|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
1537-1898 |
4.04e-134 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 426.31 E-value: 4.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1537 GTGTDAPLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGKVSM 1616
Cdd:cd01303 81 GSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1617 DRLSPDDYVEQLEDGLRDAEAFVQYTLGrKCSRIQPCITPRFIPTCTPELMRGLAELARKY-GTHIQSHISECCGEVNCV 1695
Cdd:cd01303 161 DRNAPEYYRDTAESSYRDTKRLIERWHG-KSGRVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHISENLDEIAWV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1696 REMHPEYASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDV 1775
Cdd:cd01303 240 KELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1776 AGGISPSMLSAQRMAVVNSRClrahkLAVSGGTTANLemekdviTFKEALWLATVGGAQALDLADRVGTFEEGKEFDALL 1855
Cdd:cd01303 320 GGGTSFSMLDTLRQAYKVSRL-----LGYELGGHAKL-------SPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVV 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1004138820 1856 VDTNLGGTDGPfDVFPGEDDLERFEKFINLGDDRNLLEVYVQG 1898
Cdd:cd01303 388 IDPSATPLLAD-RMFRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
1539-1898 |
2.11e-115 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 372.36 E-value: 2.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1539 GTDAPLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGKVSMDR 1618
Cdd:TIGR02967 62 SYGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1619 LSPDDYVEQLEDGLRDAEAFVQYTLGRkcSRIQPCITPRFIPTCTPELMRGLAELARKY-GTHIQSHISECCGEVNCVRE 1697
Cdd:TIGR02967 142 NAPDYLRDTAESSYDESKALIERWHGK--GRLLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1698 MHPEYASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAG 1777
Cdd:TIGR02967 220 LFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1778 GISPSMLSAQRMAVVNSRcLRAHKLavsggttanlemekdviTFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVD 1857
Cdd:TIGR02967 300 GTSFSMLQTLREAYKVSQ-LQGARL-----------------SPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLD 361
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1004138820 1858 TNLggTDGPFDVFPGEDDLE-RFEKFINLGDDRNLLEVYVQG 1898
Cdd:TIGR02967 362 PAA--TPLLALRFEGADTLEdKLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
1534-1904 |
1.31e-90 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 301.75 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1534 LFTGTGTDAPLMDWLKKYTFPAEGSYrDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGK 1613
Cdd:COG0402 72 LLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1614 VSMDRLSPDDYVEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGEVN 1693
Cdd:COG0402 151 GLMDRGFPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1694 CVREMHPeyASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGT 1773
Cdd:COG0402 231 WVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1774 DVAGG-ISPSMLSAQRMAvvnsrcLRAHKLAvsggttanlEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFD 1852
Cdd:COG0402 309 DGAASnNSLDMFEEMRLA------ALLQRLR---------GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRAD 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1004138820 1853 ALLVDTNLGGTDGPFDVfpgeddlerFEKFINLGDDRNLLEVYVQGVCVKRG 1904
Cdd:COG0402 374 LVVLDLDAPHLAPLHDP---------LSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1542-1904 |
8.21e-81 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 273.99 E-value: 8.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1542 APLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGKVSMDRLSP 1621
Cdd:PRK09228 90 EQLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQSVDALFEAAEARNMRMIAGKVLMDRNAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1622 DDYVEQLEDGLRDAEAFVQYTLGRkcSRIQPCITPRFIPTCTPELMRGLAELARKY-GTHIQSHISECCGEVNCVREMHP 1700
Cdd:PRK09228 170 DGLRDTAESGYDDSKALIERWHGK--GRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1701 EYASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGGIS 1780
Cdd:PRK09228 248 EARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1781 PSMLsaQRMavvnsrcLRAHKLAvsggttanlEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTNL 1860
Cdd:PRK09228 328 FSML--QTM-------NEAYKVQ---------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAA 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1004138820 1861 GgtdgpfdvfP--------GEDDLERFEKFINLGDDRNLLEVYVQGVCVKRG 1904
Cdd:PRK09228 390 T---------PllalrtarAESLEELLFALMTLGDDRAVAETYVAGRPVYRR 432
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
68-530 |
1.16e-74 |
|
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: 254.32 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 68 LHFDCDCFYAQVEEVRNPALRDVPLGVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGEDLGPYRQASKSIH 147
Cdd:cd01703 1 IHLDLDCFYAQVEEIRDPSLKSKPLGIQQKYIVVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNGEDLTPFRDMSKKVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 148 AVLSRY---GTAERLGMDETYVDCTEEVLrrvrsgayeppappprLVGHRhtarcaVAADTRYRPQDlrarqpdggggdg 224
Cdd:cd01703 81 RLLRSYswnDRVERLGFDENFMDVTEMRL----------------LVASH------IAYEMRERIEN------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 225 gddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaavraETG 304
Cdd:cd01703 126 -----------------------------------------------------------------------------ELG 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 305 FRSSAGIAPNKLLAKLVSGLHKPDDQTIIHP---DQAADFLAPLPVRALPGVGYKTEQLLSERCGAASAADVRRCGQQR- 380
Cdd:cd01703 129 LTCCAGIASNKLLAKLVGSVNKPNQQTTLLPpscADLMDFMDLHDLRKIPGIGYKTAAKLEAHGISSVRDLQEFSNRNRq 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 381 -------------LAEALGDKTAAMLWELAWGCDSSPV-RPTGPPRSITVEDSFKSCASWAAATAV--LRVLAPDLLARL 444
Cdd:cd01703 209 tvgaapsllelllMVKEFGEGIGQRIWKLLFGRDTSPVkPASDFPQQISIEDSYKKCSLEEIREARnkIEELLASLLERM 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 445 R----EEWAENRRRPETLTLKWRHRGS---GWSRTSASSPMPlpagalGQQQQQPAATEAQLVDQLVRASLALLQR---- 513
Cdd:cd01703 289 KqdlqEVKAGDGRRPHTLRLTLRRYTStkkHYNRESKQAPIP------SHVFQKLTGGNEIAARPIEKILMRLFRElvpp 362
|
490
....*....|....*..
gi 1004138820 514 HIREPFNLSLINLGATN 530
Cdd:cd01703 363 KNVKGFNLTLLNVCFTN 379
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
65-529 |
4.77e-56 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 198.83 E-value: 4.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 65 RVILHFDCDCFYAQVEEVRNPALRDVPLGV---TQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGeDLGPYRQ 141
Cdd:COG0389 1 RRILHVDMDAFYASVEQRDRPELRGKPVAVggdNNRGVVAAASYEARAFGVRSGMPLFQARRLCPDLVVLPP-DFELYRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 142 ASKSIHAVLSRYgTA--ERLGMDETYVDCTEevlrrvrsgayeppapPPRLVGHRHtarcAVAADTRyrpQDLRARqpdg 219
Cdd:COG0389 80 VSRRVMAILERY-TPlvEPLSIDEAFLDVTG----------------SARLFGSAE----AIARRIR---RRIRRE---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 220 gggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaav 299
Cdd:COG0389 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 300 raeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCGQQ 379
Cdd:COG0389 132 ---TGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKL-ARLGIRTIGDLAALPRA 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 380 RLAEALGdKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREEwaenRRRPETL 458
Cdd:COG0389 208 ELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFgEDLTDLEELEAALRRLAERLAERLRRQ----GLGARTV 282
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 459 TLKWRHrgSGWSRTSASSPMPLPAGALgqqqqqpaateaqlvDQLVRASLALLQRHIREPFNLSLINLGAT 529
Cdd:COG0389 283 TVKLRT--SDFRTTTRSRTLPEPTDDT---------------AELLRAARELLERIYRPGRPVRLLGVRLS 336
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
72-461 |
5.16e-48 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 175.69 E-value: 5.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 72 CDCFYAQVEEVRNPALRDVPL---------GVtqkylIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGeDLGPYRQA 142
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVavggspgrrGV-----ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPG-RFDVYKEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 143 SKSIHAVLSRYgTA--ERLGMDETYVDCTEevlrrvrSGAYEPPAppprlvghrhTArcaVAadtryrpQDLRArqpdgg 220
Cdd:PRK02406 75 SRQIREIFRRY-TDliEPLSLDEAYLDVTD-------NKLCIGSA----------TL---IA-------QEIRQ------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 221 ggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpseDSWETllaigsmvaaearaavr 300
Cdd:PRK02406 121 ----------------------------------------------------------DIFEE----------------- 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 301 aeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCGQQR 380
Cdd:PRK02406 126 --LGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKL-HALGIYTCADLQKYDLAE 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 381 LAEALGdKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREewAENRRRPETLT 459
Cdd:PRK02406 203 LIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFaEDLYDLEACLAELPRLAEKLERRLER--AKPDKRIKTVG 279
|
..
gi 1004138820 460 LK 461
Cdd:PRK02406 280 VK 281
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1561-1901 |
2.59e-33 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 132.63 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1561 DLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERL--GQRAVVGKVSMDRLSPDDYVEQLEDGLRDAEAF 1638
Cdd:pfam01979 24 PPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALLEAAEELplGLRFLGPGCSLDTDGELEGRKALREKLKAGAEF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1639 VQYTLGrkcSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGEV-NCV-----REMHPEYASDAAvfEEM 1712
Cdd:pfam01979 104 IKGMAD---GVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVeDAIaafggGIEHGTHLEVAE--SGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1713 GLLTSRTVMAHGTLLSDDDIRHLASR--GTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAG-GISPSMLSAQRM 1789
Cdd:pfam01979 179 LLDIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1790 AVVNSrclrahklavsggttanlEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTNLggtdgpfdv 1869
Cdd:pfam01979 259 ALELQ------------------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------- 311
|
330 340 350
....*....|....*....|....*....|..
gi 1004138820 1870 fpgeddlerFEKFINLGDDRNLLEVYVQGVCV 1901
Cdd:pfam01979 312 ---------LAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
947-1072 |
7.46e-32 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 122.30 E-value: 7.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 947 VDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFV-AVSYEARAAGIRCGDgvgsggraaiaylknmgavSVAEARRRCPG 1025
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGIVaAASYEARKYGVRSGM-------------------PVFEAKKLCPN 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1004138820 1026 LVVRPMRTDRYRQVAEQVHSLLRSFSPDgEVEKASYDDFYLDVTRHC 1072
Cdd:pfam00817 62 LIVVPPDLELYRRASRKIFEILRRFSTP-KVEQASIDEAFLDLTGLE 107
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
942-1069 |
1.51e-30 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 124.87 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFV-AVSYEARAAGIRCGdgvgsggraaiaylknMgavSVAEAR 1020
Cdd:COG0389 1 RRILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGVVaAASYEARAFGVRSG----------------M---PLFQAR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1004138820 1021 RRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:COG0389 62 RLCPDLVVLPPDFELYRDVSRRVMAILERYTP--LVEPLSIDEAFLDVT 108
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
945-1069 |
6.55e-29 |
|
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: 119.93 E-value: 6.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 945 LHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFVA-VSYEARAAGIRcgdgvgSGgraaiaylknMgavSVAEARRRC 1023
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVGGSSDRGVVStASYEARKFGVR------SA----------M---PIFQAKKLC 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1004138820 1024 PGLVVRPMRTDRYRQVAEQVHSLLRSFSPDgeVEKASYDDFYLDVT 1069
Cdd:cd03586 62 PNLIFVPPRFDKYREVSRQIMEILREYTPL--VEPLSIDEAYLDVT 105
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
71-170 |
2.04e-27 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 109.59 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 71 DCDCFYAQVEEVRNPALRDVPLGVTQKY---LIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSgEDLGPYRQASKSIH 147
Cdd:pfam00817 2 DMDAFFASVELLRDPELKGKPVAVGGGNgrgIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVP-PDLELYRRASRKIF 80
|
90 100
....*....|....*....|....*
gi 1004138820 148 AVLSRYGTA--ERLGMDETYVDCTE 170
Cdd:pfam00817 81 EILRRFSTPkvEQASIDEAFLDLTG 105
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
942-1069 |
2.72e-23 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 104.73 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVT---QFNSGGFVAVSYEARAAGIRCgdgvgsggraaiaylknmgAVSVAE 1018
Cdd:PRK01810 5 RVIFHVDMNSFFASVEIAYDPSLQGKPLAVAgneKERKGIIVTCSYEARAYGIRT-------------------TMPLWE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1019 ARRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:PRK01810 66 AKRLCPQLIVRRPNFDRYREASRQMFQILSEFTP--LVQPVSIDEGYLDIT 114
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
1286-1458 |
1.55e-16 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 83.27 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1286 VQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP--------TLAR---KT 1354
Cdd:COG0389 118 EAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWgvgpktaeKLARlgiRT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1355 GAsvvaalgggglvgDLSAFSRAQLVARFGAQLGGLLA------DLPdggpappaaaaapgggggamggsVRERGPQKSI 1428
Cdd:COG0389 198 IG-------------DLAALPRAELRRRFGKVGERLYRlargidPRP-----------------------VEPRRPRKSI 241
|
170 180 190
....*....|....*....|....*....|.
gi 1004138820 1429 LVERSFPA-ITRFGGVKDALVPMVGALWERL 1458
Cdd:COG0389 242 GVERTFGEdLTDLEELEAALRRLAERLAERL 272
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
1285-1487 |
9.96e-12 |
|
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: 68.70 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1285 GVQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP-----TLAR------K 1353
Cdd:cd03586 114 ATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPgvgkvTAEKlkelgiK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1354 TGAsvvaalgggglvgDLSAFSRAQLVARFGAqLGGLLADLpdggpappaaaaapggGGGAMGGSVRERGPQKSILVERS 1433
Cdd:cd03586 194 TIG-------------DLAKLDVELLKKLFGK-SGRRLYEL----------------ARGIDNRPVEPDRERKSIGVERT 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1004138820 1434 FP-AITRFGGVKDALVPMVGALWERLtedaARHSRVPAKLLLTWRQGYGAPKTRS 1487
Cdd:cd03586 244 FSeDLTDPEELLEELLELAEELAERL----RKRGLKGRTVTVKLKYADFSTRTRS 294
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
1288-1459 |
1.06e-06 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 52.81 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1288 IAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP-----TLAR------KTGA 1356
Cdd:PRK02406 114 IAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPgvgkvTAEKlhalgiYTCA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1357 svvaalgggglvgDLSAFSRAQLVARFGAqLGGLLADL----------PDggpappaaaaapgggggamggsvRERgpqK 1426
Cdd:PRK02406 194 -------------DLQKYDLAELIRHFGK-FGRRLYERargiderpvkPD-----------------------RER---K 233
|
170 180 190
....*....|....*....|....*....|....
gi 1004138820 1427 SILVERSFPA-ITRFGGVKDALVPMVGALWERLT 1459
Cdd:PRK02406 234 SVGVERTFAEdLYDLEACLAELPRLAEKLERRLE 267
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
1286-1317 |
3.22e-04 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 42.95 E-value: 3.22e-04
10 20 30
....*....|....*....|....*....|..
gi 1004138820 1286 VQIAQRLRAALKEALSMTVSVGVGPTKLTARL 1317
Cdd:pfam00817 114 EALAKRLRREIAEETGLTCSIGIAPNKLLAKL 145
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
1537-1898 |
4.04e-134 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 426.31 E-value: 4.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1537 GTGTDAPLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGKVSM 1616
Cdd:cd01303 81 GSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1617 DRLSPDDYVEQLEDGLRDAEAFVQYTLGrKCSRIQPCITPRFIPTCTPELMRGLAELARKY-GTHIQSHISECCGEVNCV 1695
Cdd:cd01303 161 DRNAPEYYRDTAESSYRDTKRLIERWHG-KSGRVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHISENLDEIAWV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1696 REMHPEYASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDV 1775
Cdd:cd01303 240 KELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1776 AGGISPSMLSAQRMAVVNSRClrahkLAVSGGTTANLemekdviTFKEALWLATVGGAQALDLADRVGTFEEGKEFDALL 1855
Cdd:cd01303 320 GGGTSFSMLDTLRQAYKVSRL-----LGYELGGHAKL-------SPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVV 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1004138820 1856 VDTNLGGTDGPfDVFPGEDDLERFEKFINLGDDRNLLEVYVQG 1898
Cdd:cd01303 388 IDPSATPLLAD-RMFRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
1539-1898 |
2.11e-115 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 372.36 E-value: 2.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1539 GTDAPLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGKVSMDR 1618
Cdd:TIGR02967 62 SYGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1619 LSPDDYVEQLEDGLRDAEAFVQYTLGRkcSRIQPCITPRFIPTCTPELMRGLAELARKY-GTHIQSHISECCGEVNCVRE 1697
Cdd:TIGR02967 142 NAPDYLRDTAESSYDESKALIERWHGK--GRLLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1698 MHPEYASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAG 1777
Cdd:TIGR02967 220 LFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1778 GISPSMLSAQRMAVVNSRcLRAHKLavsggttanlemekdviTFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVD 1857
Cdd:TIGR02967 300 GTSFSMLQTLREAYKVSQ-LQGARL-----------------SPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLD 361
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1004138820 1858 TNLggTDGPFDVFPGEDDLE-RFEKFINLGDDRNLLEVYVQG 1898
Cdd:TIGR02967 362 PAA--TPLLALRFEGADTLEdKLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
1534-1904 |
1.31e-90 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 301.75 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1534 LFTGTGTDAPLMDWLKKYTFPAEGSYrDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGK 1613
Cdd:COG0402 72 LLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1614 VSMDRLSPDDYVEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGEVN 1693
Cdd:COG0402 151 GLMDRGFPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1694 CVREMHPeyASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGT 1773
Cdd:COG0402 231 WVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1774 DVAGG-ISPSMLSAQRMAvvnsrcLRAHKLAvsggttanlEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFD 1852
Cdd:COG0402 309 DGAASnNSLDMFEEMRLA------ALLQRLR---------GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRAD 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1004138820 1853 ALLVDTNLGGTDGPFDVfpgeddlerFEKFINLGDDRNLLEVYVQGVCVKRG 1904
Cdd:COG0402 374 LVVLDLDAPHLAPLHDP---------LSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1542-1904 |
8.21e-81 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 273.99 E-value: 8.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1542 APLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERLGQRAVVGKVSMDRLSP 1621
Cdd:PRK09228 90 EQLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQSVDALFEAAEARNMRMIAGKVLMDRNAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1622 DDYVEQLEDGLRDAEAFVQYTLGRkcSRIQPCITPRFIPTCTPELMRGLAELARKY-GTHIQSHISECCGEVNCVREMHP 1700
Cdd:PRK09228 170 DGLRDTAESGYDDSKALIERWHGK--GRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1701 EYASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGGIS 1780
Cdd:PRK09228 248 EARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1781 PSMLsaQRMavvnsrcLRAHKLAvsggttanlEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTNL 1860
Cdd:PRK09228 328 FSML--QTM-------NEAYKVQ---------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAA 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1004138820 1861 GgtdgpfdvfP--------GEDDLERFEKFINLGDDRNLLEVYVQGVCVKRG 1904
Cdd:PRK09228 390 T---------PllalrtarAESLEELLFALMTLGDDRAVAETYVAGRPVYRR 432
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
68-530 |
1.16e-74 |
|
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: 254.32 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 68 LHFDCDCFYAQVEEVRNPALRDVPLGVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGEDLGPYRQASKSIH 147
Cdd:cd01703 1 IHLDLDCFYAQVEEIRDPSLKSKPLGIQQKYIVVTCNYEARRLGVKKLMSIKDAKEICPDLVLVNGEDLTPFRDMSKKVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 148 AVLSRY---GTAERLGMDETYVDCTEEVLrrvrsgayeppappprLVGHRhtarcaVAADTRYRPQDlrarqpdggggdg 224
Cdd:cd01703 81 RLLRSYswnDRVERLGFDENFMDVTEMRL----------------LVASH------IAYEMRERIEN------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 225 gddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaavraETG 304
Cdd:cd01703 126 -----------------------------------------------------------------------------ELG 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 305 FRSSAGIAPNKLLAKLVSGLHKPDDQTIIHP---DQAADFLAPLPVRALPGVGYKTEQLLSERCGAASAADVRRCGQQR- 380
Cdd:cd01703 129 LTCCAGIASNKLLAKLVGSVNKPNQQTTLLPpscADLMDFMDLHDLRKIPGIGYKTAAKLEAHGISSVRDLQEFSNRNRq 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 381 -------------LAEALGDKTAAMLWELAWGCDSSPV-RPTGPPRSITVEDSFKSCASWAAATAV--LRVLAPDLLARL 444
Cdd:cd01703 209 tvgaapsllelllMVKEFGEGIGQRIWKLLFGRDTSPVkPASDFPQQISIEDSYKKCSLEEIREARnkIEELLASLLERM 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 445 R----EEWAENRRRPETLTLKWRHRGS---GWSRTSASSPMPlpagalGQQQQQPAATEAQLVDQLVRASLALLQR---- 513
Cdd:cd01703 289 KqdlqEVKAGDGRRPHTLRLTLRRYTStkkHYNRESKQAPIP------SHVFQKLTGGNEIAARPIEKILMRLFRElvpp 362
|
490
....*....|....*..
gi 1004138820 514 HIREPFNLSLINLGATN 530
Cdd:cd01703 363 KNVKGFNLTLLNVCFTN 379
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1534-1859 |
2.07e-59 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 211.29 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1534 LFTGTGTDAPLMDWLKKYTFPAEGSyRDLDSARQ--RYALLvkRFLANGTTTA--MYYgslhLEPNTVlVDTIERLGQRA 1609
Cdd:cd01298 69 LLRGLADDLPLMEWLKDLIWPLERL-LTEEDVYLgaLLALA--EMIRSGTTTFadMYF----FYPDAV-AEAAEELGIRA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1610 VVGKVSMDRlsPDDYVEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECC 1689
Cdd:cd01298 141 VLGRGIMDL--GTEDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1690 GEVNCVREMHPEyaSDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKV 1769
Cdd:cd01298 219 DEVEESLEKYGK--RPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1770 GLGTD-VAGGISPSMLSAQRMAVVnsrclrAHKLAvsggttanlEMEKDVITFKEALWLATVGGAQALDLADrVGTFEEG 1848
Cdd:cd01298 297 GLGTDgAASNNNLDMFEEMRLAAL------LQKLA---------HGDPTALPAEEALEMATIGGAKALGLDE-IGSLEVG 360
|
330
....*....|.
gi 1004138820 1849 KEFDALLVDTN 1859
Cdd:cd01298 361 KKADLILIDLD 371
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
65-529 |
4.77e-56 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 198.83 E-value: 4.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 65 RVILHFDCDCFYAQVEEVRNPALRDVPLGV---TQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGeDLGPYRQ 141
Cdd:COG0389 1 RRILHVDMDAFYASVEQRDRPELRGKPVAVggdNNRGVVAAASYEARAFGVRSGMPLFQARRLCPDLVVLPP-DFELYRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 142 ASKSIHAVLSRYgTA--ERLGMDETYVDCTEevlrrvrsgayeppapPPRLVGHRHtarcAVAADTRyrpQDLRARqpdg 219
Cdd:COG0389 80 VSRRVMAILERY-TPlvEPLSIDEAFLDVTG----------------SARLFGSAE----AIARRIR---RRIRRE---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 220 gggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaav 299
Cdd:COG0389 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 300 raeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCGQQ 379
Cdd:COG0389 132 ---TGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWGVGPKTAEKL-ARLGIRTIGDLAALPRA 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 380 RLAEALGdKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREEwaenRRRPETL 458
Cdd:COG0389 208 ELRRRFG-KVGERLYRLARGIDPRPVEPRRPRKSIGVERTFgEDLTDLEELEAALRRLAERLAERLRRQ----GLGARTV 282
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 459 TLKWRHrgSGWSRTSASSPMPLPAGALgqqqqqpaateaqlvDQLVRASLALLQRHIREPFNLSLINLGAT 529
Cdd:COG0389 283 TVKLRT--SDFRTTTRSRTLPEPTDDT---------------AELLRAARELLERIYRPGRPVRLLGVRLS 336
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
68-463 |
1.82e-52 |
|
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: 188.50 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 68 LHFDCDCFYAQVEEVRNPALRDVPLGV---TQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGeDLGPYRQASK 144
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVggsSDRGVVSTASYEARKFGVRSAMPIFQAKKLCPNLIFVPP-RFDKYREVSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 145 SIHAVLSRY-GTAERLGMDETYVDCTEevlrrvrsgaYEPPAPPPRLVGHRhtarcavaadtryrpqdLRARqpdggggd 223
Cdd:cd03586 80 QIMEILREYtPLVEPLSIDEAYLDVTD----------YVRLFGSATEIAKE-----------------IRAR-------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 224 ggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaIgsmvaaearaavRAET 303
Cdd:cd03586 125 ---------------------------------------------------------------I------------REET 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 304 GFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSERcGAASAADVRRCGQQRLAE 383
Cdd:cd03586 130 GLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPGVGKVTAEKLKEL-GIKTIGDLAKLDVELLKK 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 384 ALGdKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREEwaenRRRPETLTLKW 462
Cdd:cd03586 209 LFG-KSGRRLYELARGIDNRPVEPDRERKSIGVERTFsEDLTDPEELLEELLELAEELAERLRKR----GLKGRTVTVKL 283
|
.
gi 1004138820 463 R 463
Cdd:cd03586 284 K 284
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
69-530 |
2.92e-51 |
|
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: 185.98 E-value: 2.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 69 HFDCDCFYAQVEEVRNPALRDVPLGVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLV------SGED------- 135
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAVVQWNSIIAVSYAARAFGVTRFMTIDEAKKKCPDLILAhvatykKGEDeadyhen 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 136 ---------LGPYRQASKSIHAVLSRYGTA-ERLGMDETYVDCTEEVLRRVRSGAYEPpappprlvghrhtarcavaadt 205
Cdd:cd01702 82 psparhkvsLDPYRRASRKILNILKRFGDVvEKASIDEAYLDLGSRIVEEIRQQVYDE---------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 206 ryrpqdlrarqpdggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetll 285
Cdd:cd01702 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 286 aigsmvaaearaavraeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSERC 365
Cdd:cd01702 140 -----------------LGYTCSAGIAHNKMLAKLASGMNKPNAQTILRNDAVASFLSSLPITSIRGLGGKLGEEIIDLL 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 366 GAASAADVR--RCGQQRLAEALGDKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF--KSCASWAAATAVLRVLAPDLL 441
Cdd:cd01702 203 GLPTEGDVAgfRSSESDLQEHFGEKLGEWLYNLLRGIDHEPVKPRPLPKSMGSSKNFpgKTALSTEDVQHWLLVLASELN 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 442 ARLREEWAENRRRPETLTLKWRHRGSGwSRTSASSPMPLPAgalgqqqqqpaateaqlVDQLVRASLALLQ----RHIRE 517
Cdd:cd01702 283 SRLEDDRYENNRRPKTLVLSLRQRGDG-VRRSRSCALPRYD-----------------AQKIVKDAFKLIKaineEGLGL 344
|
490
....*....|....*
gi 1004138820 518 PFN--LSLINLGATN 530
Cdd:cd01702 345 AWNypLTLLSLSFTK 359
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
72-461 |
5.16e-48 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 175.69 E-value: 5.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 72 CDCFYAQVEEVRNPALRDVPL---------GVtqkylIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGeDLGPYRQA 142
Cdd:PRK02406 1 MDCFYAAVEMRDNPELRGKPVavggspgrrGV-----ISTCNYEARKFGVRSAMPTAQALKLCPDLIFVPG-RFDVYKEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 143 SKSIHAVLSRYgTA--ERLGMDETYVDCTEevlrrvrSGAYEPPAppprlvghrhTArcaVAadtryrpQDLRArqpdgg 220
Cdd:PRK02406 75 SRQIREIFRRY-TDliEPLSLDEAYLDVTD-------NKLCIGSA----------TL---IA-------QEIRQ------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 221 ggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpseDSWETllaigsmvaaearaavr 300
Cdd:PRK02406 121 ----------------------------------------------------------DIFEE----------------- 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 301 aeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCGQQR 380
Cdd:PRK02406 126 --LGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPGVGKVTAEKL-HALGIYTCADLQKYDLAE 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 381 LAEALGdKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREewAENRRRPETLT 459
Cdd:PRK02406 203 LIRHFG-KFGRRLYERARGIDERPVKPDRERKSVGVERTFaEDLYDLEACLAELPRLAEKLERRLER--AKPDKRIKTVG 279
|
..
gi 1004138820 460 LK 461
Cdd:PRK02406 280 VK 281
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1534-1859 |
1.51e-45 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 171.72 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1534 LFTGTGTDAPLMDWLKKYTFPAEGSyrdLDSARQRYA--LLVKRFLANGTTTAMYYGSL-HLEPNtvlVDTIERLGQRAV 1610
Cdd:PRK07228 69 LFRGIADDLELLDWLKDRIWPLEAA---HDAESMYYSalLGIGELIESGTTTIVDMESVhHTDSA---FEAAGESGIRAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1611 VGKVSMDRL--SPDDYVEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISEC 1688
Cdd:PRK07228 143 LGKVMMDYGddVPEGLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASEN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1689 CGEVNCVREMHPEyaSDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLK 1768
Cdd:PRK07228 223 RGEIETVEEETGM--RNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGIN 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1769 VGLGTDVAggisP-----SMLSAQRMAVVnsrclrAHKLAVSGGTtanlemekdVITFKEALWLATVGGAQALDLADRVG 1843
Cdd:PRK07228 301 VALGADGA----PcnntlDPFTEMRQAAL------IQKVDRLGPT---------AMPARTVFEMATLGGAKAAGFEDEIG 361
|
330
....*....|....*.
gi 1004138820 1844 TFEEGKEFDALLVDTN 1859
Cdd:PRK07228 362 SLEEGKKADLAILDLD 377
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
68-481 |
8.35e-36 |
|
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: 140.19 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 68 LHFDCDCFYAQVEEVRNPALRDVPLGVTQKY----LIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSgEDLGPYRQAS 143
Cdd:cd00424 1 LHIDFDNFFASVEQLARPELKGRPVVVVPFNsdstCVIACSYEARKYGVKRGMPVREARKMCPNLILVP-ARLDLYRRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 144 KSIHAVLSRYG-TAERLGMDETYVDcteevlrrvRSGAYEPPAPPPRlvghrhtarcaVAADTRyrpQDLRARqpdgggg 222
Cdd:cd00424 80 ERLLSELEEVApLVEVASIDELFLD---------LTGSARLLGLGSE-----------VALRIK---RHIAEQ------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 223 dggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaIGsmvaaearaavrae 302
Cdd:cd00424 130 ----------------------------------------------------------------LG-------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 303 tGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCGQQRLA 382
Cdd:cd00424 132 -GITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAKRL-EAVGINPIGDLLAASPDALL 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 383 EALGDKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSFKSCAS-WAAATAVLRVLAPDLLARLREEwaenRRRPETLTLK 461
Cdd:cd00424 210 ALWGGVSGERLWYALRGIDDEPLSPPRPRKSFSHERVLPRDSRnAEDARPLLRLLLEKLARRLRRD----GRGATRLRLW 285
|
410 420
....*....|....*....|....
gi 1004138820 462 WRHRGSGWS----RTSASSPMPLP 481
Cdd:cd00424 286 LRTVDGRWSghadIPSRSAPRPIS 309
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1514-1859 |
1.83e-33 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 135.70 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1514 DAAGQRSISSFA---TRQPPAayLFTGTGTDAPLMDWLKKYTFPAEGSYRDLDSARQRYALLVKrFLANGTTT--AMYYg 1588
Cdd:PRK08393 46 DASGSVVSPGFInahTHSPMV--LLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTfvDMYF- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1589 slHLEPntvLVDTIERLGQRAVVGKVSMDRLSPddyvEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMR 1668
Cdd:PRK08393 122 --HMEE---VAKATLEVGLRGYLSYGMVDLGDE----EKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1669 GLAELARKYGTHIQSHISECCGEVNCVREMHPEyaSDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLS 1748
Cdd:PRK08393 193 WVREKAREWNKLITIHLSETMDEIKQIREKYGK--SPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPAS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1749 NFFFGDAFFRVNHALSLGLKVGLGTD-VAGGISPSMLSAQRMAVVnsrclrAHKLAVSGGTTANLEmekdvitfkEALWL 1827
Cdd:PRK08393 271 NMKLGSGVMPLRKLLNAGVNVALGTDgAASNNNLDMLREMKLAAL------LHKVHNLDPTIADAE---------TVFRM 335
|
330 340 350
....*....|....*....|....*....|..
gi 1004138820 1828 ATVGGAQALDLadRVGTFEEGKEFDALLVDTN 1859
Cdd:PRK08393 336 ATQNGAKALGL--KAGVIKEGYLADIAVIDFN 365
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1561-1901 |
2.59e-33 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 132.63 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1561 DLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVDTIERL--GQRAVVGKVSMDRLSPDDYVEQLEDGLRDAEAF 1638
Cdd:pfam01979 24 PPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALLEAAEELplGLRFLGPGCSLDTDGELEGRKALREKLKAGAEF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1639 VQYTLGrkcSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGEV-NCV-----REMHPEYASDAAvfEEM 1712
Cdd:pfam01979 104 IKGMAD---GVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVeDAIaafggGIEHGTHLEVAE--SGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1713 GLLTSRTVMAHGTLLSDDDIRHLASR--GTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAG-GISPSMLSAQRM 1789
Cdd:pfam01979 179 LLDIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1790 AVVNSrclrahklavsggttanlEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTNLggtdgpfdv 1869
Cdd:pfam01979 259 ALELQ------------------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------- 311
|
330 340 350
....*....|....*....|....*....|..
gi 1004138820 1870 fpgeddlerFEKFINLGDDRNLLEVYVQGVCV 1901
Cdd:pfam01979 312 ---------LAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
947-1072 |
7.46e-32 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 122.30 E-value: 7.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 947 VDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFV-AVSYEARAAGIRCGDgvgsggraaiaylknmgavSVAEARRRCPG 1025
Cdd:pfam00817 1 IDMDAFFASVELLRDPELKGKPVAVGGGNGRGIVaAASYEARKYGVRSGM-------------------PVFEAKKLCPN 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1004138820 1026 LVVRPMRTDRYRQVAEQVHSLLRSFSPDgEVEKASYDDFYLDVTRHC 1072
Cdd:pfam00817 62 LIVVPPDLELYRRASRKIFEILRRFSTP-KVEQASIDEAFLDLTGLE 107
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
942-1069 |
1.51e-30 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 124.87 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFV-AVSYEARAAGIRCGdgvgsggraaiaylknMgavSVAEAR 1020
Cdd:COG0389 1 RRILHVDMDAFYASVEQRDRPELRGKPVAVGGDNNRGVVaAASYEARAFGVRSG----------------M---PLFQAR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1004138820 1021 RRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:COG0389 62 RLCPDLVVLPPDFELYRDVSRRVMAILERYTP--LVEPLSIDEAFLDVT 108
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
1534-1857 |
1.77e-30 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 126.95 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1534 LFTGTGTDAPLMDWLKKYTFPAEGSYRDLDSARQRYALLVKRFLANGTTTA--MYYgslHLEpntVLVDTIERLGQRAVV 1611
Cdd:PRK09045 79 LLRGLADDLPLMTWLQDHIWPAEGAWVSEEFVRDGTLLAIAEMLRGGTTCFndMYF---FPE---AAAEAAHQAGMRAQI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1612 GKVSMD-----RLSPDDYveqLEDGLrdaEAFVQYtlgRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHIS 1686
Cdd:PRK09045 153 GMPVLDfptawASDADEY---LAKGL---ELHDQW---RHHPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLH 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1687 ECCGEV-NCVRE--MHPeyasdAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHAL 1763
Cdd:PRK09045 224 ETAQEIaDSLKQhgQRP-----LARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1764 SLGLKVGLGTD-VAGGISPSMLSAQRMAvvnsrCLRAHklAVSGGTTAnlemekdvITFKEALWLATVGGAQALDLADRV 1842
Cdd:PRK09045 299 QAGVNVALGTDgAASNNDLDLFGEMRTA-----ALLAK--AVAGDATA--------LPAHTALRMATLNGARALGLDDEI 363
|
330
....*....|....*
gi 1004138820 1843 GTFEEGKEFDALLVD 1857
Cdd:PRK09045 364 GSLEPGKQADLVAVD 378
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
945-1069 |
6.55e-29 |
|
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: 119.93 E-value: 6.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 945 LHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFVA-VSYEARAAGIRcgdgvgSGgraaiaylknMgavSVAEARRRC 1023
Cdd:cd03586 1 IHIDMDAFYASVEQRDNPELKGKPVAVGGSSDRGVVStASYEARKFGVR------SA----------M---PIFQAKKLC 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1004138820 1024 PGLVVRPMRTDRYRQVAEQVHSLLRSFSPDgeVEKASYDDFYLDVT 1069
Cdd:cd03586 62 PNLIFVPPRFDKYREVSRQIMEILREYTPL--VEPLSIDEAYLDVT 105
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
71-170 |
2.04e-27 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 109.59 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 71 DCDCFYAQVEEVRNPALRDVPLGVTQKY---LIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSgEDLGPYRQASKSIH 147
Cdd:pfam00817 2 DMDAFFASVELLRDPELKGKPVAVGGGNgrgIVAAASYEARKYGVRSGMPVFEAKKLCPNLIVVP-PDLELYRRASRKIF 80
|
90 100
....*....|....*....|....*
gi 1004138820 148 AVLSRYGTA--ERLGMDETYVDCTE 170
Cdd:pfam00817 81 EILRRFSTPkvEQASIDEAFLDLTG 105
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1514-1859 |
2.69e-27 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 117.16 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1514 DAAGQRSISSFA-TRQPPAAYLFTGTGTDAPLMDWLKKYTFPAEGSYRDLDS-ARQRYALLvkRFLANGTTT--AMYYgs 1589
Cdd:PRK06038 47 DAKGSVVMPGLVnTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLTAEDVyAGSLLACL--EMIKSGTTSfaDMYF-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1590 lHLEPntvLVDTIERLGQRAVVGKVSMDRLSPDDYVEQLEDGLRdaeaFVQYTLGRKCSRIQPCITPRFIPTCTPELMRG 1669
Cdd:PRK06038 123 -YMDE---VAKAVEESGLRAALSYGMIDLGDDEKGEAELKEGKR----FVKEWHGAADGRIKVMYGPHAPYTCSEEFLSK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1670 LAELARKYGTHIQSHISECCGEVNCVREMHPEyaSDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSN 1749
Cdd:PRK06038 195 VKKLANKDGVGIHIHVLETEAELNQMKEQYGM--CSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1750 FFFGDAFFRVNHALSLGLKVGLGTD-VAGGISPSMLSAQRMAVVnsrclrAHKLAVsggttanleMEKDVITFKEALWLA 1828
Cdd:PRK06038 273 MKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAAL------LHKVNT---------MDPTALPARQVLEMA 337
|
330 340 350
....*....|....*....|....*....|.
gi 1004138820 1829 TVGGAQALDLadRVGTFEEGKEFDALLVDTN 1859
Cdd:PRK06038 338 TVNGAKALGI--NTGMLKEGYLADIIIVDMN 366
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1525-1852 |
9.84e-27 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 116.10 E-value: 9.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1525 ATRQPPAAylftgtgTDAPLMDWLKK-YTFPAEGSYRDLD-SARQRYALLvkrfLANGTTTAMYYgsLHLEPN---TVLV 1599
Cdd:PRK08203 72 LTRALPAA-------QDAELFPWLTTlYPVWARLTPEMVRvATQTALAEL----LLSGCTTSSDH--HYLFPNglrDALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1600 DTIE---RLGQRAVVGKVSMDR------LSPDDYVEQLEDGLRDAEAFV-QYTLGRKCSRIQ----PCiTPrFipTCTPE 1665
Cdd:PRK08203 139 DQIEaarEIGMRFHATRGSMSLgesdggLPPDSVVEDEDAILADSQRLIdRYHDPGPGAMLRialaPC-SP-F--SVSRE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1666 LMRGLAELARKYGTHIQSHISECCGEVNCVREMH---P-EYAsdaavfEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTA 1741
Cdd:PRK08203 215 LMRESAALARRLGVRLHTHLAETLDEEAFCLERFgmrPvDYL------EDLGWLGPDVWLAHCVHLDDAEIARLARTGTG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1742 VSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTD-VAGGISPSMLSAQRMAVVNSRclrahklaVSGGTTAnlemekdvIT 1820
Cdd:PRK08203 289 VAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQALLLQR--------LRYGPDA--------MT 352
|
330 340 350
....*....|....*....|....*....|..
gi 1004138820 1821 FKEALWLATVGGAQALDLADrVGTFEEGKEFD 1852
Cdd:PRK08203 353 AREALEWATLGGARVLGRDD-IGSLAPGKLAD 383
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
1531-1910 |
2.64e-23 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 105.09 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1531 AAYLFTGTGTDAPLMDWLKKYTFPAEGSYR-DLDSARQRYALlvKRFLANGTTT--AMYygslhlEPNTVLVDTIERlgq 1607
Cdd:PRK06687 68 AMTGLRGIRDDSNLHEWLNDYIWPAESEFTpDMTTNAVKEAL--TEMLQSGTTTfnDMY------NPNGVDIQQIYQ--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1608 raVVGKVSMD-RLSPDDY---VEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQS 1683
Cdd:PRK06687 137 --VVKTSKMRcYFSPTLFsseTETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1684 HISECCGEVNCVREMHPEyaSDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHAL 1763
Cdd:PRK06687 215 HVAETKEESGIILKRYGK--RPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1764 SLGLKVGLGTD-VAGGISPSMLSAQRMAVVnsrcLRAHKlavSGGTTAnlemekdvITFKEALWLATVGGAQALDLADRV 1842
Cdd:PRK06687 293 KAGVAVGIATDsVASNNNLDMFEEGRTAAL----LQKMK---SGDASQ--------FPIETALKVLTIEGAKALGMENQI 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004138820 1843 GTFEEGKEFDALLVDTNlggtdGPFDVFPGEDDLERFEKFINLGDdrnLLEVYVQG-VCVKRGNVFELE 1910
Cdd:PRK06687 358 GSLEVGKQADFLVIQPQ-----GKIHLQPQENMLSHLVYAVKSSD---VDDVYIAGeQVVKQGQVLTVE 418
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
942-1069 |
2.72e-23 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 104.73 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVT---QFNSGGFVAVSYEARAAGIRCgdgvgsggraaiaylknmgAVSVAE 1018
Cdd:PRK01810 5 RVIFHVDMNSFFASVEIAYDPSLQGKPLAVAgneKERKGIIVTCSYEARAYGIRT-------------------TMPLWE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1019 ARRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:PRK01810 66 AKRLCPQLIVRRPNFDRYREASRQMFQILSEFTP--LVQPVSIDEGYLDIT 114
|
|
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
64-468 |
3.90e-22 |
|
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: 101.24 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 64 KRVILHFDCDCFYAQVEEVRNPALRDVPLGVTQ-KYL---IVTSNYPARAAGVTKLMGIRDAQARCPGLVLVsGEDLGPY 139
Cdd:cd01701 46 QRIIMHVDFDCFFVSVSIRNRPDLKGKPVAVCHgKGPnseIASCNYEARSYGIKNGMWVGQAKKLCPQLVTL-PYDFEAY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 140 RQASKSIHAVLSRYGTA-ERLGMDETYVDCTEEVlrrvrSGAYEPPAPpprlvghrhtarcaVAADTRyrpQDLRARqpd 218
Cdd:cd01701 125 EEVSLTFYEILASYTDNiEAVSCDEALIDITSLL-----EETYELPEE--------------LAEAIR---NEIRET--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 219 ggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaa 298
Cdd:cd01701 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 299 vraeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSERCGaasaadvRRCGQ 378
Cdd:cd01701 180 ----TGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFG-------DTCGG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 379 QRLAEA--------LGDKTAAMLWELAWGCDSSPVRPTGPPRSITVEdsfkscASWAAAT-------AVLRVLAPDLLAR 443
Cdd:cd01701 249 LELRSKtkeklqkvLGPKTGEKLYDYCRGIDDRPVTGEKERKSVSAE------INYGIRFtnvddveQFLQRLSEELSKR 322
|
410 420
....*....|....*....|....*
gi 1004138820 444 LREEWAENRRRpeTLTLKWRHRGSG 468
Cdd:cd01701 323 LEESNVTGRQI--TLKLMKRAPGAP 345
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
65-420 |
8.78e-22 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 100.78 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 65 RVILHFDCDCFYAQVEEVRNPALRDVPL---GVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVsgedLGP--- 138
Cdd:PRK03348 5 RWVLHLDMDAFFASVEQLTRPTLRGRPVlvgGLGGRGVVAGASYEARVFGARSAMPMHQARRLVGNGAVV----LPPrfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 139 -YRQASKSIHAVL-SRYGTAERLGMDETYVDcteevlrrvrsgayeppapPPRLVGhrhtarcAVAADTRYRPQDLRARq 216
Cdd:PRK03348 81 vYRAASRRVFDTLrELSPVVEQLSFDEAFVE-------------------PAELAG-------ASAEEVEAFAERLRAR- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 217 pdggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaear 296
Cdd:PRK03348 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 297 aaVRAETGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSeRCGAASAADVRRC 376
Cdd:PRK03348 134 --VREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEEKLH-RLGIETIGDLAAL 210
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1004138820 377 GQQRLAEALGDKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF 420
Cdd:PRK03348 211 SEAEVANLLGATVGPALHRLARGIDDRPVAERAEAKQISAESTF 254
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
945-1077 |
1.06e-21 |
|
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: 98.97 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 945 LHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGF--VAVSYEARAAGIRCGDGVgsggraaiaylknmgavsvAEARRR 1022
Cdd:cd00424 1 LHIDFDNFFASVEQLARPELKGRPVVVVPFNSDSTcvIACSYEARKYGVKRGMPV-------------------REARKM 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1004138820 1023 CPGLVVRPMRTDRYRQVAEQVHSLLRSFSPDGEVekASYDDFYLDVTRHCVDARP 1077
Cdd:cd00424 62 CPNLILVPARLDLYRRLSERLLSELEEVAPLVEV--ASIDELFLDLTGSARLLGL 114
|
|
| PRK01810 |
PRK01810 |
DNA polymerase IV; Validated |
65-446 |
1.69e-21 |
|
DNA polymerase IV; Validated
Pssm-ID: 179337 [Multi-domain] Cd Length: 407 Bit Score: 99.33 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 65 RVILHFDCDCFYAQVEEVRNPALRDVPLGVT-----QKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSgEDLGPY 139
Cdd:PRK01810 5 RVIFHVDMNSFFASVEIAYDPSLQGKPLAVAgnekeRKGIIVTCSYEARAYGIRTTMPLWEAKRLCPQLIVRR-PNFDRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 140 RQASKSIHAVLSRYG-TAERLGMDETYVDCTEevlrrvrsgayEPPAPPPrlvghrhtarCAVAADTRYRpqdlrarqpd 218
Cdd:PRK01810 84 REASRQMFQILSEFTpLVQPVSIDEGYLDITD-----------CYALGSP----------LEIAKMIQQR---------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 219 ggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedSWETLLaigsmvaaearaa 298
Cdd:PRK01810 133 -------------------------------------------------------------LLTELQ------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 299 vraetgFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSErCGAASAADVRRCGQ 378
Cdd:PRK01810 139 ------LPCSIGIAPNKFLAKMASDMKKPLGITVLRKRDVPEMLWPLPVGEMHGIGEKTAEKLKD-IGIQTIGDLAKADE 211
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004138820 379 QRLAEALGdKTAAMLWELAWGCDSSPVRPTgpprsiTVEDsFKSCAS----------WAAATAVLRVLAPDLLARLRE 446
Cdd:PRK01810 212 HILRAKLG-INGVRLQRRANGIDDRPVDPE------AIYQ-FKSVGNsttlshdmdeEKELLDVLRRLSKSVSKRLQK 281
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
945-1069 |
1.97e-20 |
|
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: 95.61 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 945 LHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSggFVAVSYEARAAGIRcgdgvgsggraaiaylKNMgavSVAEARRRCP 1024
Cdd:cd01703 1 IHLDLDCFYAQVEEIRDPSLKSKPLGIQQKYI--VVTCNYEARRLGVK----------------KLM---SIKDAKEICP 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1004138820 1025 GLV-VRPMRTDRYRQVAEQVHSLLRSFSPDGEVEKASYDDFYLDVT 1069
Cdd:cd01703 60 DLVlVNGEDLTPFRDMSKKVYRLLRSYSWNDRVERLGFDENFMDVT 105
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
1546-1868 |
2.24e-20 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 97.03 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1546 DWLKKYTFPA---EGSYRDLDSARQ-----RYALlvKRFLANGTTTAMYYGSL-------HLEPNTVLVDTIERLGQRAV 1610
Cdd:PRK06151 80 GWAKGRVWSRdyvEAGRREMYTPEElafqkRYAF--AQLLRNGITTAMPIASLfyrqwaeTYAEFAAAAEAAGRLGLRVY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1611 VGKVSMD---------RLSPDDYVEQLEDGLRDAEAFVQYTLGRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHI 1681
Cdd:PRK06151 158 LGPAYRSggsvleadgSLEVVFDEARGLAGLEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1682 QSHISECCGEVNCVREMHPEYASDaaVFEEMGLLTSRTVMAHGTLLSD---------DDIRHLASRGTAVSHCPLSNFFF 1752
Cdd:PRK06151 238 RLHCAQGVLEVETVRRLHGTTPLE--WLADVGLLGPRLLIPHATYISGsprlnysggDDLALLAEHGVSIVHCPLVSARH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1753 GDAFFRVNHALSLGLKVGLGTDVAggiSPSMLSAQRMAVVNSRclrahklAVSGGTTAnlemekdvITFKEALWLATVGG 1832
Cdd:PRK06151 316 GSALNSFDRYREAGINLALGTDTF---PPDMVMNMRVGLILGR-------VVEGDLDA--------ASAADLFDAATLGG 377
|
330 340 350
....*....|....*....|....*....|....*.
gi 1004138820 1833 AQALDLADrVGTFEEGKEFDALLVDTNlGGTDGPFD 1868
Cdd:PRK06151 378 ARALGRDD-LGRLAPGAKADIVVFDLD-GLHMGPVF 411
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1534-1857 |
4.08e-20 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 95.51 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1534 LFTGTGTDAPLMDWLKKYTFPAEGSYR-DLDSARQRYALLvkRFLANGTTT-AMYYGSLHLEPNTVLvDTIERLGQRAVV 1611
Cdd:PRK15493 72 LLRGIGDDMLLQPWLETRIWPLESQFTpELAVASTELGLL--EMVKSGTTSfSDMFNPIGVDQDAIM-ETVSRSGMRAAV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1612 GKVSMDRLSPDDYVEQLEDglrdAEAFVQYTLgRKCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGE 1691
Cdd:PRK15493 149 SRTLFSFGTKEDEKKAIEE----AEKYVKRYY-NESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETERE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1692 VncvREMHPEYASDAAVF-EEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVG 1770
Cdd:PRK15493 224 V---RDIEAQYGKRPVEYaASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1771 LGTD-VAGGISPSMLSAQRMAVVNSRclrahklavsggttaNLEMEKDVITFKEALWLATVGGAQALDLaDRVGTFEEGK 1849
Cdd:PRK15493 301 IATDsVASNNNLDMFEEMRIATLLQK---------------GIHQDATALPVETALTLATKGAAEVIGM-KQTGSLEVGK 364
|
....*...
gi 1004138820 1850 EFDALLVD 1857
Cdd:PRK15493 365 CADFITID 372
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
67-461 |
6.66e-20 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 94.61 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 67 ILHFDCDCFYAQVEEVRNPALRDVPL--GVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGeDLGPYRQASK 144
Cdd:PRK02794 38 IAHIDCDAFYASVEKRDNPELRDKPViiGGGKRGVVSTACYIARIHGVRSAMPMFKALKLCPDAVVIKP-DMEKYVRVGR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 145 SIHAVLSRYGTA-ERLGMDETYVDCTE-EVLRRvrsgayeppAPPPRLVghrhtARCAvaadtryrpqdlrarqpdgggg 222
Cdd:PRK02794 117 EVRAMMQALTPLvEPLSIDEAFLDLSGtERLHG---------APPAVVL-----ARFA---------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 223 dggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggRPSEDswetllaigsmvaaearaavraE 302
Cdd:PRK02794 161 ----------------------------------------------------RRVER----------------------E 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 303 TGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCGQQRLA 382
Cdd:PRK02794 167 IGITVSVGLSYNKFLAKIASDLDKPRGFSVIGRAEALAFLAPKPVGIIWGVGPATAARL-ARDGIRTIGDLQRADEADLM 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 383 EALGDkTAAMLWELAWGCDSSPVRPTGPPRSITVEDSFKS-CASWAAATAVLRVLAPDLLARLREEWAENRrrpeTLTLK 461
Cdd:PRK02794 246 RRFGS-MGLRLWRLARGIDDRKVSPDREAKSVSAETTFETdLSDFEDLEPILWRLSEKVSRRLKAAGLAGR----TVTLK 320
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1535-1857 |
1.02e-19 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 94.18 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1535 FTGTGTDAPLMDWLKKyTFpaegsyrDLDSARQRY-----ALL-VKRFLANGTTT--AMYYGSlhlepnTVLVDTIERLG 1606
Cdd:PRK06380 68 SKGLFDDVDLEEFLMK-TF-------KYDSKRTREgiynsAKLgMYEMINSGITAfvDLYYSE------DIIAKAAEELG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1607 QRAVVGKVSMDrlspDDYVEQLEDGLRDAEAFVQYTLGRKcsRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHIS 1686
Cdd:PRK06380 134 IRAFLSWAVLD----EEITTQKGDPLNNAENFIREHRNEE--LVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1687 ECCGEVNCVREMHPEYASDAavFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGD-AFFRVNHALSL 1765
Cdd:PRK06380 208 ETRKEVYDHVKRTGERPVEH--LEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1766 GLKVGLGTDVAGG-ISPSMLSAQRMAVVnsrclrahklavsggTTANLEMEKDVITFKEALWLATVGGAQALDLadRVGT 1844
Cdd:PRK06380 286 GINVTIGTDSNGSnNSLDMFEAMKFSAL---------------SVKNERWDASIIKAQEILDFATINAAKALEL--NAGS 348
|
330
....*....|...
gi 1004138820 1845 FEEGKEFDALLVD 1857
Cdd:PRK06380 349 IEVGKLADLVILD 361
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
950-1069 |
4.11e-19 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 90.95 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 950 DCFYCQVERLDDPSLMGVPLAVtqfnsGGFV-------AVSYEARAAGIRcgdgvgSggraaiaylknmgAVSVAEARRR 1022
Cdd:PRK02406 2 DCFYAAVEMRDNPELRGKPVAV-----GGSPgrrgvisTCNYEARKFGVR------S-------------AMPTAQALKL 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1004138820 1023 CPGLVVRPMRTDRYRQVAEQVHSLLRSFSPDgeVEKASYDDFYLDVT 1069
Cdd:PRK02406 58 CPDLIFVPGRFDVYKEVSRQIREIFRRYTDL--IEPLSLDEAYLDVT 102
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
67-481 |
5.75e-19 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 91.59 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 67 ILHFDCDCFYAQVEEVRNPALRDVPLGVTQKYLIVTSnYPARAAGVTKLMGIRDAQARCPGLVLVSGEdLGPYRQASKSI 146
Cdd:PRK03858 6 ILHADLDSFYASVEQRDDPALRGRPVIVGGGVVLAAS-YEAKAYGVRTAMGGRQARRLCPQAVVVPPR-MSAYSRASKAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 147 HAVLsRYGT--AERLGMDETYVDCTEevLRRVrSGayeppapPPRLVGHRhtarcavaadtryrpqdLRARqpdggggdg 224
Cdd:PRK03858 84 FEVF-RDTTplVEGLSIDEAFLDVGG--LRRI-SG-------TPVQIAAR-----------------LRRR--------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 225 gddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaaVRAETG 304
Cdd:PRK03858 127 --------------------------------------------------------------------------VREEVG 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 305 FRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSERcGAASAADVRRCGQQRLAEA 384
Cdd:PRK03858 133 LPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFLHPLPVRRLWGVGPVTAAKLRAH-GITTVGDVAELPESALVSL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 385 LGDKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREEwaenRRRPETLTLkwR 463
Cdd:PRK03858 212 LGPAAGRHLHALAHNRDPRRVETGRRRRSVGAQRALgRGPNSPAEVDAVVVALVDRVARRMRAA----GRTGRTVVL--R 285
|
410
....*....|....*...
gi 1004138820 464 HRGSGWSRTSASSPMPLP 481
Cdd:PRK03858 286 LRFDDFTRATRSHTLPRP 303
|
|
| PolY_Pol_eta |
cd01702 |
DNA Polymerase eta; Pol eta, also called Rad30A, is a translesion synthesis (TLS) polymerase. ... |
946-1069 |
1.66e-18 |
|
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: 89.68 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 946 HVDVDCFYCQVERLDDPSLMGVPLAVTQFNSggFVAVSYEARAAGIRCGDgvgsggraaiaylknmgavSVAEARRRCPG 1025
Cdd:cd01702 2 HIDMDAFFAQVEQVRLGLLRNDPVAVVQWNS--IIAVSYAARAFGVTRFM-------------------TIDEAKKKCPD 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004138820 1026 LV---VRPMR--------------------TDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:cd01702 61 LIlahVATYKkgedeadyhenpsparhkvsLDPYRRASRKILNILKRFGD--VVEKASIDEAYLDLG 125
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1662-1904 |
8.49e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 88.52 E-value: 8.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1662 CTPELMRGLAELARKYGTHIQSHISeccgevncvreMHPEYASDAAV--FEEMGLLTSRTVMAHGTLLSDDDIRHLASRG 1739
Cdd:PRK08204 198 SSWEVARADFRLARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1740 TAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGGISPSMLSAQRMAV------VNSRCLRAHKLAVsggttanle 1813
Cdd:PRK08204 267 GSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRFALqaerarDNAVHLREGGMPP--------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1814 mEKDVITFKEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTnlggTDgpFDVFPGEDDlerFEKFINLGDDRNLLE 1893
Cdd:PRK08204 338 -PRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDA----TD--LNLAPVHDP---VGAVVQSAHPGNVDS 407
|
250
....*....|.
gi 1004138820 1894 VYVQGVCVKRG 1904
Cdd:PRK08204 408 VMVAGRAVKRN 418
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
1539-1859 |
6.04e-17 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 85.89 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1539 GTDAPLMDWLKKYTFPAEGSYrDLDSARQRYALLVKRFLANGTTTA-----MYYGSLHLEPNTVLVDTIERLGQRAVV-- 1611
Cdd:PRK12393 79 GINQSLTAWLAAVPYRFRARF-DEDLFRLAARIGLVELLRSGCTTVadhhyLYHPGMPFDTGDILFDEAEALGMRFVLcr 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1612 -GKVSMDRLSPDDYV----EQLEDGLRDAEAFVQ-YTLGRKCSRIQPCITPRFIP-TCTPELMRGLAELARKYGTHIQSH 1684
Cdd:PRK12393 158 gGATQTRGDHPGLPTalrpETLDQMLADVERLVSrYHDASPDSLRRVVVAPTTPTfSLPPELLREVARAARGMGLRLHSH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1685 ISECCGEVNCVREMhpeYASDAAVF-EEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHAL 1763
Cdd:PRK12393 238 LSETVDYVDFCREK---YGMTPVQFvAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAME 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1764 SLGLKVGLGTD-VAGGISPSMLSAQRMAVVNSRclrahklAVSGGTTANLEmekDVITfkealWlATVGGAQALDLaDRV 1842
Cdd:PRK12393 315 AAGVPVSLGVDgAASNESADMLSEAHAAWLLHR-------AEGGADATTVE---DVVH-----W-GTAGGARVLGL-DAI 377
|
330
....*....|....*..
gi 1004138820 1843 GTFEEGKEFDALLVDTN 1859
Cdd:PRK12393 378 GTLAVGQAADLAIYDLD 394
|
|
| DinP |
COG0389 |
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination ... |
1286-1458 |
1.55e-16 |
|
Nucleotidyltransferase/DNA polymerase DinP involved in DNA repair [Replication, recombination and repair];
Pssm-ID: 440158 [Multi-domain] Cd Length: 336 Bit Score: 83.27 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1286 VQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP--------TLAR---KT 1354
Cdd:COG0389 118 EAIARRIRRRIRRETGLTVSVGIAPNKFLAKIASDLAKPDGLTVIPPGEVAAFLAPLPVEKLWgvgpktaeKLARlgiRT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1355 GAsvvaalgggglvgDLSAFSRAQLVARFGAQLGGLLA------DLPdggpappaaaaapgggggamggsVRERGPQKSI 1428
Cdd:COG0389 198 IG-------------DLAALPRAELRRRFGKVGERLYRlargidPRP-----------------------VEPRRPRKSI 241
|
170 180 190
....*....|....*....|....*....|.
gi 1004138820 1429 LVERSFPA-ITRFGGVKDALVPMVGALWERL 1458
Cdd:COG0389 242 GVERTFGEdLTDLEELEAALRRLAERLAERL 272
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
942-1069 |
2.13e-16 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 82.84 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFVAV-SYEARAAGIRcgdgvgsggraaiaylknmGAVSVAEAR 1020
Cdd:PRK14133 3 RVIIHVDMDAFFASVEQMDNPKLKGKPVIVGGISERGVVSTcSYEARKYGVH-------------------SAMPVFMAK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1004138820 1021 RRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:PRK14133 64 KRCPHGIFLPVRHERYKEVSKNIFKILYEVTP--IVEPVSIDEAYLDIT 110
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
945-1069 |
2.61e-15 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 80.42 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 945 LHVDVDCFYCQVERLDDPSLMGVPLAVtqfnSGGFV-AVSYEARAAGIRcgdgVGSGGRaaiaylknmgavsvaEARRRC 1023
Cdd:PRK03858 7 LHADLDSFYASVEQRDDPALRGRPVIV----GGGVVlAASYEAKAYGVR----TAMGGR---------------QARRLC 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1004138820 1024 PGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:PRK03858 64 PQAVVVPPRMSAYSRASKAVFEVFRDTTP--LVEGLSIDEAFLDVG 107
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
943-1070 |
8.15e-15 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 78.29 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 943 VFLHVDVDCFYCQVERLDDPSLMGVPLAVTQFN-----SGGFVAVSYEARAAGIRCGdgvgsggraaiaylknmgaVSVA 1017
Cdd:PRK01216 2 IILFVDFDYFFAQVEEVLNPSLKGKPVVVCVYSgrfedSGAVATANYEARKLGIKAG-------------------MPIV 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1004138820 1018 EARRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVTR 1070
Cdd:PRK01216 63 EAKKILPNAVYLPMRKEVYQQVSNRIMKLLREYSE--KIEIASIDEAYLDISD 113
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1555-1835 |
1.06e-14 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 76.60 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1555 AEGSYRDLDSARQRYALLVKRFLANGTTTAMYYGSLHLEPNTVLVD------TIERLGQRAVVGKVSMDRLSP--DDYVE 1626
Cdd:cd01292 23 KEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIeavaeaARASAGIRVVLGLGIPGVPAAvdEDAEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1627 QLEDGLRDAEAFVQYTLGrkcsriqpCITPRFIPTCTPELMRGLAELARKYGTHIQSHiseCCGEVNCVREMhpeyaSDA 1706
Cdd:cd01292 103 LLLELLRRGLELGAVGLK--------LAGPYTATGLSDESLRRVLEEARKLGLPVVIH---AGELPDPTRAL-----EDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1707 AVFEEMGLltsRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFF---GDAFFRVNHALSLGLKVGLGTDVAGGISPSM 1783
Cdd:cd01292 167 VALLRLGG---RVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLgrdGEGAEALRRLLELGIRVTLGTDGPPHPLGTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1004138820 1784 LSAQ-RMAvvnsrclrahklavsggttanLEMEKDVITFKEALWLATVGGAQA 1835
Cdd:cd01292 244 LLALlRLL---------------------LKVLRLGLSLEEALRLATINPARA 275
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
1646-1865 |
5.23e-14 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238637 [Multi-domain] Cd Length: 381 Bit Score: 75.95 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1646 KCSRIQPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGEVNCVRE-------------MHPE---YASDAAVF 1709
Cdd:cd01312 144 ESQLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEEskgwfkhfwesflKLPKpkkLATAIDFL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1710 EEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTD-VAGGISPSMLSAQR 1788
Cdd:cd01312 224 DMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004138820 1789 MAvvnsrcLRAHKlavsggttanleMEKDVITFKEALWLATVGGAQALDLAdrVGTFEEGKEFDALLVDTNLGGTDG 1865
Cdd:cd01312 304 AL------LDLHP------------EEDLLELASELLLMATLGGARALGLN--NGEIEAGKRADFAVFELPGPGIKE 360
|
|
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
939-1072 |
7.62e-14 |
|
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: 75.81 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 939 RPLRVFLHVDVDCFYCQVERLDDPSLMGVPLAVTqfNSGGFVA----VSYEARAAGIRCGdgvgsggraaiaylknMgav 1014
Cdd:cd01701 44 DLQRIIMHVDFDCFFVSVSIRNRPDLKGKPVAVC--HGKGPNSeiasCNYEARSYGIKNG----------------M--- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1004138820 1015 SVAEARRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSpdGEVEKASYDDFYLDVTRHC 1072
Cdd:cd01701 103 WVGQAKKLCPQLVTLPYDFEAYEEVSLTFYEILASYT--DNIEAVSCDEALIDITSLL 158
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
945-1076 |
6.62e-13 |
|
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: 72.20 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 945 LHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFVAVSYEARAAGIRcgdgvgsggraaiaylknMGAVSVaEARRRCP 1024
Cdd:cd01700 1 ALVDCNSFYASCERVFRPLLLGRPLVVLSNNDGCVIARSPEAKALGIK------------------MGSPYF-KVPDLLE 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1004138820 1025 --GLVVRPMRTDRYRQVAEQVHSLLRSFSPDgeVEKASYDDFYLDVT--RHCVDAR 1076
Cdd:cd01700 62 rhGVAVFSSNYALYGDMSRRIMSILERFSPD--VEVYSIDESFLDLTgsLRFGDLE 115
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
1721-1859 |
1.62e-12 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 71.52 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1721 MAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGGISP--SMLSAQRMAVVNSRclr 1798
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPtsSMPLVMHLACRLMR--- 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1799 ahklavsggttanLEMEkdvitfkEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTN 1859
Cdd:cd01296 310 -------------MTPE-------EALTAATINAAAALGLGETVGSLEVGKQADLVILDAP 350
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
62-464 |
3.22e-12 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 70.05 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 62 QEKRVILHFDCDCFYAQVEEVRNPALRDVPLGV------TQKYLIV-TSNYPARAAGVTKLMGIRDAQARCPGLVLVSgE 134
Cdd:PRK03352 2 AMPRWVLHVDLDQFIAAVELLRRPELAGLPVIVggngdpTEPRKVVtCASYEARAFGVRAGMPLRTAARRCPDAVFLP-S 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 135 DLGPYRQASKSIHAVLSRYG-TAERLGMDETYVdcteevlrrvrsgAYEPPAPPprlvghrhtarcAVAADTRyrpQDLR 213
Cdd:PRK03352 81 DPAAYDAASEEVMATLRDLGvPVEVWGWDEAFL-------------GVDTDDPE------------ALAEEIR---AAVL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 214 ARqpdggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaa 293
Cdd:PRK03352 133 ER------------------------------------------------------------------------------ 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 294 earaavraeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSErCGAASAADV 373
Cdd:PRK03352 135 ---------TGLSCSVGIGDNKLRAKIATGFAKPAGVFRLTDANWMAVMGDRPTDALWGVGPKTAKRLAA-LGITTVADL 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 374 RRCGQQRLAEALGDKTAAMLWELAWGCDSSPVRPTG-PPRSITVEDSF-KSCASWAAATAVLRVLApdllARLREEWAEN 451
Cdd:PRK03352 205 AAADPAELAATFGPTTGPWLLLLARGGGDTEVSAEPwVPRSRSREVTFpQDLTDRAEVESAVRELA----RRVLDEVVAE 280
|
410
....*....|...
gi 1004138820 452 RRRPETLTLKWRH 464
Cdd:PRK03352 281 GRPVTRVAVKVRT 293
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
66-407 |
5.69e-12 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 69.43 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 66 VILHFDCDCFYAQVEEVRNPALRDVPL------GVTQKY-LIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVsgedlgP 138
Cdd:PRK01216 2 IILFVDFDYFFAQVEEVLNPSLKGKPVvvcvysGRFEDSgAVATANYEARKLGIKAGMPIVEAKKILPNAVYL------P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 139 -----YRQASKSIHAVLSRYGTA-ERLGMDETYVDCTEEVlrrvrsgayeppappprlvghrhtarcavaadtryrpqdl 212
Cdd:PRK01216 76 mrkevYQQVSNRIMKLLREYSEKiEIASIDEAYLDISDKV---------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 213 rarqpdggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggRPSEDSWETLLAIgsmva 292
Cdd:PRK01216 116 --------------------------------------------------------------KNYQDAYNLGLEI----- 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 293 aeaRAAVRAETGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSErCGAASAAD 372
Cdd:PRK01216 129 ---KNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIPGIGDITAEKLKK-LGVNKLVD 204
|
330 340 350
....*....|....*....|....*....|....*
gi 1004138820 373 VRRCGQQRLAEALGDKTAAMLWELAWGCDSSPVRP 407
Cdd:PRK01216 205 TLRIEFDELKGIIGEAKAKYLFSLARNEYNEPVRA 239
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
939-1067 |
6.01e-12 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 70.35 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 939 RPLRVFLHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFVA-VSYEARAAGIRcgdgvgsggraaiaylknmGAVSVA 1017
Cdd:PRK03348 2 RAQRWVLHLDMDAFFASVEQLTRPTLRGRPVLVGGLGGRGVVAgASYEARVFGAR-------------------SAMPMH 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1018 EARRRCP-GLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLD 1067
Cdd:PRK03348 63 QARRLVGnGAVVLPPRFVVYRAASRRVFDTLRELSP--VVEQLSFDEAFVE 111
|
|
| PolY_Pol_IV_kappa |
cd03586 |
DNA Polymerase IV/Kappa; Pol IV, also known as Pol kappa, DinB, and Dpo4, is a translesion ... |
1285-1487 |
9.96e-12 |
|
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: 68.70 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1285 GVQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP-----TLAR------K 1353
Cdd:cd03586 114 ATEIAKEIRARIREETGLTASAGIAPNKFLAKIASDLNKPNGLTVIPPEDVEEFLAPLPVRKIPgvgkvTAEKlkelgiK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1354 TGAsvvaalgggglvgDLSAFSRAQLVARFGAqLGGLLADLpdggpappaaaaapggGGGAMGGSVRERGPQKSILVERS 1433
Cdd:cd03586 194 TIG-------------DLAKLDVELLKKLFGK-SGRRLYEL----------------ARGIDNRPVEPDRERKSIGVERT 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1004138820 1434 FP-AITRFGGVKDALVPMVGALWERLtedaARHSRVPAKLLLTWRQGYGAPKTRS 1487
Cdd:cd03586 244 FSeDLTDPEELLEELLELAEELAERL----RKRGLKGRTVTVKLKYADFSTRTRS 294
|
|
| PRK14133 |
PRK14133 |
DNA polymerase IV; Provisional |
64-421 |
1.05e-11 |
|
DNA polymerase IV; Provisional
Pssm-ID: 184529 [Multi-domain] Cd Length: 347 Bit Score: 68.59 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 64 KRVILHFDCDCFYAQVEEVRNPALRDVPL---GVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSGEdLGPYR 140
Cdd:PRK14133 2 DRVIIHVDMDAFFASVEQMDNPKLKGKPVivgGISERGVVSTCSYEARKYGVHSAMPVFMAKKRCPHGIFLPVR-HERYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 141 QASKSIHAVL-SRYGTAERLGMDETYVDCTEevlrrvrsgayeppappprlvGHRHTARCAvaadtRYRPQDLRARqpdg 219
Cdd:PRK14133 81 EVSKNIFKILyEVTPIVEPVSIDEAYLDITN---------------------IKEEPIKIA-----KYIKKKVKKE---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 220 gggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaaearaav 299
Cdd:PRK14133 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 300 raeTGFRSSAGIAPNKLLAKLVSGLHKPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLSErCGAASAADVRRCGQQ 379
Cdd:PRK14133 131 ---TGLTLSVGISYNKFLAKLASDWNKPDGIKIITEDMIPDILKPLPISKVHGIGKKSVEKLNN-IGIYTIEDLLKLSRE 206
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1004138820 380 RLAEALGdKTAAMLWELAWGCDSSPVRPTGPPRSITVEDSFK 421
Cdd:PRK14133 207 FLIEYFG-KFGVEIYERIRGIDYREVEVSRERKSIGKETTLK 247
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1553-1859 |
1.20e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 68.83 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1553 FPAEGSYRDLDSARQRYALLVKRFLANGTTTA--MYYGSLHLEPNTVLVDTIERLGQRAVVGKVSMDRLS--PDDYVEQL 1628
Cdd:COG1228 84 FEAGGGITPTVDLVNPADKRLRRALAAGVTTVrdLPGGPLGLRDAIIAGESKLLPGPRVLAAGPALSLTGgaHARGPEEA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1629 EDGLRD-AEAFVQYtLGRKCSRIQPCITPrfiptctpELMRGLAELARKYGTHIQSHIseccgevncvremhpEYASDAA 1707
Cdd:COG1228 164 RAALRElLAEGADY-IKVFAEGGAPDFSL--------EELRAILEAAHALGLPVAAHA---------------HQADDIR 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1708 VFEEMGLLTsrtvMAHGTLLSDDDIRHLASRGTAVShcpLSNFFFGDAFFRVNHALSL--------------------GL 1767
Cdd:COG1228 220 LAVEAGVDS----IEHGTYLDDEVADLLAEAGTVVL---VPTLSLFLALLEGAAAPVAakarkvreaalanarrlhdaGV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1768 KVGLGTDvAGGISPSMLSAQRMAvvnsrclrahKLAVSGGttanlemekdvITFKEALWLATVGGAQALDLADRVGTFEE 1847
Cdd:COG1228 293 PVALGTD-AGVGVPPGRSLHREL----------ALAVEAG-----------LTPEEALRAATINAAKALGLDDDVGSLEP 350
|
330
....*....|..
gi 1004138820 1848 GKEFDALLVDTN 1859
Cdd:COG1228 351 GKLADLVLLDGD 362
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
942-1069 |
1.32e-11 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 68.88 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVT---QFNSGGFVAVSYEARAAGIRCGDGVGsggraaiaylknmgavsvaE 1018
Cdd:PRK03103 3 RVILLVDMQSFYASVEKAANPELKGRPVIVSgdpERRSGVVLAACPLAKAYGVKTAERLW-------------------E 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1019 ARRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPdgEVEKASYDDFYLDVT 1069
Cdd:PRK03103 64 AQQKCPDLVVVKPRMQRYIDVSLQITRILEDFTD--LVEPFSIDEQFLDVT 112
|
|
| PRK03103 |
PRK03103 |
DNA polymerase IV; Reviewed |
64-407 |
1.96e-10 |
|
DNA polymerase IV; Reviewed
Pssm-ID: 235104 [Multi-domain] Cd Length: 409 Bit Score: 65.02 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 64 KRVILHFDCDCFYAQVEEVRNPALRDVPLGV-----TQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSgedlgP 138
Cdd:PRK03103 2 ERVILLVDMQSFYASVEKAANPELKGRPVIVsgdpeRRSGVVLAACPLAKAYGVKTAERLWEAQQKCPDLVVVK-----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 139 YRQA----SKSIHAVLSRYGT-AERLGMDETYVDCTeevlrrvrsGAYEPPAPPPRLvghrhtarcAVAADTRYRPQdlr 213
Cdd:PRK03103 77 RMQRyidvSLQITRILEDFTDlVEPFSIDEQFLDVT---------GSQKLFGSPLEI---------AQKIQQRIMRE--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 214 arqpdggggdggddgggnaaagtgegcagtalgaapevaataagdasgggvatlgagggggrpsedswetllaigsmvaa 293
Cdd:PRK03103 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 294 earaavraeTGFRSSAGIAPNKLLAKLVSGLH---KPDDQTIIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASA 370
Cdd:PRK03103 136 ---------TGVYARVGIGPNKLLAKMACDNFakkNPDGLFTLDKEDVPADLWPLPVRKLFGVGSRMEKHL-RRMGIRTI 205
|
330 340 350
....*....|....*....|....*....|....*..
gi 1004138820 371 ADVRRCGQQRLAEALGdKTAAMLWELAWGCDSSPVRP 407
Cdd:PRK03103 206 GQLANTPLERLKKRWG-INGEVLWRTANGIDYSPVTP 241
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
1620-1859 |
8.59e-10 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238638 [Multi-domain] Cd Length: 418 Bit Score: 63.24 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1620 SPDDYVEQLEDGLRDAEAFVQYTLGrkcsriqpcITPRFIPTCTPELMRGLAELA-RKYGTHIqsHISECCGEVNCVREM 1698
Cdd:cd01313 171 GYEDFLGLLEKALRAVKEHAAARIG---------VAPHSLRAVPAEQLAALAALAsEKAPVHI--HLAEQPKEVDDCLAA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1699 HPEYASDaaVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGG 1778
Cdd:cd01313 240 HGRRPVE--LLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNAR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1779 IspSMLSAQRMAVVNSRCLRAHK--LAVSGGTTAnlemekdvitfkEALWL-ATVGGAQALDLAdrVGTFEEGKEFDALL 1855
Cdd:cd01313 318 I--DLLEELRQLEYSQRLRDRARnvLATAGGSSA------------RALLDaALAGGAQALGLA--TGALEAGARADLLS 381
|
....
gi 1004138820 1856 VDTN 1859
Cdd:cd01313 382 LDLD 385
|
|
| PolY_Pol_iota |
cd01703 |
DNA Polymerase iota; Pol iota, also called Rad30B, is a translesion synthesis (TLS) polymerase. ... |
1285-1479 |
2.32e-09 |
|
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: 61.72 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1285 GVQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVL---PAARVRDFMAGVKIQSIPTLARKTgaSVVAA 1361
Cdd:cd01703 112 ASHIAYEMRERIENELGLTCCAGIASNKLLAKLVGSVNKPNQQTTLlppSCADLMDFMDLHDLRKIPGIGYKT--AAKLE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1362 LGGGGLVGDLSAFSRAQLVARFGAQLGGLLADLPDGGPAPPAAAAAPGGGGGAMGGSVRERGPQKSILVERSFPAITRFG 1441
Cdd:cd01703 190 AHGISSVRDLQEFSNRNRQTVGAAPSLLELLLMVKEFGEGIGQRIWKLLFGRDTSPVKPASDFPQQISIEDSYKKCSLEE 269
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1004138820 1442 G--VKDALVPMVGALWER----LTEDAARHSRVPAKLLLTWRQG 1479
Cdd:cd01703 270 IreARNKIEELLASLLERmkqdLQEVKAGDGRRPHTLRLTLRRY 313
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
1579-1790 |
5.70e-09 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 60.72 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1579 NGTTT-----AMYY---GSLhlepnTVLVDTIERLGQRAVVGKVSMDRlspdDYVEQLEDGLRDAEAFVQYTLGRKCSRI 1650
Cdd:PRK07203 120 NGVTTvfdhhASPNyigGSL-----FTIADAAKKVGLRAMLCYETSDR----DGEKELQEGVEENIRFIKHIDEAKDDMV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1651 QPCITPRFIPTCTPELMRGLAELARKYGTHIQSHISECCGEVNcvrEMHPEYASDAAV-FEEMGLLTSRTVMAHGTLLSD 1729
Cdd:PRK07203 191 EAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVS---DSHKKYGKDIVErLADFGLLGEKTLAAHCIYLSD 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004138820 1730 DDIRHLASRGTAVSHCPLSNffFGDAfFRVNHALSL---GLKVGLGTDvagGISPSMLSAQRMA 1790
Cdd:PRK07203 268 EEIDLLKETDTFVVHNPESN--MGNA-VGYNPVLEMiknGILLGLGTD---GYTSDMFESYKVA 325
|
|
| PolY_Pol_V_umuC |
cd01700 |
umuC subunit of DNA Polymerase V; umuC subunit of Pol V. Pol V is a bacterial translesion ... |
303-447 |
1.73e-08 |
|
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: 58.71 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 303 TGFRSSAGIAPNKLLAKLVSGLHKPDDQT-----IIHPDQAADFLAPLPVRALPGVGYKTEQLLsERCGAASAADVRRCG 377
Cdd:cd01700 129 TGIPVTVGIGPTKTLAKLANDLAKKKNPYggvvdLTDEEVRDKLLKILPVGDVWGIGRRTAKKL-NAMGIHTAGDLAQAD 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004138820 378 QQRLAEALGdKTAAMLWELAWGCDSSPVRPTGPPR-SITVEDSF-KSCASWAAATAVLRVLAPDLLARLREE 447
Cdd:cd01700 208 PDLLRKKFG-VVGERLVRELNGIDCLPLEEYPPPKkSIGSSRSFgRDVTDLDELKQALAEYAERAAEKLRRQ 278
|
|
| PRK03352 |
PRK03352 |
DNA polymerase IV; Validated |
942-1069 |
1.70e-07 |
|
DNA polymerase IV; Validated
Pssm-ID: 179564 [Multi-domain] Cd Length: 346 Bit Score: 55.41 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 942 RVFLHVDVDCFYCQVERLDDPSLMGVPLAVtqfnsGG---------FVA-VSYEARAAgircgdGVGSGGRAAIAYlknm 1011
Cdd:PRK03352 5 RWVLHVDLDQFIAAVELLRRPELAGLPVIV-----GGngdpteprkVVTcASYEARAF------GVRAGMPLRTAA---- 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1004138820 1012 gavsvaearRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFspDGEVEKASYDDFYLDVT 1069
Cdd:PRK03352 70 ---------RRCPDAVFLPSDPAAYDAASEEVMATLRDL--GVPVEVWGWDEAFLGVD 116
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
1671-1785 |
1.84e-07 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 54.71 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1671 AELARKYGTHIQSHISEccgevncVREMHPEYASDAAVFEEMGLLTsrtvmaHGTLLSDDDIRHLASRGTAVSHCPLSNF 1750
Cdd:cd01305 131 LELLRRRGKLFAIHASE-------TRESVGMTDIERALDLEPDLLV------HGTHLTDEDLELVRENGVPVVLCPRSNL 197
|
90 100 110
....*....|....*....|....*....|....*
gi 1004138820 1751 FFGDAFFRVNHALSLGLKVGLGTDVAGGISPSMLS 1785
Cdd:cd01305 198 YFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWA 232
|
|
| PRK02794 |
PRK02794 |
DNA polymerase IV; Provisional |
946-1069 |
3.64e-07 |
|
DNA polymerase IV; Provisional
Pssm-ID: 179473 [Multi-domain] Cd Length: 419 Bit Score: 54.94 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 946 HVDVDCFYCQVERLDDPSLMGVPLAVTQFNSGGFVAVSYEARAAGIRcgdgvgsggraaiaylknmGAVSVAEARRRCPG 1025
Cdd:PRK02794 40 HIDCDAFYASVEKRDNPELRDKPVIIGGGKRGVVSTACYIARIHGVR-------------------SAMPMFKALKLCPD 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1004138820 1026 LVVRPMRTDRYRQVAEQVHSLLRSFSPDgeVEKASYDDFYLDVT 1069
Cdd:PRK02794 101 AVVIKPDMEKYVRVGREVRAMMQALTPL--VEPLSIDEAFLDLS 142
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
68-174 |
3.75e-07 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 55.02 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 68 LHFDCDCFYAQVEEVRNPALRDVPLGVTQKYLIVTSNYPARAAGVTKLMGIRDAQARCPGLVLVSgEDLGPYRQASKSIH 147
Cdd:PTZ00205 136 IHLDMDMFYAAVEIKKHPEYAAIPLAIGTMTMLQTANYVARGRGIRQGMPGFLALKICPNLLILP-PDFDAYNEESNTVR 214
|
90 100
....*....|....*....|....*...
gi 1004138820 148 AVLSRYG-TAERLGMDETYVDCTEEVLR 174
Cdd:PTZ00205 215 RIVAEYDpNYISFGLDELTLEVSAYIER 242
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
1662-1934 |
3.92e-07 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 54.86 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1662 CTPELMRGLAELARKYG-THIqsHISECCGEVN-CVREMHpeyASDAAVFEEMGLLTSRTVMAHGTLLSDDDIRHLASRG 1739
Cdd:PRK09229 213 VTPDQLAAVLALAAPDGpVHI--HIAEQTKEVDdCLAWSG---ARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1740 TAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGGISPS----ML-SAQRMAvvnsRCLRAHKLAVSGGTTAnlem 1814
Cdd:PRK09229 288 AVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSDSHVSIDLVeelrLLeYGQRLR----DRRRNVLAAAAQPSVG---- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1815 ekdvitfkEALWL-ATVGGAQALDLAdrVGTFEEGKEFDALLVDTN---LGGTDgpfdvfpGEDDLERfekFINLGDDRN 1890
Cdd:PRK09229 360 --------RRLFDaALAGGAQALGRA--IGGLAVGARADLVVLDLDhpaLAGRE-------GDALLDR---WVFAGGDAA 419
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1004138820 1891 LLEVYVQGVCVKRGNVFELEEGARSDLMSAptpaepdLGALLGD 1934
Cdd:PRK09229 420 VRDVWVAGRWVVRDGRHRLREAIAAAFRAA-------LAALLAA 456
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
1656-1852 |
6.26e-07 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 54.21 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1656 PRFIPTCT--------PELMRGLAELARKYGTHIQSHISECCGEVNCVRE-------------MHPEYASDAAVFEEMgL 1714
Cdd:PRK08418 173 KKFIPAIAihspysvhPILAKKALQLAKKENLLVSTHFLESKAEREWLEEskgwfkkffekflKEPKPLYTPKEFLEL-F 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1715 LTSRTVMAHGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTD-VAGGISPSMLSAQRMAvvn 1793
Cdd:PRK08418 252 KGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAA--- 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1794 srcLRAHKlavsggttanlemEKDVITF-KEALWLATVGGAQALDLadRVGTFEEGKEFD 1852
Cdd:PRK08418 329 ---LLTHA-------------NMPLLELaKILLLSATRYGAKALGL--NNGEIKEGKDAD 370
|
|
| PolY_Rev1 |
cd01701 |
DNA polymerase Rev1; Rev1 is a translesion synthesis (TLS) polymerase found in eukaryotes. ... |
1287-1394 |
6.93e-07 |
|
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: 53.86 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1287 QIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIPTLARKTGASVVAALGGGG 1366
Cdd:cd01701 167 ELAEAIRNEIRETTGCSASVGIGPNILLARLATRKAKPDGQYHLSAEKVEEFLSQLKVGDLPGVGSSLAEKLVKLFGDTC 246
|
90 100
....*....|....*....|....*...
gi 1004138820 1367 LVGDLSAFSRAQLVARFGAQLGGLLADL 1394
Cdd:cd01701 247 GGLELRSKTKEKLQKVLGPKTGEKLYDY 274
|
|
| PRK02406 |
PRK02406 |
DNA polymerase IV; Validated |
1288-1459 |
1.06e-06 |
|
DNA polymerase IV; Validated
Pssm-ID: 235035 [Multi-domain] Cd Length: 343 Bit Score: 52.81 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1288 IAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP-----TLAR------KTGA 1356
Cdd:PRK02406 114 IAQEIRQDIFEELGLTASAGVAPNKFLAKIASDWNKPNGLFVITPEEVDAFLATLPVEKIPgvgkvTAEKlhalgiYTCA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1357 svvaalgggglvgDLSAFSRAQLVARFGAqLGGLLADL----------PDggpappaaaaapgggggamggsvRERgpqK 1426
Cdd:PRK02406 194 -------------DLQKYDLAELIRHFGK-FGRRLYERargiderpvkPD-----------------------RER---K 233
|
170 180 190
....*....|....*....|....*....|....
gi 1004138820 1427 SILVERSFPA-ITRFGGVKDALVPMVGALWERLT 1459
Cdd:PRK02406 234 SVGVERTFAEdLYDLEACLAELPRLAEKLERRLE 267
|
|
| PolY |
cd00424 |
Y-family of DNA polymerases; Y-family DNA polymerases are a specialized subset of polymerases ... |
1282-1491 |
6.12e-06 |
|
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: 50.44 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1282 LRRGVQIAQRLRAALKEAL-SMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIPTLARKTGAsvVA 1360
Cdd:cd00424 112 LGLGSEVALRIKRHIAEQLgGITASIGIASNKLLAKLAAKYAKPDGLTILDPEDLPGFLSKLPLTDLPGIGAVTAK--RL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1361 ALGGGGLVGDLSAFSRAQLVARFGAQLGGLLADLpdggpappaaaaapggGGGAMGGSVRERGPQKSILVERSFPAITRf 1440
Cdd:cd00424 190 EAVGINPIGDLLAASPDALLALWGGVSGERLWYA----------------LRGIDDEPLSPPRPRKSFSHERVLPRDSR- 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1004138820 1441 ggVKDALVPMVGALWERLTEDAARHSRVPAKLLLT-------WRQGYGAPkTRSADVS 1491
Cdd:cd00424 253 --NAEDARPLLRLLLEKLARRLRRDGRGATRLRLWlrtvdgrWSGHADIP-SRSAPRP 307
|
|
| PRK01216 |
PRK01216 |
DNA polymerase IV; Validated |
1283-1348 |
2.25e-05 |
|
DNA polymerase IV; Validated
Pssm-ID: 179251 [Multi-domain] Cd Length: 351 Bit Score: 49.02 E-value: 2.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1004138820 1283 RRGVQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIP 1348
Cdd:PRK01216 119 QDAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRFINELDIADIP 184
|
|
| IMS_C |
pfam11799 |
impB/mucB/samB family C-terminal domain; These proteins are involved in UV protection (Swiss). |
411-534 |
2.75e-05 |
|
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: 44.86 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 411 PRSITVEDSF-KSCASWAAATAVLRVLAPDLLARLREEwaenRRRPETLTLKwrHRGSGWSRTSASSPMPLPAGALgqqq 489
Cdd:pfam11799 1 RKSIGAERTFgRDLTDLEELREALLELAEELAERLRRQ----GLVARTVTVK--IRYSDFRTITRSVTLPSPTDDT---- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1004138820 490 qqpaateaqlvDQLVRASLALLQRHIRePFNLSLINLGATNFKQE 534
Cdd:pfam11799 71 -----------DEIYRAALRLLRRLYR-GRPVRLLGVSLSNLVPE 103
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
1723-1859 |
3.07e-05 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 48.50 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1723 HGTLLSDDDIRHLASRGTAVSHCPLSNFFFGDAFFRVNHALSLGLKVGLGTDVAGGISPSMLSaqrmavvnsrclrahkl 1802
Cdd:PRK07213 233 HATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMANSPSIFR----------------- 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1803 avsggttanlEME---KDV-ITFKEALWLATVGGAQALDLaDRVGTFEEGKEFDALLVDTN 1859
Cdd:PRK07213 296 ----------EMEfiyKLYhIEPKEILKMATINGAKILGL-INVGLIEEGFKADFTFIKPT 345
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
1723-1859 |
3.89e-05 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 48.06 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1723 HGTLLSDDDIRHLASRGTAVSHCPLSN----------FFFGDAFFRVNHALSL-----------GLKVGLGTDVAGGIsp 1781
Cdd:cd01299 199 HGFLIDDETIELMKEKGIFLVPTLATYealaaegaapGLPADSAEKVALVLEAgrdalrrahkaGVKIAFGTDAGFPV-- 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004138820 1782 smlsaqRMAVVNSRCLRAhkLAVSGGTTAnlemekdvitfkEALWLATVGGAQALDLADRVGTFEEGKEFDALLVDTN 1859
Cdd:cd01299 277 ------PPHGWNARELEL--LVKAGGTPA------------EALRAATANAAELLGLSDELGVIEAGKLADLLVVDGD 334
|
|
| PRK03348 |
PRK03348 |
DNA polymerase IV; Provisional |
1287-1464 |
6.64e-05 |
|
DNA polymerase IV; Provisional
Pssm-ID: 235118 [Multi-domain] Cd Length: 454 Bit Score: 47.62 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1287 QIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFMAGVKIQSIPTLARKTGAsvVAALGGGG 1366
Cdd:PRK03348 125 AFAERLRARVREETGLPASVGAGSGKQIAKIASGLAKPDGIRVVPPGEERELLAPLPVRRLWGIGPVTEE--KLHRLGIE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1367 LVGDLSAFSRAQLVARFGAQLG-GL--LA----DLPdggpappaaaaapgggggamggsVRERGPQKSILVERSFPA-IT 1438
Cdd:PRK03348 203 TIGDLAALSEAEVANLLGATVGpALhrLArgidDRP-----------------------VAERAEAKQISAESTFAVdLT 259
|
170 180
....*....|....*....|....*...
gi 1004138820 1439 RFGGVKDALVPMVGALWERLTED--AAR 1464
Cdd:PRK03348 260 TRAQLREAIERIAEHAHRRLLKDgrGAR 287
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
1706-1901 |
9.55e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1706 AAVFEEMGLlTSRTVMAHGT---LLSDDDIRHLASRGTAVSHCPLSNFFFGDAF------------FRVNHALSLGLKVG 1770
Cdd:pfam07969 284 EAVAEKLGN-QGRVRIEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGDWLqdrlgaerarglTPVKELLNAGVKVA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1771 LGTDVAGGISPSMLSAQRM----AVVNSRCLRAHKLavsggttanlemekdvITFKEALWLATVGGAQALDLADRVGTFE 1846
Cdd:pfam07969 363 LGSDAPVGPFDPWPRIGAAvmrqTAGGGEVLGPDEE----------------LSLEEALALYTSGPAKALGLEDRKGTLG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1004138820 1847 EGKEFDALLVDTNlggtdgPFDVFPGEDDLERfekfinlgddrnLLEVYVQGVCV 1901
Cdd:pfam07969 427 VGKDADLVVLDDD------PLTVDPPAIADIR------------VRLTVVDGRVV 463
|
|
| PTZ00205 |
PTZ00205 |
DNA polymerase kappa; Provisional |
929-1069 |
1.15e-04 |
|
DNA polymerase kappa; Provisional
Pssm-ID: 140232 [Multi-domain] Cd Length: 571 Bit Score: 46.94 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 929 EGQAGAQRRarpLRVFLHVDVDCFYCQVERLDDPSLMGVPLAVTQFNSggFVAVSYEARAAGIRCGdgvgsggraAIAYL 1008
Cdd:PTZ00205 123 EQELEATRR---LGTYIHLDMDMFYAAVEIKKHPEYAAIPLAIGTMTM--LQTANYVARGRGIRQG---------MPGFL 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004138820 1009 knmgavsvaeARRRCPGLVVRPMRTDRYRQVAEQVHSLLRSFSPDGEVekASYDDFYLDVT 1069
Cdd:PTZ00205 189 ----------ALKICPNLLILPPDFDAYNEESNTVRRIVAEYDPNYIS--FGLDELTLEVS 237
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
1659-1849 |
1.72e-04 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 46.53 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1659 IPTCTPELMRGLAELARKYGTHIQSHiseCCGevncvremhpeyasDAAV------FEEM----GLLTSRTVMAHGTLLS 1728
Cdd:cd01300 289 LLLISPEELEELVRAADEAGLQVAIH---AIG--------------DRAVdtvldaLEAAlkdnPRADHRHRIEHAQLVS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1729 DDDIRHLASRGTAVSHCPLSNFFFGDAF-------------FRVNHALSLGLKVGLGTDvaggiSPsmlsaqrMAVVNSr 1795
Cdd:cd01300 352 PDDIPRFAKLGVIASVQPNHLYSDGDAAedrrlgeerakrsYPFRSLLDAGVPVALGSD-----AP-------VAPPDP- 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1004138820 1796 cLRAHKLAVSGGT--TANLEMEKDVITFKEALWLATVGGAQALDLADRVGTFEEGK 1849
Cdd:cd01300 419 -LLGIWAAVTRKTpgGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGK 473
|
|
| IMS |
pfam00817 |
impB/mucB/samB family; These proteins are involved in UV protection (Swiss). |
1286-1317 |
3.22e-04 |
|
impB/mucB/samB family; These proteins are involved in UV protection (Swiss).
Pssm-ID: 425885 [Multi-domain] Cd Length: 148 Bit Score: 42.95 E-value: 3.22e-04
10 20 30
....*....|....*....|....*....|..
gi 1004138820 1286 VQIAQRLRAALKEALSMTVSVGVGPTKLTARL 1317
Cdd:pfam00817 114 EALAKRLRREIAEETGLTCSIGIAPNKLLAKL 145
|
|
| IMS_HHH |
pfam11798 |
IMS family HHH motif; These proteins are involved in UV protection, eg. |
335-361 |
3.15e-03 |
|
IMS family HHH motif; These proteins are involved in UV protection, eg.
Pssm-ID: 432081 [Multi-domain] Cd Length: 32 Bit Score: 36.99 E-value: 3.15e-03
10 20
....*....|....*....|....*..
gi 1004138820 335 PDQAADFLAPLPVRALPGVGYKTEQLL 361
Cdd:pfam11798 1 PDDVPEFLWPLPISKIPGIGKKLAEKL 27
|
|
| PRK03858 |
PRK03858 |
DNA polymerase IV; Validated |
1286-1339 |
5.13e-03 |
|
DNA polymerase IV; Validated
Pssm-ID: 179663 [Multi-domain] Cd Length: 396 Bit Score: 41.51 E-value: 5.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1004138820 1286 VQIAQRLRAALKEALSMTVSVGVGPTKLTARLVGPLHKPDSITVLPAARVRDFM 1339
Cdd:PRK03858 117 VQIAARLRRRVREEVGLPITVGVARTKFLAKVASQVAKPDGLLVVPPDRELAFL 170
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
1619-1774 |
9.54e-03 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 40.26 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1619 LSPDDYVEQLEDGLRDAEAfvQYTLGRK----CSRIQP---CItpRFIPTCTPELMRGLA-------------------- 1671
Cdd:cd01320 104 LSFDEVVEAVLRGLDEAEA--EFGIKARlilcGLRHLSpesAQ--ETLELALKYRDKGVVgfdlagdevgfppekfvraf 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004138820 1672 ELARKYGTHIQSHisecCGEVNCvremhPEYASDAavFEEMGllTSRtvMAHGTLLSDDD--IRHLASRGTAVSHCPLSN 1749
Cdd:cd01320 180 QRAREAGLRLTAH----AGEAGG-----PESVRDA--LDLLG--AER--IGHGIRAIEDPelVKRLAERNIPLEVCPTSN 244
|
170 180
....*....|....*....|....*....
gi 1004138820 1750 FFFGDAFFRVNHAL----SLGLKVGLGTD 1774
Cdd:cd01320 245 VQTGAVKSLAEHPLrellDAGVKVTINTD 273
|
|
| |
