|
Name |
Accession |
Description |
Interval |
E-value |
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
8-606 |
0e+00 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 878.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 8 QFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKY 87
Cdd:PRK00558 6 EKLKTLPDSPGVYRMKDANGTVIYVGKAKNLKNRVRSYFRKSHDSPKTRAMVSEIADIEYIVTRSETEALLLENNLIKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 88 QPRYNILLRDDKSYPYILLTS-HKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRARSRPCL 166
Cdd:PRK00558 86 KPRYNVLLRDDKSYPYIKITTnEEFPRLAITRGVAKDKGRYFGPYPSAGAVRETLDLLQKLFPLRTCEDSVFKNRKRPCL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 167 QYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQSIS-G 245
Cdd:PRK00558 166 LYQIGRCLAPCVGLISKEEYAELVDEAKLFLSGKTDEVLKELEEKMEEASENLEFERAARYRDQIQALRRVQEKQKVSlK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 246 NFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSgQEEILTSFLGQYYLApgatGRIAKEIILPFEIEEsS 325
Cdd:PRK00558 246 DGEDADVIAIAVDGGWACVQVFFVRGGKLLGRRSYFPKVSETE-LEEILEAFLGQFYLQ----KSIPKEILVPHELDD-E 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 326 ALSEALtqISERKVSLKVVTRGERAQYLQLANKNALNSITVKQSTQDSINKRYAQLKATLGLDD-INRMECFDISHTMGE 404
Cdd:PRK00558 320 ELAEAL--LAGRKVKIRVPQRGDKKELLELAEKNAREALERKLSDQSTQQQALEELAELLGLPEpPYRIECFDISHIQGT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 405 NTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDE-DKIPDVIFIDGGKGQLGRAEQYFATWphA 483
Cdd:PRK00558 398 ATVASMVVFEDGGPDKSEYRRYNIKGVTGGDDYAAMREVLTRRYSRLLKEfGPLPDLILIDGGKGQLNAAKEVLEEL--G 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 484 KMPLLVGVAKGTSRKPGLETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLLEEINGVGSKR 563
Cdd:PRK00558 476 LDIPVVGLAKGDKRKAGTEELFFPGEPEPIILPPDSPALYLLQRIRDEAHRFAITFHRKKRSKARLTSALDDIPGIGPKR 555
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 490727043 564 RQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIFNHLHDK 606
Cdd:PRK00558 556 RKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
|
|
| UvrC |
COG0322 |
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]; |
1-606 |
0e+00 |
|
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
Pssm-ID: 440091 [Multi-domain] Cd Length: 603 Bit Score: 867.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 1 MSEFDHAQFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLE 80
Cdd:COG0322 1 MDPFDLKEKLKTLPTSPGVYLMKDANGEVIYVGKAKNLKNRVSSYFQKSDLSPKTRRMVSEIADIEYIVTDTETEALLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 81 NNLIKKYQPRYNILLRDDKSYPYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRA 160
Cdd:COG0322 81 NNLIKKHKPRYNILLKDDKSYPYIKITNEEFPRIFVTRGVKKDGGRYFGPYPSAGAVRETLDLLQKLFPLRTCSDSLFKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 161 RSRPCLQYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQ 240
Cdd:COG0322 161 RSRPCLLYQIGRCSAPCVGLISEEEYREDVEQARRFLEGKTKELIKELEEKMEEAAEELEFERAARLRDQIRALEKVQEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 241 QSI-SGNFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSGQEEILTSFLGQYYLapgATGRIAKEIILPF 319
Cdd:COG0322 241 QKVvLPDGGDADVIAIARDGGEACVQVFFVRGGRLIGRRSFFLEKVLDEDDEELLEAFLAQYYL---DRPSIPKEILVPE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 320 EIEESSALSEALTQISERKVSLKVVTRGERAQYLQLANKNALNSI----TVKQSTQDSINKRYAQLKATLGLDDI-NRME 394
Cdd:COG0322 318 ELEDAELLEEWLSERRGRKVKIRVPQRGEKKKLLELAEKNAREALerklAERERDEARQERALEELAEALGLPELpRRIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 395 CFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDED-KIPDVIFIDGGKGQLGRA 473
Cdd:COG0322 398 CFDISHIQGTNTVASMVVFEDGKPDKSDYRRFKIKTVEGGDDYASMREVLTRRYKRLLEEDePLPDLILIDGGKGQLNAA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 474 EQYFATWPHAKMPlLVGVAKgtsRKpglETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLL 553
Cdd:COG0322 478 REVLEELGLDDIP-VIGLAK---RD---EELFLPGDSEPIILPRNSPALYLLQRIRDEAHRFAITFHRKLRSKARLKSVL 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 490727043 554 EEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIFNHLHDK 606
Cdd:COG0322 551 DEIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE 603
|
|
| uvrC |
TIGR00194 |
excinuclease ABC, C subunit; This family consists of the DNA repair enzyme UvrC, an ABC ... |
7-584 |
0e+00 |
|
excinuclease ABC, C subunit; This family consists of the DNA repair enzyme UvrC, an ABC excinuclease subunit which interacts with the UvrA/UvrB complex to excise UV-damaged nucleotide segments. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 272953 [Multi-domain] Cd Length: 574 Bit Score: 644.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 7 AQFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTdSKTRVLVSNICDIEVTLTNTETEALLLENNLIKK 86
Cdd:TIGR00194 2 KEKLKNLPDKPGCYLMKDRNGQVLYVGKAKNLKKRVSSYFRENNS-AKTQALVKQIADIEYILTKNENEALILEANLIKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 87 YQPRYNILLRDDKSYPYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDayyRARSRPCL 166
Cdd:TIGR00194 81 YQPRYNVLLKDDKGYPYIYITHEKYPRLLITRKLKQDKGKYFGPFTNAFALRETLDLLLKLFPLRKCAK---HNRNRPCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 167 QYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQSIS-G 245
Cdd:TIGR00194 158 YYQIGRCLGPCVKEITEEEYQQIVEKIELFFNGRPQEVIKELEQKMEKASENLEFEEAARIRDQIAAVRELNEKQHVSlT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 246 NFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSGQEEILTsFLGQYYLAPGATGRIAKEIILPFEIEESS 325
Cdd:TIGR00194 238 DLIDLDIIAVAFDGNVAAIQVFFIRQGKLIGRDQFDFSLPGTDLDELVET-FLIQFYQQGYQNRLIPSEILVSLSLEDLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 326 ALSEALTQISERKVSLKVVTRGERAQYLQLANKNALNSITVKQSTQDSINKRYAQLKATLGLDDINRMECFDISHTMGEN 405
Cdd:TIGR00194 317 LLEDLLSEQRGRKINVHQPKKGDKKKLLELAIKNAKYALKQKWTQFERKTQALEDLASLLNLPKIKRIEIFDISHIDGSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 406 TVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDEDKIP--DVIFIDGGKGQLGRAEQYFATWPHA 483
Cdd:TIGR00194 397 TVGSMVVFEDGKPLKASYRRYNINSITGGDDYAAMREVLRRRYSSIQKKNNLPlpDLILIDGGKGQLNAALEVLKSLGVV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 484 KMPLLVGVAKGTsRKPGLETLLIDggRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLLEEINGVGSKR 563
Cdd:TIGR00194 477 NKPIVIGLAKAK-RHETDIFLIGD--KQGINIDLNSPALQLLQHIRDEAHRFAISFHRKKRLKASLQSPLLKIPGVGEKR 553
|
570 580
....*....|....*....|.
gi 490727043 564 RQTLLKYLGGMQGVKAANIEQ 584
Cdd:TIGR00194 554 VQKLLKYFGSLKGIKKASVEE 574
|
|
| UvrC_RNaseH_dom |
pfam08459 |
UvrC RNAse H endonuclease domain; This domain is found in the C subunits of the bacterial and ... |
382-536 |
1.64e-60 |
|
UvrC RNAse H endonuclease domain; This domain is found in the C subunits of the bacterial and archaeal UvrABC system which catalyzes nucleotide excision repair in a multi-step process. UvrC catalyzes the first incision on the fourth or fifth phosphodiester bond 3' and on the eighth phosphodiester bond 5' from the damage that is to be excised. The domain described here represents the RNAse H endonuclease domain, located at the C-terminal, between the UvrBC and the (HhH)2 domains, nearby the N-terminal of the HhH. Despite the lack of sequence homology, the endonuclease domain has an RNase H-like fold, which is characteriztic of enzymes with nuclease or polynucleotide transferase activities. RNase H-related enzymes typically contain a highly conserved carboxylate triad, usually DDE, in their catalytic centre. However, instead of a third carboxylate, UvrC of Thermotoga maritima was found to contain a highly conserved histidine (H488) on helix-4 in close proximity to two aspartates.
Pssm-ID: 462484 [Multi-domain] Cd Length: 150 Bit Score: 198.05 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 382 KATLGLDD-INRMECFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDED-KIPD 459
Cdd:pfam08459 1 QEALGLPKlPRRIECFDISHIQGTDTVASMVVFEDGKPDKSDYRRFNIKTTVGPDDYASMREVLTRRFSRLLEEFgPLPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490727043 460 VIFIDGGKGQLGRAEQYFATWpHAKMPlLVGVAKGTSRKpgletLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFA 536
Cdd:pfam08459 81 LILIDGGKGQLNAALEVLEEL-GLDIP-VIGLAKDDKHK-----IDTDGREEEIILPRDSPALHLLQRIRDEAHRFA 150
|
|
| GIY-YIG_UvrC_Cho |
cd10434 |
Catalytic GIY-YIG domain of nucleotide excision repair endonucleases UvrC, Cho, and similar ... |
13-93 |
1.31e-39 |
|
Catalytic GIY-YIG domain of nucleotide excision repair endonucleases UvrC, Cho, and similar proteins; UvrC is essential for nucleotide excision repair (NER). The N-terminal catalytic GIY-YIG domain of UvrC (also known as Uri domain) is responsible for the 3' incision reaction and the C-terminal half of UvrC, consisting of an UvrB-binding domain (UvrBb), EndoV-like nuclease domain and a helix-hairpin-helix (HhH) DNA-binding domain, contains the residues involved in 5' incision. The N- and C-terminal regions are joined by a common Cys-rich domain containing four conserved Cys residues. Besides UvrC, protein Cho (UvrC homolog) serves as a second endonuclease in E. coli NER. Cho contains GIY-YIG motif followed by a Cys-rich region and shares sequence homology with the N-terminal half of UvrC. It is capable of incising the DNA at the 3' side of a lesion in the presence of the UvrA and UvrB proteins during NER. The C-terminal half of Cho is a unique uncharacterized domain, which is distinct from that of UvrC. Moreover, unlike UvrC, Cho does not require the UvrC-binding domain of UvrB for the 3' incision reaction, which might cause the shift in incision position and the difference in incision efficiencies between Cho and UvrC on different damaged substrates. Due to this, the range of NER in E. coli can be broadened by combining action of Cho and UvrC. This family also includes many uncharacterized epsilon proofreading subunits of DNA polymerase III, which have an additional N-terminal ExoIII domain and a 3'-5' exonuclease domain homolog, fused to an UvrC-like region or a Cho-like region. The UvrC-like region includes a GIY-YIG motif, followed by a Cys-rich region, and an UvrB-binding domain (UvrBb), but lacks the EndoV-like nuclease domain and the helix-hairpin-helix (HhH) DNA-binding domain. The Cho-like region consists of a GIY-YIG motif, followed by the Cys-rich region, and the unique uncharacterized domain presenting in the C-terminal half of Cho. Some family members may not carry the Cys-rich region. This family also includes a specific Cho-like protein from G. violaceus, which possesses only UvrBb domain at the C-terminus, but lacks the additional N-terminal ExoIII domain. The oother two remote homologs of UvrC, Bacillus-I and -II, are included in this family as well. Both of them contain a GIY-YIG domain, but no Cys-rich region. Moreover, the whole C-terminal region of Bacillus-I is replaces by an unknown domain, and Bacillus-II possesses another unknown N-terminal extension.
Pssm-ID: 198381 [Multi-domain] Cd Length: 81 Bit Score: 139.54 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 13 LSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQPRYN 92
Cdd:cd10434 1 LPDSPGVYLFKDADGEVLYVGKAKNLRKRVSSYFTGERHSPKTRRLVEEIRDIEYIVTDSELEALLLEANLIKKYKPRYN 80
|
.
gi 490727043 93 I 93
Cdd:cd10434 81 I 81
|
|
| GIYc |
smart00465 |
GIY-YIG type nucleases (URI domain); |
16-97 |
2.57e-16 |
|
GIY-YIG type nucleases (URI domain);
Pssm-ID: 214677 [Multi-domain] Cd Length: 84 Bit Score: 73.99 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 16 EPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFR-SNLTDSKTRVLVSNICDIE-VTLTNTETEALLLENNLIKKYQPRYNI 93
Cdd:smart00465 1 KPGVYYITNKKNGKLYVGKAKNLRNRLKRHFSgSRKGRLLIDALLKYGGNFEfIILESFDESALELEKYLIKEYKPKYNL 80
|
....
gi 490727043 94 LLRD 97
Cdd:smart00465 81 LLKG 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
8-606 |
0e+00 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 878.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 8 QFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKY 87
Cdd:PRK00558 6 EKLKTLPDSPGVYRMKDANGTVIYVGKAKNLKNRVRSYFRKSHDSPKTRAMVSEIADIEYIVTRSETEALLLENNLIKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 88 QPRYNILLRDDKSYPYILLTS-HKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRARSRPCL 166
Cdd:PRK00558 86 KPRYNVLLRDDKSYPYIKITTnEEFPRLAITRGVAKDKGRYFGPYPSAGAVRETLDLLQKLFPLRTCEDSVFKNRKRPCL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 167 QYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQSIS-G 245
Cdd:PRK00558 166 LYQIGRCLAPCVGLISKEEYAELVDEAKLFLSGKTDEVLKELEEKMEEASENLEFERAARYRDQIQALRRVQEKQKVSlK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 246 NFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSgQEEILTSFLGQYYLApgatGRIAKEIILPFEIEEsS 325
Cdd:PRK00558 246 DGEDADVIAIAVDGGWACVQVFFVRGGKLLGRRSYFPKVSETE-LEEILEAFLGQFYLQ----KSIPKEILVPHELDD-E 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 326 ALSEALtqISERKVSLKVVTRGERAQYLQLANKNALNSITVKQSTQDSINKRYAQLKATLGLDD-INRMECFDISHTMGE 404
Cdd:PRK00558 320 ELAEAL--LAGRKVKIRVPQRGDKKELLELAEKNAREALERKLSDQSTQQQALEELAELLGLPEpPYRIECFDISHIQGT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 405 NTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDE-DKIPDVIFIDGGKGQLGRAEQYFATWphA 483
Cdd:PRK00558 398 ATVASMVVFEDGGPDKSEYRRYNIKGVTGGDDYAAMREVLTRRYSRLLKEfGPLPDLILIDGGKGQLNAAKEVLEEL--G 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 484 KMPLLVGVAKGTSRKPGLETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLLEEINGVGSKR 563
Cdd:PRK00558 476 LDIPVVGLAKGDKRKAGTEELFFPGEPEPIILPPDSPALYLLQRIRDEAHRFAITFHRKKRSKARLTSALDDIPGIGPKR 555
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 490727043 564 RQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIFNHLHDK 606
Cdd:PRK00558 556 RKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
|
|
| UvrC |
COG0322 |
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]; |
1-606 |
0e+00 |
|
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
Pssm-ID: 440091 [Multi-domain] Cd Length: 603 Bit Score: 867.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 1 MSEFDHAQFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLE 80
Cdd:COG0322 1 MDPFDLKEKLKTLPTSPGVYLMKDANGEVIYVGKAKNLKNRVSSYFQKSDLSPKTRRMVSEIADIEYIVTDTETEALLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 81 NNLIKKYQPRYNILLRDDKSYPYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRA 160
Cdd:COG0322 81 NNLIKKHKPRYNILLKDDKSYPYIKITNEEFPRIFVTRGVKKDGGRYFGPYPSAGAVRETLDLLQKLFPLRTCSDSLFKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 161 RSRPCLQYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQ 240
Cdd:COG0322 161 RSRPCLLYQIGRCSAPCVGLISEEEYREDVEQARRFLEGKTKELIKELEEKMEEAAEELEFERAARLRDQIRALEKVQEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 241 QSI-SGNFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSGQEEILTSFLGQYYLapgATGRIAKEIILPF 319
Cdd:COG0322 241 QKVvLPDGGDADVIAIARDGGEACVQVFFVRGGRLIGRRSFFLEKVLDEDDEELLEAFLAQYYL---DRPSIPKEILVPE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 320 EIEESSALSEALTQISERKVSLKVVTRGERAQYLQLANKNALNSI----TVKQSTQDSINKRYAQLKATLGLDDI-NRME 394
Cdd:COG0322 318 ELEDAELLEEWLSERRGRKVKIRVPQRGEKKKLLELAEKNAREALerklAERERDEARQERALEELAEALGLPELpRRIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 395 CFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDED-KIPDVIFIDGGKGQLGRA 473
Cdd:COG0322 398 CFDISHIQGTNTVASMVVFEDGKPDKSDYRRFKIKTVEGGDDYASMREVLTRRYKRLLEEDePLPDLILIDGGKGQLNAA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 474 EQYFATWPHAKMPlLVGVAKgtsRKpglETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLL 553
Cdd:COG0322 478 REVLEELGLDDIP-VIGLAK---RD---EELFLPGDSEPIILPRNSPALYLLQRIRDEAHRFAITFHRKLRSKARLKSVL 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 490727043 554 EEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIFNHLHDK 606
Cdd:COG0322 551 DEIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE 603
|
|
| uvrC |
TIGR00194 |
excinuclease ABC, C subunit; This family consists of the DNA repair enzyme UvrC, an ABC ... |
7-584 |
0e+00 |
|
excinuclease ABC, C subunit; This family consists of the DNA repair enzyme UvrC, an ABC excinuclease subunit which interacts with the UvrA/UvrB complex to excise UV-damaged nucleotide segments. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 272953 [Multi-domain] Cd Length: 574 Bit Score: 644.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 7 AQFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTdSKTRVLVSNICDIEVTLTNTETEALLLENNLIKK 86
Cdd:TIGR00194 2 KEKLKNLPDKPGCYLMKDRNGQVLYVGKAKNLKKRVSSYFRENNS-AKTQALVKQIADIEYILTKNENEALILEANLIKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 87 YQPRYNILLRDDKSYPYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDayyRARSRPCL 166
Cdd:TIGR00194 81 YQPRYNVLLKDDKGYPYIYITHEKYPRLLITRKLKQDKGKYFGPFTNAFALRETLDLLLKLFPLRKCAK---HNRNRPCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 167 QYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQSIS-G 245
Cdd:TIGR00194 158 YYQIGRCLGPCVKEITEEEYQQIVEKIELFFNGRPQEVIKELEQKMEKASENLEFEEAARIRDQIAAVRELNEKQHVSlT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 246 NFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDSGQEEILTsFLGQYYLAPGATGRIAKEIILPFEIEESS 325
Cdd:TIGR00194 238 DLIDLDIIAVAFDGNVAAIQVFFIRQGKLIGRDQFDFSLPGTDLDELVET-FLIQFYQQGYQNRLIPSEILVSLSLEDLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 326 ALSEALTQISERKVSLKVVTRGERAQYLQLANKNALNSITVKQSTQDSINKRYAQLKATLGLDDINRMECFDISHTMGEN 405
Cdd:TIGR00194 317 LLEDLLSEQRGRKINVHQPKKGDKKKLLELAIKNAKYALKQKWTQFERKTQALEDLASLLNLPKIKRIEIFDISHIDGSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 406 TVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDEDKIP--DVIFIDGGKGQLGRAEQYFATWPHA 483
Cdd:TIGR00194 397 TVGSMVVFEDGKPLKASYRRYNINSITGGDDYAAMREVLRRRYSSIQKKNNLPlpDLILIDGGKGQLNAALEVLKSLGVV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 484 KMPLLVGVAKGTsRKPGLETLLIDggRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLLEEINGVGSKR 563
Cdd:TIGR00194 477 NKPIVIGLAKAK-RHETDIFLIGD--KQGINIDLNSPALQLLQHIRDEAHRFAISFHRKKRLKASLQSPLLKIPGVGEKR 553
|
570 580
....*....|....*....|.
gi 490727043 564 RQTLLKYLGGMQGVKAANIEQ 584
Cdd:TIGR00194 554 VQKLLKYFGSLKGIKKASVEE 574
|
|
| uvrC |
PRK14669 |
excinuclease ABC subunit C; Provisional |
5-602 |
1.73e-137 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 237784 [Multi-domain] Cd Length: 624 Bit Score: 414.31 E-value: 1.73e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 5 DHAQFLKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYF-RSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNL 83
Cdd:PRK14669 2 DLRDKIRTLPTSPGVYLYKNAGGEVIYVGKAKNLRSRVRSYFsEDKLGNIKTGSLIREAVDIDYILVDNEKEALALENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 84 IKKYQPRYNILLRDDKSYPYILLT-SHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRARS 162
Cdd:PRK14669 82 IKQYKPRFNILLRDDKTYPYVKLTlGEKYPRVYVTRRLRKDGAQYYGPFFPANLAYRLVDLIHRHFLVPSCKVDLTRYHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 163 RPCLQYQLKRCSAPCVNKVT-EQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQ 241
Cdd:PRK14669 162 RPCLQFYIHRCLGPCVQGLTtDEAYAEAVRDVRLFLEGRHSDLARSLRARMEAAALEMQFELAAKYRDLITTVEELEEKQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 242 SI-SGNFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYF------PKVPKDSGQEEILTSFLGQYYLApgaTGRIAKE 314
Cdd:PRK14669 242 RMaAAKGDDADVFGYHYENPMVAVNLFHMRGGKIVDRREFFwedlgeVQVEFEYDEGLFFSSLLKQIYLD---QQYVPRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 315 IILPFEIEESSALSEALTQISERKVSLKVVTRGERAQYLQLANKNALNS----ITVKQSTQDSINKryaQLKATLGLDDI 390
Cdd:PRK14669 319 IYVPVEFEDREALEELLTEQRHRRIEIRVPQRGDKRSLLDLVEQNAKQSydqrFRVMKPSSRAIQE---ALQDALNLPEL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 391 -NRMECFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDEDK-IPDVIFIDGGKG 468
Cdd:PRK14669 396 pSRIECFDISHIQGAETVASMVVWEDGKMKKSDYRKFIIKTVVGVDDFASMREVVTRRYSRLQEEKQpMPGLVLIDGGLG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 469 QLGRAEQYFATWPHAKMPLlVGVAKgtsrkpgLETLLIDGGRKTIP--MDSDAPALHLIQHIRDESHRFAIAGHRNKRQK 546
Cdd:PRK14669 476 QLHAAAEALEAIGITDQPL-ASIAK-------REEIIYVFGQEDEPivLDRFSPVLHLVQSIRDEAHRFAITFHRKRRET 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 490727043 547 QRTQSLLEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISpdMAEKIFNH 602
Cdd:PRK14669 548 RDRTSELLEIPGVGAKTVQRLLKHFGSLERVRAATETQLAAVVGRA--AAEAIIAH 601
|
|
| uvrC |
PRK14668 |
excinuclease ABC subunit C; Provisional |
11-603 |
2.39e-113 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 184785 [Multi-domain] Cd Length: 577 Bit Score: 350.22 E-value: 2.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 11 KTLSSEPGVYRMLDSEQqVIYVGKAKNLKKRVSSYF--RSnltdSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQ 88
Cdd:PRK14668 11 AELPREPGVYQFVAGGT-VLYVGKAVDLRDRVRSYAdpRS----ERIRRMVERADDIDFAVTDTETQALLLEANLIKRHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 89 PRYNILLRDDKSYPYILLTSHKHPRLAFHRGSRKvKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRARSRPCLQY 168
Cdd:PRK14668 86 PRYNVRLKDDKSYPLVQLTDHPVPRIEVTRDPDE-GATVFGPYTDKGRVETVVKALRETYGLRGCSDHKYSNRDRPCLDY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 169 QLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHeVIAD-LIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQ----SI 243
Cdd:PRK14668 165 EMGLCTAPCTGEIDEEAYAEDVESAERFFEGETG-VLADpLRREMEAAAQAQEFERAANLRDRLEAVEAFHGGGgeavSS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 244 SGNFAEMDVVG---------FAHLNGLNGihLLMIRDHKVLgsktyfpKVPKDSGQ-EEILTSFLGQYYlapgATGRIAK 313
Cdd:PRK14668 244 TGDERAVDVLGvaiegdratVARLHAEGG--QLVDRDRHRL-------EAPDGEDRgAAVLAAFIVQYY----AERELPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 314 EIILPfeieESSALSEALTQISERKVSLKVVTRGERAQYLQLANKNALNsitvKQSTQDSInkryAQLKATLGLDDINRM 393
Cdd:PRK14668 311 ALLLS----ERPGDDDVRAWLEAEGVDVRVPGAGREATLVDLALKNARR----RGGRDDEV----GALADALGIDRPERI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 394 ECFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTgiTGGDDYAAMEFALNKRYNKVV---DEDKIPDVIFIDGGKGQL 470
Cdd:PRK14668 379 EGFDVSHAQGRAVVGSNVCFVDGSAETADYRRKKLT--ERNDDYANMRELVRWRAERAVegrDDRPDPDLLLIDGGDGQL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 471 GRAEQYFAT--WphaKMPlLVGVAKGtsrkpglETLLIDGGRkTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQR 548
Cdd:PRK14668 457 GAARDALAEtgW---DVP-AIALAKA-------EELVVTPDR-TYDWPDDAPQLHLLQRVRDEAHRFAVQYHQTLRDDVS 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 490727043 549 TqsLLEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIFNHL 603
Cdd:PRK14668 525 T--VLDDVPGVGPETRKRLLRRFGSVEGVREASVEDLRDVPGVGEKTAETIRERL 577
|
|
| uvrC |
PRK14667 |
excinuclease ABC subunit C; Provisional |
1-605 |
7.53e-111 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 237783 [Multi-domain] Cd Length: 567 Bit Score: 343.64 E-value: 7.53e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 1 MSEFDHAQFLKTLSSEPGVYrMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLE 80
Cdd:PRK14667 1 AKTMDALELIEKAPEEPGVY-LFKKKKRYIYIGKAKNIKNRLLQHYKQSETDPKERAIFSESSSLEWIITRNEYEALVLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 81 NNLIKKYQPRYNILLRDDKSYPYILLTSHKHPRLAFHRGSRKvKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDayYRA 160
Cdd:PRK14667 80 IDLIQQYKPKYNVLLKSGSGYPMLLITDDEYPTVKIVRGTGE-KGEYFGPFLPARKARKVKKLIHKLFKLRTCDP--MPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 161 RSRPCLQYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQ 240
Cdd:PRK14667 157 RKEPCMDYHLGLCSGPCCGKISKEDYELSVKSAKAFLSGNVKEVLPELYDKIEEYSQKLMFEKAAVIRDQILALENLIKG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 241 QSISG-NFAEMDVVGFAHlnglNGIHLLMIRDHKVLGSKTYfpKVPKDSGQE-EILTSFlgqYYLAPgatgrIAKEIILP 318
Cdd:PRK14667 237 QEVSGlPIEEADIFYFMG----SRLGLFLVRSSKLVGKEEF--RLESEEQEEeEVILGY---YYSNY-----IPQKIITN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 319 FEIEEssalsEALTQISERKvslkvvtrGERAQYLQLANKNALNSItvKQSTQDSINkrYAQLKA----TLGLDDINRME 394
Cdd:PRK14667 303 FELSD-----NLKQWLSKRK--------GGDVEFLTLIPKELEKFI--EENIGIKVD--LEVLKEefkkTFGFPLPERIE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 395 CFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVD-EDKIPDVIFIDGGKGQLGRA 473
Cdd:PRK14667 366 GFDISHFYGEFTVGSCVVWEDGSMNKKEYRRYKIKTVDGIDDYASLREVLTRRARRYKEgENPMPDLWLIDGGKGQLSVG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 474 EQYFATWphaKMPLLV-GVAKGTsrkpglETLLIDGGRKtIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSL 552
Cdd:PRK14667 446 IEVRDRL---GLNIKVfSLAKKE------EILYTEDGKE-IPLKENPILYKVFGLIRDEAHRFALSYNRKLREKEGLKDI 515
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 490727043 553 LEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVpGISPDMAEKIFNHLHD 605
Cdd:PRK14667 516 LDKIKGIGEVKKEIIYRNFKTLYDFLKADDEELKKL-GIPPSVKQEVKKYLSG 567
|
|
| uvrC |
PRK14666 |
excinuclease ABC subunit C; Provisional |
10-603 |
2.17e-109 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 237782 [Multi-domain] Cd Length: 694 Bit Score: 343.79 E-value: 2.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 10 LKTLSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFR--SNLTdSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKY 87
Cdd:PRK14666 6 LSTIPLTPGVYLYKDEAGRIIYVGKARHLRRRVASYFRdvSALT-PKTVAMLRHAVTIDTLSTTTEKEALLLEASLIKKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 88 QPRYNILLRDDKSYPYILLTS-HKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYRARSRPCL 166
Cdd:PRK14666 85 RPRYNIVLRDDKQYVLFRLGAkHPYPRLEIVRKARRDGARYFGPFTSASAARETWKTIHRAFPLRRCSDRAFGNRVRACL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 167 QYQLKRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLL-RKMQEQQSISG 245
Cdd:PRK14666 165 YHFMGQCLGPCVNDVPRETYAALVRKVEMLLSGRSGELVDALRTEMEAASEALEFERAAVLRDQIRAVeRTVERQAAVLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 246 NFAEMDVVGFAHLNGLNGIHLLMIRDHKVLGSKTYF-PKVPKDSGqEEILTSFLGQYYlAPGATgrIAKEIILPFEIEE- 323
Cdd:PRK14666 245 GGGDLDVVGLVEAEGGLALGVLFVRQGVLLDGRAFFwPGLGFEEA-PELLWSFLGQFY-GPQST--IPPRIVVPWLPDTe 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 324 -------------------------SSALSEA------LTQISERKVSLKVVTRGERAQYL-----------QLANKNAL 361
Cdd:PRK14666 321 gregddlaptavctdagllpdtpllPDAPEGSsdpvvpVAAATPVDASLPDVRTGTAPTSLanvshadpavaQPTQAATL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 362 NSITVKQSTQDSINKRYAQLK------------------------------------------ATLGLD-DINRMECFDI 398
Cdd:PRK14666 401 AGAAPKGATHLMLEETLADLRggpvrivpprnpaenrlvdmamsnareearrkaetplqdllaRALHLSgPPHRIEAVDV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 399 SHTMGENTVASCVVFDSQGPNNKEYRRYNVTGiTGGDDYAAMEFALNKRynkVVDEDKIPDVIFIDGGKGQLGRAEQYFA 478
Cdd:PRK14666 481 SHTGGRNTRVGMVVFEDGKPARDAYRTYAFED-GEGDDYGTLAAWAGRR---VESGPPWPDLLLVDGGRGQLAAVVRALE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 479 TWPHAKMPLLVGVAKGTS------RKPG--LETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQ 550
Cdd:PRK14666 557 EAGMGGLFAVASIAKARTeegradRRAGnvADRIFLPGRANPLPLRAGAPELLFLQHVRDTVHDYAIGRHRRARAGAALT 636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 490727043 551 SLLEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIFNHL 603
Cdd:PRK14666 637 GELQRVEGIGPATARLLWERFGSLQAMAAAGEEGLAAVPGIGPARAAALHEHL 689
|
|
| uvrC |
PRK14670 |
excinuclease ABC subunit C; Provisional |
22-599 |
2.76e-85 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 173133 [Multi-domain] Cd Length: 574 Bit Score: 277.18 E-value: 2.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 22 MLDSEQQVIYVGKAKNLKKRVSSYFrSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQPRYNILLRDDKSY 101
Cdd:PRK14670 1 MYSENNKILYIGKAKNLRSRVKNYF-LEKISHKTKILMKNVKNIEVITTNSEYEALLLECNLIKTHKPDYNIKLKDDKGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 102 PYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEdayyRARSRPCLQYQLKRCSAPCVNKV 181
Cdd:PRK14670 80 PMIRITCEKYPRIFKTRKIINDGSEYFGPYVNVKKLDLVLDLINKTFKTRKCK----KKSKNPCLYFHMGQCLGVCYRED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 182 TEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQSISG-NFAEMDVVGFAHLNG 260
Cdd:PRK14670 156 LEKEYQKEVDKIKHILNGNISKLLSQIEIKMKEAIQKEDFEAAIKLKETKRSLIEISQTQIITKiNKLSIDYVYIHPTEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 261 LNGIHLLMIRDHKVLGSKTYFPKVPKDsgQEEILTSFLGQYYLAPGAtgrIAKEIILPFEIEESSALSEALTQISERKVS 340
Cdd:PRK14670 236 LNTIVILKYKDGKLVEKDINFDESIYE--EDELILQFITQYYTSINM---IVPDKIHIFKKIDTKNITKLINELKNTKTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 341 LKVVTRGERAQYLQLANKNAlnSITVKQSTQDSiNKRYAQLKATLGLDDINR-MECFDISHTMGENTVASCVVFDSQGPN 419
Cdd:PRK14670 311 IIYKETKEIIKIMEMAISNA--KLALREYENEK-NKALESLKIILEMDKLPKtIEGFDIAHLNGQKTVASLVTFKMGKPF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 420 NKEYRRYNVTGITGG--DDYAAMEFALNKRYNKVVDED-KIPDVIFIDGGKGQLGRAeqyFATWPHAKMPLLVGVAKGTS 496
Cdd:PRK14670 388 KDGYRVYKINSLLKGeiDDFKAIKEVISRRYSKLINEQlELPNLILIDGGKGQLNAA---YSILKGLKIENKVKVCALAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 497 RKpglETLLIDGGRKTIPMDSDAPALHLIQHIRDESHRfaIAGHRNKRQKQRTQSLLEEINGVGSKRRQTLLKYLGGMQG 576
Cdd:PRK14670 465 KE---ETIFLPNKKQGIKLPKGNPALRILQNVRDEAHR--KANGFNKKLRENIKLNYTKIKGIGEKKAKKILKSLGTYKD 539
|
570 580
....*....|....*....|...
gi 490727043 577 VKAANIEQLKKVPGISPDMAEKI 599
Cdd:PRK14670 540 ILLLNEDEIAEKMKINIKMAKKI 562
|
|
| uvrC |
PRK14672 |
excinuclease ABC subunit C; Provisional |
15-601 |
3.54e-79 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 173135 [Multi-domain] Cd Length: 691 Bit Score: 264.29 E-value: 3.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 15 SEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNlTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQPRYNIL 94
Cdd:PRK14672 20 STSGVYLWKDVHGVVIYVGKAKSLRTRLTSYFRCR-HDPKTRVLMSRAAALEYLQTQHEYEALLLENTLIKKHTPRYNIC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 95 LRDDKSYPYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCedAYYRARSRPCLQYQLKRCS 174
Cdd:PRK14672 99 LKDGKTYPLLKLTCEPFPRIFRTRQFCQDGARYFGPFPDVQILDSFLKLILRTYKIRTC--TTLRKRKNPCLYYHLKRCD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 175 APCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQeQQSISGNFAE--MDV 252
Cdd:PRK14672 177 APCCGWVSPRTYQKDIHEITLLLEGNIDATVARLEKRMKRAVRQEAFEAAARIRDDIQAIRCIT-HKSLVQDMDEraRDY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 253 VGFAHLNGLNGIHLLMIRDHKVLGSKTYFPKVPKDsgQEEILTSFLGQYY---------------------LAPGATGRI 311
Cdd:PRK14672 256 IAWSSTGAIVTFAVLRMRGGKLNGRELFRTRSLKN--EEEILSEFLITYYsdhtipphlfvhssaglaehwLSHKAGTQC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 312 AKEII----LPFEIEESSALSEALTQISERKVSLKVVTRGERA-------QYLQLANKNALNSITVKQST-QDSINKRY- 378
Cdd:PRK14672 334 TVTLIplhtFPTPQTPSSTVTTNAPTLAASQNSNAVQDSGLRScsetstmHTLQKAHDACTASEGTRENTpHESAHTPHh 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 379 ------AQLKA---------TLGLDDINR--------------MECFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVT 429
Cdd:PRK14672 414 railamAQLNAheditrylkNRGADDALKelqkqlhlariptlIEGFDISHLGGKYTVASLICFKNGAPDTKNYRLFNLR 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 430 G-ITGGDDYAAMEFALNKRYNKVVDEDKIPDVIFIDGGKGQLGrAEQYFATWPHAKMPlLVGVAKGTsrkpglETLLIDG 508
Cdd:PRK14672 494 AhDTRIDDFASMREAIARRYTHTPEGYTLPDLILVDGGIGHVS-AAQHVLDALGLSIP-LVGLAKRA------EELFIPN 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 509 GRKTIPMDSDAPALHLIQHIRDESHRFAIAGHRNKRQKQRTQSLLEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKV 588
Cdd:PRK14672 566 SPTPLVLDRRNPALHMLQRIRDEAHRFAITRNRHLRTKKELVLSFERLPHVGKVRAHRLLAHFGSFRSLQSATPQDIATA 645
|
650
....*....|...
gi 490727043 589 PGISPDMAEKIFN 601
Cdd:PRK14672 646 IHIPLTQAHTILH 658
|
|
| UvrC_RNaseH_dom |
pfam08459 |
UvrC RNAse H endonuclease domain; This domain is found in the C subunits of the bacterial and ... |
382-536 |
1.64e-60 |
|
UvrC RNAse H endonuclease domain; This domain is found in the C subunits of the bacterial and archaeal UvrABC system which catalyzes nucleotide excision repair in a multi-step process. UvrC catalyzes the first incision on the fourth or fifth phosphodiester bond 3' and on the eighth phosphodiester bond 5' from the damage that is to be excised. The domain described here represents the RNAse H endonuclease domain, located at the C-terminal, between the UvrBC and the (HhH)2 domains, nearby the N-terminal of the HhH. Despite the lack of sequence homology, the endonuclease domain has an RNase H-like fold, which is characteriztic of enzymes with nuclease or polynucleotide transferase activities. RNase H-related enzymes typically contain a highly conserved carboxylate triad, usually DDE, in their catalytic centre. However, instead of a third carboxylate, UvrC of Thermotoga maritima was found to contain a highly conserved histidine (H488) on helix-4 in close proximity to two aspartates.
Pssm-ID: 462484 [Multi-domain] Cd Length: 150 Bit Score: 198.05 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 382 KATLGLDD-INRMECFDISHTMGENTVASCVVFDSQGPNNKEYRRYNVTGITGGDDYAAMEFALNKRYNKVVDED-KIPD 459
Cdd:pfam08459 1 QEALGLPKlPRRIECFDISHIQGTDTVASMVVFEDGKPDKSDYRRFNIKTTVGPDDYASMREVLTRRFSRLLEEFgPLPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490727043 460 VIFIDGGKGQLGRAEQYFATWpHAKMPlLVGVAKGTSRKpgletLLIDGGRKTIPMDSDAPALHLIQHIRDESHRFA 536
Cdd:pfam08459 81 LILIDGGKGQLNAALEVLEEL-GLDIP-VIGLAKDDKHK-----IDTDGREEEIILPRDSPALHLLQRIRDEAHRFA 150
|
|
| PRK07883 |
PRK07883 |
DEDD exonuclease domain-containing protein; |
13-238 |
1.15e-56 |
|
DEDD exonuclease domain-containing protein;
Pssm-ID: 236123 [Multi-domain] Cd Length: 557 Bit Score: 200.14 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 13 LSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQPRYN 92
Cdd:PRK07883 214 LPHAPGVYLFRGPSGEVLYVGTAVNLRRRVRSYFTAAETRGRMREMVALAERVDHVECAHALEAEVRELRLIAAHKPPYN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 93 ILLRDDKSYPYILLTSHKHPRLAFHRGSRKVKGEYFGPFPSAGAVSESLRLMQKIFPVRQCEDAYYR--ARSRPCLQYQL 170
Cdd:PRK07883 294 RRSKFPERRWWVRLTDEAFPRLSVVRAVEDDGAAYLGPFRSRRAAEEAAEALARAFPLRQCTDRLSRraRHGPACALAEL 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490727043 171 KRCSAPCVNKVTEQEYGEQVDYVRKFLTGKSHEVIADLIKKMEAASKDLNFELAAKVRDQ----IMLLRKMQ 238
Cdd:PRK07883 374 GRCPAPCDGRESAAEYAEAVARARAALTGDDDAVLAALRARIDRLAAAERFEEAARLRDRlaalLRALARAQ 445
|
|
| GIY-YIG_UvrC_Cho |
cd10434 |
Catalytic GIY-YIG domain of nucleotide excision repair endonucleases UvrC, Cho, and similar ... |
13-93 |
1.31e-39 |
|
Catalytic GIY-YIG domain of nucleotide excision repair endonucleases UvrC, Cho, and similar proteins; UvrC is essential for nucleotide excision repair (NER). The N-terminal catalytic GIY-YIG domain of UvrC (also known as Uri domain) is responsible for the 3' incision reaction and the C-terminal half of UvrC, consisting of an UvrB-binding domain (UvrBb), EndoV-like nuclease domain and a helix-hairpin-helix (HhH) DNA-binding domain, contains the residues involved in 5' incision. The N- and C-terminal regions are joined by a common Cys-rich domain containing four conserved Cys residues. Besides UvrC, protein Cho (UvrC homolog) serves as a second endonuclease in E. coli NER. Cho contains GIY-YIG motif followed by a Cys-rich region and shares sequence homology with the N-terminal half of UvrC. It is capable of incising the DNA at the 3' side of a lesion in the presence of the UvrA and UvrB proteins during NER. The C-terminal half of Cho is a unique uncharacterized domain, which is distinct from that of UvrC. Moreover, unlike UvrC, Cho does not require the UvrC-binding domain of UvrB for the 3' incision reaction, which might cause the shift in incision position and the difference in incision efficiencies between Cho and UvrC on different damaged substrates. Due to this, the range of NER in E. coli can be broadened by combining action of Cho and UvrC. This family also includes many uncharacterized epsilon proofreading subunits of DNA polymerase III, which have an additional N-terminal ExoIII domain and a 3'-5' exonuclease domain homolog, fused to an UvrC-like region or a Cho-like region. The UvrC-like region includes a GIY-YIG motif, followed by a Cys-rich region, and an UvrB-binding domain (UvrBb), but lacks the EndoV-like nuclease domain and the helix-hairpin-helix (HhH) DNA-binding domain. The Cho-like region consists of a GIY-YIG motif, followed by the Cys-rich region, and the unique uncharacterized domain presenting in the C-terminal half of Cho. Some family members may not carry the Cys-rich region. This family also includes a specific Cho-like protein from G. violaceus, which possesses only UvrBb domain at the C-terminus, but lacks the additional N-terminal ExoIII domain. The oother two remote homologs of UvrC, Bacillus-I and -II, are included in this family as well. Both of them contain a GIY-YIG domain, but no Cys-rich region. Moreover, the whole C-terminal region of Bacillus-I is replaces by an unknown domain, and Bacillus-II possesses another unknown N-terminal extension.
Pssm-ID: 198381 [Multi-domain] Cd Length: 81 Bit Score: 139.54 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 13 LSSEPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQPRYN 92
Cdd:cd10434 1 LPDSPGVYLFKDADGEVLYVGKAKNLRKRVSSYFTGERHSPKTRRLVEEIRDIEYIVTDSELEALLLEANLIKKYKPRYN 80
|
.
gi 490727043 93 I 93
Cdd:cd10434 81 I 81
|
|
| GIYc |
smart00465 |
GIY-YIG type nucleases (URI domain); |
16-97 |
2.57e-16 |
|
GIY-YIG type nucleases (URI domain);
Pssm-ID: 214677 [Multi-domain] Cd Length: 84 Bit Score: 73.99 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 16 EPGVYRMLDSEQQVIYVGKAKNLKKRVSSYFR-SNLTDSKTRVLVSNICDIE-VTLTNTETEALLLENNLIKKYQPRYNI 93
Cdd:smart00465 1 KPGVYYITNKKNGKLYVGKAKNLRNRLKRHFSgSRKGRLLIDALLKYGGNFEfIILESFDESALELEKYLIKEYKPKYNL 80
|
....
gi 490727043 94 LLRD 97
Cdd:smart00465 81 LLKG 84
|
|
| PRK10545 |
PRK10545 |
excinuclease Cho; |
9-188 |
3.31e-13 |
|
excinuclease Cho;
Pssm-ID: 182535 Cd Length: 286 Bit Score: 70.47 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 9 FLKTLSSEPGVYRML-DSEQQVIYVGKAKNLKKRVSSYFRsnlTDSKTRVL-----VSNICdievtlTNTETEALLLENN 82
Cdd:PRK10545 27 FLEDLPKLPGVYLFHgESDTMPLYIGKSVNIRSRVLSHLR---TPDEAAMLrqsrrISWIC------TAGEIGALLLEAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 83 LIKKYQPRYNILLRDDKSYPYILLTSHKhPRLAFhrgSRKVKGEY----FGPFPSAGAVSESLRLM---QKI-FPVRQCE 154
Cdd:PRK10545 98 LIKEQQPLFNKRLRRNRQLCSLQLNEGR-VDVVY---AKEVDFSRapnlFGLFANRRAALQALQSIadeQKLcYGLLGLE 173
|
170 180 190
....*....|....*....|....*....|....
gi 490727043 155 DAyyrARSRPCLQYQLKRCSAPCVNKVTEQEYGE 188
Cdd:PRK10545 174 PL---SRGRACFRSALKRCAGACCGKESHEAHAL 204
|
|
| GIY-YIG_SF |
cd00719 |
GIY-YIG nuclease domain superfamily; The GIY-YIG nuclease domain superfamily includes a large ... |
18-87 |
2.15e-10 |
|
GIY-YIG nuclease domain superfamily; The GIY-YIG nuclease domain superfamily includes a large and diverse group of proteins involved in many cellular processes, such as class I homing GIY-YIG family endonucleases, prokaryotic nucleotide excision repair proteins UvrC and Cho, type II restriction enzymes, the endonuclease/reverse transcriptase of eukaryotic retrotransposable elements, and a family of eukaryotic enzymes that repair stalled replication forks. All of these members contain a conserved GIY-YIG nuclease domain that may serve as a scaffold for the coordination of a divalent metal ion required for catalysis of the phosphodiester bond cleavage. By combining with different specificity, targeting, or other domains, the GIY-YIG nucleases may perform different functions.
Pssm-ID: 198380 [Multi-domain] Cd Length: 69 Bit Score: 56.60 E-value: 2.15e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 18 GVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSkTRVLVSNICDIEVTLTNTETEALLLENNLIKKY 87
Cdd:cd00719 1 GVYVLYDEDNGLIYVGQTKNLRNRIKEHLRKQRSDW-TKGLKPFEILYLEVAPEAESELLDLEAALIKKL 69
|
|
| GIY-YIG |
pfam01541 |
GIY-YIG catalytic domain; This domain called GIY-YIG is found in the amino terminal region of ... |
17-92 |
6.62e-10 |
|
GIY-YIG catalytic domain; This domain called GIY-YIG is found in the amino terminal region of excinuclease abc subunit c (uvrC), bacteriophage T4 endonucleases segA, segB, segC, segD and segE; it is also found in putative endonucleases encoded by group I introns of fungi and phage. The structure of I-TevI a GIY-YIG endonuclease, reveals a novel alpha/beta-fold with a central three-stranded antiparallel beta-sheet flanked by three helices. The most conserved and putative catalytic residues are located on a shallow, concave surface and include a metal coordination site.
Pssm-ID: 426314 [Multi-domain] Cd Length: 78 Bit Score: 55.81 E-value: 6.62e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490727043 17 PGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLVSNICDIEVTLTNTETEALLLENNLIKKYQP-RYN 92
Cdd:pfam01541 2 GGIYIIRNKDNKLLYVGSTKNLERRLNQHNAGKGAKYTRGKGVEPFKLIYLEEFPTKSEALELEKYLIKLYRPnKYN 78
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
203-236 |
1.71e-08 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 50.47 E-value: 1.71e-08
10 20 30
....*....|....*....|....*....|....
gi 490727043 203 EVIADLIKKMEAASKDLNFELAAKVRDQIMLLRK 236
Cdd:pfam02151 2 KLIKELEEEMEEAAENEDFEKAAKLRDQINALKK 35
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
203-237 |
1.24e-07 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 54.63 E-value: 1.24e-07
10 20 30
....*....|....*....|....*....|....*
gi 490727043 203 EVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKM 237
Cdd:COG0556 623 KLIKELEKEMKEAAKNLEFEEAARLRDEIKELKKE 657
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
203-242 |
2.91e-07 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 53.51 E-value: 2.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490727043 203 EVIADLIKKMEAASKDLNFELAAKVRDQIMLLRKMQEQQS 242
Cdd:PRK05298 613 KLIKELEKQMKEAAKNLEFEEAARLRDEIKELKEELLGLS 652
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
546-600 |
1.56e-06 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 49.40 E-value: 1.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490727043 546 KQRTQSLLEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKIF 600
Cdd:COG1948 150 REQQLYVVESLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERIR 204
|
|
| GIY-YIG_bI1_like |
cd10445 |
Catalytic GIY-YIG domain of putative intron-encoded endonuclease bI1 and similar proteins; The ... |
17-95 |
1.09e-05 |
|
Catalytic GIY-YIG domain of putative intron-encoded endonuclease bI1 and similar proteins; The prototype of this family is a putative intron-encoded mitochondrial DNA endonuclease bI1 found in mitochondrion Ustilago maydis. This protein may arise from proteolytic cleavage of an in-frame translation of COB exon 1 plus intron 1, containing the bI1 open reading frame. It contains an N-terminal truncated non-functional cytochrome b region and a C-terminal intron-encoded endonuclease bI1 region. The bI1 region shows high sequence similarity to endonucleases of group I introns of fungi and phage and might be involved in intron homing. Many uncharacterized bI1 homologs existing in fungi and chlorophyta in this family do not contain the cytochrome b region, but have a standalone bI1-like region, which contains a GIY-YIG domain and a minor-groove binding alpha-helix nuclease-associated modular domain (NUMOD). This family also includes a Yarrowia lipolytica mobile group-II intron COX1-i1, also called intron alpha, encoding protein with reverse transcriptase activity. The group-II intron COX1-i1 may be involv ed both in the generation of the circular multimeric DNA molecules (senDNA alpha) which amplify during the senescence syndrome and in the generation of the site-specific deletion which accumulates in the premature-death syndrome.
Pssm-ID: 198392 [Multi-domain] Cd Length: 88 Bit Score: 44.14 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 17 PGVYRMLDSEQQVIYVGKAKNLKKRVSSYFRSNLTDSKTRVLV-------SNIC--DIEVTLTNTETEALLLENNLIKKY 87
Cdd:cd10445 1 SGIYIWINKINGKIYVGSSINLYKRLRSYLNPSYLKKNSPILRallkyglSNFTltILEYYNGENKEELLELEQYYIDLL 80
|
....*...
gi 490727043 88 QPRYNILL 95
Cdd:cd10445 81 KPEYNILK 88
|
|
| ComEA |
COG1555 |
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ... |
549-603 |
1.82e-05 |
|
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];
Pssm-ID: 441164 [Multi-domain] Cd Length: 72 Bit Score: 42.93 E-value: 1.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490727043 549 TQSLLEEINGVGSKRRQTLLKY---LGGMQgvkaaNIEQLKKVPGISPDMAEKIFNHL 603
Cdd:COG1555 19 TAEELQTLPGIGPKLAQRIVEYrekNGPFK-----SVEDLLEVKGIGPKTLEKLKPYL 71
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
552-605 |
7.06e-05 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 40.93 E-value: 7.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490727043 552 LLEEINGVGSKRRQTLLKYLGG-MQGVKAANIEQLKKVPGISPDMAEKIFNHLHD 605
Cdd:pfam14520 3 ELLSISGIGPKTALALLSAGIGtVEDLAEADVDELAEIPGIGEKTAQRIILELRD 57
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
575-602 |
1.01e-04 |
|
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 39.71 E-value: 1.01e-04
10 20
....*....|....*....|....*...
gi 490727043 575 QGVKAANIEQLKKVPGISPDMAEKIFNH 602
Cdd:pfam00633 3 EGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| GIY-YIG_EndoII_Hpy188I_like |
cd10436 |
Catalytic GIY-YIG domain of coliphage T4 non-specific endonuclease II, type II restriction ... |
27-93 |
1.32e-04 |
|
Catalytic GIY-YIG domain of coliphage T4 non-specific endonuclease II, type II restriction endonuclease R.Hpy188I, and similar proteins; This family includes two different GIY-YIG enzymes, coliphage T4 non-specific endonuclease II (EndoII), and type II restriction endonuclease R.Hpy188I. They display high sequence similarity to each other, and both of them contain an extra N-terminal hairpin that lacks counterparts in other GIY-YIG enzymes. EndoII encoded by gene denA catalyzes the initial step in degradation of host DNA, which permits scavenging of host-derived nucleotides for phage DNA synthesis. R.Hpy188I recognizes the unique sequence, 5'-TCNGA-3', and cleaves the DNA between nucleotides N and G in its recognition sequence to generate a single nucleotide 3'-overhang. EndoII binds to two DNA substrates as an X-shaped tetrameric structure composed as a dimer of dimers. In contrast, two subunits of R.Hpy188I form a dimer to embrace one bound DNA. Divalent metal-ion cofactors are required for their catalytic events, but not for the substrates binding.
Pssm-ID: 198383 [Multi-domain] Cd Length: 97 Bit Score: 41.18 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 27 QQVIYVGKAKNLKKRVSSYFRS------NLTDSK--------------TRVLVSNICDIEVTLTNTETEALLLENNLIKK 86
Cdd:cd10436 10 GEIVYIGETQDLRKRFNSYRGGisprngQTTNCRinklilkalkkgkvVELYVKQPEELVITLGDPVNTAKGLEDELIEK 89
|
....*..
gi 490727043 87 YQPRYNI 93
Cdd:cd10436 90 IKPEWNS 96
|
|
| ruvA |
TIGR00084 |
Holliday junction DNA helicase, RuvA subunit; RuvA specifically binds Holliday junctions as a ... |
553-606 |
3.18e-03 |
|
Holliday junction DNA helicase, RuvA subunit; RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129193 [Multi-domain] Cd Length: 191 Bit Score: 39.28 E-value: 3.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490727043 553 LEEINGVGSKrrqTLLKYLGGM------QGVKAANIEQLKKVPGISPDMAEKIFNHLHDK 606
Cdd:TIGR00084 74 LIKVNGVGPK---LALAILSNMspeefvYAIETEEVKALVKIPGVGKKTAERLLLELKGK 130
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|
| HHH_3 |
pfam12836 |
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain. |
549-599 |
3.44e-03 |
|
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
Pssm-ID: 463723 [Multi-domain] Cd Length: 62 Bit Score: 36.31 E-value: 3.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490727043 549 TQSLLEEINGVGSKRRQTLLKY---LGGMqgvkaANIEQLKKVPGISPDMAEKI 599
Cdd:pfam12836 10 SAELLSRVPGLGPKLAKNIVEYreeNGPF-----RSREDLLKVKGLGPKTFEQL 58
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|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
546-599 |
3.69e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 40.24 E-value: 3.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490727043 546 KQRTQSLLEEINGVGSKRRQTLLKYLGGMQGVKAANIEQLKKVPGISPDMAEKI 599
Cdd:PRK13766 710 KEQQEYIVESLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRI 763
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