT /ligand_note="agonist"
197
+ FT /evidence="ECO:0000250|UniProtKB:P28222"
198
+ FT SITE 355
199
+ FT /note="Important for species-specific agonist sensitivity"
200
+ FT /evidence="ECO:0000250"
201
+ FT LIPID 388
202
+ FT /note="S-palmitoyl cysteine"
203
+ FT /evidence="ECO:0000255"
204
+ FT CARBOHYD 24
205
+ FT /note="N-linked (GlcNAc...) asparagine"
206
+ FT /evidence="ECO:0000255"
207
+ FT CARBOHYD 32
208
+ FT /note="N-linked (GlcNAc...) asparagine"
209
+ FT /evidence="ECO:0000255"
210
+ FT DISULFID 122..199
211
+ FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
212
+ FT CONFLICT 5
213
+ FT /note="G -> S (in Ref. 1 and 3)"
214
+ FT /evidence="ECO:0000305"
215
+ FT CONFLICT 7
216
+ FT /note="Q -> R (in Ref. 1 and 3)"
217
+ FT /evidence="ECO:0000305"
218
+ FT CONFLICT 14
219
+ FT /note="Missing (in Ref. 1 and 3)"
220
+ FT /evidence="ECO:0000305"
221
+ FT CONFLICT 171
222
+ FT /note="R -> A (in Ref. 1 and 3)"
223
+ FT /evidence="ECO:0000305"
224
+ SQ SEQUENCE 390 AA; 43496 MW; C22EBC077C6C897D CRC64;
225
+ MEEPGAQCAP PLAAGSQIAV PQANLSAAHS HNCSAEGYIY QDSIALPWKV LLVLLLALFT
226
+ LATTLSNAFV VATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV
227
+ VCDLWLSSDI TCCTASIMHL CVIALDRYWA ITDAVEYSAK RTPKRAAIMI RLVWVFSICI
228
+ SLPPFFWRQA KAEEEVSECL VNTDHVLYTV YSTVGAFYLP TLLLIALYGR IYVEARSRIL
229
+ KQTPNRTGKR LTRAQLITDS PGSTTSVTSI NSRAPDVPSE SGSPVYVNQV KVRVSDALLE
230
+ KKKLMAARER KATKTLGIIL GVFIVCWLPF FIISLVMPIC KDACWFHQAI FDFFTWLGYV
231
+ NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
232
+ //
@@ -187,8 +187,10 @@ module Bio
187
187
  return
188
188
  end
189
189
  assert_equal('', str.to_s.strip)
190
+ assert_equal('', err.to_s.strip)
190
191
  str, err = Bio::Command.query_command_open3(ary, @data)
191
192
  assert_equal(@sorted, str.to_s.strip.split(/\s+/))
193
+ assert_equal('', err.to_s.strip)
192
194
  end
193
195
  end #class FuncTestCommandQuery
194
196
 
@@ -38,7 +38,8 @@ module Bio
38
38
  "H01457 Diabetic retinopathy",
39
39
  "H01459 Diabetic neuropathy",
40
40
  "H01529 Avascular necrosis of femoral head",
41
- "H01709 Glucocorticoid-induced osteonecrosis"]
41
+ "H01709 Glucocorticoid-induced osteonecrosis",
42
+ "H02559 Microvascular complications of diabetes"]
42
43
 
43
44
  assert_equal(expected, @obj.diseases_as_strings)
44
45
  end
@@ -48,41 +49,54 @@ module Bio
48
49
  "H01457"=>"Diabetic retinopathy",
49
50
  "H01459"=>"Diabetic neuropathy",
50
51
  "H01529"=>"Avascular necrosis of femoral head",
51
- "H01709"=>"Glucocorticoid-induced osteonecrosis"}
52
+ "H01709"=>"Glucocorticoid-induced osteonecrosis",
53
+ "H02559"=>"Microvascular complications of diabetes"}
52
54
  assert_equal(expected, @obj.diseases_as_hash)
53
55
  end
54
56
 
55
57
  def test_drug_targets_as_strings
56
58
  expected = ["Abicipar pegol: D11517",
57
- "Aflibercept: D09574",
58
- "Aflibercept beta: D10819",
59
- "Bevacizumab: D06409",
59
+ "Aflibercept: D09574<JP/US>",
60
+ "Aflibercept beta: D10819<JP>",
61
+ "Bevacizumab: D06409<JP/US>",
60
62
  "Bevasiranib sodium: D08874",
61
- "Brolucizumab: D11083",
62
- "Faricimab: D11516",
63
+ "Brolucizumab: D11083<JP/US>",
64
+ "Dilpacimab: D11642",
65
+ "Emvododstat: D11890",
66
+ "Faricimab: D11516<JP/US>",
63
67
  "Navicixizumab: D11126",
64
68
  "Pegaptanib: D05386",
65
- "Ranibizumab: D05697",
69
+ "Ranibizumab: D05697<JP/US>",
70
+ "Tarcocimab: D12507",
71
+ "Tarcocimab tedromer: D12508",
66
72
  "Vanucizumab: D11244"]
67
73
  assert_equal(expected, @obj.drug_targets_as_strings)
68
74
  end
69
75
 
70
76
  def test_networks_as_strings
71
- expected = ["nt06114 PI3K signaling (virus)",
72
- "nt06124 Chemokine signaling (virus)",
77
+ expected = ["nt06124 Chemokine signaling (viruses)",
73
78
  "nt06164 Kaposi sarcoma-associated herpesvirus (KSHV)",
74
- "nt06214 PI3K signaling",
75
79
  "nt06219 JAK-STAT signaling",
76
80
  "nt06224 CXCR signaling",
77
81
  "nt06225 HIF-1 signaling",
82
+ "nt06227 Nuclear receptor signaling",
78
83
  "nt06262 Pancreatic cancer",
79
84
  "nt06264 Renal cell carcinoma",
85
+ "nt06360 Cushing syndrome",
86
+ "nt06526 MAPK signaling",
87
+ "nt06528 Calcium signaling",
88
+ "nt06530 PI3K signaling",
80
89
  "N00079 HIF-1 signaling pathway",
81
90
  "N00080 Loss of VHL to HIF-1 signaling pathway",
82
91
  "N00081 Mutation-inactivated VHL to HIF-1 signaling pathway",
83
92
  "N00095 ERBB2-overexpression to EGF-Jak-STAT signaling pathway",
84
93
  "N00157 KSHV vGPCR to GNB/G-ERK signaling pathway",
85
- "N00179 KSHV K1 to PI3K-NFKB signaling pathway"]
94
+ "N00317 AhR signaling pathway",
95
+ "N01412 Metals to HTF-1 signaling pathway",
96
+ "N01592 GF-RTK-RAS-ERK signaling pathway",
97
+ "N01641 RTK-PLCG-ITPR signaling pathway",
98
+ "N01656 GF-RTK-PI3K signaling pathway",
99
+ "N01658 GF-RTK-RAS-PI3K signaling pathway"]
86
100
  assert_equal(expected, @obj.networks_as_strings)
87
101
  end
88
102