NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2057772350|ref|NP_001382324|]
View 

general transcription factor IIH subunit 2 isoform e [Homo sapiens]

Protein Classification

general transcription factor IIH subunit 2 family protein( domain architecture ID 1004485)

general transcription factor IIH subunit 2 (GTF2H2) family protein such as GTF2H2, a component of the transcription factor TFIIH core which is involved in nucleotide excision repair (NER) of damaged DNA and in RNA transcription by RNA polymerase II

Gene Ontology:  GO:0006289|GO:0006351|GO:0000439
PubMed:  30798933

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SSL1 super family cl34921
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
 11-368 2.82e-90

RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair];


The actual alignment was detected with superfamily member COG5151:

Pssm-ID: 227480 [Multi-domain]  Cd Length: 421  Bit Score: 278.03  E-value: 2.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLK---- 86
Cdd:COG5151    40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKyaeg 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  87 -------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDmtCHGEPSLYNSLSIAMQTLKHMPGHTSREVLII 153
Cdd:COG5151   120 fvpeffsqnpisqLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 154 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELLTHHVS-PPPASSSS 228
Cdd:COG5151   198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMRELSHpTDFNGTKT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 229 ECSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHL 308
Cdd:COG5151   278 DLSLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYHHL 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057772350 309 FPLDAFQEIPLEEYNGERFCYGCQG-----------ELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 368
Cdd:COG5151   346 YPLKPFVEKPEGTNPKSTHCFVCQGpfpkppvspfdESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGC 416
 
Name Accession Description Interval E-value
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
 11-368 2.82e-90

RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227480 [Multi-domain]  Cd Length: 421  Bit Score: 278.03  E-value: 2.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLK---- 86
Cdd:COG5151    40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKyaeg 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  87 -------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDmtCHGEPSLYNSLSIAMQTLKHMPGHTSREVLII 153
Cdd:COG5151   120 fvpeffsqnpisqLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 154 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELLTHHVS-PPPASSSS 228
Cdd:COG5151   198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMRELSHpTDFNGTKT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 229 ECSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHL 308
Cdd:COG5151   278 DLSLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYHHL 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057772350 309 FPLDAFQEIPLEEYNGERFCYGCQG-----------ELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 368
Cdd:COG5151   346 YPLKPFVEKPEGTNPKSTHCFVCQGpfpkppvspfdESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGC 416
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
 56-219 1.19e-88

Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.


Pssm-ID: 238730  Cd Length: 183  Bit Score: 265.35  E-value: 1.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLK-----------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAv 118
Cdd:cd01453     1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKllelfieeffdqnpisqLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 119 dMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 198
Cdd:cd01453    80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158

                         170       180
                  ....*....|....*....|.
gi 2057772350 199 GGTYHVILDESHYKELLTHHV 219
Cdd:cd01453   159 NGTYKVILDETHLKELLLEHV 179
Ssl1 pfam04056
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.
 64-219 4.02e-86

Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.


Pssm-ID: 461149  Cd Length: 178  Bit Score: 258.51  E-value: 4.02e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  64 VVDGSRTMEDQDLKPNRLTCTLK-----------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDMTCHGEP 126
Cdd:pfam04056   1 VLDCSRSMEEKDLRPSRFACTIKyletfveeffdqnpisqIGLITCKDGRAHRLTDLTGNPRVHIKALKSLREAECGGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 127 SLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVIL 206
Cdd:pfam04056  81 SLQNALELARASLKHVPSHGSREVLIIFGSLSTCDPGDIYSTIDTLKKEKIRCSVIGLSAEVFICKELCKATNGTYSVAL 160

                         170
                  ....*....|...
gi 2057772350 207 DESHYKELLTHHV 219
Cdd:pfam04056 161 DETHLKELLLEHV 173
ssl1 TIGR00622
transcription factor ssl1; All proteins in this family for which functions are known are ...
 271-371 2.89e-57

transcription factor ssl1; All proteins in this family for which functions are known are components of the TFIIH complex which is involved in the initiaiton of transcription and nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129709  Cd Length: 112  Bit Score: 182.44  E-value: 2.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 271 GYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQ-----------GELKDQH 339
Cdd:TIGR00622   1 GYFCPQCRAKVCELPVECPICGLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCFGCQgpfpkppvspfDELKDSH 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2057772350 340 VYVCAVCQNVFCVDCDVFVHDSLHCCPGCIHK 371
Cdd:TIGR00622  81 RYVCAVCKNVFCVDCDVFVHESLHCCPGCIHK 112
C1_4 smart01047
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ...
 328-369 2.12e-16

TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription activity. This regions binds three zinc atoms through two independent domain. The first contains a C4 zinc finger motif, whereas the second is characterised by a CX(2)CX(2-4)FCADCD motif. The solution structure of the second C-terminal domain revealed homology with the regulatory domain of protein kinase C.


Pssm-ID: 214993  Cd Length: 49  Bit Score: 72.39  E-value: 2.12e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2057772350  328 CYGCQGEL---KDQHV----YVCAVCQNVFCVDCDVFVHDSLHCCPGCI 369
Cdd:smart01047   1 CFGCQSPFpnsKDKSVtssrYRCTKCKQVFCIDCDVFIHETLHNCPGCE 49
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 284-368 2.89e-03

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 39.71  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 284 LPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQgelKDQHVYVC-------AVCQNVFCVDCDV 356
Cdd:PLN03144    9 LPSDIPIVGCELTPYVLLRRPDGTLTTDDVPESAPLDGYFLRYRWYRIQ---SDRKVAVCsvhpsepATLQCVGCVKAKL 85

                          90
                  ....*....|..
gi 2057772350 357 FVHDSLHCCPGC 368
Cdd:PLN03144   86 PVSKSYHCSPKC 97
 
Name Accession Description Interval E-value
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
 11-368 2.82e-90

RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit SSL1 [Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227480 [Multi-domain]  Cd Length: 421  Bit Score: 278.03  E-value: 2.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLK---- 86
Cdd:COG5151    40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKyaeg 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  87 -------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDmtCHGEPSLYNSLSIAMQTLKHMPGHTSREVLII 153
Cdd:COG5151   120 fvpeffsqnpisqLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 154 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELLTHHVS-PPPASSSS 228
Cdd:COG5151   198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMRELSHpTDFNGTKT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 229 ECSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHL 308
Cdd:COG5151   278 DLSLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYHHL 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057772350 309 FPLDAFQEIPLEEYNGERFCYGCQG-----------ELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 368
Cdd:COG5151   346 YPLKPFVEKPEGTNPKSTHCFVCQGpfpkppvspfdESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGC 416
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
 56-219 1.19e-88

Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.


Pssm-ID: 238730  Cd Length: 183  Bit Score: 265.35  E-value: 1.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLK-----------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAv 118
Cdd:cd01453     1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKllelfieeffdqnpisqLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 119 dMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 198
Cdd:cd01453    80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158

                         170       180
                  ....*....|....*....|.
gi 2057772350 199 GGTYHVILDESHYKELLTHHV 219
Cdd:cd01453   159 NGTYKVILDETHLKELLLEHV 179
Ssl1 pfam04056
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.
 64-219 4.02e-86

Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.


Pssm-ID: 461149  Cd Length: 178  Bit Score: 258.51  E-value: 4.02e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  64 VVDGSRTMEDQDLKPNRLTCTLK-----------------IGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDMTCHGEP 126
Cdd:pfam04056   1 VLDCSRSMEEKDLRPSRFACTIKyletfveeffdqnpisqIGLITCKDGRAHRLTDLTGNPRVHIKALKSLREAECGGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 127 SLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVIL 206
Cdd:pfam04056  81 SLQNALELARASLKHVPSHGSREVLIIFGSLSTCDPGDIYSTIDTLKKEKIRCSVIGLSAEVFICKELCKATNGTYSVAL 160

                         170
                  ....*....|...
gi 2057772350 207 DESHYKELLTHHV 219
Cdd:pfam04056 161 DETHLKELLLEHV 173
ssl1 TIGR00622
transcription factor ssl1; All proteins in this family for which functions are known are ...
 271-371 2.89e-57

transcription factor ssl1; All proteins in this family for which functions are known are components of the TFIIH complex which is involved in the initiaiton of transcription and nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129709  Cd Length: 112  Bit Score: 182.44  E-value: 2.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 271 GYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQ-----------GELKDQH 339
Cdd:TIGR00622   1 GYFCPQCRAKVCELPVECPICGLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCFGCQgpfpkppvspfDELKDSH 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2057772350 340 VYVCAVCQNVFCVDCDVFVHDSLHCCPGCIHK 371
Cdd:TIGR00622  81 RYVCAVCKNVFCVDCDVFVHESLHCCPGCIHK 112
C1_4 smart01047
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ...
 328-369 2.12e-16

TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription activity. This regions binds three zinc atoms through two independent domain. The first contains a C4 zinc finger motif, whereas the second is characterised by a CX(2)CX(2-4)FCADCD motif. The solution structure of the second C-terminal domain revealed homology with the regulatory domain of protein kinase C.


Pssm-ID: 214993  Cd Length: 49  Bit Score: 72.39  E-value: 2.12e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2057772350  328 CYGCQGEL---KDQHV----YVCAVCQNVFCVDCDVFVHDSLHCCPGCI 369
Cdd:smart01047   1 CFGCQSPFpnsKDKSVtssrYRCTKCKQVFCIDCDVFIHETLHNCPGCE 49
C1_4 pfam07975
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ...
 327-368 1.58e-12

TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription activity. This regions binds three zinc atoms through two independent domain. The first contains a C4 zinc finger motif, whereas the second is characterized by a CX(2)CX(2-4)FCADCD motif. The solution structure of the second C-terminal domain revealed homology with the regulatory domain of protein kinase C (pfam00130).


Pssm-ID: 336887  Cd Length: 55  Bit Score: 61.73  E-value: 1.58e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2057772350 327 FCYGCQ-----------GELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 368
Cdd:pfam07975   1 NCYGCQkkfpkginkktDELLTSSRYRCPKCKQDFCIDCDVFIHESLHNCPGC 53
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 60-210 2.66e-09

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: 55.92  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350   60 HLYVVVDGSRTMEDQDLKP-----NRLTCTLKIGI------IVTKSKRAEKLTELsgNPRKHITSLKKAVDM---TCHGE 125
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELakefvLKLVEQLDIGPdgdrvgLVTFSDDARVLFPL--NDSRSKDALLEALASlsyKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  126 PSLYNSLSIAMQTLKHMPGHTSRE---VLIIFSSLT-TCDPSNIYDLIKTLKAAKIRVSVIGLSAEV--RVCTVLARETG 199
Cdd:smart00327  79 TNLGAALQYALENLFSKSAGSRRGapkVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKKLASAPG 158

                          170
                   ....*....|.
gi 2057772350  200 GTYHVILDESH 210
Cdd:smart00327 159 GVYVFLPELLD 169
VWA_2 pfam13519
von Willebrand factor type A domain;
61-153 4.06e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.06  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  61 LYVVVDGSRTMEDQDLKPNRLTCTL-------------KIGIIVTkSKRAEKLTELSGNPRKHITSLKKAVDMTchGEPS 127
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKdavlallkslpgdRVGLVTF-GDGPEVLIPLTKDRAKILRALRRLEPKG--GGTN 77

                          90       100
                  ....*....|....*....|....*.
gi 2057772350 128 LYNSLSIAMQTLKHMPGHTSREVLII 153
Cdd:pfam13519  78 LAAALQLARAALKHRRKNQPRRIVLI 103
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 59-188 4.30e-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: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  59 RHLYVVVDGSRTMEDQDLkpNRLTCTLKIGI-------------IVTKSKRAEklTELSGNPRKHITSLKKAVD---MTC 122
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKL--DKAKEALKALVsslsasppgdrvgLVTFGSNAR--VVLPLTTDTDKADLLEAIDalkKGL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2057772350 123 HGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSS-LTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV 188
Cdd:cd00198    77 GGGTNIGAALRLALELLKSAKRPNARRVIILLTDgEPNDGPELLAEAARELRKLGITVYTIGIGDDA 143
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 59-209 6.81e-06

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: 47.24  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350  59 RHLYVVVDGSRTMEDQdlkpNRLTcTLK---------------IGIIVTkSKRAEKLTELSGNprkhITSLKKAVD-MTC 122
Cdd:COG1240    93 RDVVLVVDASGSMAAE----NRLE-AAKgalldflddyrprdrVGLVAF-GGEAEVLLPLTRD----REALKRALDeLPP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 123 HGEPSLYNSLSIAMQTLKHMPGHTSReVLIIFS-SLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV---RVCTVLARET 198
Cdd:COG1240   163 GGGTPLGDALALALELLKRADPARRK-VIVLLTdGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAvdeGLLREIAEAT 241

                         170
                  ....*....|.
gi 2057772350 199 GGTYHVILDES 209
Cdd:COG1240   242 GGRYFRADDLS 252
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 284-368 2.89e-03

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 39.71  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772350 284 LPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQgelKDQHVYVC-------AVCQNVFCVDCDV 356
Cdd:PLN03144    9 LPSDIPIVGCELTPYVLLRRPDGTLTTDDVPESAPLDGYFLRYRWYRIQ---SDRKVAVCsvhpsepATLQCVGCVKAKL 85

                          90
                  ....*....|..
gi 2057772350 357 FVHDSLHCCPGC 368
Cdd:PLN03144   86 PVSKSYHCSPKC 97
 
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