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Conserved domains on  [gi|2057772486|ref|NP_001382319|]
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general transcription factor IIH subunit 2 isoform f [Homo sapiens]

Protein Classification

vWA_transcription_factor_IIH_type and C1_4 domain-containing protein( domain architecture ID 10106913)

vWA_transcription_factor_IIH_type and C1_4 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
56-236 4.46e-107

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: 311.19  E-value: 4.46e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAv 135
Cdd:cd01453     1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 136 dMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 215
Cdd:cd01453    80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158
                         170       180
                  ....*....|....*....|.
gi 2057772486 216 GGTYHVILDESHYKELLTHHV 236
Cdd:cd01453   159 NGTYKVILDETHLKELLLEHV 179
C1_4 super family cl06838
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ...
288-345 1.35e-27

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).


The actual alignment was detected with superfamily member TIGR00622:

Pssm-ID: 352591  Cd Length: 112  Bit Score: 104.63  E-value: 1.35e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2057772486 288 GYFCPQCRAKYCELPVECKIC-LTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGESWRF 345
Cdd:TIGR00622   1 GYFCPQCRAKVCELPVECPICgLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCF 59
 
Name Accession Description Interval E-value
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
56-236 4.46e-107

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: 311.19  E-value: 4.46e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAv 135
Cdd:cd01453     1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 136 dMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 215
Cdd:cd01453    80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158
                         170       180
                  ....*....|....*....|.
gi 2057772486 216 GGTYHVILDESHYKELLTHHV 236
Cdd:cd01453   159 NGTYKVILDETHLKELLLEHV 179
Ssl1 pfam04056
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.
64-236 2.95e-105

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


Pssm-ID: 461149  Cd Length: 178  Bit Score: 306.66  E-value: 2.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  64 VVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDMTCHGEP 143
Cdd:pfam04056   1 VLDCSRSMEEKDLRPSRFACTIKYLETFVEEFFDQNPISQIGLITCKDGRAHRLTDLTGNPRVHIKALKSLREAECGGDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 144 SLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVIL 223
Cdd:pfam04056  81 SLQNALELARASLKHVPSHGSREVLIIFGSLSTCDPGDIYSTIDTLKKEKIRCSVIGLSAEVFICKELCKATNGTYSVAL 160
                         170
                  ....*....|...
gi 2057772486 224 DESHYKELLTHHV 236
Cdd:pfam04056 161 DETHLKELLLEHV 173
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
11-355 2.75e-86

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: 266.86  E-value: 2.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEY 90
Cdd:COG5151    40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKYAEG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  91 FVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDmtCHGEPSLYNSLSIAMQTLKHMPGHTSREVLII 170
Cdd:COG5151   120 FVPEFFSQNPISQLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 171 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELLTHHVS-PPPASSSS 245
Cdd:COG5151   198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMRELSHpTDFNGTKT 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 246 ECSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKIC-LTLVSAPHLARSYHHL 324
Cdd:COG5151   278 DLSLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICsLQLILSTHLARSYHHL 345
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2057772486 325 FPLDAFQEIPleeyngESWRFIAKNCEESQS 355
Cdd:COG5151   346 YPLKPFVEKP------EGTNPKSTHCFVCQG 370
ssl1 TIGR00622
transcription factor ssl1; All proteins in this family for which functions are known are ...
288-345 1.35e-27

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: 104.63  E-value: 1.35e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2057772486 288 GYFCPQCRAKYCELPVECKIC-LTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGESWRF 345
Cdd:TIGR00622   1 GYFCPQCRAKVCELPVECPICgLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCF 59
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
60-227 3.78e-15

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: 72.49  E-value: 3.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486   60 HLYVVVDGSRTMEdqdlkPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTkSKRAEKLTELsgNPRKHITSLKKAVDM-- 137
Cdd:smart00327   1 DVVFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPL--NDSRSKDALLEALASls 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  138 -TCHGEPSLYNSLSIAMQTLKHMPGHTSRE---VLIIFSSLT-TCDPSNIYDLIKTLKAAKIRVSVIGLSAEV--RVCTV 210
Cdd:smart00327  73 yKLGGGTNLGAALQYALENLFSKSAGSRRGapkVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKK 152
                          170
                   ....*....|....*..
gi 2057772486  211 LARETGGTYHVILDESH 227
Cdd:smart00327 153 LASAPGGVYVFLPELLD 169
 
Name Accession Description Interval E-value
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
56-236 4.46e-107

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: 311.19  E-value: 4.46e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAv 135
Cdd:cd01453     1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 136 dMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 215
Cdd:cd01453    80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158
                         170       180
                  ....*....|....*....|.
gi 2057772486 216 GGTYHVILDESHYKELLTHHV 236
Cdd:cd01453   159 NGTYKVILDETHLKELLLEHV 179
Ssl1 pfam04056
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.
64-236 2.95e-105

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


Pssm-ID: 461149  Cd Length: 178  Bit Score: 306.66  E-value: 2.95e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  64 VVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDMTCHGEP 143
Cdd:pfam04056   1 VLDCSRSMEEKDLRPSRFACTIKYLETFVEEFFDQNPISQIGLITCKDGRAHRLTDLTGNPRVHIKALKSLREAECGGDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 144 SLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVIL 223
Cdd:pfam04056  81 SLQNALELARASLKHVPSHGSREVLIIFGSLSTCDPGDIYSTIDTLKKEKIRCSVIGLSAEVFICKELCKATNGTYSVAL 160
                         170
                  ....*....|...
gi 2057772486 224 DESHYKELLTHHV 236
Cdd:pfam04056 161 DETHLKELLLEHV 173
SSL1 COG5151
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ...
11-355 2.75e-86

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: 266.86  E-value: 2.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEY 90
Cdd:COG5151    40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKYAEG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  91 FVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDmtCHGEPSLYNSLSIAMQTLKHMPGHTSREVLII 170
Cdd:COG5151   120 FVPEFFSQNPISQLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 171 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELLTHHVS-PPPASSSS 245
Cdd:COG5151   198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMRELSHpTDFNGTKT 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 246 ECSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKIC-LTLVSAPHLARSYHHL 324
Cdd:COG5151   278 DLSLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICsLQLILSTHLARSYHHL 345
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2057772486 325 FPLDAFQEIPleeyngESWRFIAKNCEESQS 355
Cdd:COG5151   346 YPLKPFVEKP------EGTNPKSTHCFVCQG 370
ssl1 TIGR00622
transcription factor ssl1; All proteins in this family for which functions are known are ...
288-345 1.35e-27

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: 104.63  E-value: 1.35e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2057772486 288 GYFCPQCRAKYCELPVECKIC-LTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGESWRF 345
Cdd:TIGR00622   1 GYFCPQCRAKVCELPVECPICgLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCF 59
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
60-227 3.78e-15

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: 72.49  E-value: 3.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486   60 HLYVVVDGSRTMEdqdlkPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTkSKRAEKLTELsgNPRKHITSLKKAVDM-- 137
Cdd:smart00327   1 DVVFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPL--NDSRSKDALLEALASls 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  138 -TCHGEPSLYNSLSIAMQTLKHMPGHTSRE---VLIIFSSLT-TCDPSNIYDLIKTLKAAKIRVSVIGLSAEV--RVCTV 210
Cdd:smart00327  73 yKLGGGTNLGAALQYALENLFSKSAGSRRGapkVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKK 152
                          170
                   ....*....|....*..
gi 2057772486  211 LARETGGTYHVILDESH 227
Cdd:smart00327 153 LASAPGGVYVFLPELLD 169
VWA_2 pfam13519
von Willebrand factor type A domain;
61-170 3.46e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.31  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  61 LYVVVDGSRTMEDQDLKPNRLTctlkLLEYFVEEYFDQNPISQIGIIVTkSKRAEKLTELSGNPRKHITSLKKAVDMTch 140
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLE----AAKDAVLALLKSLPGDRVGLVTF-GDGPEVLIPLTKDRAKILRALRRLEPKG-- 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 2057772486 141 GEPSLYNSLSIAMQTLKHMPGHTSREVLII 170
Cdd:pfam13519  74 GGTNLAAALQLARAALKHRRKNQPRRIVLI 103
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
59-205 2.58e-09

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: 55.65  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  59 RHLYVVVDGSRTMEDQDLKPnrltcTLKLLEYFVEEYFDQNPISQIGIiVTKSKRAEklTELSGNPRKHITSLKKAVD-- 136
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDK-----AKEALKALVSSLSASPPGDRVGL-VTFGSNAR--VVLPLTTDTDKADLLEAIDal 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2057772486 137 -MTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSS-LTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV 205
Cdd:cd00198    73 kKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDgEPNDGPELLAEAARELRKLGITVYTIGIGDDA 143
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
59-226 3.06e-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: 57.26  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  59 RHLYVVVDGSRTMEDQdlkpNRLTCTLKLLEYFVEEYFDQNpisQIGIIVTkSKRAEKLTELSGNprkhITSLKKAVD-M 137
Cdd:COG1240    93 RDVVLVVDASGSMAAE----NRLEAAKGALLDFLDDYRPRD---RVGLVAF-GGEAEVLLPLTRD----REALKRALDeL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486 138 TCHGEPSLYNSLSIAMQTLKHMPGHTSReVLIIFS-SLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV---RVCTVLAR 213
Cdd:COG1240   161 PPGGGTPLGDALALALELLKRADPARRK-VIVLLTdGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAvdeGLLREIAE 239
                         170
                  ....*....|...
gi 2057772486 214 ETGGTYHVILDES 226
Cdd:COG1240   240 ATGGRYFRADDLS 252
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
63-199 3.43e-03

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 38.11  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057772486  63 VVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSL-KKAVDMTCHg 141
Cdd:cd01452     8 ICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLhDVQPKGKAN- 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2057772486 142 epsLYNSLSIAMQTLKHMPGHTSREVLIIF-SSLTTCDPSNIYDLIKTLKAAKIRVSVI 199
Cdd:cd01452    87 ---FITGIQIAQLALKHRQNKNQKQRIVAFvGSPIEEDEKDLVKLAKRLKKNNVSVDII 142
 
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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