NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74188152|dbj|BAE37170|]
View 

unnamed protein product, partial [Mus musculus]

Protein Classification

MoaD/ThiS family protein; Ubl5/Hub1 family ubiquitin-like protein( domain architecture ID 13892551)

MoaD/ThiS family protein is a ubiquitin-like protein, may be involved in sulfur transfer| Ubl5/Hub1 family ubiquitin-like protein similar to Saccharomyces cerevisiae Hub1 that plays a role in splice-site usage and alternative splicing

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RA_Rin2 cd16131
Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras ...
 542-632 1.01e-62

Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras association domain family 4, or Ras inhibitor JC265, or Ras interaction/interference protein 2, is a Rab5 GDP/GTP exchange factor with the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains. Rin2 connects three GTPases, R-Ras, Rab5 and Rac1, to promote endothelial cell adhesion through the regulation of integrin internalization and Rac1 activation. Rin2 is involved in the regulation of Rab5-mediated early endocytosis. The deficiency of Rin2 can cause the RIN2 syndrome, an autosomal recessive connective tissue disorder.


:

Pssm-ID: 340548  Cd Length: 91  Bit Score: 202.40  E-value: 1.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 542 FQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELHSRPQP 621
Cdd:cd16131   1 FQNYLRVAFQEVNSGCTAKTLLVRPYTTTEEVCQLCAQKFKVQDPENYSLFLLIDDTWQQLAEDTYPQKIKAELHSRPQP 80

                        90
                ....*....|.
gi 74188152 622 HIFHFVYKRIK 632
Cdd:cd16131  81 QIFHFVYKRIP 91
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 405-521 7.02e-51

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


:

Pssm-ID: 128469  Cd Length: 117  Bit Score: 171.87  E-value: 7.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152    405 ELEKIKLKFMTMQKmySPEKKVMLLLRVCKLIYTVMENNSGRMYGADDFLPVLTYVIAQCDMLELDTEIEYMMELLDPSL 484
Cdd:smart00167   3 EIEQIELKFLQLYK--SPSDKIKCLLRACKLIYTLLETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 74188152    485 LHGEGGYYLTSAYGALSLIKNFQEEQAARLLSSEARD 521
Cdd:smart00167  81 LTGEGGYYLTSLSAALALIKGLTEAHALPLSPEQELE 117
 
Name Accession Description Interval E-value
RA_Rin2 cd16131
Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras ...
 542-632 1.01e-62

Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras association domain family 4, or Ras inhibitor JC265, or Ras interaction/interference protein 2, is a Rab5 GDP/GTP exchange factor with the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains. Rin2 connects three GTPases, R-Ras, Rab5 and Rac1, to promote endothelial cell adhesion through the regulation of integrin internalization and Rac1 activation. Rin2 is involved in the regulation of Rab5-mediated early endocytosis. The deficiency of Rin2 can cause the RIN2 syndrome, an autosomal recessive connective tissue disorder.


Pssm-ID: 340548  Cd Length: 91  Bit Score: 202.40  E-value: 1.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 542 FQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELHSRPQP 621
Cdd:cd16131   1 FQNYLRVAFQEVNSGCTAKTLLVRPYTTTEEVCQLCAQKFKVQDPENYSLFLLIDDTWQQLAEDTYPQKIKAELHSRPQP 80

                        90
                ....*....|.
gi 74188152 622 HIFHFVYKRIK 632
Cdd:cd16131  81 QIFHFVYKRIP 91
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 405-521 7.02e-51

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 171.87  E-value: 7.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152    405 ELEKIKLKFMTMQKmySPEKKVMLLLRVCKLIYTVMENNSGRMYGADDFLPVLTYVIAQCDMLELDTEIEYMMELLDPSL 484
Cdd:smart00167   3 EIEQIELKFLQLYK--SPSDKIKCLLRACKLIYTLLETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 74188152    485 LHGEGGYYLTSAYGALSLIKNFQEEQAARLLSSEARD 521
Cdd:smart00167  81 LTGEGGYYLTSLSAALALIKGLTEAHALPLSPEQELE 117
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 406-507 4.95e-26

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 102.67  E-value: 4.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152   406 LEKIKLKFMTMQKMYSPEKKVMLLLRVCKLIYTVMEN-NSGRMYGADDFLPVLTYVIAQCDMLELDTEIEYMMELLDPSL 484
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKsNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|...
gi 74188152   485 LHGEGGYYLTSAYGALSLIKNFQ 507
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIESLD 103
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 542-630 8.53e-16

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.14  E-value: 8.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152   542 FQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVE-DPEEYSLFLFV--DETWQQLAEDTYPQKIKAELHSR 618
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEdDPRDYVLVEVLerGGGERRLPDDECPLQIQLQWPRD 80

                          90
                  ....*....|..
gi 74188152   619 pqPHIFHFVYKR 630
Cdd:pfam00788  81 --ASDSRFLLRK 90
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 542-630 4.86e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 68.09  E-value: 4.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152    542 FQNYLRVAFqEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVED-PEEYSLFLFV-DETWQQLAEDTYPQKIKAELHsrP 619
Cdd:smart00314   1 DTFVLRVYV-DDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdPEEYVLVEVLpDGKERVLPDDENPLQLQKLWP--R 77

                           90
                   ....*....|.
gi 74188152    620 QPHIFHFVYKR 630
Cdd:smart00314  78 RGPNLRFVLRK 88
 
Name Accession Description Interval E-value
RA_Rin2 cd16131
Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras ...
 542-632 1.01e-62

Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras association domain family 4, or Ras inhibitor JC265, or Ras interaction/interference protein 2, is a Rab5 GDP/GTP exchange factor with the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains. Rin2 connects three GTPases, R-Ras, Rab5 and Rac1, to promote endothelial cell adhesion through the regulation of integrin internalization and Rac1 activation. Rin2 is involved in the regulation of Rab5-mediated early endocytosis. The deficiency of Rin2 can cause the RIN2 syndrome, an autosomal recessive connective tissue disorder.


Pssm-ID: 340548  Cd Length: 91  Bit Score: 202.40  E-value: 1.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 542 FQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELHSRPQP 621
Cdd:cd16131   1 FQNYLRVAFQEVNSGCTAKTLLVRPYTTTEEVCQLCAQKFKVQDPENYSLFLLIDDTWQQLAEDTYPQKIKAELHSRPQP 80

                        90
                ....*....|.
gi 74188152 622 HIFHFVYKRIK 632
Cdd:cd16131  81 QIFHFVYKRIP 91
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 405-521 7.02e-51

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 171.87  E-value: 7.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152    405 ELEKIKLKFMTMQKmySPEKKVMLLLRVCKLIYTVMENNSGRMYGADDFLPVLTYVIAQCDMLELDTEIEYMMELLDPSL 484
Cdd:smart00167   3 EIEQIELKFLQLYK--SPSDKIKCLLRACKLIYTLLETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 74188152    485 LHGEGGYYLTSAYGALSLIKNFQEEQAARLLSSEARD 521
Cdd:smart00167  81 LTGEGGYYLTSLSAALALIKGLTEAHALPLSPEQELE 117
RA_Rin cd01776
Ras-associating (RA) domain of Ras and Rab interactor (Rin) protein family; Family of ...
 543-632 1.76e-34

Ras-associating (RA) domain of Ras and Rab interactor (Rin) protein family; Family of Ras-interaction/interference (Rin) proteins, also known as Ras and Rab interactors, is composed of Rin1, Rin2, and Rin3, which have multifunctional domains, including SH2 and proline-rich domains in the N-terminal region, and RH, VPS9, and RA domains in the C-terminal region. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domains of Rin1, Rin2, and Rin3 are well conserved and they all have Ras binding characteristics.


Pssm-ID: 340474  Cd Length: 90  Bit Score: 125.87  E-value: 1.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 543 QNYLRVAFQEVNSGC-TGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELHSRPQP 621
Cdd:cd01776   1 QGFLRVAVPDENNGSiVSKTLPVRPSMTAREVCKMIAHKFRVTNPQDYGLFLLVDGEEIQLEDNECPQLIKGELLATSKK 80

                        90
                ....*....|.
gi 74188152 622 HiFHFVYKRIK 632
Cdd:cd01776  81 P-CYFAYKRID 90
RA_Rin3 cd16130
Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3); Rin3, also termed Ras ...
 543-631 8.92e-27

Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3); Rin3, also termed Ras interaction/interference protein 3, is a RAS effector and a RAB5-activating guanine nucleotide exchange factor (GEF) specifically for GTPase Rab31. It functions as a negative regulator of mast cell responses to Stem Cell Factor (SCF). Rin3 contains the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains.


Pssm-ID: 340547  Cd Length: 88  Bit Score: 104.04  E-value: 8.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 543 QNYLRVAFQEVnsGCTGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELHSRPQPH 622
Cdd:cd16130   1 QDFISVSFLEP--GSNTRTLAIRPDTTAEDLCKQCAEKFEVLDPENYGLFVLVDGRCLQLADDALPHHIKSDLLKSEPRK 78


                ....*....
gi 74188152 623 IFHFVYKRI 631
Cdd:cd16130  79 DFHFLYKQL 87
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 406-507 4.95e-26

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 102.67  E-value: 4.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152   406 LEKIKLKFMTMQKMYSPEKKVMLLLRVCKLIYTVMEN-NSGRMYGADDFLPVLTYVIAQCDMLELDTEIEYMMELLDPSL 484
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKsNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|...
gi 74188152   485 LHGEGGYYLTSAYGALSLIKNFQ 507
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIESLD 103
RA_Rin1 cd17215
Ras-associating (RA) domain found in Ras and Rab interactor 1 (Rin1); Rin1, also termed Ras ...
 543-630 5.94e-24

Ras-associating (RA) domain found in Ras and Rab interactor 1 (Rin1); Rin1, also termed Ras inhibitor JC99, or Ras interaction/interference protein 1, is a downstream Ras effector that represents a unique class of Ras effector connected to two independent signaling pathways. The first effector pathway is the direct activation of RAB5-mediated endocytosis and the second pathway involves direct activation of ABL tyrosine kinase activity. Rin1 functions as a guanine nucleotide exchange factor (GEF) for RAB5 GTPases. The RAB5 GEF activity of Rin1 promotes early endosome fusion, an early event in transit to the lysosome. Rin1 binds the SH3 and SH2 domains of ABL proteins, ABL1 and ABL2, and activates their tyrosine kinase activity. Rin1 contains SH2 and proline-rich domains in the N-terminal region, and RH, VPS9, and RA domains in the C-terminal region. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340735  Cd Length: 88  Bit Score: 96.20  E-value: 5.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 543 QNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELhsRPQPH 622
Cdd:cd17215   1 QNFLRVAYQDPSSGCTSKTLAVPPSATVADLNQLCATKFKVTQPETYGIFLYKEQGYQRLPPDALPQRIKAQL--KEKGS 78


                ....*...
gi 74188152 623 IFHFVYKR 630
Cdd:cd17215  79 TFYFVYQR 86
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 545-630 3.40e-17

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 76.97  E-value: 3.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152 545 YLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKV-EDPEEYSLFLFVD--ETWQQLAEDTYPQKIKAElhSRPQP 621
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLeEDPEDYSLYEVSEkqETERVLHDDECPLLIQLE--WGPQG 78


                ....*....
gi 74188152 622 HIFHFVYKR 630
Cdd:cd17043  79 TEFRFVLKR 87
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 542-630 8.53e-16

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.14  E-value: 8.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152   542 FQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVE-DPEEYSLFLFV--DETWQQLAEDTYPQKIKAELHSR 618
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEdDPRDYVLVEVLerGGGERRLPDDECPLQIQLQWPRD 80

                          90
                  ....*....|..
gi 74188152   619 pqPHIFHFVYKR 630
Cdd:pfam00788  81 --ASDSRFLLRK 90
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 542-630 4.86e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 68.09  E-value: 4.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74188152    542 FQNYLRVAFqEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVED-PEEYSLFLFV-DETWQQLAEDTYPQKIKAELHsrP 619
Cdd:smart00314   1 DTFVLRVYV-DDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdPEEYVLVEVLpDGKERVLPDDENPLQLQKLWP--R 77

                           90
                   ....*....|.
gi 74188152    620 QPHIFHFVYKR 630
Cdd:smart00314  78 RGPNLRFVLRK 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH