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Conserved domains on  [gi|1491308475|gb|RLI72202|]
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MAG: hypothetical protein DRP02_02525 [Candidatus Gerdarchaeota archaeon]

Protein Classification

vWA domain-containing protein( domain architecture ID 10076759)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ChlD super family cl34203
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 179-355 1.99e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


The actual alignment was detected with superfamily member COG1240:

Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 58.41  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 179 WLARQLPARPVNDTIVRPRGKIHKKKTFEHSIFTSQTIPPKSIDIDDIVVMKKDRNAQIYLIVDTSQSMRNvvqgthFSR 258
Cdd:COG1240    37 DLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAA------ENR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 259 LEGA--LLTSLAifyyfkrqgRTRRTNQR----AFRTA---VVPISktrqiiTSEDQLERFLLTATAKGRTPMSASIKTA 329
Cdd:COG1240   111 LEAAkgALLDFL---------DDYRPRDRvglvAFGGEaevLLPLT------RDREALKRALDELPPGGGTPLGDALALA 175

                         170       180
                  ....*....|....*....|....*.
gi 1491308475 330 IEHakVKKNTQNRDVHLIIVTDGRPN 355
Cdd:COG1240   176 LEL--LKRADPARRKVIVLLTDGRDN 199
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 179-355 1.99e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 58.41  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 179 WLARQLPARPVNDTIVRPRGKIHKKKTFEHSIFTSQTIPPKSIDIDDIVVMKKDRNAQIYLIVDTSQSMRNvvqgthFSR 258
Cdd:COG1240    37 DLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAA------ENR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 259 LEGA--LLTSLAifyyfkrqgRTRRTNQR----AFRTA---VVPISktrqiiTSEDQLERFLLTATAKGRTPMSASIKTA 329
Cdd:COG1240   111 LEAAkgALLDFL---------DDYRPRDRvglvAFGGEaevLLPLT------RDREALKRALDELPPGGGTPLGDALALA 175

                         170       180
                  ....*....|....*....|....*.
gi 1491308475 330 IEHakVKKNTQNRDVHLIIVTDGRPN 355
Cdd:COG1240   176 LEL--LKRADPARRKVIVLLTDGRDN 199
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 235-356 6.29e-06

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 46.40  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 235 AQIYLIVDTSQSMRNvvqgthfSRLEGALLTSLAIFYYFKRQGRTRRTNQRAFRTAVVPISKTRQIITSEDQLERF-LLT 313
Cdd:cd00198     1 ADIVFLLDVSGSMGG-------EKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIdALK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1491308475 314 ATAKGRTPMSASIKTAIEHAKVKKNTQNRDVhLIIVTDGRPNE 356
Cdd:cd00198    74 KGLGGGTNIGAALRLALELLKSAKRPNARRV-IILLTDGEPND 115
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 237-362 1.87e-04

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 42.06  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475  237 IYLIVDTSQSMRNvvqgthfSRLEGALLTSLAIFYYFKRQGRTRRTNQRAFRTAVVPISKTRQIiTSEDQLERFL--LTA 314
Cdd:smart00327   2 VVFLLDGSGSMGG-------NRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALasLSY 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1491308475  315 TAKGRTPMSASIKTAIEHAKVKKNTQNRDV--HLIIVTDGRPNELIPGYE 362
Cdd:smart00327  74 KLGGGTNLGAALQYALENLFSKSAGSRRGApkVVILITDGESNDGPKDLL 123
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 179-355 1.99e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 58.41  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 179 WLARQLPARPVNDTIVRPRGKIHKKKTFEHSIFTSQTIPPKSIDIDDIVVMKKDRNAQIYLIVDTSQSMRNvvqgthFSR 258
Cdd:COG1240    37 DLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAA------ENR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 259 LEGA--LLTSLAifyyfkrqgRTRRTNQR----AFRTA---VVPISktrqiiTSEDQLERFLLTATAKGRTPMSASIKTA 329
Cdd:COG1240   111 LEAAkgALLDFL---------DDYRPRDRvglvAFGGEaevLLPLT------RDREALKRALDELPPGGGTPLGDALALA 175

                         170       180
                  ....*....|....*....|....*.
gi 1491308475 330 IEHakVKKNTQNRDVHLIIVTDGRPN 355
Cdd:COG1240   176 LEL--LKRADPARRKVIVLLTDGRDN 199
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 231-379 1.38e-06

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 49.68  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 231 KDRNAQIYLIVDTSQSMRNvvqgthfSRLEGALLTSLAIfyyFKRQGRTRRTNQRAFRTAVV---PISKTRQIitseDQL 307
Cdd:COG2425   115 PLLEGPVVLCVDTSGSMAG-------SKEAAAKAAALAL---LRALRPNRRFGVILFDTEVVedlPLTADDGL----EDA 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491308475 308 ERFLLTATAKGRTPMSASIKTAIEHAkvkKNTQNRDVHLIIVTDgrpnelipGYEPTPSQSLINYFEEERSG 379
Cdd:COG2425   181 IEFLSGLFAGGGTDIAPALRAALELL---EEPDYRNADIVLITD--------GEAGVSPEELLREVRAKESG 241
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 235-356 6.29e-06

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 46.40  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 235 AQIYLIVDTSQSMRNvvqgthfSRLEGALLTSLAIFYYFKRQGRTRRTNQRAFRTAVVPISKTRQIITSEDQLERF-LLT 313
Cdd:cd00198     1 ADIVFLLDVSGSMGG-------EKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIdALK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1491308475 314 ATAKGRTPMSASIKTAIEHAKVKKNTQNRDVhLIIVTDGRPNE 356
Cdd:cd00198    74 KGLGGGTNIGAALRLALELLKSAKRPNARRV-IILLTDGEPND 115
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 237-362 1.87e-04

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 42.06  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475  237 IYLIVDTSQSMRNvvqgthfSRLEGALLTSLAIFYYFKRQGRTRRTNQRAFRTAVVPISKTRQIiTSEDQLERFL--LTA 314
Cdd:smart00327   2 VVFLLDGSGSMGG-------NRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALasLSY 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1491308475  315 TAKGRTPMSASIKTAIEHAKVKKNTQNRDV--HLIIVTDGRPNELIPGYE 362
Cdd:smart00327  74 KLGGGTNLGAALQYALENLFSKSAGSRRGApkVVILITDGESNDGPKDLL 123
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 236-379 2.30e-03

VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 38.48  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 236 QIYLIVDTSQSMRNVVQGTHFSrLEGALLTSLAIfyyfkrqgRTRRTNQRAFRTAVV--PISKTRQIitseDQLERFLLT 313
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKA-VALALLRIALA--------ENRDTYLILFDSEFQtkIVDKTDDL----EEPVEFLSG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491308475 314 ATAKGRTpmsaSIKTAIEHA-KVKKNTQNRDVHLIIVTDgrpnelipGYEPTPSQSLINYFEEERSG 379
Cdd:cd01462    69 VQLGGGT----DINKALRYAlELIERRDPRKADIVLITD--------GYEGGVSDELLREVELKRSR 123
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
232-351 5.33e-03

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 38.65  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308475 232 DRNAQIYLIVDTSQSMRnvVQGTHFSRLEGALLTSLAIFYYFKRQG-RTR-RTNQRAFRTAVVPISKTRQIitseDQLER 309
Cdd:COG1721   145 ERELTVVLLLDTSASMR--FGSGGPSKLDLAVEAAASLAYLALRQGdRVGlLTFGDRVRRYLPPRRGRRHL----LRLLE 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1491308475 310 FLLTATAKGRTPMSASIKTAIEHAKvkkntqnRDVHLIIVTD 351
Cdd:COG1721   219 ALARLEPAGETDLAAALRRLARRLP-------RRSLVVLISD 253
 
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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