|
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 ... |
56-235 |
8.23e-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: 311.96 E-value: 8.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAv 135
Cdd:cd01453 1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 136 dMTCHGEPSLYNSLSMAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 215
Cdd:cd01453 80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158
|
170 180
....*....|....*....|
gi 2462489475 216 GGTYHVILDESHYKELLTHH 235
Cdd:cd01453 159 NGTYKVILDETHLKELLLEH 178
|
|
| SSL1 super family |
cl34921 |
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ... |
11-385 |
1.09e-104 |
|
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: 315.40 E-value: 1.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEY 90
Cdd:COG5151 40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKYAEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 91 FVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAVDmtCHGEPSLYNSLSMAMQTLKHMPGHTSREVLII 170
Cdd:COG5151 120 FVPEFFSQNPISQLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 171 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELL---THHLSPPPASS 243
Cdd:COG5151 198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMrelSHPTDFNGTKT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 244 SSecSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYH 323
Cdd:COG5151 278 DL--SLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYH 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462489475 324 HLFPLDAFQEIPLEEYNGERFCYGCQG-----------ELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 385
Cdd:COG5151 344 HLYPLKPFVEKPEGTNPKSTHCFVCQGpfpkppvspfdESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGC 416
|
|
| |
|
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 ... |
56-235 |
8.23e-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: 311.96 E-value: 8.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAv 135
Cdd:cd01453 1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 136 dMTCHGEPSLYNSLSMAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 215
Cdd:cd01453 80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158
|
170 180
....*....|....*....|
gi 2462489475 216 GGTYHVILDESHYKELLTHH 235
Cdd:cd01453 159 NGTYKVILDETHLKELLLEH 178
|
|
| SSL1 |
COG5151 |
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ... |
11-385 |
1.09e-104 |
|
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: 315.40 E-value: 1.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEY 90
Cdd:COG5151 40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKYAEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 91 FVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAVDmtCHGEPSLYNSLSMAMQTLKHMPGHTSREVLII 170
Cdd:COG5151 120 FVPEFFSQNPISQLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 171 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELL---THHLSPPPASS 243
Cdd:COG5151 198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMrelSHPTDFNGTKT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 244 SSecSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYH 323
Cdd:COG5151 278 DL--SLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYH 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462489475 324 HLFPLDAFQEIPLEEYNGERFCYGCQG-----------ELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 385
Cdd:COG5151 344 HLYPLKPFVEKPEGTNPKSTHCFVCQGpfpkppvspfdESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGC 416
|
|
| Ssl1 |
pfam04056 |
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex. |
64-235 |
1.70e-104 |
|
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.
Pssm-ID: 461149 Cd Length: 178 Bit Score: 305.89 E-value: 1.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 64 VVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAVDMTCHGEP 143
Cdd:pfam04056 1 VLDCSRSMEEKDLRPSRFACTIKYLETFVEEFFDQNPISQIGLITCKDGRAHRLTDLTGNPRVHIKALKSLREAECGGDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 144 SLYNSLSMAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVIL 223
Cdd:pfam04056 81 SLQNALELARASLKHVPSHGSREVLIIFGSLSTCDPGDIYSTIDTLKKEKIRCSVIGLSAEVFICKELCKATNGTYSVAL 160
|
170
....*....|..
gi 2462489475 224 DESHYKELLTHH 235
Cdd:pfam04056 161 DETHLKELLLEH 172
|
|
| ssl1 |
TIGR00622 |
transcription factor ssl1; All proteins in this family for which functions are known are ... |
288-388 |
2.03e-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: 183.21 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 288 GYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQ-----------GELKDQH 356
Cdd:TIGR00622 1 GYFCPQCRAKVCELPVECPICGLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCFGCQgpfpkppvspfDELKDSH 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462489475 357 VYVCAVCQNVFCVDCDVFVHDSLHCCPGCIHK 388
Cdd:TIGR00622 81 RYVCAVCKNVFCVDCDVFVHESLHCCPGCIHK 112
|
|
| C1_4 |
smart01047 |
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ... |
345-386 |
1.50e-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: 72.78 E-value: 1.50e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462489475 345 CYGCQGEL---KDQHV----YVCAVCQNVFCVDCDVFVHDSLHCCPGCI 386
Cdd:smart01047 1 CFGCQSPFpnsKDKSVtssrYRCTKCKQVFCIDCDVFIHETLHNCPGCE 49
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
60-227 |
1.19e-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: 74.41 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 60 HLYVVVDGSRTMEdqdlkPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTkSKRAEKLTELsgNPRKHITSLKEAVDM-- 137
Cdd:smart00327 1 DVVFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPL--NDSRSKDALLEALASls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 138 -TCHGEPSLYNSLSMAMQTLKHMPGHTSRE---VLIIFSSLT-TCDPSNIYDLIKTLKAAKIRVSVIGLSAEV--RVCTV 210
Cdd:smart00327 73 yKLGGGTNLGAALQYALENLFSKSAGSRRGapkVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKK 152
|
170
....*....|....*..
gi 2462489475 211 LARETGGTYHVILDESH 227
Cdd:smart00327 153 LASAPGGVYVFLPELLD 169
|
|
| C1_4 |
pfam07975 |
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ... |
344-385 |
1.20e-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: 62.11 E-value: 1.20e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462489475 344 FCYGCQ-----------GELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 385
Cdd:pfam07975 1 NCYGCQkkfpkginkktDELLTSSRYRCPKCKQDFCIDCDVFIHESLHNCPGC 53
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
59-226 |
1.06e-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: 58.80 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 59 RHLYVVVDGSRTMEDQdlkpNRLTCTLKLLEYFVEEYFDQNpisQIGIIVTkSKRAEKLTELSGNprkhITSLKEAVD-M 137
Cdd:COG1240 93 RDVVLVVDASGSMAAE----NRLEAAKGALLDFLDDYRPRD---RVGLVAF-GGEAEVLLPLTRD----REALKRALDeL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 138 TCHGEPSLYNSLSMAMQTLKHMPGHTSReVLIIFS-SLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV---RVCTVLAR 213
Cdd:COG1240 161 PPGGGTPLGDALALALELLKRADPARRK-VIVLLTdGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAvdeGLLREIAE 239
|
170
....*....|...
gi 2462489475 214 ETGGTYHVILDES 226
Cdd:COG1240 240 ATGGRYFRADDLS 252
|
|
| PLN03144 |
PLN03144 |
Carbon catabolite repressor protein 4 homolog; Provisional |
301-385 |
3.02e-03 |
|
Carbon catabolite repressor protein 4 homolog; Provisional
Pssm-ID: 178689 [Multi-domain] Cd Length: 606 Bit Score: 39.71 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 301 LPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQgelKDQHVYVC-------AVCQNVFCVDCDV 373
Cdd:PLN03144 9 LPSDIPIVGCELTPYVLLRRPDGTLTTDDVPESAPLDGYFLRYRWYRIQ---SDRKVAVCsvhpsepATLQCVGCVKAKL 85
|
90
....*....|..
gi 2462489475 374 FVHDSLHCCPGC 385
Cdd:PLN03144 86 PVSKSYHCSPKC 97
|
|
| |
|
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 ... |
56-235 |
8.23e-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: 311.96 E-value: 8.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 56 GMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAv 135
Cdd:cd01453 1 GIMRHLIIVIDCSRSMEEQDLKPSRLAVVLKLLELFIEEFFDQNPISQLGIISIKNGRAEKLTDLTGNPRKHIQALKTA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 136 dMTCHGEPSLYNSLSMAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARET 215
Cdd:cd01453 80 -RECSGEPSLQNGLEMALESLKHMPSHGSREVLIIFSSLSTCDPGNIYETIDKLKKENIRVSVIGLSAEMHICKEICKAT 158
|
170 180
....*....|....*....|
gi 2462489475 216 GGTYHVILDESHYKELLTHH 235
Cdd:cd01453 159 NGTYKVILDETHLKELLLEH 178
|
|
| SSL1 |
COG5151 |
RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit ... |
11-385 |
1.09e-104 |
|
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: 315.40 E-value: 1.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 11 WEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEY 90
Cdd:COG5151 40 WEQEYKRSWDDVNDDKEGSLVGVVAEFNLETKAPYSNNRTTPLQRGIIRHLHLILDVSEAMDESDFLPTRRANVIKYAEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 91 FVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAVDmtCHGEPSLYNSLSMAMQTLKHMPGHTSREVLII 170
Cdd:COG5151 120 FVPEFFSQNPISQLSIISIRDGCAKYTSSMDGNPQAHIGQLKSKRD--CSGNFSLQNALEMARIELMKNTMHGTREVLII 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 171 FSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETG----GTYHVILDESHYKELL---THHLSPPPASS 243
Cdd:COG5151 198 FGSTSTRDPGDIAETIDKLVAYNIRVHFIGLCAEVAICKEICKATNssteGRYYVPVDEGHLSELMrelSHPTDFNGTKT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 244 SSecSLIRMGFPQHTIASLsdqdakPSFSMAHLDgntepgLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYH 323
Cdd:COG5151 278 DL--SLVKMGFPSPMMEQL------PSVCACHSE------VKGGGYECPVCKTKVCSLPISCPICSLQLILSTHLARSYH 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462489475 324 HLFPLDAFQEIPLEEYNGERFCYGCQG-----------ELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 385
Cdd:COG5151 344 HLYPLKPFVEKPEGTNPKSTHCFVCQGpfpkppvspfdESTSSGRYQCELCKSTFCSDCDVFIHETLHFCIGC 416
|
|
| Ssl1 |
pfam04056 |
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex. |
64-235 |
1.70e-104 |
|
Ssl1-like; Ssl1-like proteins are 40kDa subunits of the Transcription factor II H complex.
Pssm-ID: 461149 Cd Length: 178 Bit Score: 305.89 E-value: 1.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 64 VVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAVDMTCHGEP 143
Cdd:pfam04056 1 VLDCSRSMEEKDLRPSRFACTIKYLETFVEEFFDQNPISQIGLITCKDGRAHRLTDLTGNPRVHIKALKSLREAECGGDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 144 SLYNSLSMAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVIL 223
Cdd:pfam04056 81 SLQNALELARASLKHVPSHGSREVLIIFGSLSTCDPGDIYSTIDTLKKEKIRCSVIGLSAEVFICKELCKATNGTYSVAL 160
|
170
....*....|..
gi 2462489475 224 DESHYKELLTHH 235
Cdd:pfam04056 161 DETHLKELLLEH 172
|
|
| ssl1 |
TIGR00622 |
transcription factor ssl1; All proteins in this family for which functions are known are ... |
288-388 |
2.03e-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: 183.21 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 288 GYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQ-----------GELKDQH 356
Cdd:TIGR00622 1 GYFCPQCRAKVCELPVECPICGLTLILSTHLARSYHHLFPLKAFQEIPLEEYNGSRFCFGCQgpfpkppvspfDELKDSH 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462489475 357 VYVCAVCQNVFCVDCDVFVHDSLHCCPGCIHK 388
Cdd:TIGR00622 81 RYVCAVCKNVFCVDCDVFVHESLHCCPGCIHK 112
|
|
| C1_4 |
smart01047 |
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ... |
345-386 |
1.50e-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: 72.78 E-value: 1.50e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462489475 345 CYGCQGEL---KDQHV----YVCAVCQNVFCVDCDVFVHDSLHCCPGCI 386
Cdd:smart01047 1 CFGCQSPFpnsKDKSVtssrYRCTKCKQVFCIDCDVFIHETLHNCPGCE 49
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
60-227 |
1.19e-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: 74.41 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 60 HLYVVVDGSRTMEdqdlkPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTkSKRAEKLTELsgNPRKHITSLKEAVDM-- 137
Cdd:smart00327 1 DVVFLLDGSGSMG-----GNRFELAKEFVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPL--NDSRSKDALLEALASls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 138 -TCHGEPSLYNSLSMAMQTLKHMPGHTSRE---VLIIFSSLT-TCDPSNIYDLIKTLKAAKIRVSVIGLSAEV--RVCTV 210
Cdd:smart00327 73 yKLGGGTNLGAALQYALENLFSKSAGSRRGapkVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKK 152
|
170
....*....|....*..
gi 2462489475 211 LARETGGTYHVILDESH 227
Cdd:smart00327 153 LASAPGGVYVFLPELLD 169
|
|
| C1_4 |
pfam07975 |
TFIIH C1-like domain; The carboxyl-terminal region of TFIIH is essential for transcription ... |
344-385 |
1.20e-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: 62.11 E-value: 1.20e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462489475 344 FCYGCQ-----------GELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGC 385
Cdd:pfam07975 1 NCYGCQkkfpkginkktDELLTSSRYRCPKCKQDFCIDCDVFIHESLHNCPGC 53
|
|
| VWA_2 |
pfam13519 |
von Willebrand factor type A domain; |
61-170 |
1.35e-12 |
|
von Willebrand factor type A domain;
Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 63.47 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 61 LYVVVDGSRTMEDQDLKPNRLTctlkLLEYFVEEYFDQNPISQIGIIVTkSKRAEKLTELSGNPRKHITSLKEAVDMTch 140
Cdd:pfam13519 1 LVFVLDTSGSMRNGDYGPTRLE----AAKDAVLALLKSLPGDRVGLVTF-GDGPEVLIPLTKDRAKILRALRRLEPKG-- 73
|
90 100 110
....*....|....*....|....*....|
gi 2462489475 141 GEPSLYNSLSMAMQTLKHMPGHTSREVLII 170
Cdd:pfam13519 74 GGTNLAAALQLARAALKHRRKNQPRRIVLI 103
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
59-226 |
1.06e-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: 58.80 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 59 RHLYVVVDGSRTMEDQdlkpNRLTCTLKLLEYFVEEYFDQNpisQIGIIVTkSKRAEKLTELSGNprkhITSLKEAVD-M 137
Cdd:COG1240 93 RDVVLVVDASGSMAAE----NRLEAAKGALLDFLDDYRPRD---RVGLVAF-GGEAEVLLPLTRD----REALKRALDeL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 138 TCHGEPSLYNSLSMAMQTLKHMPGHTSReVLIIFS-SLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV---RVCTVLAR 213
Cdd:COG1240 161 PPGGGTPLGDALALALELLKRADPARRK-VIVLLTdGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAvdeGLLREIAE 239
|
170
....*....|...
gi 2462489475 214 ETGGTYHVILDES 226
Cdd:COG1240 240 ATGGRYFRADDLS 252
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
59-205 |
1.24e-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: 56.81 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 59 RHLYVVVDGSRTMEDQDLKPnrltcTLKLLEYFVEEYFDQNPISQIGIiVTKSKRAEklTELSGNPRKHITSLKEAVD-- 136
Cdd:cd00198 1 ADIVFLLDVSGSMGGEKLDK-----AKEALKALVSSLSASPPGDRVGL-VTFGSNAR--VVLPLTTDTDKADLLEAIDal 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462489475 137 -MTCHGEPSLYNSLSMAMQTLKHMPGHTSREVLIIFSS-LTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEV 205
Cdd:cd00198 73 kKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDgEPNDGPELLAEAARELRKLGITVYTIGIGDDA 143
|
|
| PLN03144 |
PLN03144 |
Carbon catabolite repressor protein 4 homolog; Provisional |
301-385 |
3.02e-03 |
|
Carbon catabolite repressor protein 4 homolog; Provisional
Pssm-ID: 178689 [Multi-domain] Cd Length: 606 Bit Score: 39.71 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489475 301 LPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQgelKDQHVYVC-------AVCQNVFCVDCDV 373
Cdd:PLN03144 9 LPSDIPIVGCELTPYVLLRRPDGTLTTDDVPESAPLDGYFLRYRWYRIQ---SDRKVAVCsvhpsepATLQCVGCVKAKL 85
|
90
....*....|..
gi 2462489475 374 FVHDSLHCCPGC 385
Cdd:PLN03144 86 PVSKSYHCSPKC 97
|
|
| |
