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Conserved domains on  [gi|755551141|ref|XP_011243794|]
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otoconin-90 isoform X5 [Mus musculus]

Protein Classification

otoconin_90 domain-containing protein( domain architecture ID 10271500)

otoconin_90 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 190-305 1.54e-47

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


:

Pssm-ID: 153096  Cd Length: 117  Bit Score: 156.87  E-value: 1.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141 190 QLGEMLFCLTSHCPEEFETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGCLHGRRSQSSVVCEDHMAKCVGQSLC 269
Cdd:cd04707    1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDHKPKCEGVSVC 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755551141 270 EKLLCACDQMAAECMASAFFNQSLKSPDGAECQGEP 305
Cdd:cd04707   81 EKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQV 116
PLA2_like super family cl05417
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 1-66 4.17e-16

PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


The actual alignment was detected with superfamily member cd04707:

Pssm-ID: 471240  Cd Length: 117  Bit Score: 73.66  E-value: 4.17e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551141   1 MDCLQDpAKLSADVDCTNKQITCESEDPCERLLCTCDKAAVECLAQSGINSSLNFLDASFCLPQTP 66
Cdd:cd04707   53 MGCLQD-RKLSTEVTCVDHKPKCEGVSVCEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
 
Name Accession Description Interval E-value
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 190-305 1.54e-47

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 156.87  E-value: 1.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141 190 QLGEMLFCLTSHCPEEFETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGCLHGRRSQSSVVCEDHMAKCVGQSLC 269
Cdd:cd04707    1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDHKPKCEGVSVC 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755551141 270 EKLLCACDQMAAECMASAFFNQSLKSPDGAECQGEP 305
Cdd:cd04707   81 EKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQV 116
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 188-294 1.53e-39

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 135.81  E-value: 1.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141  188 MLQLGEMLFCLT-SHCPEEFETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGCLHGRRSQSSVVCEDHMAKCVGQ 266
Cdd:pfam00068   1 LWQFGEMIKCTTgRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGNPYLLSYNYSCSDGTITCSGN 80

                          90       100
                  ....*....|....*....|....*...
gi 755551141  267 SLCEKLLCACDQMAAECMASAFFNQSLK 294
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARATYNKKYK 108
PA2c smart00085
Phospholipase A2;
188-290 3.00e-16

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 73.78  E-value: 3.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141   188 MLQLGEMLFCLTshcPEE----FETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGClHGRRSQSSVVCEDHMAKC 263
Cdd:smart00085   2 LWQFGNMIQCAT---GKRawlsYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGC-NPKTTTYSYSCDNGFITC 77

                           90       100
                   ....*....|....*....|....*...
gi 755551141   264 VG-QSLCEKLLCACDQMAAECMASAFFN 290
Cdd:smart00085  78 GGkNTACLVFVCECDRAAAICFAKNPYN 105
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 1-66 4.17e-16

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 73.66  E-value: 4.17e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551141   1 MDCLQDpAKLSADVDCTNKQITCESEDPCERLLCTCDKAAVECLAQSGINSSLNFLDASFCLPQTP 66
Cdd:cd04707   53 MGCLQD-RKLSTEVTCVDHKPKCEGVSVCEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 3-53 7.79e-10

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 55.69  E-value: 7.79e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755551141    3 CLQdPAKLSADVDCTNKQITCESEDPCERLLCTCDKAAVECLAQSGINSSL 53
Cdd:pfam00068  58 CGN-PYLLSYNYSCSDGTITCSGNSSCEKQLCECDKAAAECFARATYNKKY 107
PA2c smart00085
Phospholipase A2;
15-47 3.70e-05

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 42.58  E-value: 3.70e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755551141    15 DCTNKQITCESE-DPCERLLCTCDKAAVECLAQS 47
Cdd:smart00085  69 SCDNGFITCGGKnTACLVFVCECDRAAAICFAKN 102
 
Name Accession Description Interval E-value
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 190-305 1.54e-47

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 156.87  E-value: 1.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141 190 QLGEMLFCLTSHCPEEFETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGCLHGRRSQSSVVCEDHMAKCVGQSLC 269
Cdd:cd04707    1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDHKPKCEGVSVC 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755551141 270 EKLLCACDQMAAECMASAFFNQSLKSPDGAECQGEP 305
Cdd:cd04707   81 EKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQV 116
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 188-294 1.53e-39

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 135.81  E-value: 1.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141  188 MLQLGEMLFCLT-SHCPEEFETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGCLHGRRSQSSVVCEDHMAKCVGQ 266
Cdd:pfam00068   1 LWQFGEMIKCTTgRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGNPYLLSYNYSCSDGTITCSGN 80

                          90       100
                  ....*....|....*....|....*...
gi 755551141  267 SLCEKLLCACDQMAAECMASAFFNQSLK 294
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARATYNKKYK 108
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 187-301 3.28e-22

PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153091  Cd Length: 115  Bit Score: 90.00  E-value: 3.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141 187 AMLQLGEMLFCLTSHCPEEFETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGCL------HGRRSQSSVVCEDhm 260
Cdd:cd00125    1 NLLQFGKMIKCTTGRSALDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSpyftsySYTCSDGQITCSD-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755551141 261 akcvGQSLCEKLLCACDQMAAECMASAFFNQSLKSPDGAEC 301
Cdd:cd00125   79 ----ANDKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
PA2c smart00085
Phospholipase A2;
188-290 3.00e-16

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 73.78  E-value: 3.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141   188 MLQLGEMLFCLTshcPEE----FETYGCYCGREGRGEPRDTLDRCCLSHHCCLEQMRQVGClHGRRSQSSVVCEDHMAKC 263
Cdd:smart00085   2 LWQFGNMIQCAT---GKRawlsYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGC-NPKTTTYSYSCDNGFITC 77

                           90       100
                   ....*....|....*....|....*...
gi 755551141   264 VG-QSLCEKLLCACDQMAAECMASAFFN 290
Cdd:smart00085  78 GGkNTACLVFVCECDRAAAICFAKNPYN 105
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 1-66 4.17e-16

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 73.66  E-value: 4.17e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551141   1 MDCLQDpAKLSADVDCTNKQITCESEDPCERLLCTCDKAAVECLAQSGINSSLNFLDASFCLPQTP 66
Cdd:cd04707   53 MGCLQD-RKLSTEVTCVDHKPKCEGVSVCEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 208-287 5.47e-15

PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153092  Cd Length: 83  Bit Score: 69.52  E-value: 5.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551141 208 TYGCYCGREGR----GEPRDTLDRCCLSHHCCLEQMRQVGCLHGRRSQSsvVCEDHMAKCVGQSLCEKLLCACDQMAAEC 283
Cdd:cd00618    2 PYGCYCGPGGSacpsGQPVDETDRCCRKHDCCYDQISDGGCCDGCLSYS--FSEGGVTCLTNSDLCTRSHCDCDRRLAIC 79


                 ....
gi 755551141 284 MASA 287
Cdd:cd00618   80 LARA 83
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 3-53 7.79e-10

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 55.69  E-value: 7.79e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755551141    3 CLQdPAKLSADVDCTNKQITCESEDPCERLLCTCDKAAVECLAQSGINSSL 53
Cdd:pfam00068  58 CGN-PYLLSYNYSCSDGTITCSGNSSCEKQLCECDKAAAECFARATYNKKY 107
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 15-61 2.30e-08

PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153091  Cd Length: 115  Bit Score: 51.87  E-value: 2.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755551141  15 DCTNKQITC-ESEDPCERLLCTCDKAAVECLAQSGINSSLNFLDASFC 61
Cdd:cd00125   68 TCSDGQITCsDANDKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
PA2c smart00085
Phospholipase A2;
15-47 3.70e-05

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 42.58  E-value: 3.70e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755551141    15 DCTNKQITCESE-DPCERLLCTCDKAAVECLAQS 47
Cdd:smart00085  69 SCDNGFITCGGKnTACLVFVCECDRAAAICFAKN 102
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 16-47 2.68e-03

PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153092  Cd Length: 83  Bit Score: 36.39  E-value: 2.68e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755551141  16 CTNKQITCESEDPCERLLCTCDKAAVECLAQS 47
Cdd:cd00618   52 SEGGVTCLTNSDLCTRSHCDCDRRLAICLARA 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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