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Conserved domains on  [gi|1009287561|ref|NP_001308389|]
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DNA repair protein REV1 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PolY_Rev1 cd01701
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ...
 1-301 2.67e-167

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: 486.82  E-value: 2.67e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTK 80
Cdd:cd01701   102 MWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  81 CAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQK 158
Cdd:cd01701   182 CSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 159 EFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRK 238
Cdd:cd01701   262 VLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRA 341

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009287561 239 PGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 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 1.88e-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: 148.96  E-value: 1.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 634 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 713
Cdd:cd12145     1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80

                          90
                  ....*....|....
gi 1009287561 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, ...
 482-517 1.60e-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: 70.72  E-value: 1.60e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1009287561 482 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 517
Cdd:cd19318     1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 406-439 3.86e-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: 61.09  E-value: 3.86e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1009287561 406 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 439
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 2.67e-167

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: 486.82  E-value: 2.67e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTK 80
Cdd:cd01701   102 MWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  81 CAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQK 158
Cdd:cd01701   182 CSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 159 EFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRK 238
Cdd:cd01701   262 VLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRA 341

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009287561 239 PGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 301
Cdd:cd01701   342 PGAPIEPPKYMGHGICDSFSKSSTLGVATDDSGVIGTEAKKLFRDLSIPPEELRGVGIQVTKL 404
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 6-298 3.06e-70

Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];


Pssm-ID: 440158 [Multi-domain]  Cd Length: 336  Bit Score: 232.73  E-value: 3.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASV 85
Cdd:COG0389    60 ARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  86 GIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTG 165
Cdd:COG0389   139 GIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVG 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvET 245
Cdd:COG0389   218 ERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVKL---------RT 288

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1009287561 246 AKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHV 298
Cdd:COG0389   289 SDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
PRK02406 PRK02406
DNA polymerase IV; Validated
 4-234 2.89e-59

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 203.81  E-value: 2.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   4 GHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE----ILAETKLtpdefANAVRMEIKDQT 79
Cdd:PRK02406   52 AQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIGSATLI-----AQEIRQDIFEEL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  80 KCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKE 159
Cdd:PRK02406  127 GLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRH 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1009287561 160 FGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGM--KGKRLTLKI 234
Cdd:PRK02406  207 FG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 282
Rev1_C cd12145
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ...
 634-727 1.88e-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: 148.96  E-value: 1.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 634 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 713
Cdd:cd12145     1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80

                          90
                  ....*....|....
gi 1009287561 714 QVVLQQTYGSTLKV 727
Cdd:cd12145    81 QNRVKQTYGSPLKI 94
IMS pfam00817
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
 4-99 2.47e-26

impB/mucB/samB family; These proteins are involved in UV protection (Swiss).


Pssm-ID: 425885 [Multi-domain]  Cd Length: 148  Bit Score: 104.96  E-value: 2.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   4 GHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASY-THNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCA 82
Cdd:pfam00817  53 FEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLT 131

                          90
                  ....*....|....*..
gi 1009287561  83 ASVGIGSNILLARMATR 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 3.00e-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: 77.27  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 644 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 714
Cdd:pfam16727   1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80

                          90
                  ....*....|.
gi 1009287561 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, ...
 482-517 1.60e-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: 70.72  E-value: 1.60e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1009287561 482 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 517
Cdd:cd19318     1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 406-439 3.86e-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: 61.09  E-value: 3.86e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1009287561 406 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 439
Cdd:cd19318     3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 488-519 4.24e-03

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 35.17  E-value: 4.24e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1009287561 488 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 519
Cdd:pfam14377   3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
 
Name Accession Description Interval E-value
PolY_Rev1 cd01701
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ...
 1-301 2.67e-167

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: 486.82  E-value: 2.67e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTK 80
Cdd:cd01701   102 MWVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYTDNIEAVSCDEALIDITSLLEETYELPEELAEAIRNEIRETTG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  81 CAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD--LQYMTMAKLQK 158
Cdd:cd01701   182 CSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTCGGleLRSKTKEKLQK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 159 EFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRK 238
Cdd:cd01701   262 VLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAEINYGIRFTNVDDVEQFLQRLSEELSKRLEESNVTGRQITLKLMKRA 341

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009287561 239 PGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQL 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 ...
 5-301 9.47e-74

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: 242.04  E-value: 9.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   5 HAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAAS 84
Cdd:cd03586    56 QAKKLCPNLIFVPPRFDKYREVSRQIMEILREYTPLVEPLSIDEAYLDVTDYVRLFG-SATEIAKEIRARIREETGLTAS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  85 VGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKT 164
Cdd:cd03586   135 AGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKELGIKTIGDLAKLDVELLKKLFG-KS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 165 GQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapve 244
Cdd:cd03586   214 GRRLYELARGIDNRPVEPDRERKSIGVERTFSEDLTDPEELLEELLELAEELAERLRKRGLKGRTVTVKL---------- 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1009287561 245 taKFGGHgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISdMRGVGIHVNQL 301
Cdd:cd03586   284 --KYADF---STRTRSRTLPEPTDDAEDIYELALELLEELLDGRP-IRLLGVRLSGL 334
DinP COG0389
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ...
 6-298 3.06e-70

Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];


Pssm-ID: 440158 [Multi-domain]  Cd Length: 336  Bit Score: 232.73  E-value: 3.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASV 85
Cdd:COG0389    60 ARRLCPDLVVLPPDFELYRDVSRRVMAILERYTPLVEPLSIDEAFLDVTGSARLFG-SAEAIARRIRRRIRRETGLTVSV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  86 GIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTG 165
Cdd:COG0389   139 GIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKLARLGIRTIGDLAALPRAELRRRFG-KVG 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvET 245
Cdd:COG0389   218 ERLYRLARGIDPRPVEPRRPRKSIGVERTFGEDLTDLEELEAALRRLAERLAERLRRQGLGARTVTVKL---------RT 288

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1009287561 246 AKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHV 298
Cdd:COG0389   289 SDF------RTTTRSRTLPEPTDDTAELLRAARELLERIYRPGRPVRLLGVRL 335
PRK02406 PRK02406
DNA polymerase IV; Validated
 4-234 2.89e-59

DNA polymerase IV; Validated


Pssm-ID: 235035 [Multi-domain]  Cd Length: 343  Bit Score: 203.81  E-value: 2.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   4 GHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITE----ILAETKLtpdefANAVRMEIKDQT 79
Cdd:PRK02406   52 AQALKLCPDLIFVPGRFDVYKEVSRQIREIFRRYTDLIEPLSLDEAYLDVTDnklcIGSATLI-----AQEIRQDIFEEL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  80 KCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKE 159
Cdd:PRK02406  127 GLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKLHALGIYTCADLQKYDLAELIRH 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1009287561 160 FGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGM--KGKRLTLKI 234
Cdd:PRK02406  207 FG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFAEDLYDLEACLAELPRLAEKLERRLERAKPdkRIKTVGVKL 282
Rev1_C cd12145
C-terminal domain of the Y-family polymerase Rev1; Rev1 is a eukaryotic translesion synthesis ...
 634-727 1.88e-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: 148.96  E-value: 1.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 634 PNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNV 713
Cdd:cd12145     1 PTLSGATSLEEVKTLLKEWITSTPGPNEEDVELFVKYLSRLIDEKNLEKVDLLLKYLKRLVQQSGNSTWEEAYDRIIDVV 80

                          90
                  ....*....|....
gi 1009287561 714 QVVLQQTYGSTLKV 727
Cdd:cd12145    81 QNRVKQTYGSPLKI 94
PRK03348 PRK03348
DNA polymerase IV; Provisional
 1-273 2.78e-42

DNA polymerase IV; Provisional


Pssm-ID: 235118 [Multi-domain]  Cd Length: 454  Bit Score: 159.71  E-value: 2.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFFGHAKQLCPNLQAV-PYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQT 79
Cdd:PRK03348   59 MPMHQARRLVGNGAVVlPPRFVVYRAASRRVFDTLRELSPVVEQLSFDEAFVEPAELAGASAEEVEAFAERLRARVREET 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  80 KCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKE 159
Cdd:PRK03348  139 GLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLHRLGIETIGDLAALSEAEVANL 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 160 FGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKimVRKP 239
Cdd:PRK03348  219 LGATVGPALHRLARGIDDRPVAERAEAKQISAESTFAVDLTTRAQLREAIERIAEHAHRRLLKDGRGARTVTVK--LRKS 296

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1009287561 240 GAPVETakfgghgicdniaRTVTLDQATDNAKII 273
Cdd:PRK03348  297 DFSTLT-------------RSATLPYATDDAAVL 317
PolY cd00424
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ...
 5-232 1.40e-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: 149.43  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   5 HAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlAETKLTPDEFANAVRMEIKDQTK-CAA 83
Cdd:cd00424    57 EARKMCPNLILVPARLDLYRRLSERLLSELEEVAPLVEVASIDELFLDLTGS-ARLLGLGSEVALRIKRHIAEQLGgITA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  84 SVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPK 163
Cdd:cd00424   136 SIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRLEAVGINPIGDLLAASPDALLALWGGV 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009287561 164 TGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTL 232
Cdd:cd00424   216 SGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRNAEDARPLLRLLLEKLARRLRRDGRGATRLRL 284
PRK02794 PRK02794
DNA polymerase IV; Provisional
 1-278 1.57e-37

DNA polymerase IV; Provisional


Pssm-ID: 179473 [Multi-domain]  Cd Length: 419  Bit Score: 145.46  E-value: 1.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFfgHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDI--TEIL--AETKLTPDEFANAVRMEIK 76
Cdd:PRK02794   91 MF--KALKLCPDAVVIKPDMEKYVRVGREVRAMMQALTPLVEPLSIDEAFLDLsgTERLhgAPPAVVLARFARRVEREIG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  77 dqtkCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKL 156
Cdd:PRK02794  169 ----ITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARLARDGIRTIGDLQRADEADL 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 157 QKEFGpKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImv 236
Cdd:PRK02794  245 MRRFG-SMGLRLWRLARGIDDRKVSPDREAKSVSAETTFETDLSDFEDLEPILWRLSEKVSRRLKAAGLAGRTVTLKL-- 321

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1009287561 237 rkpgapvETAKFGGHgicdniARTVTLDQATDNAKII---GKAML 278
Cdd:PRK02794  322 -------KTADFRLR------TRRRTLEDPTQLADRIfrtARELL 353
PRK03103 PRK03103
DNA polymerase IV; Reviewed
 6-303 2.23e-37

DNA polymerase IV; Reviewed


Pssm-ID: 235104 [Multi-domain]  Cd Length: 409  Bit Score: 144.76  E-value: 2.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILaetKL--TPDEFANAVRMEIKDQTKCAA 83
Cdd:PRK03103   64 AQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTDLVEPFSIDEQFLDVTGSQ---KLfgSPLEIAQKIQQRIMRETGVYA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  84 SVGIGSNILLARMAT---RKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEF 160
Cdd:PRK03103  141 RVGIGPNKLLAKMACdnfAKKNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHLRRMGIRTIGQLANTPLERLKKRW 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 161 GpKTGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKrlTLKIMVRk 238
Cdd:PRK03103  221 G-INGEVLWRTANGIDYSPVtpHSLDRQKAIGHQMTLPRDYRGFEEIKVVLLELCEEVCRRARAKGYMGR--TVSVSLR- 296

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009287561 239 pGAPVETAKfgghgicdNIARTVTLDQATDNAKIIGKAMLNMFHTMkLNISDMRGVGIHVNQLVP 303
Cdd:PRK03103  297 -GADFDWPT--------GFSRQMTLPEPTNLAMEVYEAACKLFHRH-WDGKPVRRVGVTLSNLVS 351
PRK14133 PRK14133
DNA polymerase IV; Provisional
 6-251 1.22e-34

DNA polymerase IV; Provisional


Pssm-ID: 184529 [Multi-domain]  Cd Length: 347  Bit Score: 135.23  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlaetKLTPDEFANAVRMEIKDQTKCAASV 85
Cdd:PRK14133   62 AKKRCPHGIFLPVRHERYKEVSKNIFKILYEVTPIVEPVSIDEAYLDITNI----KEEPIKIAKYIKKKVKKETGLTLSV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  86 GIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGpKTG 165
Cdd:PRK14133  138 GISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNNIGIYTIEDLLKLSREFLIEYFG-KFG 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 166 QMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapvET 245
Cdd:PRK14133  217 VEIYERIRGIDYREVEVSRERKSIGKETTLKKDTKDKEELKKYLKDFSNIISEELKKRNLYGKTVTVKI---------KT 287


                  ....*.
gi 1009287561 246 AKFGGH 251
Cdd:PRK14133  288 SDFQTH 293
PRK01810 PRK01810
DNA polymerase IV; Validated
 1-281 3.39e-33

DNA polymerase IV; Validated


Pssm-ID: 179337 [Multi-domain]  Cd Length: 407  Bit Score: 132.46  E-value: 3.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAetKLTPDEFANAVRMEIKDQTK 80
Cdd:PRK01810   61 MPLWEAKRLCPQLIVRRPNFDRYREASRQMFQILSEFTPLVQPVSIDEGYLDITDCYA--LGSPLEIAKMIQQRLLTELQ 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  81 CAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEF 160
Cdd:PRK01810  139 LPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKDIGIQTIGDLAKADEHILRAKL 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 161 GpKTGQMLYRFCRGLDDRPVRTEK--ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKrlTLKIMVRk 238
Cdd:PRK01810  219 G-INGVRLQRRANGIDDRPVDPEAiyQFKSVGNSTTLSHDMDEEKELLDVLRRLSKSVSKRLQKKTVVSY--NVQIMIR- 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1009287561 239 pgapveTAKFgghgicDNIARTVTLDQATDNAKIIGKAMLNMF 281
Cdd:PRK01810  295 ------YHDR------RTITRSKTLKNPIWEKRDIFQAASRLF 325
PRK03858 PRK03858
DNA polymerase IV; Validated
 4-268 1.66e-31

DNA polymerase IV; Validated


Pssm-ID: 179663 [Multi-domain]  Cd Length: 396  Bit Score: 127.41  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   4 GHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCAA 83
Cdd:PRK03858   57 RQARRLCPQAVVVPPRMSAYSRASKAVFEVFRDTTPLVEGLSIDEAFLDVGG-LRRISGTPVQIAARLRRRVREEVGLPI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  84 SVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPK 163
Cdd:PRK03858  136 TVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAHGITTVGDVAELPESALVSLLGPA 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 164 TGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKImvrkpgapv 243
Cdd:PRK03858  216 AGRHLHALAHNRDPRRVETGRRRRSVGAQRALGRGPNSPAEVDAVVVALVDRVARRMRAAGRTGRTVVLRL--------- 286

                         250       260
                  ....*....|....*....|....*
gi 1009287561 244 etaKFGGHGicdNIARTVTLDQATD 268
Cdd:PRK03858  287 ---RFDDFT---RATRSHTLPRPTA 305
PRK03352 PRK03352
DNA polymerase IV; Validated
 10-234 1.19e-27

DNA polymerase IV; Validated


Pssm-ID: 179564 [Multi-domain]  Cd Length: 346  Bit Score: 114.73  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  10 CPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVditeiLAETKlTPDEFANAVRMEIKDQTKCAASVGIGS 89
Cdd:PRK03352   72 CPDAVFLPSDPAAYDAASEEVMATLRDLGVPVEVWGWDEAFL-----GVDTD-DPEALAEEIRAAVLERTGLSCSVGIGD 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  90 NILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLY 169
Cdd:PRK03352  146 NKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAALGITTVADLAAADPAELAATFGPTTGPWLL 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287561 170 RFCRGLDDRPVRTEK-ERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 234
Cdd:PRK03352  226 LLARGGGDTEVSAEPwVPRSRSREVTFPQDLTDRAEVESAVRELARRVLDEVVAEGRPVTRVAVKV 291
IMS pfam00817
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
 4-99 2.47e-26

impB/mucB/samB family; These proteins are involved in UV protection (Swiss).


Pssm-ID: 425885 [Multi-domain]  Cd Length: 148  Bit Score: 104.96  E-value: 2.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   4 GHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASY-THNIEAVSCDEALVDITEiLAETKLTPDEFANAVRMEIKDQTKCA 82
Cdd:pfam00817  53 FEAKKLCPNLIVVPPDLELYRRASRKIFEILRRFsTPKVEQASIDEAFLDLTG-LEKLFGAEEALAKRLRREIAEETGLT 131

                          90
                  ....*....|....*..
gi 1009287561  83 ASVGIGSNILLARMATR 99
Cdd:pfam00817 132 CSIGIAPNKLLAKLASD 148
PRK01216 PRK01216
DNA polymerase IV; Validated
 6-188 1.60e-24

DNA polymerase IV; Validated


Pssm-ID: 179251 [Multi-domain]  Cd Length: 351  Bit Score: 105.64  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKlTPDEFANAVRMEIKDQTKCAASV 85
Cdd:PRK01216   64 AKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSEKIEIASIDEAYLDISDKVKNYQ-DAYNLGLEIKNKILEKEKITVTV 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  86 GIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTG 165
Cdd:PRK01216  143 GISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKKLGVNKLVDTLRIEFDELKGIIGEAKA 222

                         170       180
                  ....*....|....*....|...
gi 1009287561 166 QMLYRFCRGLDDRPVRTeKERKS 188
Cdd:PRK01216  223 KYLFSLARNEYNEPVRA-RVRKS 244
PolY_Pol_V_umuC cd01700
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ...
 6-234 5.78e-24

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: 103.78  E-value: 5.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCP--NLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILaeTKLTPDEFANAVRMEIKDQTKCAA 83
Cdd:cd01700    56 VPDLLErhGVAVFSSNYALYGDMSRRIMSILERFSPDVEVYSIDESFLDLTGSL--RFGDLEELARKIRRRILQETGIPV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  84 SVGIGSNILLARMATRKAK----PDGQYHLKPEEVDDFIRGQL-VTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQK 158
Cdd:cd01700   134 TVGIGPTKTLAKLANDLAKkknpYGGVVDLTDEEVRDKLLKILpVGDVWGIGRRTAKKLNAMGIHTAGDLAQADPDLLRK 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1009287561 159 EFGpKTGQMLYRFCRGLDDRPVRTEKE-RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKI 234
Cdd:cd01700   214 KFG-VVGERLVRELNGIDCLPLEEYPPpKKSIGSSRSFGRDVTDLDELKQALAEYAERAAEKLRRQKSVARTISVFI 289
PolY_Pol_eta cd01702
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ...
 6-283 2.31e-22

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: 99.31  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQ----------AVPYDFHA-------------YKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETkl 62
Cdd:cd01702    54 AKKKCPDLIlahvatykkgEDEADYHEnpsparhkvsldpYRRASRKILNILKRFGDVVEKASIDEAYLDLGSRIVEE-- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  63 tpdefanaVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSM-ESKLASLG 141
Cdd:cd01702   132 --------IRQQVYDELGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLgEEIIDLLG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 142 IKTCGDLQYM--TMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINY-GIRFTQPKEAEAFLLSLSEEIQR 218
Cdd:cd01702   204 LPTEGDVAGFrsSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpGKTALSTEDVQHWLLVLASELNS 283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009287561 219 RLE----ATGMKGKRLTLKIMVRKPGAPVEtakfgghgICDNIARTVTLDQATDNAKIIGKAMLNMFHT 283
Cdd:cd01702   284 RLEddryENNRRPKTLVLSLRQRGDGVRRS--------RSCALPRYDAQKIVKDAFKLIKAINEEGLGL 344
IMS_C pfam11799
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss).
 186-305 1.27e-20

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: 87.23  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 186 RKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMvrkpgapveTAKFgghgicDNIARTVTLDQ 265
Cdd:pfam11799   1 RKSIGAERTFGRDLTDLEELREALLELAEELAERLRRQGLVARTVTVKIR---------YSDF------RTITRSVTLPS 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1009287561 266 ATDNAKIIGKAMLNMFHTMKLNIsDMRGVGIHVNQLVPTN 305
Cdd:pfam11799  66 PTDDTDEIYRAALRLLRRLYRGR-PVRLLGVSLSNLVPEG 104
PTZ00205 PTZ00205
DNA polymerase kappa; Provisional
 8-234 4.23e-19

DNA polymerase kappa; Provisional


Pssm-ID: 140232 [Multi-domain]  Cd Length: 571  Bit Score: 91.62  E-value: 4.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   8 QLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILA--ETKLTPDEFANAVRMEIKDQTKCAASV 85
Cdd:PTZ00205  191 KICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYISFGLDELTLEVSAYIErfEGTKTAEDVASELRVRVFGETKLTASA 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  86 GIGSNILLARMATRKAKPDGQYHLK---PEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGD-------LQYMTMAK 155
Cdd:PTZ00205  271 GIGPTAALAKIASNINKPNGQHDLNlhtRGDVMTYVRDLGLRSVPGVGKVTEALLKGLGITTLSDiynrrveLCYILHNN 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 156 LQK-EFGPKTGQMLY-RFCRGLDDRPVR--TEKERKSVSAEINYGIrFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLT 231
Cdd:PTZ00205  351 LFRfLLGASIGIMQWpDAATAANTENCEgaTGGQRKAISSERSFTT-PRTKEGLQEMVDTVFNGAYEEMRKSELMCRQIS 429


                  ...
gi 1009287561 232 LKI 234
Cdd:PTZ00205  430 LTI 432
PolY_like cd03468
DNA Polymerase Y-family; Y-family DNA polymerases are a specialized subset of polymerases that ...
 1-233 3.37e-18

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: 86.67  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   1 MFFGHAKQLCPNLQAVPYD----FHAYKEVAQTLYEtlasYTHNIEAVSCDEALVDITeilAETKLTPDEFANAVRMEIK 76
Cdd:cd03468    52 MPLAEALALCPNLQVVEYDpeadARALQELALWLLR----FTPLVALDGPDGLLLDVT---GCLHLFGGEDALAASLRAA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  77 DQTKC-AASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAK 155
Cdd:cd03468   125 LATLGlSARAGIADTPGAAWLLARAGGGRGVLRREALAAALVLLAPLPVAALRLPPETVELLARLGLRTLGDLAALPRAE 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 156 LQKEFGPKtGQMLYRFCRGLDDRPV--RTEKERKSVSAEINYGIRFTQPKEAEafLLSLSEEIQRRLEATGMKGKRLTLK 233
Cdd:cd03468   205 LARRFGLA-LLLRLDQAYGRDPEPLlfSPPPPAFDFRLELQLEEPIARGLLFP--LRRLLEQLCAFLALRGLGARRLSLT 281
PolY_Pol_iota cd01703
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ...
 6-239 3.87e-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: 87.14  E-value: 3.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561   6 AKQLCPNLQAVP-YDFHAYKEVAQTLYETLASYTHN--IEAVSCDEALVDITEIlaeTKLTPDEFANAVRMEIKDQTKCA 82
Cdd:cd01703    54 AKEICPDLVLVNgEDLTPFRDMSKKVYRLLRSYSWNdrVERLGFDENFMDVTEM---RLLVASHIAYEMRERIENELGLT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  83 ASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFI--RGQL-VTNLPGVGHSMESKLASLGIKTCGDLQ---------- 149
Cdd:cd01703   131 CCAGIASNKLLAKLVGSVNKPNQQTTLLPPSCADLMdfMDLHdLRKIPGIGYKTAAKLEAHGISSVRDLQefsnrnrqtv 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 150 -----YMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKER-KSVSAEINYG-IRFTQPKEAEAFLLSLSEEIQRRL-- 220
Cdd:cd01703   211 gaapsLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFpQQISIEDSYKkCSLEEIREARNKIEELLASLLERMkq 290

                         250       260
                  ....*....|....*....|...
gi 1009287561 221 ----EATGMKGKRLTLKIMVRKP 239
Cdd:cd01703   291 dlqeVKAGDGRRPHTLRLTLRRY 313
REV1_C pfam16727
DNA repair protein REV1 C-terminal domain; This is the C-terminal domain of DNA repair protein ...
 644-725 3.00e-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: 77.27  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 644 DVKTLLREWITTISD--PMEEDILQVVKYCTDLI-EEKDLEKLDLVIKYMKRLMQQS------VESVWNMAFDFILDNVQ 714
Cdd:pfam16727   1 DVRDLLEAWVESFRDegPHEEDVEALAKYLVRVVlEERDLEKAVAVLKWLRWLVEEEggggeeGGEAWWKAFREVKEAVQ 80

                          90
                  ....*....|.
gi 1009287561 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, ...
 482-517 1.60e-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: 70.72  E-value: 1.60e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1009287561 482 INLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQ 517
Cdd:cd19318     1 GPIIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 406-439 3.86e-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: 61.09  E-value: 3.86e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1009287561 406 SIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQ 439
Cdd:cd19318     3 IIALPSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
umuC PRK03609
translesion error-prone DNA polymerase V subunit UmuC;
23-200 1.05e-05

translesion error-prone DNA polymerase V subunit UmuC;


Pssm-ID: 179607 [Multi-domain]  Cd Length: 422  Bit Score: 48.61  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561  23 YKEVAQTLYETLASYTHNIEAVSCDEALVDITEIlaETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAK 102
Cdd:PRK03609   77 YADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGV--RNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287561 103 P-DGQYH-----LKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFgpktGQMLYRFCRGLD 176
Cdd:PRK03609  155 KwQRQTGgvvdlSNLERQRKLLSLQPVEEVWGVGRRISKKLNAMGIKTALDLADTNIRFIRKHF----NVVLERTVRELR 230

                         170       180
                  ....*....|....*....|....*...
gi 1009287561 177 DRPVRTEKERKSVSAEI----NYGIRFT 200
Cdd:PRK03609  231 GEPCLSLEEFAPTKQEIvcsrSFGERIT 258
IMS_HHH pfam11798
IMS family HHH motif; These proteins are involved in UV protection, eg.
 111-142 1.58e-03

IMS family HHH motif; These proteins are involved in UV protection, eg.


Pssm-ID: 432081 [Multi-domain]  Cd Length: 32  Bit Score: 36.61  E-value: 1.58e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1009287561 111 PEEVDDFIRGQLVTNLPGVGHSMESKLASLGI 142
Cdd:pfam11798   1 PDDVPEFLWPLPISKIPGIGKKLAEKLKALGI 32
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 488-519 4.24e-03

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 35.17  E-value: 4.24e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1009287561 488 PAFSQVDPEVFAALPAELQRELKAAYDQRQRQ 519
Cdd:pfam14377   3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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