|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09263 |
PRK09263 |
anaerobic ribonucleoside triphosphate reductase; Provisional |
1-706 |
0e+00 |
|
anaerobic ribonucleoside triphosphate reductase; Provisional
Pssm-ID: 236436 [Multi-domain] Cd Length: 711 Bit Score: 1442.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 1 MKPIVIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAIYALNVALAVELQLKDHDEVHIHEIQDLVENELMQGPYKALARS 80
Cdd:PRK09263 1 MMPKVIKRDGRKVPFDSEKIKNAIEKAAKAVEVDDEDYCATVAAEIASRVEGRDEVDIEEIQDAVENQLMAGPYKALARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 81 YIEYRHDRDIAREKQSALTREIEGLIEESNLDLINENANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIH 160
Cdd:PRK09263 81 YIEYRHDRDIAREKATDLNEEIRGLIEQSNEAVLNENANKDSKVFSTQRDLLAGIVSKHYALRHLLPRDVVNAHEKGDIH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 161 YHDLDYAPFFPMFNCMLIDLKGMLTHGFKMGNAEIDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSY 240
Cdd:PRK09263 161 YHDLDYSPFFPMFNCCLIDLKGMLTNGFKIGNAEIESPKSIQTATAVTAQIIAQVASSQYGGCTINRIDEVLAPYAEKSY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 241 EKHLEIAKEWNIAE-PEEFAKARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWASRLIQQSILKNRIAGLG 319
Cdd:PRK09263 241 EKHLKDAEEWVIEEkAEAYARARTEKEIYDAMQSLEYEINTLHTSNGQTPFVTLGFGLGTSWESRLIQKAILRNRIAGLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 320 KNRKTAVFPKLVFGIKDGLNHKAEDPNYDIKKLALECASKRMYPDILNYDKVVEVTGSFKTPMGCRSFLGTYE-EDGELI 398
Cdd:PRK09263 321 KERKTAIFPKLVFAIKDGLNLKPGDPNYDIKQLALECATKRMYPDILNYDKIVELTGSFKTPMGCRSFLQGWKdENGEEV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 399 HEGRNNLGVVSLNLPRIALRAKGSEEKFYELLDDRLRLARKALETRISRLENVKARVAPILYMEGACGVRLKADDSIAEI 478
Cdd:PRK09263 401 HDGRNNLGVVTLNLPRIALEAKGDEDKFWEILDERLELAKKALMTRIERLKGAKPRVAPILYMYGAFGVRLKADDDVDEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 479 FKNGRASISLGYIGVHETINALFGTEAHVydDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDT 558
Cdd:PRK09263 481 FKNGRATISLGYIGLYETINALYGGSWEV--NPEAKAFALAIVKRMKDACDQWKKETGYGFSLYSTPSESLTDRFCRLDT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 559 KEFGLIEGVTDKGYYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSYTRVPYYGTN 638
Cdd:PRK09263 559 EKFGVIPGITDKGYYTNSFHYDVRKKVNPFEKLDFEKPYPPLASGGFIHYCEYPNLQHNLKALEAVWDYSYDRVGYLGTN 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505126155 639 TPIDECYECGYTGEFECTSKGFTCPSCGNHDSTKVSVTRRVCGYLGSPDARPFNFGKQEEVKRRVKHL 706
Cdd:PRK09263 639 TPIDECYECGFTGEFECTEKGFTCPKCGNHDPKTVSVTRRTCGYLGNPDARPFNHGRQEEIKRRVKHM 706
|
|
| NrdD |
COG1328 |
Anaerobic ribonucleoside-triphosphate reductase [Nucleotide transport and metabolism]; ... |
1-695 |
0e+00 |
|
Anaerobic ribonucleoside-triphosphate reductase [Nucleotide transport and metabolism]; Anaerobic ribonucleoside-triphosphate reductase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 440939 [Multi-domain] Cd Length: 671 Bit Score: 889.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 1 MKPIVIKRDGSRAPFNRDRIQAAVEAAAE--NKDKDVAIYALNVALAVELQLK---DHDEVHIHEIQDLVENELMQGPYK 75
Cdd:COG1328 1 MMLKVIKRDGRVVPFDPEKIANAIKKAAKavGGEDRDEELAEEIADEVEKELErlgGGGTITVEEIQDIVEKVLMESGHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 76 ALARSYIEYRHDRDIAREKQSALTREIEgLIEESNLDLINENANKdGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHE 155
Cdd:COG1328 81 EVAKAYILYREQRTRLREARTTLVDDIE-LLDEYDDWRVNENANK-SYSFSTQRDLIAGEVSKEYALNKILPPEVADAHR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 156 VGDIHYHDLDYAPFfpMFNCMLIDLKGMLTHGFKMGNAEIDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPY 235
Cdd:COG1328 159 NGDIHIHDLDYLPR--MTNCCLWDLRDLLKNGFNGGNGKVEPPKHIQTALAQMAQIIATVQSEQAGGQAFSRFDTYLAPY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 236 VmtsyeKHLEIakewniaepeefaKARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGT----SWASRLIQQSIL 311
Cdd:COG1328 237 V-----RKDKL-------------EGKTYKEIKQAMQSLEYNLNTLPSRRGQTPFTSITFGLGTpedfSWEMRMINKAIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 312 KNRIAGLGkNRKTAVFPKLVFGIKDGLNHKAEDPNYDIKKLALECASKRMYPDILNYDKVVEV-TGSFKTPMGCRSFLGT 390
Cdd:COG1328 299 EVRIEGDG-EGRTFIFPKLIFNITEGFNWEPEDPNYDLLQLAFECTAKRGYPYFLNYDNSDELyKGSFKRSMGCRLFLDG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 391 YEEDGELiHEGRNNLGVVSLNLPRIALRAKGSEEKFYELLDDRLRLARKALETRISRLE-NVKARVAPILYMEGACGVRL 469
Cdd:COG1328 378 WENGEEL-NRGRGNLGVVTLNLPRIAYEAKGDEEKFFEILDERLDLAKEALEIKRKRLQkLAKAGLAPILYQTGAYLGRL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 470 KADDSIAEIFKNGRASIslGYIGVHETINALFGTeaHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENL 549
Cdd:COG1328 457 KPDDSIDELFKNGFSTI--GYIGLNEMLLNFTGK--HHIESEEAKAFALEILKHMRERADEWQEETGYLYSLYATPAESL 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 550 CSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSY 629
Cdd:COG1328 533 TYRFAKLDKKRFGDIIGVTDKPYYTNSFHLPVRKTIDPFEKLDFEDEYQPLYTGGTISYVELGELQPNPEALEAVVRYAY 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505126155 630 --TRVPYYGTNTPIDECYECGYTGEFECtskgfTCPSCGNHDstKVSVTRRVCGYLGSPDarPFNFGK 695
Cdd:COG1328 613 dnYRIGYLGINPPFDICPKCGYLGGEHD-----ECPKCGNED--TVEVIRRTCGYLGNVQ--PWNDGK 671
|
|
| NRDD |
pfam13597 |
Anaerobic ribonucleoside-triphosphate reductase; |
117-705 |
0e+00 |
|
Anaerobic ribonucleoside-triphosphate reductase;
Pssm-ID: 463930 [Multi-domain] Cd Length: 554 Bit Score: 716.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 117 NANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIHYHDLDYAPFFpMFNCMLIDLKGMLTHGFKMGNAEID 196
Cdd:pfam13597 1 NANKDSYSPSGQRLYIAGEVSKDYALRKLLPPEIADAHEEGDIHIHDLDYYALR-TPYCCGIDLRDLLENGFVTGNGVSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 197 TPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSYEKHLeiakewniaepeefaKARTEKECYDAFQSLEY 276
Cdd:pfam13597 80 PPKHIETACAQAVNILATVQNEQAGGQAFSSFDTYLAPFVRKDYEKHL---------------KGLTYKEVKQAMQAFVY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 277 EVNTLHTANG-QTPFVTFGFGLGTSWASR----LIQQSILKNRIAGLGKNRKTAVFPKLVFGIKDGLNHKAEDPNYDIKK 351
Cdd:pfam13597 145 NLNTMPSRRGgQTPFTNINLGLDTPKEGRdemdMIIKALLEVMLEGDGNGGTPFTFPIPIYKLKEGFNWDEGDPNYDLFE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 352 LALECASKRMYPDILNYDKVVEVTGSFKTPMGCRSFLGTYEEDGelIHEG-RNNLGVVSLNLPRIALRAKGSEEKFYELL 430
Cdd:pfam13597 225 LAFECTAKRGYPYFSNFDSDLLPGDGYVASMGCRLRLDLRPNRK--RFGGlRGNIGVVTINLPRIAYEAAGDEDKFFELL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 431 DDRLRLARKALETRISRLENVKARV-APILYMEGAcgvrlkaddsiaeiFKNGRASISLGYIGVHETINALFGteAHVYD 509
Cdd:pfam13597 303 DERLELAKEALLIRREVLKKLLAKGlLPFLMGEGY--------------LRGGNHTLTIGFIGLNEALKALTG--KHHGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 510 DAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVNPYD 589
Cdd:pfam13597 367 SEEAKEFALKILKHMREKADEWKEETGLNFSLEATPAESLSYRFAKLDKKRFGEIKGVTDKPYYTNSFHVPVDYTIDAFE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 590 KIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSY-TRVPYYGTNTPIDECYECGYTGEFEctskgfTCPSCGNH 668
Cdd:pfam13597 447 KLKLEAPFQPLTTGGHISHVELGEAQPNPEALEKLVRIAYdTGIGYFSINPPIDVCPDCGYTGEIE------ECPNCGNH 520
|
570 580 590
....*....|....*....|....*....|....*..
gi 505126155 669 DStKVSVTRRVCGYLGSPDArpFNFGKQEEVKRRVKH 705
Cdd:pfam13597 521 DE-KVEVIRRITGYLRPVSD--WNKGKQAELKDRVKH 554
|
|
| NrdD |
TIGR02487 |
anaerobic ribonucleoside-triphosphate reductase; This model represents the oxygen-sensitive ... |
115-705 |
0e+00 |
|
anaerobic ribonucleoside-triphosphate reductase; This model represents the oxygen-sensitive (anaerobic, class III) ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centered radical, a C-terminal zinc binding site, and a set of conserved active site cysteines and asparagines. This enzyme requires an activating component, NrdG, a radical-SAM domain containing enzyme (TIGR02491). Together the two form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 274159 [Multi-domain] Cd Length: 579 Bit Score: 707.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 115 NENANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIHYHDLDYaPFFPMFNCMLIDLKGMLTHGFKMGNAE 194
Cdd:TIGR02487 1 NENANMDSPTPSTQRKLIASEVSKDYALLHLLPKDIARAHLNGDIHIHDLDY-ALTLTTNCCLHDLRNLLKYGFRTGNIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 195 IDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSYEKHLEIAKEWNIA--EPEEFAKARTEKECYDAFQ 272
Cdd:TIGR02487 80 SKPPKHIDVALNHIVNILQSLQNEQYGGQSFPEFDTLLAPYIEKTNLKHRKVLQQLQLLlfEATEYAARRTFTDVTQAMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 273 SLEYEVNTLHTANGQTPFVTFGFGLGTSWASRLIQQSILKNRIAGLGKnRKTAVFPKLVFGIKDGLNHKAEDPnYDIKKL 352
Cdd:TIGR02487 160 GPEYNPNTLHSAGGQTPFESIGYGTETSKEGRMIAKALLDVRMEGDGK-GEPFIFPKIIFKVREGFNWDEPDP-YDLFEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 353 ALECASKRMYPDILNYDKVVEVTGSFKTPMGCRSFLGT-YEEDGELIHEGRNNLGVVSLNLPRIALRAKGSEEKFYELLD 431
Cdd:TIGR02487 238 AFECAAKRGYPYFLNLDPEDNVKEDVRYPMGCRTFLSPnENGDGEESYIGRGNIGVTSINLPRIAYKSRGDEEEFFEELD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 432 DRLRLARKALETRISRLENVKARVAPILYMEGA-CGVRLKaDDSIAEIFKNGraSISLGYIGVHETINALFGTeaHVYDD 510
Cdd:TIGR02487 318 EYLEIAKEALEIRREYLKKMLAKDLPPMYSQGGwDGGNLL-DESVEEILKSG--TNSIGFIGLNEALVALTGK--HLHEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 511 AVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVNPYDK 590
Cdd:TIGR02487 393 EEARELAIRILEFIRDKADEFKKETGLNYSVYATPAESLCGRFAKKDREEFGEIPGVTDKPYYTNSFHVPVYEDVNLGEK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 591 IDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSY-TRVPYYGTNTPIDECYECGYTGEFECtskgFTCPSCGNHD 669
Cdd:TIGR02487 473 IDIEAPFHPLTNGGHITYIELDEAIPDPEALKDITKKAMkNGIGYFGINPPVDVCEDCGYTGEGLN----DKCPKCGSHD 548
|
570 580 590
....*....|....*....|....*....|....*.
gi 505126155 670 stkVSVTRRVCGYLGspDARPFNFGKQEEVKRRVKH 705
Cdd:TIGR02487 549 ---IEVISRITGYLG--PVENWNDGKQAEFKDRKKH 579
|
|
| RNR_III |
cd01675 |
Class III ribonucleotide reductase; Ribonucleotide reductase (RNR) catalyzes the reductive ... |
116-685 |
0e+00 |
|
Class III ribonucleotide reductase; Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in strict or facultative anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). The class III enzyme from phage T4 consists of two subunits, this model covers the larger subunit which contains the active and allosteric sites.
Pssm-ID: 153084 [Multi-domain] Cd Length: 555 Bit Score: 642.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 116 ENANKDGKVIPTQRDLLAGIVAKHYAKtHILPRDVVQAHEVGDIHYHDLDYAPffPMFNCMLIDLKGMLTHGFKMGNAEI 195
Cdd:cd01675 1 ENANVDSSPGSTMKDLAAGIVKKYYLL-KILPKEIARAHLNGDIHIHDLDYLP--LTPYCCGWDLRPLLEKGFTTGNGII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 196 DTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSYEKHLEIAkewniaepeefakarTEKECYDAFQSLE 275
Cdd:cd01675 78 EPPKHLSSALGHIVNFLGTVQNEQAGGQAFPEFDTYLAPFVRKDYLKYRLTA---------------TRKEIKQAMQGFI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 276 YEVNTLHTANGQTPFVTFGFGL-------------------GTSWASRLIQQSILKNRIAGLGKnRKTAVFPKLVFGIKD 336
Cdd:cd01675 143 YNLNTLSRRGGQTPFTNITLGLvcpkdlefegggepvftygDTDKEARMIQKAFLEVRLEGDAK-GRPFTFPIPTFNVTE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 337 GLNHkaeDPNYDIKKLALECASKRMYPDILNYDKVVEVTGSfKTPMGCRSFLGTYE----EDGELIHEGRNNLGVVSLNL 412
Cdd:cd01675 222 GFNL---DPNYDLKELAFECAAKRGYPYFLNFDNSDNVPGD-VRAMGCRLFLDKNElkrgGGLEGSGDGTGNIGVVTINL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 413 PRIALRAKGSEEKFYELLDDRLRLARKALETRISRLENVKARVAPILYMEGACGVRLKaddsiaeiFKNGRASISLGYIG 492
Cdd:cd01675 298 PRIAYEARGDEEKFFELLDEYLELAKDALEIRRKRLKEALARGLPPLYQEGLGGGKLL--------FILKRHTLTIGFIG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 493 VHETINALFGTeaHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFG-LIEGVTDKG 571
Cdd:cd01675 370 LNEAAEALTGK--GIGESEEAREFGIRILEHIRERADEFKEETGLLYSVEATPAESLAYRFAKKDRKKYGdIIPGVTDKP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 572 YYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSYTR-VPYYGTNTPIDECYECGYT 650
Cdd:cd01675 448 YYTNSFHVPVYEDIDPFEKIDIEAKLHPLTTGGHILHIELGEAKPNPEALEALVKKAAKRgVIYFGINTPIDICNDCGYI 527
|
570 580 590
....*....|....*....|....*....|....*
gi 505126155 651 GEFEctskGFTCPSCGNHDstkVSVTRRVCGYLGS 685
Cdd:cd01675 528 GEGE----GFKCPKCGSED---VEVISRITGYLGP 555
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09263 |
PRK09263 |
anaerobic ribonucleoside triphosphate reductase; Provisional |
1-706 |
0e+00 |
|
anaerobic ribonucleoside triphosphate reductase; Provisional
Pssm-ID: 236436 [Multi-domain] Cd Length: 711 Bit Score: 1442.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 1 MKPIVIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAIYALNVALAVELQLKDHDEVHIHEIQDLVENELMQGPYKALARS 80
Cdd:PRK09263 1 MMPKVIKRDGRKVPFDSEKIKNAIEKAAKAVEVDDEDYCATVAAEIASRVEGRDEVDIEEIQDAVENQLMAGPYKALARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 81 YIEYRHDRDIAREKQSALTREIEGLIEESNLDLINENANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIH 160
Cdd:PRK09263 81 YIEYRHDRDIAREKATDLNEEIRGLIEQSNEAVLNENANKDSKVFSTQRDLLAGIVSKHYALRHLLPRDVVNAHEKGDIH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 161 YHDLDYAPFFPMFNCMLIDLKGMLTHGFKMGNAEIDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSY 240
Cdd:PRK09263 161 YHDLDYSPFFPMFNCCLIDLKGMLTNGFKIGNAEIESPKSIQTATAVTAQIIAQVASSQYGGCTINRIDEVLAPYAEKSY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 241 EKHLEIAKEWNIAE-PEEFAKARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWASRLIQQSILKNRIAGLG 319
Cdd:PRK09263 241 EKHLKDAEEWVIEEkAEAYARARTEKEIYDAMQSLEYEINTLHTSNGQTPFVTLGFGLGTSWESRLIQKAILRNRIAGLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 320 KNRKTAVFPKLVFGIKDGLNHKAEDPNYDIKKLALECASKRMYPDILNYDKVVEVTGSFKTPMGCRSFLGTYE-EDGELI 398
Cdd:PRK09263 321 KERKTAIFPKLVFAIKDGLNLKPGDPNYDIKQLALECATKRMYPDILNYDKIVELTGSFKTPMGCRSFLQGWKdENGEEV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 399 HEGRNNLGVVSLNLPRIALRAKGSEEKFYELLDDRLRLARKALETRISRLENVKARVAPILYMEGACGVRLKADDSIAEI 478
Cdd:PRK09263 401 HDGRNNLGVVTLNLPRIALEAKGDEDKFWEILDERLELAKKALMTRIERLKGAKPRVAPILYMYGAFGVRLKADDDVDEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 479 FKNGRASISLGYIGVHETINALFGTEAHVydDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDT 558
Cdd:PRK09263 481 FKNGRATISLGYIGLYETINALYGGSWEV--NPEAKAFALAIVKRMKDACDQWKKETGYGFSLYSTPSESLTDRFCRLDT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 559 KEFGLIEGVTDKGYYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSYTRVPYYGTN 638
Cdd:PRK09263 559 EKFGVIPGITDKGYYTNSFHYDVRKKVNPFEKLDFEKPYPPLASGGFIHYCEYPNLQHNLKALEAVWDYSYDRVGYLGTN 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505126155 639 TPIDECYECGYTGEFECTSKGFTCPSCGNHDSTKVSVTRRVCGYLGSPDARPFNFGKQEEVKRRVKHL 706
Cdd:PRK09263 639 TPIDECYECGFTGEFECTEKGFTCPKCGNHDPKTVSVTRRTCGYLGNPDARPFNHGRQEEIKRRVKHM 706
|
|
| NrdD |
COG1328 |
Anaerobic ribonucleoside-triphosphate reductase [Nucleotide transport and metabolism]; ... |
1-695 |
0e+00 |
|
Anaerobic ribonucleoside-triphosphate reductase [Nucleotide transport and metabolism]; Anaerobic ribonucleoside-triphosphate reductase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 440939 [Multi-domain] Cd Length: 671 Bit Score: 889.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 1 MKPIVIKRDGSRAPFNRDRIQAAVEAAAE--NKDKDVAIYALNVALAVELQLK---DHDEVHIHEIQDLVENELMQGPYK 75
Cdd:COG1328 1 MMLKVIKRDGRVVPFDPEKIANAIKKAAKavGGEDRDEELAEEIADEVEKELErlgGGGTITVEEIQDIVEKVLMESGHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 76 ALARSYIEYRHDRDIAREKQSALTREIEgLIEESNLDLINENANKdGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHE 155
Cdd:COG1328 81 EVAKAYILYREQRTRLREARTTLVDDIE-LLDEYDDWRVNENANK-SYSFSTQRDLIAGEVSKEYALNKILPPEVADAHR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 156 VGDIHYHDLDYAPFfpMFNCMLIDLKGMLTHGFKMGNAEIDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPY 235
Cdd:COG1328 159 NGDIHIHDLDYLPR--MTNCCLWDLRDLLKNGFNGGNGKVEPPKHIQTALAQMAQIIATVQSEQAGGQAFSRFDTYLAPY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 236 VmtsyeKHLEIakewniaepeefaKARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGT----SWASRLIQQSIL 311
Cdd:COG1328 237 V-----RKDKL-------------EGKTYKEIKQAMQSLEYNLNTLPSRRGQTPFTSITFGLGTpedfSWEMRMINKAIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 312 KNRIAGLGkNRKTAVFPKLVFGIKDGLNHKAEDPNYDIKKLALECASKRMYPDILNYDKVVEV-TGSFKTPMGCRSFLGT 390
Cdd:COG1328 299 EVRIEGDG-EGRTFIFPKLIFNITEGFNWEPEDPNYDLLQLAFECTAKRGYPYFLNYDNSDELyKGSFKRSMGCRLFLDG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 391 YEEDGELiHEGRNNLGVVSLNLPRIALRAKGSEEKFYELLDDRLRLARKALETRISRLE-NVKARVAPILYMEGACGVRL 469
Cdd:COG1328 378 WENGEEL-NRGRGNLGVVTLNLPRIAYEAKGDEEKFFEILDERLDLAKEALEIKRKRLQkLAKAGLAPILYQTGAYLGRL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 470 KADDSIAEIFKNGRASIslGYIGVHETINALFGTeaHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENL 549
Cdd:COG1328 457 KPDDSIDELFKNGFSTI--GYIGLNEMLLNFTGK--HHIESEEAKAFALEILKHMRERADEWQEETGYLYSLYATPAESL 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 550 CSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSY 629
Cdd:COG1328 533 TYRFAKLDKKRFGDIIGVTDKPYYTNSFHLPVRKTIDPFEKLDFEDEYQPLYTGGTISYVELGELQPNPEALEAVVRYAY 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505126155 630 --TRVPYYGTNTPIDECYECGYTGEFECtskgfTCPSCGNHDstKVSVTRRVCGYLGSPDarPFNFGK 695
Cdd:COG1328 613 dnYRIGYLGINPPFDICPKCGYLGGEHD-----ECPKCGNED--TVEVIRRTCGYLGNVQ--PWNDGK 671
|
|
| NRDD |
pfam13597 |
Anaerobic ribonucleoside-triphosphate reductase; |
117-705 |
0e+00 |
|
Anaerobic ribonucleoside-triphosphate reductase;
Pssm-ID: 463930 [Multi-domain] Cd Length: 554 Bit Score: 716.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 117 NANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIHYHDLDYAPFFpMFNCMLIDLKGMLTHGFKMGNAEID 196
Cdd:pfam13597 1 NANKDSYSPSGQRLYIAGEVSKDYALRKLLPPEIADAHEEGDIHIHDLDYYALR-TPYCCGIDLRDLLENGFVTGNGVSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 197 TPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSYEKHLeiakewniaepeefaKARTEKECYDAFQSLEY 276
Cdd:pfam13597 80 PPKHIETACAQAVNILATVQNEQAGGQAFSSFDTYLAPFVRKDYEKHL---------------KGLTYKEVKQAMQAFVY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 277 EVNTLHTANG-QTPFVTFGFGLGTSWASR----LIQQSILKNRIAGLGKNRKTAVFPKLVFGIKDGLNHKAEDPNYDIKK 351
Cdd:pfam13597 145 NLNTMPSRRGgQTPFTNINLGLDTPKEGRdemdMIIKALLEVMLEGDGNGGTPFTFPIPIYKLKEGFNWDEGDPNYDLFE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 352 LALECASKRMYPDILNYDKVVEVTGSFKTPMGCRSFLGTYEEDGelIHEG-RNNLGVVSLNLPRIALRAKGSEEKFYELL 430
Cdd:pfam13597 225 LAFECTAKRGYPYFSNFDSDLLPGDGYVASMGCRLRLDLRPNRK--RFGGlRGNIGVVTINLPRIAYEAAGDEDKFFELL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 431 DDRLRLARKALETRISRLENVKARV-APILYMEGAcgvrlkaddsiaeiFKNGRASISLGYIGVHETINALFGteAHVYD 509
Cdd:pfam13597 303 DERLELAKEALLIRREVLKKLLAKGlLPFLMGEGY--------------LRGGNHTLTIGFIGLNEALKALTG--KHHGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 510 DAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVNPYD 589
Cdd:pfam13597 367 SEEAKEFALKILKHMREKADEWKEETGLNFSLEATPAESLSYRFAKLDKKRFGEIKGVTDKPYYTNSFHVPVDYTIDAFE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 590 KIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSY-TRVPYYGTNTPIDECYECGYTGEFEctskgfTCPSCGNH 668
Cdd:pfam13597 447 KLKLEAPFQPLTTGGHISHVELGEAQPNPEALEKLVRIAYdTGIGYFSINPPIDVCPDCGYTGEIE------ECPNCGNH 520
|
570 580 590
....*....|....*....|....*....|....*..
gi 505126155 669 DStKVSVTRRVCGYLGSPDArpFNFGKQEEVKRRVKH 705
Cdd:pfam13597 521 DE-KVEVIRRITGYLRPVSD--WNKGKQAELKDRVKH 554
|
|
| NrdD |
TIGR02487 |
anaerobic ribonucleoside-triphosphate reductase; This model represents the oxygen-sensitive ... |
115-705 |
0e+00 |
|
anaerobic ribonucleoside-triphosphate reductase; This model represents the oxygen-sensitive (anaerobic, class III) ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centered radical, a C-terminal zinc binding site, and a set of conserved active site cysteines and asparagines. This enzyme requires an activating component, NrdG, a radical-SAM domain containing enzyme (TIGR02491). Together the two form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 274159 [Multi-domain] Cd Length: 579 Bit Score: 707.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 115 NENANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIHYHDLDYaPFFPMFNCMLIDLKGMLTHGFKMGNAE 194
Cdd:TIGR02487 1 NENANMDSPTPSTQRKLIASEVSKDYALLHLLPKDIARAHLNGDIHIHDLDY-ALTLTTNCCLHDLRNLLKYGFRTGNIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 195 IDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSYEKHLEIAKEWNIA--EPEEFAKARTEKECYDAFQ 272
Cdd:TIGR02487 80 SKPPKHIDVALNHIVNILQSLQNEQYGGQSFPEFDTLLAPYIEKTNLKHRKVLQQLQLLlfEATEYAARRTFTDVTQAMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 273 SLEYEVNTLHTANGQTPFVTFGFGLGTSWASRLIQQSILKNRIAGLGKnRKTAVFPKLVFGIKDGLNHKAEDPnYDIKKL 352
Cdd:TIGR02487 160 GPEYNPNTLHSAGGQTPFESIGYGTETSKEGRMIAKALLDVRMEGDGK-GEPFIFPKIIFKVREGFNWDEPDP-YDLFEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 353 ALECASKRMYPDILNYDKVVEVTGSFKTPMGCRSFLGT-YEEDGELIHEGRNNLGVVSLNLPRIALRAKGSEEKFYELLD 431
Cdd:TIGR02487 238 AFECAAKRGYPYFLNLDPEDNVKEDVRYPMGCRTFLSPnENGDGEESYIGRGNIGVTSINLPRIAYKSRGDEEEFFEELD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 432 DRLRLARKALETRISRLENVKARVAPILYMEGA-CGVRLKaDDSIAEIFKNGraSISLGYIGVHETINALFGTeaHVYDD 510
Cdd:TIGR02487 318 EYLEIAKEALEIRREYLKKMLAKDLPPMYSQGGwDGGNLL-DESVEEILKSG--TNSIGFIGLNEALVALTGK--HLHEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 511 AVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVNPYDK 590
Cdd:TIGR02487 393 EEARELAIRILEFIRDKADEFKKETGLNYSVYATPAESLCGRFAKKDREEFGEIPGVTDKPYYTNSFHVPVYEDVNLGEK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 591 IDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSY-TRVPYYGTNTPIDECYECGYTGEFECtskgFTCPSCGNHD 669
Cdd:TIGR02487 473 IDIEAPFHPLTNGGHITYIELDEAIPDPEALKDITKKAMkNGIGYFGINPPVDVCEDCGYTGEGLN----DKCPKCGSHD 548
|
570 580 590
....*....|....*....|....*....|....*.
gi 505126155 670 stkVSVTRRVCGYLGspDARPFNFGKQEEVKRRVKH 705
Cdd:TIGR02487 549 ---IEVISRITGYLG--PVENWNDGKQAEFKDRKKH 579
|
|
| RNR_III |
cd01675 |
Class III ribonucleotide reductase; Ribonucleotide reductase (RNR) catalyzes the reductive ... |
116-685 |
0e+00 |
|
Class III ribonucleotide reductase; Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in strict or facultative anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). The class III enzyme from phage T4 consists of two subunits, this model covers the larger subunit which contains the active and allosteric sites.
Pssm-ID: 153084 [Multi-domain] Cd Length: 555 Bit Score: 642.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 116 ENANKDGKVIPTQRDLLAGIVAKHYAKtHILPRDVVQAHEVGDIHYHDLDYAPffPMFNCMLIDLKGMLTHGFKMGNAEI 195
Cdd:cd01675 1 ENANVDSSPGSTMKDLAAGIVKKYYLL-KILPKEIARAHLNGDIHIHDLDYLP--LTPYCCGWDLRPLLEKGFTTGNGII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 196 DTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSYEKHLEIAkewniaepeefakarTEKECYDAFQSLE 275
Cdd:cd01675 78 EPPKHLSSALGHIVNFLGTVQNEQAGGQAFPEFDTYLAPFVRKDYLKYRLTA---------------TRKEIKQAMQGFI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 276 YEVNTLHTANGQTPFVTFGFGL-------------------GTSWASRLIQQSILKNRIAGLGKnRKTAVFPKLVFGIKD 336
Cdd:cd01675 143 YNLNTLSRRGGQTPFTNITLGLvcpkdlefegggepvftygDTDKEARMIQKAFLEVRLEGDAK-GRPFTFPIPTFNVTE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 337 GLNHkaeDPNYDIKKLALECASKRMYPDILNYDKVVEVTGSfKTPMGCRSFLGTYE----EDGELIHEGRNNLGVVSLNL 412
Cdd:cd01675 222 GFNL---DPNYDLKELAFECAAKRGYPYFLNFDNSDNVPGD-VRAMGCRLFLDKNElkrgGGLEGSGDGTGNIGVVTINL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 413 PRIALRAKGSEEKFYELLDDRLRLARKALETRISRLENVKARVAPILYMEGACGVRLKaddsiaeiFKNGRASISLGYIG 492
Cdd:cd01675 298 PRIAYEARGDEEKFFELLDEYLELAKDALEIRRKRLKEALARGLPPLYQEGLGGGKLL--------FILKRHTLTIGFIG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 493 VHETINALFGTeaHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFG-LIEGVTDKG 571
Cdd:cd01675 370 LNEAAEALTGK--GIGESEEAREFGIRILEHIRERADEFKEETGLLYSVEATPAESLAYRFAKKDRKKYGdIIPGVTDKP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 572 YYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALENVWDYSYTR-VPYYGTNTPIDECYECGYT 650
Cdd:cd01675 448 YYTNSFHVPVYEDIDPFEKIDIEAKLHPLTTGGHILHIELGEAKPNPEALEALVKKAAKRgVIYFGINTPIDICNDCGYI 527
|
570 580 590
....*....|....*....|....*....|....*
gi 505126155 651 GEFEctskGFTCPSCGNHDstkVSVTRRVCGYLGS 685
Cdd:cd01675 528 GEGE----GFKCPKCGSED---VEVISRITGYLGP 555
|
|
| PRK07111 |
PRK07111 |
anaerobic ribonucleoside triphosphate reductase; Provisional |
5-706 |
9.95e-171 |
|
anaerobic ribonucleoside triphosphate reductase; Provisional
Pssm-ID: 235937 [Multi-domain] Cd Length: 735 Bit Score: 506.79 E-value: 9.95e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAAAEN--KDKDVAIyALNVALAV--ELQLKDHDEVHIHEIQDLVENELMQGPYKALARS 80
Cdd:PRK07111 5 IVKRDGREVPFDEEKITNAIFKAAEAvgGELDESE-AIELTQKVikYLEEKYKEEVTVEDIQDLVEKVLIENGHAETAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 81 YIEYRHDRDIAREKQSALTREIEGLIEESNldliNENANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIH 160
Cdd:PRK07111 84 YILYRAERTRIREIKSDLMKAIEEIGNDTD----RENANVSGNTPSGKMLRIASESNKDYYNLYLLPKELAKAHENGDIH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 161 YHDLDYAPFfpMFNCMLIDLKGMLTHGFKMGNAEIDTPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVMTSY 240
Cdd:PRK07111 160 IHDLDFYNL--TTTCLQIDLKKLLERGFNTGHGYIREPKRIESAAALACIILQSNQNDMHGGQSIPNFDNDMAPFVEKTF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 241 EKH--------LEIAKEWNIAEPEEFAKA----------------------------RTEKECYDAFQSLEYEVNTLHT- 283
Cdd:PRK07111 238 RRHrkeileklLELGVGEEVDEKESLNEEeellllllaldfniakkaqekadelaekETRKRTYQAMEGFIHNLNTMHSr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 284 ANGQTPFVTFGFGLGTSWASRLIQQSILKNRIAGLGKNrKTAVFPKLVFGIKDGLNHKAEDPNYDIKKLALECASKRMYP 363
Cdd:PRK07111 318 AGAQVPFSSINYGTDTSPEGRMVCENLLLATEKGLGKG-ETPIFPIQIFRVKEGVNYNEEDPNYDLFKLACRVAAKRLFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 364 DILN---------YDKvvevtGSFKTP---MGCRsflgTY---EEDGELIHEGRNNLGVVSLNLPRIALRAKGSEEKFYE 428
Cdd:PRK07111 397 NFSFldapfnkeyYDK-----GRPPTEvatMGCR----TRvmsNVNGEEGTKGRGNLSFTTINLPRLAIEAKKDIDKFFE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 429 LLDDRLRLARKALETRISRLENVKARVAPILYMEG--ACGVRLKADDSIAEIFKNGraSISLGYIGVHETINALFGteAH 506
Cdd:PRK07111 468 LLDERLELAIEQLLHRYEVQKTLKVKDFPFLMGQGlwKGSENLGPDDSIEPVLKQG--TLGIGFIGLAETLVALTG--KH 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 507 VYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLIEGVTDKGYYTNSFHLDVEKKVN 586
Cdd:PRK07111 544 HGESEEAQELGLKIVSHMRDFCDEYKEEYKLNYSLLATPAEGLSGRFIKMDRKKFGEIKGVTDKEYYTNSFHVPVYYPIS 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 587 PYDKIDFEMPYPEISSGGFICYGEFPN-MQRNVEALENVwDYSY--TRVPYYGTNTPIDECYECGYTGEFECtskgfTCP 663
Cdd:PRK07111 624 IFEKIEIEAPYHKLTNGGHISYVELDGdPSKNVEAFEII-VKAMknTNIGYGSINHPVDRCPVCGYLGVIED-----KCP 697
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 505126155 664 SCGnhdSTKVSVTRRVCGYLGSPDArpFNFGKQEEVKRRVKHL 706
Cdd:PRK07111 698 KCG---STNIQRIRRITGYLGTLDR--FNSAKKAERRDRVKHG 735
|
|
| PRK14704 |
PRK14704 |
anaerobic ribonucleoside triphosphate reductase; Provisional |
98-706 |
1.02e-116 |
|
anaerobic ribonucleoside triphosphate reductase; Provisional
Pssm-ID: 184798 [Multi-domain] Cd Length: 618 Bit Score: 363.73 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 98 LTREIEGLIEESNLDLINENANKDGKVIPTQRDLLAGIVAKHYAKTHILPRDVVQAHEVGDIHYHDLDYAPFFPMfNCML 177
Cdd:PRK14704 11 LMRVFETIVHGNEQDLMQENANVDGRSPMGVMGTFASESAKYYAVENLLSDQVKKAINENILYPHDLDFYATGTT-TCSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 178 IDLKGMLTHGFKMGNAEIDTPKSISTATAVtAQIIAQVASHI-YGGTTINRIDEVLAPYVMTSYEKHLEIAKE--WNIAE 254
Cdd:PRK14704 90 IPLAQMLANGFHTGHGHMRQPQDIKSALAL-SSIIFQANQNMqHGGQSFALFDVDLAPYVRKTVERHKKRLQSypLTKEQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 255 PEEFAKARTEKECYDAFQSLEYEVNTLHT-ANGQTPFVTFGFGLGTSWASRLIQQSILKNRIAGLGKNrKTAVFPKLVFG 333
Cdd:PRK14704 169 IEEFAWKETENDTYQACEAFIHNSNSMHSrGGGQVPFISINYGTDTSKEGRLLIKQLLKATQAGLGKG-ETPIFPIQIFK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 334 IKDGLNHKAEDPNYDIKKLALECASKRMYPDILNYDKVVEVTGSFKTP------MGCRS-FLGTYEEDGELIheGRNNLG 406
Cdd:PRK14704 248 MKKGVNFEESDPNYDLFELALETTAERLFPNFSFLDAPFNAVHYDGRPesevcyMGCRTrVMSNIHGEETAI--GRGNLS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 407 VVSLNLPRIALrAKGSEEKFYELLDDRLRLARKALETRISRLENVKARVAPILYMEGA--CGVRLKADDSIAEIFKNGra 484
Cdd:PRK14704 326 FTSINLVKLAL-ISGSKEAFFEALNYYLDLGIKQLLERFEYQCTKRARDFRFLYSQGVwrGGEKLQPEDSVASILKQG-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 485 SISLGYIGVHETINALFGteAHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLI 564
Cdd:PRK14704 403 TLSLGFIGLAECLVALTG--KHHGEDEESWKLGYEIISFMRDRMDKATEEHELNFSVIATPAEGLSGKFVKKDREEFGVI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 565 EGVTDKGYYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFP-NMQRNVEALEN-VWDYSYTRVPYYGTNTPID 642
Cdd:PRK14704 481 SGITNHNYYTNSFHIPVYYNIQAINKIRLEGPFHALCNGGHITYIELDgAAMHNKKALKQiVQAMAEHGVGYGSINHPVD 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505126155 643 ECYECGYTGEFECtskgfTCPSCGNHDSTKVSVTRRVCGYL-GSPDArpFNFGKQEEVKRRVKHL 706
Cdd:PRK14704 561 RCKCCSYHGVIGN-----ECPSCGNEDEANIERIRRITGYLvGDMSK--WNSAKRSEEMDRVKHK 618
|
|
| PRK08270 |
PRK08270 |
ribonucleoside triphosphate reductase; |
5-666 |
9.82e-51 |
|
ribonucleoside triphosphate reductase;
Pssm-ID: 236212 [Multi-domain] Cd Length: 656 Bit Score: 187.75 E-value: 9.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAIYALNVALAVELQLKDHDEVHIHEIQDLVENELMQGPYKALARSYIEY 84
Cdd:PRK08270 5 IIKRDGRIVPFDAEKITEAIAKAFKATGEFDPSEAERLALRVIEKLEDEDIPSVEEIQDIVEKVLIEAGYFKTAKAYILY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 85 RHDRDIAREKQSALTrEIEGLIEE--SNLDL-INENANKD---GKVIPTqrdlLAGIVAKHYAKTHILPRDVVQAHEVGD 158
Cdd:PRK08270 85 REQHARLRNDKKTLL-DVEDTVDEylDREDWrVNENSNMGyslQGLILN----ISGKVTANYWLNKVYPPEIGEAHRNGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 159 IHYHDLDY-APFfpmfnCMLIDLKGMLTHGFK--MGNAEIDTPKSISTAtavtaqiIAQVASHIY-------GGTTINRI 228
Cdd:PRK08270 160 LHIHDLDMlSGY-----CAGWSLRDLLLEGFNgvPGKVESKPPKHFRSA-------LGQIVNFLGtlqnewaGAQAFSSF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 229 DEVLAPYVmtsyekhleiakewniaepeeFAKARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGlgtswasrLIQQ 308
Cdd:PRK08270 228 DTYLAPFV---------------------RKDGLSYKEVKQAIQEFVFNLNVPSRWGFQTPFTNLTFD--------LTVP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 309 SILKNRIAGLGK-----------------NR-----------KTAVFPklvFGIkdglnhkaedPNYDIKKlalecaskr 360
Cdd:PRK08270 279 EDLKDQPVIIGGeemdftygdfqkemdmiNRafievmlegdaNGRVFT---FPI----------PTYNITK--------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 361 MYP-DILNYDKVVEVTGSFKTP-----------------MGCRSFLGTYE---EDGELIheGRNNL----GVVSLNLPRI 415
Cdd:PRK08270 337 DFDwDSENADLLFEMTAKYGLPyfqnfinsdlkpedvrsMCCRLQLDLRElrkRGGGLF--GSAELtgsiGVVTINLPRL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 416 ALRAKgSEEKFYELLDDRLRLARKALETRISRLE-NVKARVAPI--LYMEGacgvrlkaddsiaeiFKNGRASIslGYIG 492
Cdd:PRK08270 415 GYLSK-DEEEFFARLDELMDLAKDSLEIKRKVIErLTDKGLYPYtkRYLGT---------------LRNHFSTI--GLNG 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 493 VHETINALFGteaHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFGLI--EGVTDK 570
Cdd:PRK08270 477 MNEACLNFLG---KDITTEEGRAFALRVLDHMRERLVEFQEETGNLYNLEATPAEGTTYRLAKEDKKRYPDIitAGTDEE 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 571 GYYTNSFHLDVEKKVNPYDKIDFEMPYPEISSGG--FICY-GE-------FPNMQRNVeaLENvwdysyTRVPYYgTNTP 640
Cdd:PRK08270 554 PYYTNSTQLPVGYTDDPFEALELQDELQTKYTGGtvFHLYlGEaisdaeaCKKLVKKA--LEN------YRLPYI-TITP 624
|
730 740 750
....*....|....*....|....*....|
gi 505126155 641 ---IdeCYECGY-TGEFEctskgfTCPSCG 666
Cdd:PRK08270 625 tfsI--CPKHGYlSGEHE------FCPKCG 646
|
|
| RNR_PFL |
cd00576 |
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and ... |
153-630 |
5.48e-49 |
|
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL) are believed to have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical.
Pssm-ID: 153083 [Multi-domain] Cd Length: 401 Bit Score: 176.95 E-value: 5.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 153 AHEVGDIHYHDLDYapffPMFNCMLIDLKGMLTHGFKMGNaeiDTPKSISTATAVTAQIIAQVASH-IYGGTTINRIDEV 231
Cdd:cd00576 7 AVKSGVITVGRPDL----PFTGCVLVDYGDSLDPGIKGVN---ETAKSINEAIQKTYQIIALAASNqNGGGVSFARASSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 232 LAPYVmtsyekhleiakewniaEPEEFAKARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWASRLIQQSIL 311
Cdd:cd00576 80 LSPYG-----------------SRDYAKGSGTETDAVEAADAFNLALKEVGQGNGRTGAATGFIGGVHKGKGDKISQEFL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 312 KNRIAGlGKNRKTAVFPKLVFGIKDGLNhKAEDPNYDIKKLALECASKRMYPDILNydkvvevtgsfktpmgcrsflgty 391
Cdd:cd00576 143 NLALAN-GGEGIPLNFPNLSVRVSSDKP-GILVKAVELKQLIAEEARKTGSPGIFN------------------------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 392 eedgeliheGRNNLGvVSLNLPRIALRA-KGSEEKFYELLDDRLRLARKALETRISRLENVKARvapilymegacgvrlk 470
Cdd:cd00576 197 ---------DELCNL-VSLNLARIMEKAiNGSMDVVLEELEELAFLAVRALDCVIDSHDERIPT---------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 471 addsiAEIFKNGRASISLGYIGVHetiNALFGTEAHVYDDAVLREKAVAIIKHLKDAVNQWADETGYGFSLYATPSENlc 550
Cdd:cd00576 251 -----IELGGDERRTVGLGIAGVA---DLLIKLGLEKVGDPEADDLAAELVDQLKKHLVKATNERGFNFLLGLSPSES-- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 551 srfcridtkefgliegVTDKGYYTNSFH-------LDVEKKVNPYDKIDFEMPYPEISSGGFICYGEFPNMQRNVEALEN 623
Cdd:cd00576 321 ----------------NSSGAPATNGVSpsrg*iaIVLNGDIGPEESLASVAILQFYADNGISDTITIPDSATNLDQLLA 384
|
....*..
gi 505126155 624 VWDYSYT 630
Cdd:cd00576 385 VIDGAAA 391
|
|
| Gly_radical |
pfam01228 |
Glycine radical; |
581-686 |
2.13e-37 |
|
Glycine radical;
Pssm-ID: 426140 [Multi-domain] Cd Length: 106 Bit Score: 134.99 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 581 VEKKVNPYDKIDFEMPYPEISSGGFICYG-EFPNMQRNVEALENVWDYsYTRVPYYGTNTPIDECYECGYTGEFECTSKg 659
Cdd:pfam01228 1 VAPGISPSHGADFEGPTAVLNSVGKIDYEvELDGISLNQKFLPAVLGY-YDEEGYANLNTLIDTYFEGGHHLQFNVVDR- 78
|
90 100
....*....|....*....|....*..
gi 505126155 660 FTCPSCGNHDSTKVSVTRRVCGYLGSP 686
Cdd:pfam01228 79 ETLPDAQKHPEKYPDLTVRVSGYSANF 105
|
|
| ATP-cone |
pfam03477 |
ATP cone domain; |
3-90 |
1.69e-24 |
|
ATP cone domain;
Pssm-ID: 397513 [Multi-domain] Cd Length: 86 Bit Score: 97.72 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 3 PIVIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAIYALNVALAVELQLkdHDEVHIHEIQDLVENELMQGPYKALARSYI 82
Cdd:pfam03477 1 MKVIKRDGRREPFDKEKIRRAIEKACEKSPDQADELASEVEEELEKSL--EDGISTEEIQDLVEKTLAEHPDYAVARAYI 78
|
....*...
gi 505126155 83 EYRHDRDI 90
Cdd:pfam03477 79 LYRNLRKE 86
|
|
| PRK08579 |
PRK08579 |
anaerobic ribonucleoside triphosphate reductase; Provisional |
102-705 |
2.88e-18 |
|
anaerobic ribonucleoside triphosphate reductase; Provisional
Pssm-ID: 236303 [Multi-domain] Cd Length: 625 Bit Score: 89.04 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 102 IEGLIEESNLDlINENANKdgkvIPTQRDLLAgIVAKHYAKTH---ILPRDVVQAHEVGDIHYHDLDYAPFFPMfnCMLI 178
Cdd:PRK08579 13 IEEYAAWNSLD-VNENANR----YPGPTGFFA-YVLEEALKESlvsLLPEPGLEAHFSGDIYIHKLPYSLYIPY--CTGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 179 DLKGMLTHGFKmgnaeidTPKSIS-------TATAVTAQIIAQVASHIYGGTTINRIDEVLAPYvmtsyekhleIAKEwn 251
Cdd:PRK08579 85 SISRLLEKGLK-------TPTIISrparhfdTFVDHVANYLITMQHYFTGAQAFSSVEWYAGPF----------IRKD-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 252 iaepeefakARTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSwASRLIQQSILKN--RIAGLGKNRKTA---- 325
Cdd:PRK08579 146 ---------GLDYRKIKQNIQRLVYNLNYPSRVGMQTPFTNFTVTLDAP-KKMLEGDYAVYDgkKVGPLGEYEEEAklfl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 326 -----------------VFP------------------KLVFGI--KDG----LNHKAEDPNydiKKLALECAskrmypd 364
Cdd:PRK08579 216 laltevlregdalgqpfTFPiptlmttakmlwddpevfEAVFTTaaKRGsfywLNTRVVDPD---ASYAMCCR------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 365 iLNYDKVvEVTGSFKT-PMGCRSFLGTYEEDGELIHEGR-----------NNLGVVSLNLPRIALRAKGSEEKFYELLDD 432
Cdd:PRK08579 286 -INIDKN-ELMYAFGVgGKSRRDLEDAEEEYLEKLEKQRfgglwampditGSVNVTTVNLPRIALEARGDDDKFWELYEE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 433 RLRLARKALETRISRLENVkARVAPILY-MegacgVRLKADDSIAEIFKngrasiSLGYIGVHETInALFGTEAHVYDDA 511
Cdd:PRK08579 364 RLELVRITLDWFRERYVKL-LKTYPEMYsM-----IKEYLEEFPSSHFN------TIGIIGLPEAA-AIYLGEPKLWTEG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 512 VLREKAVAI------IKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDTKEFG-LIEGVTDKG--YYTNSfhldve 582
Cdd:PRK08579 431 SRRDWLEAAelmkkmVEFAVEKAREWMKETGTPWNVEEVPGESAAAKLAIKDLKLFPeLREYLSDPEnpIYSTS------ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 583 kkVNPY-------DKIDFEMPYPEISSGGF---ICYGEFPnmqrNVEALEN-VWDYSYTRVPYYGTNTPIDECYECG--Y 649
Cdd:PRK08579 505 --IAPYygplelwDRIEIEEKVQQEFTGGVmmhIFLGEEP----DPEALAKlTKRIMNTKLVYWSYTPAITVCNKCGrsT 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 505126155 650 TGEFEctskgfTCPSCGNHDstkVSVTRRVCGYLgspdaRP---FNFGKQEEVKRRvKH 705
Cdd:PRK08579 579 TGLYT------RCPRCGSED---VEVWSRIIGYY-----RPlknWNPYRKKEFWLR-KH 622
|
|
| PRK06406 |
PRK06406 |
vitamin B12-dependent ribonucleotide reductase; |
5-146 |
2.69e-11 |
|
vitamin B12-dependent ribonucleotide reductase;
Pssm-ID: 235796 [Multi-domain] Cd Length: 771 Bit Score: 66.80 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAIYALNVALAVELQLKDHDEVHIHEIQDLVENELMQ-----GPYKALAR 79
Cdd:PRK06406 7 VIKRDGTVVPFDKKKIAMAIYKAMLSVKNGSMEDAEELTDKVVERLKKYERPTVEQIQDIVEKVLMTkkingKDFTDVAK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505126155 80 SYIEYRHDRDIAREKqsaltREIEGLIEESNLDLineNANK-----------DGKVIPTQRDLLAGiVAKHYAKTHIL 146
Cdd:PRK06406 87 SYILYREKRRKIREE-----KELIGVKDDLKLTL---NAIKvlearyllkdeDGKIIETPRQMFRR-VARHIAIVEAL 155
|
|
| PRK12364 |
PRK12364 |
ribonucleoside-diphosphate reductase subunit alpha; |
5-102 |
3.21e-10 |
|
ribonucleoside-diphosphate reductase subunit alpha;
Pssm-ID: 237077 [Multi-domain] Cd Length: 842 Bit Score: 63.62 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAIYAL-NVALAVELQLKDHDE----VHIHEIQDLVENELMQGPYKALAR 79
Cdd:PRK12364 3 IIKRNGTTEPYDREKIEVAIRKAFASVGKPISDEIIySLVAEVERFIKEKYPnghnVSVEEIQDLVEKTLMEHGHYAEVK 82
|
90 100
....*....|....*....|...
gi 505126155 80 SYIEYRHDRDIAREKQSALTREI 102
Cdd:PRK12364 83 SYILYRAQRTEKRKAREQIIKFF 105
|
|
| PRK12365 |
PRK12365 |
ribonucleoside-diphosphate reductase subunit alpha; |
5-108 |
3.18e-09 |
|
ribonucleoside-diphosphate reductase subunit alpha;
Pssm-ID: 171440 [Multi-domain] Cd Length: 1046 Bit Score: 60.35 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAA--AENKDKDVAIYA---------LNVALAVELQLKDHDEVHIHEIQDLVENELMQGP 73
Cdd:PRK12365 120 VIRRDGTVVHFNPMKISAALEKAfrATDKIEGMTPSSvleeinaltQNIVEEILECCSQEDRIDIEKIQDIVEQQLMVVG 199
|
90 100 110
....*....|....*....|....*....|....*
gi 505126155 74 YKALARSYIEYRHDRDIAREKQSALTREIEGLIEE 108
Cdd:PRK12365 200 HYDVAKNYILYREARARVRDNKEEDGSTEKTIAEE 234
|
|
| PRK12365 |
PRK12365 |
ribonucleoside-diphosphate reductase subunit alpha; |
5-96 |
3.71e-09 |
|
ribonucleoside-diphosphate reductase subunit alpha;
Pssm-ID: 171440 [Multi-domain] Cd Length: 1046 Bit Score: 60.35 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAAAEN-----------KDKDVAIYALN--VALAVELQLKDHDEVHIHEIQDLVENELMQ 71
Cdd:PRK12365 11 IVKRNGMFVPFNQNRIFQALEAAFRDtrsledhsplpEDLESSIRSIThqVVKEVVQKITEGQVVTVERIQDMVESQLYV 90
|
90 100
....*....|....*....|....*
gi 505126155 72 GPYKALARSYIEYRHDRDIAREKQS 96
Cdd:PRK12365 91 NGLQDVARDYIVYRDDRKAHRKKSW 115
|
|
| PRK08271 |
PRK08271 |
anaerobic ribonucleoside triphosphate reductase; Provisional |
407-705 |
2.47e-08 |
|
anaerobic ribonucleoside triphosphate reductase; Provisional
Pssm-ID: 181342 [Multi-domain] Cd Length: 623 Bit Score: 57.33 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 407 VVSLNLPRIALRAKGsEEKFYELLDDRLRLARKALetrISRLENVKARVApilymegaCGVrLKADDsiAEIFKNGRASI 486
Cdd:PRK08271 353 VITINLPRIAQEARD-RDDFLEILRERVDKIHKYQ---LAYREIMEERIA--------AGM-LPLYD--AGFISLDKQFL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 487 SLGYIGVHE--TINALFGTEAHVYDDAVlrekaVAIIKHLKDAVNQWADETGYGFSLYATPSENLCSRFCRIDtKEFGLi 564
Cdd:PRK08271 418 TIGINGMVEaaEFMGLTVGYNEEYKDFV-----QEVLKVIYEANEKASKEYGFTFNTEFVPAENLGVKLAKWD-REDGY- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 565 eGVtDKGYYTNSFHLDVEKKVNPYDKIDFE-MPYPEISSGGFICY---GEFPNMQR-----NVEALENVwdysytrvPYY 635
Cdd:PRK08271 491 -GV-PRQCYNSYSYVVEDANTDALDKFKLHgKELDKYLSGGSALHlnlDERLSEEGyrkllNIAAKTGC--------NYF 560
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 636 GTNTPIDECYECGYTGEfectSKGFTCPSCGnhdSTKVSVTRRVCGYLGSPDArpFNFGKQEEVKRRVKH 705
Cdd:PRK08271 561 AFNVKITICNDCHHIDK----RTGKRCPICG---SENIDYYTRVIGYLKRVSA--FSKVRQKEYPRRHYH 621
|
|
| PRK07207 |
PRK07207 |
ribonucleoside-diphosphate reductase subunit alpha; |
5-146 |
8.40e-08 |
|
ribonucleoside-diphosphate reductase subunit alpha;
Pssm-ID: 235966 [Multi-domain] Cd Length: 965 Bit Score: 55.74 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAV----------EAAAENKDKD-VAIYALNVALAVELQLKDHDEVHIHEIQDLVENELMQGP 73
Cdd:PRK07207 36 VIRRNGSVVPFEPSKIAVAMtkaflaveggQAAASARVREtVEQLTEQVVRALVRRRPSGGTFHIEDIQDQVELALMRSG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 74 YKALARSYIEYRHDRDIAREKQSA-----------LTRE-----------IEGLIEES--NLDLINENAnkdgKVIPTQR 129
Cdd:PRK07207 116 EHKVARAYVLYREKRAQERAAEAEaaaaeahpglnVTLDdgvrrpldmarLRALIEEAceGLEAVDAEP----ILAETLK 191
|
170
....*....|....*..
gi 505126155 130 DLLAGIVAKHYAKTHIL 146
Cdd:PRK07207 192 NLYDGVPMDEVYKALIL 208
|
|
| PRK08332 |
PRK08332 |
vitamin B12-dependent ribonucleotide reductase; |
5-132 |
2.35e-07 |
|
vitamin B12-dependent ribonucleotide reductase;
Pssm-ID: 181392 [Multi-domain] Cd Length: 1740 Bit Score: 54.39 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAA----AENKDKDVAIYALNVALAVElQLKDHDEVHIHEIQDLVENELMQGPYKALARS 80
Cdd:PRK08332 6 VMKRDGRIVPFDESRIRWAVQRAmwevGVRDEKKLDEVVKRIVQRIN-ELYDGKIPHIENIQDIVELELMRAGLFEVAKA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505126155 81 YIEYRHDR-DIAREKQSALTR----EIEGLIEESNLDLINEN---ANKDGKVIPTQRDLL 132
Cdd:PRK08332 85 YILYRKKKaEIREEKKRILNKkeldEIDKRFSINALRVLASRylkKDENGNIIESPRELF 144
|
|
| NrdR |
COG1327 |
Transcriptional regulator NrdR, contains Zn-ribbon and ATP-cone domains [Transcription]; |
3-29 |
6.94e-05 |
|
Transcriptional regulator NrdR, contains Zn-ribbon and ATP-cone domains [Transcription];
Pssm-ID: 440938 [Multi-domain] Cd Length: 153 Bit Score: 43.53 E-value: 6.94e-05
10 20
....*....|....*....|....*..
gi 505126155 3 PIVIKRDGSRAPFNRDRIQAAVEAAAE 29
Cdd:COG1327 49 LMVIKKDGRREPFDREKLLRGLLRACE 75
|
|
| PRK06539 |
PRK06539 |
ribonucleoside-diphosphate reductase subunit alpha; |
5-52 |
5.11e-03 |
|
ribonucleoside-diphosphate reductase subunit alpha;
Pssm-ID: 180610 [Multi-domain] Cd Length: 822 Bit Score: 40.29 E-value: 5.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 505126155 5 VIKRDGSRAPFNRDRIQAAVEAAAENKDKDVAiYALNVALAVELQLKD 52
Cdd:PRK06539 5 VVKRDGSKEPYDANKVNAAIEDAARGLDDAIT-WVTQLASELEITLFD 51
|
|
| |
