|
Name |
Accession |
Description |
Interval |
E-value |
| PolY super family |
cl28996 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
1-301 |
1.43e-160 |
|
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.
The actual alignment was detected with superfamily member cd01701:
Pssm-ID: 452909 [Multi-domain] Cd Length: 404 Bit Score: 469.49 E-value: 1.43e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 1 MFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTK 80
Cdd:cd01701 102 MWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 81 CAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGD--LQCLTMAKLQK 158
Cdd:cd01701 182 CSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 159 EFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMVRK 238
Cdd:cd01701 262 VLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRA 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 239 PGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 301
Cdd:cd01701 342 PGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
634-727 |
8.61e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS 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. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
:
Pssm-ID: 213388 Cd Length: 94 Bit Score: 147.03 E-value: 8.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 634 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 713
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069847 714 QVVLQQTYGSTLKV 727
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
484-519 |
4.33e-15 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
:
Pssm-ID: 412037 Cd Length: 36 Bit Score: 69.17 E-value: 4.33e-15
10 20 30
....*....|....*....|....*....|....*.
gi 1907069847 484 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 519
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
408-441 |
5.13e-12 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
:
Pssm-ID: 412037 Cd Length: 36 Bit Score: 60.70 E-value: 5.13e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069847 408 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 441
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
1-301 |
1.43e-160 |
|
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: 469.49 E-value: 1.43e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 1 MFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTK 80
Cdd:cd01701 102 MWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 81 CAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGD--LQCLTMAKLQK 158
Cdd:cd01701 182 CSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 159 EFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMVRK 238
Cdd:cd01701 262 VLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRA 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 239 PGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 301
Cdd:cd01701 342 PGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
6-298 |
2.87e-71 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 235.81 E-value: 2.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAALRIEIKDKTKCAASV 85
Cdd:COG0389 60 ARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 86 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTG 165
Cdd:COG0389 139 GIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpgapIET 245
Cdd:COG0389 218 ERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVK---------LRT 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 246 AKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQV 298
Cdd:COG0389 289 SDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
4-234 |
2.37e-57 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 198.42 E-value: 2.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 4 GYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAEtKLSPEEFAAALRIEIKDKTKCAA 83
Cdd:PRK02406 52 AQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLC-IGSATLIAQEIRQDIFEELGLTA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 84 SVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpK 163
Cdd:PRK02406 131 SAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-K 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 164 TGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGM--KGKRLTLKI 234
Cdd:PRK02406 210 FGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 282
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
634-727 |
8.61e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS 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. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 213388 Cd Length: 94 Bit Score: 147.03 E-value: 8.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 634 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 713
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069847 714 QVVLQQTYGSTLKV 727
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
4-99 |
4.76e-27 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 107.28 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 4 GYAKQLCPNLQAVPYDFHACREVAQAMYETLASY-THSIEAVSCDEALIDVTDiLAETKLSPEEFAAALRIEIKDKTKCA 82
Cdd:pfam00817 53 FEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLT 131
|
90
....*....|....*..
gi 1907069847 83 ASVGIGSNILLARMATK 99
Cdd:pfam00817 132 CSIGIAPNKLLAKLASD 148
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
644-725 |
7.70e-17 |
|
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein REV1. It interacts with REV7, POLN, POLK and POLI.
Pssm-ID: 465248 Cd Length: 91 Bit Score: 76.12 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 644 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 714
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069847 715 VVLQQTYGSTL 725
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
484-519 |
4.33e-15 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 69.17 E-value: 4.33e-15
10 20 30
....*....|....*....|....*....|....*.
gi 1907069847 484 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 519
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
408-441 |
5.13e-12 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 60.70 E-value: 5.13e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069847 408 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 441
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
1-301 |
1.43e-160 |
|
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: 469.49 E-value: 1.43e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 1 MFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTK 80
Cdd:cd01701 102 MWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 81 CAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGD--LQCLTMAKLQK 158
Cdd:cd01701 182 CSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 159 EFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMVRK 238
Cdd:cd01701 262 VLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRA 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 239 PGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQL 301
Cdd:cd01701 342 PGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
6-301 |
4.95e-76 |
|
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: 248.20 E-value: 4.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAALRIEIKDKTKCAASV 85
Cdd:cd03586 57 AKKLCPNLIFVPPRFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYVRLFG-SATEIAKEIRARIREETGLTASA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 86 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTG 165
Cdd:cd03586 136 GIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKELGIKTIGDLAKLDVELLKKLFG-KSG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKImvrkpgapiet 245
Cdd:cd03586 215 RRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVKL----------- 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069847 246 aKFGGHgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISdMRGVGIQVNQL 301
Cdd:cd03586 284 -KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVRLSGL 334
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
6-298 |
2.87e-71 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 235.81 E-value: 2.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAALRIEIKDKTKCAASV 85
Cdd:COG0389 60 ARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 86 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTG 165
Cdd:COG0389 139 GIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpgapIET 245
Cdd:COG0389 218 ERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVK---------LRT 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 246 AKFgghgicDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQV 298
Cdd:COG0389 289 SDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
4-234 |
2.37e-57 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 198.42 E-value: 2.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 4 GYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAEtKLSPEEFAAALRIEIKDKTKCAA 83
Cdd:PRK02406 52 AQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDNKLC-IGSATLIAQEIRQDIFEELGLTA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 84 SVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpK 163
Cdd:PRK02406 131 SAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRHFG-K 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069847 164 TGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGM--KGKRLTLKI 234
Cdd:PRK02406 210 FGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 282
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
6-273 |
4.34e-42 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 159.33 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAV-PYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAAS 84
Cdd:PRK03348 64 ARRLVGNGAVVlPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEPAELAGASAEEVEAFAERLRARVREETGLPAS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 85 VGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKT 164
Cdd:PRK03348 144 VGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRLGIETIGDLAALSEAEVANLLGATV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 165 GQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimVRKPGAPIE 244
Cdd:PRK03348 224 GPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRGARTVTVK--LRKSDFSTL 301
|
250 260
....*....|....*....|....*....
gi 1907069847 245 TakfgghgicdniaRTVTLDQATDSAKII 273
Cdd:PRK03348 302 T-------------RSATLPYATDDAAVL 317
|
|
| Rev1_C |
cd12145 |
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ... |
634-727 |
8.61e-42 |
|
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis (TLS) polymerase; TLS 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. The C-terminal domain modeled here is essential for TLS and has been shown to mediate interactions with the Rev7 subunit of the B-family TLS polymerase Pol zeta (Rev3/Rev7), as well as with the RIRs (Rev1-interacting regions) of polymerases kappa, iota, and eta. Rev1 is known to actively promote the introduction of mutations, potentially making it a significant target for cancer treatment.
Pssm-ID: 213388 Cd Length: 94 Bit Score: 147.03 E-value: 8.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 634 PNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 713
Cdd:cd12145 1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80
|
90
....*....|....
gi 1907069847 714 QVVLQQTYGSTLKV 727
Cdd:cd12145 81 QNRVKQTYGSPLKI 94
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
6-232 |
4.98e-39 |
|
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: 147.51 E-value: 4.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDIlAETKLSPEEFAAALRIEIKDKTK-CAAS 84
Cdd:cd00424 58 ARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS-ARLLGLGSEVALRIKRHIAEQLGgITAS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 85 VGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKT 164
Cdd:cd00424 137 IGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVGINPIGDLLAASPDALLALWGGVS 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069847 165 GQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTL 232
Cdd:cd00424 217 GERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRLRRDGRGATRLRL 284
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
6-305 |
6.28e-39 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 149.00 E-value: 6.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILaetKL--SPEEFAAALRIEIKDKTKCAA 83
Cdd:PRK03103 64 AQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGSQ---KLfgSPLEIAQKIQQRIMRETGVYA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 84 SVGIGSNILLARMAT---KKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEF 160
Cdd:PRK03103 141 RVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIGQLANTPLERLKKRW 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 161 GpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKrlTLKIMVRk 238
Cdd:PRK03103 221 G-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVLLELCEEVCRRARAKGYMGR--TVSVSLR- 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069847 239 pGAPIETAKfgghgicdNIARTVTLDQATDSAKIIGKATLNMFHTMkLNISDMRGVGIQVNQLVPAN 305
Cdd:PRK03103 297 -GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGKPVRRVGVTLSNLVSDD 353
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
1-304 |
2.90e-36 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 141.61 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 1 MFfgYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTK 80
Cdd:PRK02794 91 MF--KALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLVEPLSIDEAFLDLSGTERLHGAPPAVVLARFARRVEREIG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 81 CAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEF 160
Cdd:PRK02794 169 ITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADLMRRF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 161 GpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpg 240
Cdd:PRK02794 249 G-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLK------- 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069847 241 apIETAKFGGHgicdniARTVTLDQATDSAKIIGKATLNMFHTMkLNISDMRGVGIQVNQLVPA 304
Cdd:PRK02794 321 --LKTADFRLR------TRRRTLEDPTQLADRIFRTARELLEKE-TDGTAFRLIGIGVSDLSPA 375
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
6-310 |
2.66e-35 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 137.16 E-value: 2.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDIlaetKLSPEEFAAALRIEIKDKTKCAASV 85
Cdd:PRK14133 62 AKKRCPHGIFLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDITNI----KEEPIKIAKYIKKKVKKETGLTLSV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 86 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTG 165
Cdd:PRK14133 138 GISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNIGIYTIEDLLKLSREFLIEYFG-KFG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKimvrkpgapIET 245
Cdd:PRK14133 217 VEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKTVTVK---------IKT 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069847 246 AKFGGHgicdniARTVTLDQATDSAKIIGKATLNMFHTMKLNiSDMRGVGIQVnqlvpanSNLST 310
Cdd:PRK14133 288 SDFQTH------TKSKTLNDYIRDKEEIYNVACEILEHINIK-EPIRLIGLSV-------SNLSE 338
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
6-269 |
2.08e-34 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 135.88 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDIlaeTKLS--PEEFAAALRIEIKDKTKCAA 83
Cdd:PRK03858 59 ARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGGL---RRISgtPVQIAARLRRRVREEVGLPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 84 SVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPK 163
Cdd:PRK03858 136 TVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAHGITTVGDVAELPESALVSLLGPA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 164 TGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKImvrkpgapi 243
Cdd:PRK03858 216 AGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGRTVVLRL--------- 286
|
250 260
....*....|....*....|....*.
gi 1907069847 244 etaKFGGHGicdNIARTVTLDQATDS 269
Cdd:PRK03858 287 ---RFDDFT---RATRSHTLPRPTAS 306
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
6-281 |
1.37e-33 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 133.62 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAetKLSPEEFAAALRIEIKDKTKCAASV 85
Cdd:PRK01810 66 AKRLCPQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDCYA--LGSPLEIAKMIQQRLLTELQLPCSI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 86 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTG 165
Cdd:PRK01810 144 GIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIGIQTIGDLAKADEHILRAKLG-ING 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 166 QMLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKrlTLKIMVRkpgapi 243
Cdd:PRK01810 223 VRLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRLQKKTVVSY--NVQIMIR------ 294
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907069847 244 eTAKFgghgicDNIARTVTLDQATDSAKIIGKATLNMF 281
Cdd:PRK01810 295 -YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
4-99 |
4.76e-27 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 107.28 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 4 GYAKQLCPNLQAVPYDFHACREVAQAMYETLASY-THSIEAVSCDEALIDVTDiLAETKLSPEEFAAALRIEIKDKTKCA 82
Cdd:pfam00817 53 FEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLT 131
|
90
....*....|....*..
gi 1907069847 83 ASVGIGSNILLARMATK 99
Cdd:pfam00817 132 CSIGIAPNKLLAKLASD 148
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
10-234 |
7.96e-27 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 112.42 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 10 CPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALI--DVTDilaetklsPEEFAAALRIEIKDKTKCAASVGI 87
Cdd:PRK03352 72 CPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFLgvDTDD--------PEALAEEIRAAVLERTGLSCSVGI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 88 GSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQM 167
Cdd:PRK03352 144 GDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAALGITTVADLAAADPAELAATFGPTTGPW 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069847 168 LYRFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKI 234
Cdd:PRK03352 224 LLLLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELARRVLDEVVAEGRPVTRVAVKV 291
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
25-234 |
5.87e-26 |
|
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: 109.56 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 25 EVAQAMYETLASYTHSIEAVSCDEALIDVTDILaeTKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMAT----KK 100
Cdd:cd01700 77 DMSRRIMSILERFSPDVEVYSIDESFLDLTGSL--RFGDLEELARKIRRRILQETGIPVTVGIGPTKTLAKLANdlakKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 101 AKPDGQYHLQPDEVDDFIRGQL-VTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGpKTGQMLYRFCRGLDDRP 179
Cdd:cd01700 155 NPYGGVVDLTDEEVRDKLLKILpVGDVWGIGRRTAKKLNAMGIHTAGDLAQADPDLLRKKFG-VVGERLVRELNGIDCLP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069847 180 VRTEKE-RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKI 234
Cdd:cd01700 234 LEEYPPpKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKSVARTISVFI 289
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
6-188 |
2.55e-23 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 102.18 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKlSPEEFAAALRIEIKDKTKCAASV 85
Cdd:PRK01216 64 AKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKNYQ-DAYNLGLEIKNKILEKEKITVTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 86 GIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTG 165
Cdd:PRK01216 143 GISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKLGVNKLVDTLRIEFDELKGIIGEAKA 222
|
170 180
....*....|....*....|...
gi 1907069847 166 QMLYRFCRGLDDRPVRTeKERKS 188
Cdd:PRK01216 223 KYLFSLARNEYNEPVRA-RVRKS 244
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
186-305 |
5.47e-21 |
|
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: 88.39 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 186 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMvrkpgapieTAKFgghgicDNIARTVTLDQ 265
Cdd:pfam11799 1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907069847 266 ATDSAKIIGKATLNMFHTMKLNIsDMRGVGIQVNQLVPAN 305
Cdd:pfam11799 66 PTDDTDEIYRAALRLLRRLYRGR-PVRLLGVSLSNLVPEG 104
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
6-283 |
7.67e-21 |
|
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: 94.69 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAV----------------------------PYDfHACREVAqamyETLASYTHSIEAVSCDEALIDVTDIL 57
Cdd:cd01702 54 AKKKCPDLILAhvatykkgedeadyhenpsparhkvsldPYR-RASRKIL----NILKRFGDVVEKASIDEAYLDLGSRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 58 AETklspeefaaaLRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSM-ESK 136
Cdd:cd01702 129 VEE----------IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLgEEI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 137 LASLGIKTCGDLQCL--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINY-GIRFTQPKEAEAFLLSLS 213
Cdd:cd01702 199 IDLLGLPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpGKTALSTEDVQHWLLVLA 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069847 214 EEIQRRLEAA----GMKGKRLTLKIMVRKPGAPIEtakfgghgICDNIARTVTLDQATDSAKIIGKATLNMFHT 283
Cdd:cd01702 279 SELNSRLEDDryenNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYDAQKIVKDAFKLIKAINEEGLGL 344
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
6-239 |
2.32e-18 |
|
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: 87.53 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 6 AKQLCPNLQAV------PYdfhacREVAQAMYETLASYT--HSIEAVSCDEALIDVTDIlaeTKLSPEEFAAALRIEIKD 77
Cdd:cd01703 54 AKEICPDLVLVngedltPF-----RDMSKKVYRLLRSYSwnDRVERLGFDENFMDVTEM---RLLVASHIAYEMRERIEN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 78 KTKCAASVGIGSNILLARMATKKAKPDGQYHLQP---DEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQ----- 149
Cdd:cd01703 126 ELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLLPpscADLMDFMDLHDLRKIPGIGYKTAAKLEAHGISSVRDLQefsnr 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 150 ----------CLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINYG-IRFTQPKEAEAFLLSLSEEIQ 217
Cdd:cd01703 206 nrqtvgaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSYKkCSLEEIREARNKIEELLASLL 285
|
250 260
....*....|....*....|....*...
gi 1907069847 218 RRL------EAAGMKGKRLTLKIMVRKP 239
Cdd:cd01703 286 ERMkqdlqeVKAGDGRRPHTLRLTLRRY 313
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
4-234 |
3.69e-17 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 85.46 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 4 GY-AKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILA--ETKLSPEEFAAALRIEIKDKTK 80
Cdd:PTZ00205 186 GFlALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLDELTLEVSAYIErfEGTKTAEDVASELRVRVFGETK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 81 CAASVGIGSNILLARMATKKAKPDGQYHLQ---PDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQ------CL 151
Cdd:PTZ00205 266 LTASAGIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDIYnrrvelCY 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 152 TMAKLQKEF--GPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSAEINYGIrFTQPKEAEAFLLSLSEEIQRRLEAAGMK 226
Cdd:PTZ00205 346 ILHNNLFRFllGASIGIMQWpDAATAANTENCEgaTGGQRKAISSERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKSELM 424
|
....*...
gi 1907069847 227 GKRLTLKI 234
Cdd:PTZ00205 425 CRQISLTI 432
|
|
| PolY_like |
cd03468 |
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ... |
9-233 |
6.94e-17 |
|
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: 82.43 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 9 LCPNLQAVPYDFHAcrevAQAMYETLAS----YTHSIEAVSCDEALIDVTdilAETKLSPEEFAAALRIEIKDKTKC-AA 83
Cdd:cd03468 60 LCPNLQVVEYDPEA----DARALQELALwllrFTPLVALDGPDGLLLDVT---GCLHLFGGEDALAASLRAALATLGlSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 84 SVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPK 163
Cdd:cd03468 133 RAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLARLGLRTLGDLAALPRAELARRFGLA 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069847 164 tGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQRRLEAAGMKGKRLTLK 233
Cdd:cd03468 213 -LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLCAFLALRGLGARRLSLT 281
|
|
| REV1_C |
pfam16727 |
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ... |
644-725 |
7.70e-17 |
|
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein REV1. It interacts with REV7, POLN, POLK and POLI.
Pssm-ID: 465248 Cd Length: 91 Bit Score: 76.12 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 644 DVKTLLKEWITTISD--PMEEDILQVVRYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 714
Cdd:pfam16727 1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80
|
90
....*....|.
gi 1907069847 715 VVLQQTYGSTL 725
Cdd:pfam16727 81 EAVRERGGGPL 91
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
484-519 |
4.33e-15 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 69.17 E-value: 4.33e-15
10 20 30
....*....|....*....|....*....|....*.
gi 1907069847 484 ISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQ 519
Cdd:cd19318 1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
408-441 |
5.13e-12 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 60.70 E-value: 5.13e-12
10 20 30
....*....|....*....|....*....|....
gi 1907069847 408 SIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQ 441
Cdd:cd19318 3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| umuC |
PRK03609 |
translesion error-prone DNA polymerase V subunit UmuC; |
33-200 |
8.89e-07 |
|
translesion error-prone DNA polymerase V subunit UmuC;
Pssm-ID: 179607 [Multi-domain] Cd Length: 422 Bit Score: 52.07 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 33 TLASYTHSIEAVSCDEALIDVTDIlaETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKpdgQYHLQPD 112
Cdd:PRK03609 87 TLEELSPRVEIYSIDEAFCDLTGV--RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAK---KWQRQTG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069847 113 EVDDFIRGQ----LVTNLP-----GVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFgpktGQMLYRFCRGLDDRPVRTE 183
Cdd:PRK03609 162 GVVDLSNLErqrkLLSLQPveevwGVGRRISKKLNAMGIKTALDLADTNIRFIRKHF----NVVLERTVRELRGEPCLSL 237
|
170 180
....*....|....*....|.
gi 1907069847 184 KERKSVSAEI----NYGIRFT 200
Cdd:PRK03609 238 EEFAPTKQEIvcsrSFGERIT 258
|
|
| IMS_HHH |
pfam11798 |
IMS family HHH motif; These proteins are involved in UV protection, eg. |
111-142 |
3.24e-04 |
|
IMS family HHH motif; These proteins are involved in UV protection, eg.
Pssm-ID: 432081 [Multi-domain] Cd Length: 32 Bit Score: 38.53 E-value: 3.24e-04
10 20 30
....*....|....*....|....*....|..
gi 1907069847 111 PDEVDDFIRGQLVTNLPGVGRSMESKLASLGI 142
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
|
|
| |
