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Conserved domains on  [gi|2082445383|ref|XP_042993403|]
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26S proteasome non-ATPase regulatory subunit 4 homolog isoform X3 [Carya illinoinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 1-188 4.62e-105

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: 308.14  E-value: 4.62e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   1 MVLEATMICIDNSEWMRNGDYAPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKGVRVLVTPTSDLGKILACMHGLE 80
Cdd:cd01452     1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383  81 IGGEMNLASGIQVAQLALKHRQNKKQQQRIIVFCGSPIKHEKKLIEMIGRKLKKNSVALDIINFGEQDDGKiEKLEALLA 160
Cdd:cd01452    81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNT-EKLTAFID 159

                         170       180
                  ....*....|....*....|....*...
gi 2082445383 161 AVNNNDTSHIVHVPTGSSALSDVLINTP 188
Cdd:cd01452   160 AVNGKDGSHLVSVPPGENLLSDALLSSP 187
PSMD4_RAZUL cd22297
RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) ...
 345-389 5.06e-11

RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) and similar proteins; PSMD4 is also called 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit S5A, antisecretory factor 1, AF, ASF, or multiubiquitin chain-binding protein (MCB1). It acts as a ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. It displays a preferred selectivity for longer polyubiquitin chains. PSMD4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. The proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The model corresponds to the C-terminal Rpn10 AZUL-binding domain (RAZUL) of PSMD4, which is responsible for binding the AZUL domain of E6AP/UBE3A. AZUL stands for amino-terminal zinc-binding domain of ubiquitin E3a ligase.


:

Pssm-ID: 412092  Cd Length: 48  Bit Score: 57.20  E-value: 5.06e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2082445383 345 SSQSDLSKLLADQSFVSSILASLPGVDPNDPSVKNLLDSIQSQTE 389
Cdd:cd22297     1 SEEEDMSDVMQDPEFLQSVLGSLPGVDPNDEAVQNALGSLAKQDE 45
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 1-188 4.62e-105

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: 308.14  E-value: 4.62e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   1 MVLEATMICIDNSEWMRNGDYAPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKGVRVLVTPTSDLGKILACMHGLE 80
Cdd:cd01452     1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383  81 IGGEMNLASGIQVAQLALKHRQNKKQQQRIIVFCGSPIKHEKKLIEMIGRKLKKNSVALDIINFGEQDDGKiEKLEALLA 160
Cdd:cd01452    81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNT-EKLTAFID 159

                         170       180
                  ....*....|....*....|....*...
gi 2082445383 161 AVNNNDTSHIVHVPTGSSALSDVLINTP 188
Cdd:cd01452   160 AVNGKDGSHLVSVPPGENLLSDALLSSP 187
VWA_2 pfam13519
von Willebrand factor type A domain;
6-113 9.60e-29

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 108.15  E-value: 9.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   6 TMICIDNSEWMRNGDYAPSRFQAQADAVNLICgaktQSNPENTVGILTMAGkGVRVLVTPTSDLGKILACMHGLEI-GGE 84
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALL----KSLPGDRVGLVTFGD-GPEVLIPLTKDRAKILRALRRLEPkGGG 75

                          90       100
                  ....*....|....*....|....*....
gi 2082445383  85 MNLASGIQVAQLALKHRQnKKQQQRIIVF 113
Cdd:pfam13519  76 TNLAAALQLARAALKHRR-KNQPRRIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 7-172 3.38e-12

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: 64.40  E-value: 3.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383    7 MICIDNSEWMRngdyaPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKgVRVLVTP--TSDLGKILACMHGLEI--G 82
Cdd:smart00327   3 VFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDD-ARVLFPLndSRSKDALLEALASLSYklG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   83 GEMNLASGIQVAQLALKHRQNKKQ---QQRIIVFCGSPIKHEKKLIEMIGRKLKKNSVALDIINFGEQDD----GKIEKL 155
Cdd:smart00327  77 GGTNLGAALQYALENLFSKSAGSRrgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDeeelKKLASA 156

                          170
                   ....*....|....*..
gi 2082445383  156 EALLAAVNNNDTSHIVH 172
Cdd:smart00327 157 PGGVYVFLPELLDLLID 173
PSMD4_RAZUL cd22297
RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) ...
 345-389 5.06e-11

RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) and similar proteins; PSMD4 is also called 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit S5A, antisecretory factor 1, AF, ASF, or multiubiquitin chain-binding protein (MCB1). It acts as a ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. It displays a preferred selectivity for longer polyubiquitin chains. PSMD4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. The proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The model corresponds to the C-terminal Rpn10 AZUL-binding domain (RAZUL) of PSMD4, which is responsible for binding the AZUL domain of E6AP/UBE3A. AZUL stands for amino-terminal zinc-binding domain of ubiquitin E3a ligase.


Pssm-ID: 412092  Cd Length: 48  Bit Score: 57.20  E-value: 5.06e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2082445383 345 SSQSDLSKLLADQSFVSSILASLPGVDPNDPSVKNLLDSIQSQTE 389
Cdd:cd22297     1 SEEEDMSDVMQDPEFLQSVLGSLPGVDPNDEAVQNALGSLAKQDE 45
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 7-158 3.26e-05

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: 45.31  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   7 MICIDNSEWMRngdyAPSRFQAQADAV-NLIcgakTQSNPENTVGILTMAGKgVRVLVTPTSDLGKILACMHGLEIGGEM 85
Cdd:COG1240    96 VLVVDASGSMA----AENRLEAAKGALlDFL----DDYRPRDRVGLVAFGGE-AEVLLPLTRDREALKRALDELPPGGGT 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082445383  86 NLASGIQVAQLALKhRQNKKQQQRIIVF------CGSPikhekKLIEMIgRKLKKNSVALDIINFGEqDDGKIEKLEAL 158
Cdd:COG1240   167 PLGDALALALELLK-RADPARRKVIVLLtdgrdnAGRI-----DPLEAA-ELAAAAGIRIYTIGVGT-EAVDEGLLREI 237
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 1-188 4.62e-105

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: 308.14  E-value: 4.62e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   1 MVLEATMICIDNSEWMRNGDYAPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKGVRVLVTPTSDLGKILACMHGLE 80
Cdd:cd01452     1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383  81 IGGEMNLASGIQVAQLALKHRQNKKQQQRIIVFCGSPIKHEKKLIEMIGRKLKKNSVALDIINFGEQDDGKiEKLEALLA 160
Cdd:cd01452    81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNT-EKLTAFID 159

                         170       180
                  ....*....|....*....|....*...
gi 2082445383 161 AVNNNDTSHIVHVPTGSSALSDVLINTP 188
Cdd:cd01452   160 AVNGKDGSHLVSVPPGENLLSDALLSSP 187
VWA_2 pfam13519
von Willebrand factor type A domain;
6-113 9.60e-29

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 108.15  E-value: 9.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   6 TMICIDNSEWMRNGDYAPSRFQAQADAVNLICgaktQSNPENTVGILTMAGkGVRVLVTPTSDLGKILACMHGLEI-GGE 84
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALL----KSLPGDRVGLVTFGD-GPEVLIPLTKDRAKILRALRRLEPkGGG 75

                          90       100
                  ....*....|....*....|....*....
gi 2082445383  85 MNLASGIQVAQLALKHRQnKKQQQRIIVF 113
Cdd:pfam13519  76 TNLAAALQLARAALKHRR-KNQPRRIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 7-172 3.38e-12

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: 64.40  E-value: 3.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383    7 MICIDNSEWMRngdyaPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKgVRVLVTP--TSDLGKILACMHGLEI--G 82
Cdd:smart00327   3 VFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDD-ARVLFPLndSRSKDALLEALASLSYklG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   83 GEMNLASGIQVAQLALKHRQNKKQ---QQRIIVFCGSPIKHEKKLIEMIGRKLKKNSVALDIINFGEQDD----GKIEKL 155
Cdd:smart00327  77 GGTNLGAALQYALENLFSKSAGSRrgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDeeelKKLASA 156

                          170
                   ....*....|....*..
gi 2082445383  156 EALLAAVNNNDTSHIVH 172
Cdd:smart00327 157 PGGVYVFLPELLDLLID 173
PSMD4_RAZUL cd22297
RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) ...
 345-389 5.06e-11

RAZUL (Rpn10 AZUL-binding) domain of 26S proteasome non-ATPase regulatory subunit 4 (PSMD4) and similar proteins; PSMD4 is also called 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit S5A, antisecretory factor 1, AF, ASF, or multiubiquitin chain-binding protein (MCB1). It acts as a ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. It displays a preferred selectivity for longer polyubiquitin chains. PSMD4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. The proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The model corresponds to the C-terminal Rpn10 AZUL-binding domain (RAZUL) of PSMD4, which is responsible for binding the AZUL domain of E6AP/UBE3A. AZUL stands for amino-terminal zinc-binding domain of ubiquitin E3a ligase.


Pssm-ID: 412092  Cd Length: 48  Bit Score: 57.20  E-value: 5.06e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2082445383 345 SSQSDLSKLLADQSFVSSILASLPGVDPNDPSVKNLLDSIQSQTE 389
Cdd:cd22297     1 SEEEDMSDVMQDPEFLQSVLGSLPGVDPNDEAVQNALGSLAKQDE 45
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 44-170 6.63e-06

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 46.11  E-value: 6.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383  44 NPENTVGILTMAGKgVRVLVTPTS--DLGKILACMHGLEIGGEMNLASGIQVAQLALKHRQNKKQQQRIIVFC-GSP--- 117
Cdd:cd01465    33 RPDDRLAIVTYDGA-AETVLPATPvrDKAAILAAIDRLTAGGSTAGGAGIQLGYQEAQKHFVPGGVNRILLATdGDFnvg 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2082445383 118 IKHEKKLIEMIGRKLKKNsVALDIINFGeqdDGKIEKLEALLAAVNNNDTSHI 170
Cdd:cd01465   112 ETDPDELARLVAQKRESG-ITLSTLGFG---DNYNEDLMEAIADAGNGNTAYI 160
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 7-158 3.26e-05

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: 45.31  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   7 MICIDNSEWMRngdyAPSRFQAQADAV-NLIcgakTQSNPENTVGILTMAGKgVRVLVTPTSDLGKILACMHGLEIGGEM 85
Cdd:COG1240    96 VLVVDASGSMA----AENRLEAAKGALlDFL----DDYRPRDRVGLVAFGGE-AEVLLPLTRDREALKRALDELPPGGGT 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082445383  86 NLASGIQVAQLALKhRQNKKQQQRIIVF------CGSPikhekKLIEMIgRKLKKNSVALDIINFGEqDDGKIEKLEAL 158
Cdd:COG1240   167 PLGDALALALELLK-RADPARRKVIVLLtdgrdnAGRI-----DPLEAA-ELAAAAGIRIYTIGVGT-EAVDEGLLREI 237
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 7-158 7.43e-05

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: 42.94  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   7 MICIDNSEWMRngdyaPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKGVRVL-VTPTSDLGKILACMHGLE--IGG 83
Cdd:cd00198     4 VFLLDVSGSMG-----GEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLpLTTDTDKADLLEAIDALKkgLGG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2082445383  84 EMNLASGIQVAQLALKHRQNKKQQQRIIVF-CGSPIKHEKKLIEMIgRKLKKNSVALDIINFGeqDDGKIEKLEAL 158
Cdd:cd00198    79 GTNIGAALRLALELLKSAKRPNARRVIILLtDGEPNDGPELLAEAA-RELRKLGITVYTIGIG--DDANEDELKEI 151
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
 7-100 4.53e-03

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: 38.08  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082445383   7 MICIDNSEWMRNGDYAPSRFQAQADAVNLICGAKTQSNPENTVGILTMAGKGVRVLVTPTSDLGK-ILACMHGLEIGGEM 85
Cdd:cd01453     7 IIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKhIQALKTARECSGEP 86

                          90
                  ....*....|....*
gi 2082445383  86 NLASGIQVAQLALKH 100
Cdd:cd01453    87 SLQNGLEMALESLKH 101
 
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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