|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
381-802 |
0e+00 |
|
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. Enzymatically, it catalyzes the specific insertion of dCMP opposite abasic sites. Rev1 interacts with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7). Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 176455 [Multi-domain] Cd Length: 404 Bit Score: 583.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 381 FIRDYYARSRLHLISTLAQDMKDFVANLKLEGKLTEKcfeekelidmkSLSNEISRESTVFHVDLDCFFVSVAVRNRIDL 460
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------SNSIHPDLQRIIMHVDFDCFFVSVSIRNRPDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 461 KHKEVAITHSKGTisnsMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYVQVSRKIYEILASYTLEVRAV 540
Cdd:cd01701 70 KGKPVAVCHGKGP----NSEIASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 541 SCDEMYINMSSFCEkYEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAKPDGVFWVNAHKKNEFISEEKV 620
Cdd:cd01701 146 SCDEALIDITSLLE-ETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 621 KDLPGFGYEMMNRLTSFFGDITKCRELQLKTERELVPVFGPKLASKILRQCRGIEEDPDDfwATHVRKSVSCDINYGIRF 700
Cdd:cd01701 225 GDLPGVGSSLAEKLVKLFGDTCGGLELRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVT--GEKERKSVSAEINYGIRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 701 TKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKLMVRSANAPIQTSKFMGHGICDTFTKTCNLNVPTTRGESLTSEAMK 780
Cdd:cd01701 303 TNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKK 382
|
410 420
....*....|....*....|..
gi 17537959 781 LYAKVSPKVEDLRGVGVTCGKL 802
Cdd:cd01701 383 LFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
439-799 |
9.72e-65 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 221.94 E-value: 9.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 439 TVFHVDLDCFFVSVAVRNRIDLKHKEVAITHSkgtisNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFED 518
Cdd:COG0389 2 RILHVDMDAFYASVEQRDRPELRGKPVAVGGD-----NNRGVVAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 519 YVQVSRKIYEILASYTLEVRAVSCDEMYINMSSfCEKYeINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHA 598
Cdd:COG0389 77 YRDVSRRVMAILERYTPLVEPLSIDEAFLDVTG-SARL-FGSAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 599 KPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSfFGdITKCRELQLKTERELVPVFGPKLASkILRQCRGIEEDP 678
Cdd:COG0389 155 KPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLAR-LG-IRTIGDLAALPRAELRRRFGKVGER-LYRLARGIDPRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 679 DDfwATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKlmvrsanapIQTSKFmghgicDTF 758
Cdd:COG0389 232 VE--PRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVK---------LRTSDF------RTT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17537959 759 TKTCNLNVPTTRGESLTSEAMKLYAKVSPKVEDLRGVGVTC 799
Cdd:COG0389 295 TRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
443-596 |
1.20e-50 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 175.07 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 443 VDLDCFFVSVAVRNRIDLKHKEVAITHSkgtisNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYVQV 522
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGG-----NGRGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537959 523 SRKIYEILASY-TLEVRAVSCDEMYINMSSFCEKYEinDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATR 596
Cdd:pfam00817 76 SRKIFEILRRFsTPKVEQASIDEAFLDLTGLEKLFG--AEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
434-787 |
1.86e-39 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 150.17 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 434 ISRESTVFHVDLDCFFVSVAVRNRIDLKHKEVaITHSKGTISNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLP 513
Cdd:PRK03352 1 TAMPRWVLHVDLDQFIAAVELLRRPELAGLPV-IVGGNGDPTEPRKVVTCASYEARAFGVRAGMPLRTAARRCPDAVFLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 514 YQFEDYVQVSRKIYEILASYTLEVRAVSCDEMYINMssfcekyEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARL 593
Cdd:PRK03352 80 SDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLGV-------DTDDPEALAEEIRAAVLERTGLSCSVGIGDNKLRAKI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 594 ATRHAKPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFfgDITKCRELQLKTERELVPVFGPKLASKILRQCRG 673
Cdd:PRK03352 153 ATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAAL--GITTVADLAAADPAELAATFGPTTGPWLLLLARG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 674 IEEDPDDfwAT-HVRKSVSCDINYGIRFTKRGEviqlMTAIGAELERKLIDSKLTAGSITLKLMVRSANAPIQTSkfmgh 752
Cdd:PRK03352 231 GGDTEVS--AEpWVPRSRSREVTFPQDLTDRAE----VESAVRELARRVLDEVVAEGRPVTRVAVKVRTATFYTR----- 299
|
330 340 350
....*....|....*....|....*....|....*
gi 17537959 753 gicdtfTKTCNLNVPTTRGESLTSEAMKLYAKVSP 787
Cdd:PRK03352 300 ------TKIRKLPEPTTDPDVIEAAALDVLDRFEL 328
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
255-339 |
1.14e-23 |
|
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.
Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 95.71 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 255 IMEGFSVFVNGYTDPPALVIRDLMISHGGEYHCYYQHGITSYTIASSIATAKINRIRE--NEIFIKADWITESIAAGKPL 332
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKKarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 17537959 333 DYRDFLI 339
Cdd:cd17719 81 PEAPYLL 87
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
251-326 |
2.86e-06 |
|
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.
Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 46.13 E-value: 2.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17537959 251 NVSRIMEGFSVFVNGYTDPPALVIRDLMISHGGEYHCYYQHGITSYtIASSIATAKINRIRENEIFIKADWITESI 326
Cdd:pfam00533 1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHV-IVEARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
253-326 |
7.50e-04 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 39.28 E-value: 7.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17537959 253 SRIMEGFSVFVNGYTD-PPALVIRDLMISHGGEYHCYYQHGITSYTIASSIATAK---INRIRENEIFIKADWITESI 326
Cdd:smart00292 1 PKLFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKlelLKAIALGIPIVKEEWLLDCL 78
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
381-802 |
0e+00 |
|
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Rev1 has both structural and enzymatic roles. Structurally, it is believed to interact with other nonclassical polymerases and replication machinery to act as a scaffold. Enzymatically, it catalyzes the specific insertion of dCMP opposite abasic sites. Rev1 interacts with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7). Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 176455 [Multi-domain] Cd Length: 404 Bit Score: 583.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 381 FIRDYYARSRLHLISTLAQDMKDFVANLKLEGKLTEKcfeekelidmkSLSNEISRESTVFHVDLDCFFVSVAVRNRIDL 460
Cdd:cd01701 1 FLENFFKHSRLHHISTWKARLKDFFRELSNGSKEADP-----------SNSIHPDLQRIIMHVDFDCFFVSVSIRNRPDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 461 KHKEVAITHSKGTisnsMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYVQVSRKIYEILASYTLEVRAV 540
Cdd:cd01701 70 KGKPVAVCHGKGP----NSEIASCNYEARSYGIKNGMWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 541 SCDEMYINMSSFCEkYEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAKPDGVFWVNAHKKNEFISEEKV 620
Cdd:cd01701 146 SCDEALIDITSLLE-ETYELPEELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 621 KDLPGFGYEMMNRLTSFFGDITKCRELQLKTERELVPVFGPKLASKILRQCRGIEEDPDDfwATHVRKSVSCDINYGIRF 700
Cdd:cd01701 225 GDLPGVGSSLAEKLVKLFGDTCGGLELRSKTKEKLQKVLGPKTGEKLYDYCRGIDDRPVT--GEKERKSVSAEINYGIRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 701 TKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKLMVRSANAPIQTSKFMGHGICDTFTKTCNLNVPTTRGESLTSEAMK 780
Cdd:cd01701 303 TNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRAPGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKK 382
|
410 420
....*....|....*....|..
gi 17537959 781 LYAKVSPKVEDLRGVGVTCGKL 802
Cdd:cd01701 383 LFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
441-802 |
4.45e-65 |
|
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Known primarily as Pol IV in prokaryotes and Pol kappa in eukaryotes, this polymerase has a propensity for generating frameshift mutations. The eukaryotic Pol kappa differs from Pol IV and Dpo4 by an N-terminal extension of ~75 residues known as the "N-clasp" region. The structure of Pol kappa shows DNA that is almost totally encircled by Pol kappa, with the N-clasp region augmenting the interactions between DNA and the polymerase. Pol kappa is more resistant than Pol eta and Pol iota to bulky guanine adducts and is efficient at catalyzing the incorporation of dCTP. Bacterial pol IV has a higher error rate than other Y-family polymerases.
Pssm-ID: 176459 [Multi-domain] Cd Length: 334 Bit Score: 222.78 E-value: 4.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 441 FHVDLDCFFVSVAVRNRIDLKHKEVAITHSKGTisnSMseVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYV 520
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVGGSSDR---GV--VSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPPRFDKYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 521 QVSRKIYEILASYTLEVRAVSCDEMYINMSSFceKYEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAKP 600
Cdd:cd03586 76 EVSRQIMEILREYTPLVEPLSIDEAYLDVTDY--VRLFGSATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 601 DGVFWVNAHKKNEFISEEKVKDLPGFG---YEMMNRLtsffgDITKCRELQLKTERELVPVFGpKLASKILRQCRGIEED 677
Cdd:cd03586 154 NGLTVIPPEDVEEFLAPLPVRKIPGVGkvtAEKLKEL-----GIKTIGDLAKLDVELLKKLFG-KSGRRLYELARGIDNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 678 PDDfwATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKlmvrsanapIQTSKFmghgicDT 757
Cdd:cd03586 228 PVE--PDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVK---------LKYADF------ST 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 17537959 758 FTKTCNLNVPTTRGESLTSEAMKLYAKVSPKVEdLRGVGVTCGKL 802
Cdd:cd03586 291 RTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVRLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
439-799 |
9.72e-65 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 221.94 E-value: 9.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 439 TVFHVDLDCFFVSVAVRNRIDLKHKEVAITHSkgtisNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFED 518
Cdd:COG0389 2 RILHVDMDAFYASVEQRDRPELRGKPVAVGGD-----NNRGVVAAASYEARAFGVRSGMPLFQARRLCPDLVVLPPDFEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 519 YVQVSRKIYEILASYTLEVRAVSCDEMYINMSSfCEKYeINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHA 598
Cdd:COG0389 77 YRDVSRRVMAILERYTPLVEPLSIDEAFLDVTG-SARL-FGSAEAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 599 KPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSfFGdITKCRELQLKTERELVPVFGPKLASkILRQCRGIEEDP 678
Cdd:COG0389 155 KPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLAR-LG-IRTIGDLAALPRAELRRRFGKVGER-LYRLARGIDPRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 679 DDfwATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKlmvrsanapIQTSKFmghgicDTF 758
Cdd:COG0389 232 VE--PRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVK---------LRTSDF------RTT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17537959 759 TKTCNLNVPTTRGESLTSEAMKLYAKVSPKVEDLRGVGVTC 799
Cdd:COG0389 295 TRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
443-596 |
1.20e-50 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 175.07 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 443 VDLDCFFVSVAVRNRIDLKHKEVAITHSkgtisNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYVQV 522
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGG-----NGRGIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVPPDLELYRRA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537959 523 SRKIYEILASY-TLEVRAVSCDEMYINMSSFCEKYEinDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATR 596
Cdd:pfam00817 76 SRKIFEILRRFsTPKVEQASIDEAFLDLTGLEKLFG--AEEALAKRLRREIAEETGLTCSIGIAPNKLLAKLASD 148
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
441-798 |
6.20e-49 |
|
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Most TLS polymerases are members of the Y-family, including Pol eta, Pol kappa/IV, Pol iota, Rev1, and Pol V, which is found exclusively in bacteria. In eukaryotes, the B-family polymerase Pol zeta also functions as a TLS polymerase. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention.
Pssm-ID: 176453 [Multi-domain] Cd Length: 343 Bit Score: 177.55 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 441 FHVDLDCFFVSVAVRNRIDLKHKEVAITHSKgtiSNSMSeVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYV 520
Cdd:cd00424 1 LHIDFDNFFASVEQLARPELKGRPVVVVPFN---SDSTC-VIACSYEARKYGVKRGMPVREARKMCPNLILVPARLDLYR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 521 QVSRKIYEILASYTLEVRAVSCDEMYINMSSFCEKYEinDPTILAEHIRKVIREKT-QCPASVGIGSTSLLARLATRHAK 599
Cdd:cd00424 77 RLSERLLSELEEVAPLVEVASIDELFLDLTGSARLLG--LGSEVALRIKRHIAEQLgGITASIGIASNKLLAKLAAKYAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 600 PDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFFgdITKCRELQLKTERELVPVFGPKLASKILRQCRGIeeDPD 679
Cdd:cd00424 155 PDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVG--INPIGDLLAASPDALLALWGGVSGERLWYALRGI--DDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 680 DFWATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLidSKLTAGSITLKLMVRSANAPIqtskfMGHgiCDTFT 759
Cdd:cd00424 231 PLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRL--RRDGRGATRLRLWLRTVDGRW-----SGH--ADIPS 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17537959 760 KTCNLNVPTTRGESLtSEAMKLYAKV--SPKVEDLRGVGVT 798
Cdd:cd00424 302 RSAPRPISTEDGELL-HALDKLWRALldDKGPRRLRRLGVR 341
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
434-787 |
1.86e-39 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 150.17 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 434 ISRESTVFHVDLDCFFVSVAVRNRIDLKHKEVaITHSKGTISNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLP 513
Cdd:PRK03352 1 TAMPRWVLHVDLDQFIAAVELLRRPELAGLPV-IVGGNGDPTEPRKVVTCASYEARAFGVRAGMPLRTAARRCPDAVFLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 514 YQFEDYVQVSRKIYEILASYTLEVRAVSCDEMYINMssfcekyEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARL 593
Cdd:PRK03352 80 SDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLGV-------DTDDPEALAEEIRAAVLERTGLSCSVGIGDNKLRAKI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 594 ATRHAKPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFfgDITKCRELQLKTERELVPVFGPKLASKILRQCRG 673
Cdd:PRK03352 153 ATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAAL--GITTVADLAAADPAELAATFGPTTGPWLLLLARG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 674 IEEDPDDfwAT-HVRKSVSCDINYGIRFTKRGEviqlMTAIGAELERKLIDSKLTAGSITLKLMVRSANAPIQTSkfmgh 752
Cdd:PRK03352 231 GGDTEVS--AEpWVPRSRSREVTFPQDLTDRAE----VESAVRELARRVLDEVVAEGRPVTRVAVKVRTATFYTR----- 299
|
330 340 350
....*....|....*....|....*....|....*
gi 17537959 753 gicdtfTKTCNLNVPTTRGESLTSEAMKLYAKVSP 787
Cdd:PRK03352 300 ------TKIRKLPEPTTDPDVIEAAALDVLDRFEL 328
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
446-735 |
2.48e-37 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 143.72 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 446 DCFFVSVAVRNRIDLKHKEVAIthskGTISNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYVQVSRK 525
Cdd:PRK02406 2 DCFYAAVEMRDNPELRGKPVAV----GGSPGRRGVISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPGRFDVYKEVSRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 526 IYEILASYTLEVRAVSCDEMYINMsSFCEKYeINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAKPDGVFW 605
Cdd:PRK02406 78 IREIFRRYTDLIEPLSLDEAYLDV-TDNKLC-IGSATLIAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 606 VNAHKKNEFISEEKVKDLPGFG---YEMMNRLtsffgDITKCRELQLKTERELVPVFGpKLASKILRQCRGIEEDPDDfw 682
Cdd:PRK02406 156 ITPEEVDAFLATLPVEKIPGVGkvtAEKLHAL-----GIYTCADLQKYDLAELIRHFG-KFGRRLYERARGIDERPVK-- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17537959 683 ATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKL--IDSKLTAGSITLKL 735
Cdd:PRK02406 228 PDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLerAKPDKRIKTVGVKL 282
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
440-784 |
3.81e-32 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 130.15 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 440 VFHVDLDCFFVSVAVRNRIDLKHKEVAIThskGTISNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDY 519
Cdd:PRK01810 7 IFHVDMNSFFASVEIAYDPSLQGKPLAVA---GNEKERKGIIVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRRPNFDRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 520 VQVSRKIYEILASYTLEVRAVSCDEMYINMSsfcEKYEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAK 599
Cdd:PRK01810 84 REASRQMFQILSEFTPLVQPVSIDEGYLDIT---DCYALGSPLEIAKMIQQRLLTELQLPCSIGIAPNKFLAKMASDMKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 600 PDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSF----FGDITKCRELQLKterELVPVFGPKLaskilrQCR--G 673
Cdd:PRK01810 161 PLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIgiqtIGDLAKADEHILR---AKLGINGVRL------QRRanG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 674 IEEDPDDFWATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLidSKLTAGSITLKLMVRSANApiqtskfmghg 753
Cdd:PRK01810 232 IDDRPVDPEAIYQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRL--QKKTVVSYNVQIMIRYHDR----------- 298
|
330 340 350
....*....|....*....|....*....|.
gi 17537959 754 icDTFTKTCNLNVPTTRGESLTSEAMKLYAK 784
Cdd:PRK01810 299 --RTITRSKTLKNPIWEKRDIFQAASRLFKQ 327
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
440-803 |
2.65e-31 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 126.37 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 440 VFHVDLDCFFVSVAVRNRIDLKHKEVAIthskGTISNSmSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDY 519
Cdd:PRK14133 5 IIHVDMDAFFASVEQMDNPKLKGKPVIV----GGISER-GVVSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVRHERY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 520 VQVSRKIYEILASYTLEVRAVSCDEMYINMSSfCEKyeinDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAK 599
Cdd:PRK14133 80 KEVSKNIFKILYEVTPIVEPVSIDEAYLDITN-IKE----EPIKIAKYIKKKVKKETGLTLSVGISYNKFLAKLASDWNK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 600 PDGVfwvnahkknEFISEEKVKD----LP-----GFGYEMMNRLTSFfgDITKCRELQLKTERELVPVFGpKLASKILRQ 670
Cdd:PRK14133 155 PDGI---------KIITEDMIPDilkpLPiskvhGIGKKSVEKLNNI--GIYTIEDLLKLSREFLIEYFG-KFGVEIYER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 671 CRGIEEDPDDfwATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKlmvrsanapIQTSKFM 750
Cdd:PRK14133 223 IRGIDYREVE--VSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKTVTVK---------IKTSDFQ 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17537959 751 GHgicdtfTKTCNLNVPTTRGESLTSEAMKLYAKVSPKvEDLRGVGVTCGKLK 803
Cdd:PRK14133 292 TH------TKSKTLNDYIRDKEEIYNVACEILEHINIK-EPIRLIGLSVSNLS 337
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
439-735 |
4.74e-28 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 118.88 E-value: 4.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 439 TVFHVDLDCFFVSVAVRNRIDLKHKEVAI--THSKGTisnsmseVASCSYAARDCGVKNGMLVRDALQKCPQLT-LLPYQ 515
Cdd:PRK03348 6 WVLHLDMDAFFASVEQLTRPTLRGRPVLVggLGGRGV-------VAGASYEARVFGARSAMPMHQARRLVGNGAvVLPPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 516 FEDYVQVSRKIYEILASYTLEVRAVSCDEmyinmsSFCEKYEINDPTI-----LAEHIRKVIREKTQCPASVGIGSTSLL 590
Cdd:PRK03348 79 FVVYRAASRRVFDTLRELSPVVEQLSFDE------AFVEPAELAGASAeeveaFAERLRARVREETGLPASVGAGSGKQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 591 ARLATRHAKPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFfgDITKCRELQLKTERELVPVFGPKLASKILRQ 670
Cdd:PRK03348 153 AKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRL--GIETIGDLAALSEAEVANLLGATVGPALHRL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 671 CRGIEEDPddfwathV-----RKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKL 735
Cdd:PRK03348 231 ARGIDDRP-------VaeraeAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRGARTVTVKL 293
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
442-781 |
3.92e-27 |
|
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Unlike other Y-family members, Pol eta can efficiently and accurately replicate DNA past UV-induced lesions. Its activity is initiated by two simultaneous interactions: the PIP box in pol eta interacting with PCNA, and the UBZ (ubiquitin-binding zinc finger) in pol eta interacting with monoubiquitin attached to PCNA. Pol eta is more efficient in copying damaged DNA than undamaged DNA and seems to recognize when a lesion has been passed, facilitating a lesion-dependent dissociation from the DNA.
Pssm-ID: 176456 [Multi-domain] Cd Length: 359 Bit Score: 114.33 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 442 HVDLDCFFVSV-AVRNRIdLKHKEVAITHSKGTISnsmsevasCSYAARDCGVKNGMLVRDALQKCPQLTL--------- 511
Cdd:cd01702 2 HIDMDAFFAQVeQVRLGL-LRNDPVAVVQWNSIIA--------VSYAARAFGVTRFMTIDEAKKKCPDLILahvatykkg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 512 --------LPYQ------FEDYVQVSRKIYEILASYTLEVRAVSCDEMYINMSSfcekyeindptILAEHIRKVIREKTQ 577
Cdd:cd01702 73 edeadyheNPSParhkvsLDPYRRASRKILNILKRFGDVVEKASIDEAYLDLGS-----------RIVEEIRQQVYDELG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 578 CPASVGIGSTSLLARLATRHAKPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFFGDITKCRELQLK-TERELV 656
Cdd:cd01702 142 YTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDLLGLPTEGDVAGFRsSESDLQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 657 PVFGPKLASKILRQCRGIEEDPddFWATHVRKSVSCDINY-GIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSI--TL 733
Cdd:cd01702 222 EHFGEKLGEWLYNLLRGIDHEP--VKPRPLPKSMGSSKNFpGKTALSTEDVQHWLLVLASELNSRLEDDRYENNRRpkTL 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 17537959 734 KLMVRSANAPIQTSKFMGhgicdtftktcnlnVPTTRGESLTSEAMKL 781
Cdd:cd01702 300 VLSLRQRGDGVRRSRSCA--------------LPRYDAQKIVKDAFKL 333
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
440-678 |
2.57e-24 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 105.64 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 440 VFHVDLDCFFVSVAVRNRIDLKHKEVAITHSKGTISNSmSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDY 519
Cdd:PRK01216 3 ILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSGRFEDS-GAVATANYEARKLGIKAGMPIVEAKKILPNAVYLPMRKEVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 520 VQVSRKIYEILASYTLEVRAVSCDEMYINMSSFCEKYEinDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATRHAK 599
Cdd:PRK01216 82 QQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKNYQ--DAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537959 600 PDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFfgDITKCRELQLKTERELVPVFGPKLASKILRQCRGIEEDP 678
Cdd:PRK01216 160 PNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKL--GVNKLVDTLRIEFDELKGIIGEAKAKYLFSLARNEYNEP 236
|
|
| BRCT_Rev1 |
cd17719 |
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
255-339 |
1.14e-23 |
|
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.
Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 95.71 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 255 IMEGFSVFVNGYTDPPALVIRDLMISHGGEYHCYYQHGITSYTIASSIATAKINRIRE--NEIFIKADWITESIAAGKPL 332
Cdd:cd17719 1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRVTHIIATNLPGSKIKKLKKarNYKVVRPEWIVDSIKAGRLL 80
|
....*..
gi 17537959 333 DYRDFLI 339
Cdd:cd17719 81 PEAPYLL 87
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
437-802 |
1.16e-23 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 104.68 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 437 ESTVFHVDLDCFFVSVAVRNRIDLKHKEVAIthsKGTIsnsmseVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQF 516
Cdd:PRK03858 3 DASILHADLDSFYASVEQRDDPALRGRPVIV---GGGV------VLAASYEAKAYGVRTAMGGRQARRLCPQAVVVPPRM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 517 EDYVQVSRKIYEILASYTLEVRAVSCDEMYINMSSfCEKYEiNDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATR 596
Cdd:PRK03858 74 SAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG-LRRIS-GTPVQIAARLRRRVREEVGLPITVGVARTKFLAKVASQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 597 HAKPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTSFfgDITKCRELQLKTERELVPVFGPKLASKIlrQCRGIEE 676
Cdd:PRK03858 152 VAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAH--GITTVGDVAELPESALVSLLGPAAGRHL--HALAHNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 677 DPDDFWATHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKLmvrsanapiqtsKFmghgicD 756
Cdd:PRK03858 228 DPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGRTVVLRL------------RF------D 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17537959 757 TF---TKTCNLNVPTTRGESLTSEAMKLYAKVSPKVEDlRG---VGVTCGKL 802
Cdd:PRK03858 290 DFtraTRSHTLPRPTASTATLLAAARDLVAAAAPLIAE-RGltlVGFAVSNL 340
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
436-607 |
1.54e-23 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 104.31 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 436 RESTVFHVDLDCFFVSVAVRNRIDLKHKEVAIThskGTISNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQ 515
Cdd:PRK03103 1 MERVILLVDMQSFYASVEKAANPELKGRPVIVS---GDPERRSGVVLAACPLAKAYGVKTAERLWEAQQKCPDLVVVKPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 516 FEDYVQVSRKIYEILASYTLEVRAVSCDEMYINMSSfCEKYeINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLAT 595
Cdd:PRK03103 78 MQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTG-SQKL-FGSPLEIAQKIQQRIMRETGVYARVGIGPNKLLAKMAC 155
|
170
....*....|....*
gi 17537959 596 RHA---KPDGVFWVN 607
Cdd:PRK03103 156 DNFakkNPDGLFTLD 170
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
436-735 |
7.47e-23 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 104.33 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 436 RESTVFHVDLDCFFVSVAVRnridlKHKEVA-ITHSKGTisnsMSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPY 514
Cdd:PTZ00205 131 RLGTYIHLDMDMFYAAVEIK-----KHPEYAaIPLAIGT----MTMLQTANYVARGRGIRQGMPGFLALKICPNLLILPP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 515 QFEDYVQVSRKIYEILASYTLEVRAVSCDEMYINMSSFCEKYE-INDPTILAEHIRKVIREKTQCPASVGIGSTSLLARL 593
Cdd:PTZ00205 202 DFDAYNEESNTVRRIVAEYDPNYISFGLDELTLEVSAYIERFEgTKTAEDVASELRVRVFGETKLTASAGIGPTAALAKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 594 ATRHAKPDGVFWVNAHKKNE---FISEEKVKDLPGFGyEMMNRLTSFFGdITKCRELQLKtERELVPVFGPKLASKILRQ 670
Cdd:PTZ00205 282 ASNINKPNGQHDLNLHTRGDvmtYVRDLGLRSVPGVG-KVTEALLKGLG-ITTLSDIYNR-RVELCYILHNNLFRFLLGA 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537959 671 CRGIEEDPDDFWATHV----------RKSVSCDINYGIRFTKRgEVIQLMTAIGAELERKLIDSKLTAGSITLKL 735
Cdd:PTZ00205 359 SIGIMQWPDAATAANTencegatggqRKAISSERSFTTPRTKE-GLQEMVDTVFNGAYEEMRKSELMCRQISLTI 432
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
442-668 |
2.77e-21 |
|
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Pol iota is thought to be one of the least efficient polymerases, particularly when opposite pyrimidines; it can incorporate the correct nucleotide opposite a purine much more efficiently than opposite a pyrimidine, and prefers to insert guanosine instead of adenosine opposite thymidine. Pol iota is believed to use Hoogsteen rather than Watson-Crick base pairing, which may explain the varying efficiency for different template nucleotides.
Pssm-ID: 176457 [Multi-domain] Cd Length: 379 Bit Score: 97.16 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 442 HVDLDCFFVSVAVRNRIDLKHKEVAITHSkgtisnsmSEVASCSYAARDCGVKNGMLVRDALQKCPQLTLLpyQFED--- 518
Cdd:cd01703 2 HLDLDCFYAQVEEIRDPSLKSKPLGIQQK--------YIVVTCNYEARRLGVKKLMSIKDAKEICPDLVLV--NGEDltp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 519 YVQVSRKIYEILASYTLEVRA--VSCDEMYINMSSFcekyEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATR 596
Cdd:cd01703 72 FRDMSKKVYRLLRSYSWNDRVerLGFDENFMDVTEM----RLLVASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17537959 597 HAKPDGVFWVNAHKKN---EFISEEKVKDLPGFGYEMMNRLTSFFgdITKCRELQLKTER-ELVPVFGPKLASKIL 668
Cdd:cd01703 148 VNKPNQQTTLLPPSCAdlmDFMDLHDLRKIPGIGYKTAAKLEAHG--ISSVRDLQEFSNRnRQTVGAAPSLLELLL 221
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
441-801 |
1.91e-20 |
|
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion synthesis (TLS) polymerase that consists of the heterotrimer of one umuC and two umuD subunits. Translesion synthesis is a process that allows the bypass of a variety of DNA lesions. TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. Pol V, RecA, single stranded DNA-binding protein, beta sliding clamp, and gamma clamp loading complex are responsible for inducing the SOS response in bacteria to repair UV-induced DNA damage.
Pssm-ID: 176454 [Multi-domain] Cd Length: 344 Bit Score: 94.15 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 441 FHVDLDCFFVSVAVRNRIDLKHKEVAIThskgtiSNSMSEVASCSYAARDCGVKNGMLVRDALQKCPQL--TLLPYQFED 518
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVL------SNNDGCVIARSPEAKALGIKMGSPYFKVPDLLERHgvAVFSSNYAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 519 YVQVSRKIYEILASYTLEVRAVSCDEMYINMSSFcekYEINDPTILAEHIRKVIREKTQCPASVGIGSTSLLARLATR-- 596
Cdd:cd01700 75 YGDMSRRIMSILERFSPDVEVYSIDESFLDLTGS---LRFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLANDla 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 597 --HAKPDGVF-WVNAHKKNEFISEEKVKDLPGFGYEMMNRLT----SFFGDITKCRELQLKTErelvpvFGpKLASKILR 669
Cdd:cd01700 152 kkKNPYGGVVdLTDEEVRDKLLKILPVGDVWGIGRRTAKKLNamgiHTAGDLAQADPDLLRKK------FG-VVGERLVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 670 QCRGIEEDPDDFWAThVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKlmvrsanapIQTSkf 749
Cdd:cd01700 225 ELNGIDCLPLEEYPP-PKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKSVARTISVF---------IGTS-- 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17537959 750 mGHGICDTFTKTCN-LNVPTTRGESLTSEA-MKLYAKVSPKVeDLRGVGVTCGK 801
Cdd:cd01700 293 -GFSRQPKYYSATNtLPYPTNDTREIVKAAlRLLYAIYRPGY-AYRKAGVMLSD 344
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
439-798 |
1.29e-18 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 89.61 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 439 TVFHVDLDCFFVSVAVRNRIDLKHKEVAITHSKGTIsnsmseVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFED 518
Cdd:PRK02794 37 SIAHIDCDAFYASVEKRDNPELRDKPVIIGGGKRGV------VSTACYIARIHGVRSAMPMFKALKLCPDAVVIKPDMEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 519 YVQVSRKIYEILASYTLEVRAVSCDEMYINMSSfCEKYEINDPTI-LAEHIRKVIREkTQCPASVGIGSTSLLARLATRH 597
Cdd:PRK02794 111 YVRVGREVRAMMQALTPLVEPLSIDEAFLDLSG-TERLHGAPPAVvLARFARRVERE-IGITVSVGLSYNKFLAKIASDL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 598 AKPDGVFWVNAHKKNEFISEEKVKDLPGFGYEMMNRLTS----FFGDitkcreLQLKTERELVPVFGpKLASKILRQCRG 673
Cdd:PRK02794 189 DKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARLARdgirTIGD------LQRADEADLMRRFG-SMGLRLWRLARG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 674 IEE---DPDdfwatHVRKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKLmvrsanapiQTSKFM 750
Cdd:PRK02794 262 IDDrkvSPD-----REAKSVSAETTFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKL---------KTADFR 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 17537959 751 GHgicdtfTKTCNLNVPTTRGESLTSEAMKLYAK-VSPKVEDLRGVGVT 798
Cdd:PRK02794 328 LR------TRRRTLEDPTQLADRIFRTARELLEKeTDGTAFRLIGIGVS 370
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
687-805 |
1.27e-13 |
|
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
Pssm-ID: 463354 [Multi-domain] Cd Length: 104 Bit Score: 67.58 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 687 RKSVSCDINYGIRFTKRGEVIQLMTAIGAELERKLIDSKLTAGSITLKlmvrsanapIQTSKFmghgicDTFTKTCNLNV 766
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVK---------IRYSDF------RTITRSVTLPS 65
|
90 100 110
....*....|....*....|....*....|....*....
gi 17537959 767 PTTRGESLTSEAMKLYAKVSPKvEDLRGVGVTCGKLKSK 805
Cdd:pfam11799 66 PTDDTDEIYRAALRLLRRLYRG-RPVRLLGVSLSNLVPE 103
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
452-735 |
2.29e-09 |
|
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention.
Pssm-ID: 176458 [Multi-domain] Cd Length: 335 Bit Score: 60.09 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 452 VAVRNRIDLKHKEVAITHSKGTISnsmseVASCSYAARDCGVKNGMLVRDALQKCPQLTLLPYQFEDYVQVSRKIYEILA 531
Cdd:cd03468 12 ALLRNRPADDEAPLAVVERKKAGR-----ILACNAAARAAGVRPGMPLAEALALCPNLQVVEYDPEADARALQELALWLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 532 SYTLEVRAVSCDEMYINMSSfCEKYEINDPTiLAEHIRKViREKTQCPASVGIGSTSLLARLATRHAKPDGVFWVNAHKK 611
Cdd:cd03468 87 RFTPLVALDGPDGLLLDVTG-CLHLFGGEDA-LAASLRAA-LATLGLSARAGIADTPGAAWLLARAGGGRGVLRREALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 612 NEFISEEKVKDLPGFGYEMMNRLTSfFGDITKCRELQLkTERELVPVFGPKLASKiLRQCRGIEEDPDDFWATHVRKSVS 691
Cdd:cd03468 164 ALVLLAPLPVAALRLPPETVELLAR-LGLRTLGDLAAL-PRAELARRFGLALLLR-LDQAYGRDPEPLLFSPPPPAFDFR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17537959 692 CDINYGIrftkrgEVIQLMTAIGAELERKLIDS----KLTAGSITLKL 735
Cdd:cd03468 241 LELQLEE------PIARGLLFPLRRLLEQLCAFlalrGLGARRLSLTL 282
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
251-326 |
2.86e-06 |
|
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.
Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 46.13 E-value: 2.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17537959 251 NVSRIMEGFSVFVNGYTDPPALVIRDLMISHGGEYHCYYQHGITSYtIASSIATAKINRIRENEIFIKADWITESI 326
Cdd:pfam00533 1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHV-IVEARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
253-326 |
7.50e-04 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 39.28 E-value: 7.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17537959 253 SRIMEGFSVFVNGYTD-PPALVIRDLMISHGGEYHCYYQHGITSYTIASSIATAK---INRIRENEIFIKADWITESI 326
Cdd:smart00292 1 PKLFKGKTFYITGSFDkEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKlelLKAIALGIPIVKEEWLLDCL 78
|
|
| BRCT_2 |
pfam16589 |
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
257-337 |
8.58e-04 |
|
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.
Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 39.27 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537959 257 EGFSVFVNGYTDPPALVIRDLMISHGGEYhCYYQHGITSYTIASSIATAKINRIReNEIFIKADWITESIAAGKPLDYRD 336
Cdd:pfam16589 6 EPLRFYINAIPSPSRSKLKRLIEANGGTV-VDNINPAVYIVIAPYNKTDKLAENT-KLGVVSPQWIFDCVKKGKLLPLEN 83
|
.
gi 17537959 337 F 337
Cdd:pfam16589 84 Y 84
|
|
| |
