|
Name |
Accession |
Description |
Interval |
E-value |
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-562 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 641.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 1 MIEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRADSGAIRSGSEQALVEGRWRIAADGAVAERV 80
Cdd:COG0497 1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 81 RDAGGDLDGDELLLARTLSTEGRSRAVVGGRSAPVAVLTELGEQLVVVHGQSDQLRLKSATAQREALDRFAGpeLARALT 160
Cdd:COG0497 81 EENGLDLDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAG--LEELLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 161 EYQAVHARWAQSQADLETLEADRDRRAREAEELRLAMEEIEQAAPERGEDDRLAERADRLANIEDLRLAAAQAHELIQae 240
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALS-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 241 slDEGRDAVSLIESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLDSDGGReLETVQERRAELAALVR 320
Cdd:COG0497 237 --GGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPER-LEEVEERLALLRRLAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 321 KYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDRRASALTALREAAADRLSTAVTAELAALAMPTARL 400
Cdd:COG0497 314 KYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 401 SVAVETRDEFTATGRDQVALLLQPHPGSEPRALGKGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIG 480
Cdd:COG0497 394 EVEVTPLEEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 481 RRLARLAESAQVIVVTHLAQVAAFATNHLSVVKDVDGAVTASSVRQLQGEERIAEMARLLSGLPDSESGLAHARELVAMA 560
Cdd:COG0497 474 EKLARLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLALA 553
|
..
gi 2388316540 561 SA 562
Cdd:COG0497 554 AS 555
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
1-557 |
1.36e-129 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 390.25 E-value: 1.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 1 MIEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRADSGAIRSGSEQALVEGRWRI-AADGAVAER 79
Cdd:TIGR00634 1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTeSLDDADYPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 80 VRDAGGDLDGD--ELLLARTLSTEGRSRAVVGGRSAPVAVLTELGEQLVVVHGQSDQLRLKSATAQREALDRFAGpeLAR 157
Cdd:TIGR00634 81 LQAIELEEEDEdgEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAG--ANE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 158 ALTEYQAVHARWAQSQADLETLEADRDRRAREAEELRLAMEEIEQAAPERGEDDRLAERADRLANIEDLRLAAAQAHELI 237
Cdd:TIGR00634 159 KVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 238 QAESLDEGRDAVSLIESARRTVDRVagHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLDSDGGReLETVQERRAELAA 317
Cdd:TIGR00634 239 RGDVDVQEGSLLEGLGEAQLALASV--IDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPER-LNEIEERLAQIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 318 LVRKYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDRRASALTALREAAADRLSTAVTAELAALAMPT 397
Cdd:TIGR00634 316 LKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 398 ARLSVAVETRDE------FTATGRDQVALLLQPHPGSEPRALGKGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGV 471
Cdd:TIGR00634 396 AEFTVEIKTSLPsgakarAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 472 GGASAIEIGRRLARLAESAQVIVVTHLAQVAAFATNHLSVVKDVDGAVTASSVRQLQGEERIAEMARLLSGLPDSESGLA 551
Cdd:TIGR00634 476 SGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLA 555
|
....*.
gi 2388316540 552 HARELV 557
Cdd:TIGR00634 556 HAQELL 561
|
|
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-559 |
1.27e-99 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 312.64 E-value: 1.27e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 1 MIEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRADSGAIRSGSEQALVEGRWRIAaDGAVAERV 80
Cdd:PRK10869 1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLK-DTPAALRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 81 RDAGGDLDGDELLLARTLSTEGRSRAVVGGRSAPVAVLTELGEQLVVVHGQ-SDQLRLKSaTAQREALDRFAG-PELara 158
Cdd:PRK10869 80 LEDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQhAHQLLLKP-EHQKTLLDAYANeTSL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 159 LTEYQAVHARWAQSQADLETLEADRDRRAREAEELRLAMEEIEQAAPERGEDDRLAERADRLANIEDLRLAAAQAHELIQ 238
Cdd:PRK10869 156 LQEMRAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 239 AeslDEGRDAVSLIESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLDSDGGReLETVQERRAELAAL 318
Cdd:PRK10869 236 D---GEEVNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNR-LAELEQRLSKQISL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 319 VRKYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDRRASALTALREAAADRLSTAVTAELAALAMPTA 398
Cdd:PRK10869 312 ARKHHVSPEELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 399 RLSVAVE-TRDEFTATGRDQVALLLQPHPGSEPRALGKGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAI 477
Cdd:PRK10869 392 KFTIDVKfDPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 478 EIGRRLARLAESAQVIVVTHLAQVAAFATNHLSVVKDVDGAVTASSVRQLQGEERIAEMARLLSGLPDSESGLAHARELV 557
Cdd:PRK10869 472 VVGKLLRQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELL 551
|
..
gi 2388316540 558 AM 559
Cdd:PRK10869 552 AA 553
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
414-542 |
1.40e-51 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 177.78 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 414 GRDQVALLLQPHPGSEPRALGKGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAESAQVI 493
Cdd:cd03241 148 GLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVL 227
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2388316540 494 VVTHLAQVAAFATNHLSVVKDVDGAVTASSVRQLQGEERIAEMARLLSG 542
Cdd:cd03241 228 CITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
2-149 |
1.50e-37 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 140.03 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 2 IEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRADSGAIRSGSEQALVEGRWRIaADGAVAERVR 81
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDI-SDEEEAKALL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2388316540 82 DAGGDLDGDELLLARTLSTEGRSRAVVGGRSAPVAVLTELGEQLVVVHGQSDQLRLKSATAQREALDR 149
Cdd:cd03241 80 LELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-505 |
7.52e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 117 VLTELGEQLvvvhgqsDQLRLKSATAQR-----EALDRFagpELARALTEYQAVHARWAQSQADLETLEADRDRRAREAE 191
Cdd:COG1196 194 ILGELERQL-------EPLERQAEKAERyrelkEELKEL---EAELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 192 ELRLAMEEIEQAAPERGEDDRLAERADRLANIEDLRLAAAQAHELIQAESLDEgrDAVSLIESARRTVDRVAGHDAQLVP 271
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 272 VVEALANAGFVLGEAAMQLSSYLASLDSDGGRELETVQE---RRAELAALVRKYGPSLDDVIDHLEQGSTRLLELDQDGD 348
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 349 RILELRASVDADLAELDRRASALTALREAAADRLSTAVTAE--LAALAMPTARLSVAVETRDEFTATGRDQVALLLQPHP 426
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLelLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2388316540 427 GSEPRALGKGASGGELSRVMLALEVVVAGSDPvptFIFDEVDAGVGGASAIEIGRRLARLAESAQVIVVTHLAQVAAFA 505
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE---AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
435-505 |
1.69e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 1.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2388316540 435 KGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLA-ESAQVIVVTHLAQVAAFA 505
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELA 147
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-517 |
2.39e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 52 SGAIRSGSeQALVEGRWRIAADGAVAERVRDAGGDLDGD-ELLLARTLSTEGRSRAVVGGRSAPVAVLTELGEQLVVVHG 130
Cdd:TIGR02169 652 SGAMTGGS-RAPRGGILFSRSEPAELQRLRERLEGLKRElSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 131 QSDQLRLKSA-------------TAQREALDRFAG--PELARALTEYQAV---------HARWAQSQADLETLEADRDR- 185
Cdd:TIGR02169 731 EEEKLKERLEeleedlssleqeiENVKSELKELEAriEELEEDLHKLEEAlndlearlsHSRIPEIQAELSKLEEEVSRi 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 186 --RAREAE--------ELRLAMEEIEQAAPERGE-DDRLAERADRLANIE------DLRLAAAQAHEL--------IQAE 240
Cdd:TIGR02169 811 eaRLREIEqklnrltlEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNgkkeelEEELEELEAALRdlesrlgdLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 241 SLD---EGRDAVSLIESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLDSdggreLETVQERRAELAA 317
Cdd:TIGR02169 891 RDEleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-----LEDVQAELQRVEE 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 318 LVRKYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDR-RASALTALREAAADRLSTaVTAELAAlamP 396
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKkKREVFMEAFEAINENFNE-IFAELSG---G 1041
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 397 TARLsvAVETRDEFTATGrdqvaLLLQPHPGSEPRALGKGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASA 476
Cdd:TIGR02169 1042 TGEL--ILENPDDPFAGG-----LELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNV 1114
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2388316540 477 IEIGRRLARLAESAQVIVVTHLAQVAAFATNHLSVVKDVDG 517
Cdd:TIGR02169 1115 ERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNG 1155
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
2-165 |
6.67e-07 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 51.70 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 2 IEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLL-LGD----RADSGAIRSGSEQALVEGRWriaadgav 76
Cdd:PRK00064 3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLaPGRshrtARDKELIRFGAEAAVIHGRV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 77 aervrdaggDLDGDELLLARTLSTEGRSRAVVGGrsAPVAVLTELGEQLVVV--HGQSDQLRLKSATAQREALDRFAG-- 152
Cdd:PRK00064 75 ---------EKGGRELPLGLEIDKKGGRKVRING--EPQRKLAELAGLLNVVlfTPEDLRLVKGGPSERRRFLDRLLFqi 143
|
170
....*....|....
gi 2388316540 153 -PELARALTEYQAV 165
Cdd:PRK00064 144 ePVYASALSQYERA 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
404-514 |
9.97e-07 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 48.78 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 404 VETRDEFTATGRDQVALLLQphpgsepralgkgASGGELSRVMLALEVVvagSDPvPTFIFDEVDAGVGGASAIEIGRRL 483
Cdd:cd00267 61 KDIAKLPLEELRRRIGYVPQ-------------LSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELL 123
|
90 100 110
....*....|....*....|....*....|..
gi 2388316540 484 ARLAES-AQVIVVTHLAQVAAFATNHLSVVKD 514
Cdd:cd00267 124 RELAEEgRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
438-497 |
3.29e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 3.29e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 438 SGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAESAQVIVVTH 497
Cdd:pfam02463 1079 SGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISL 1138
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-81 |
3.81e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 47.88 E-value: 3.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2388316540 5 ISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDraDSGAIRSGSEQALVEGRWRIAADGAVAERVR 81
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYG--KTSRLKRKSGGGFVKGDIRIGLEGKGKAYVE 75
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-385 |
4.27e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 14 GEARLPLGPGFTALTGETGAGKTMVVTALGLLLGdRADSGAIRSGSEQALV-EGRWRIAADGAVAERVRDAGGDLDGDEL 92
Cdd:TIGR02169 15 KKKVIPFSKGFTVISGPNGSGKSNIGDAILFALG-LSSSKAMRAERLSDLIsNGKNGQSGNEAYVTVTFKNDDGKFPDEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 93 LLARTLSTEGRSRA---VVGGRSapvAVLTELGEQL-----------VVVHGQSDQLRLKSATAQREALDRFAG-----P 153
Cdd:TIGR02169 94 EVVRRLKVTDDGKYsyyYLNGQR---VRLSEIHDFLaaagiypegynVVLQGDVTDFISMSPVERRKIIDEIAGvaefdR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 154 ELARALTEYQAVHARWAQSQA-------DLETLEADRD---------RRAREAE------ELRLAMEEIEQAAPERGE-- 209
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLiidekrqQLERLRREREkaeryqallKEKREYEgyellkEKEALERQKEAIERQLASle 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 210 ------DDRLAERADRLANIEDLRLAAA----------------QAHEL---------IQAESLDEGRDA-------VSL 251
Cdd:TIGR02169 251 eeleklTEEISELEKRLEEIEQLLEELNkkikdlgeeeqlrvkeKIGELeaeiaslerSIAEKERELEDAeerlaklEAE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 252 IESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLDSDGGRELETVQERRAELAALVRKYGPS---LDD 328
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELkreLDR 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2388316540 329 VIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDRRASALTALREAAADRLSTA 385
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
438-497 |
9.56e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.69 E-value: 9.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 438 SGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAESAQVIVVTH 497
Cdd:cd03278 115 SGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITH 174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-244 |
3.07e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 1 MIEEISIRHLGVIGE-ARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRAdSGAIRSGSEQALVEGRWRIAADGAVAER 79
Cdd:pfam02463 1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERS-AKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 80 V---RDAGGDLDGDELLLARTLSTEGRSRAVVGGRSAPVAVLTELGEQ---------LVVVHGQSDQLRLKSATAQREAL 147
Cdd:pfam02463 80 TfdnEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESqgispeaynFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 148 DRFAGPELARALTEYQAVHARWAQSQADLETLEAD-RDRRAREAEELRLAMEEIEQAAPERGE------DDRLAERADRL 220
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEElKLQELKLKEQAKKALEYYQLKEKLELEeeyllyLDYLKLNEERI 239
|
250 260
....*....|....*....|....
gi 2388316540 221 ANIEDLRLAAAQAHELIQAESLDE 244
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKE 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
56-376 |
3.61e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 56 RSGSEQALVEGRWRIAADGAVAERVRDAGGDLDGDELLL---ARTLSTEGRS--RAVVGGRSApvavLTELGEQLvvvhg 130
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELreeAAELESELEEarEAVEDRREE----IEELEEEI----- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 131 QSDQLRLKSATAQREALDRFagpeLARALTEYQAVHARWAQSQADLETLEadrdRRAREAEELRLAME--EIEQAAPERG 208
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDF----LEELREERDELREREAELEATLRTAR----ERVEEAEALLEAGKcpECGQPVEGSP 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 209 EDDRLAERADRLANIEDLRLAAAQAHE-----LIQAESLDEGRDAVSLIESARRTV-DRVAGHDAQLVPVVEALANagfv 282
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEeveerLERAEDLVEAEDRIERLEERREDLeELIAERRETIEEKRERAEE---- 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 283 LGEAAMQLSSYLASLDSDGGRELETVQERRAELAALVRKYGpSLDDVIDHLEQGSTRLLELDQDGDRILELRASVdADLA 362
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKR-EALA 619
|
330
....*....|....*
gi 2388316540 363 EL-DRRASALTALRE 376
Cdd:PRK02224 620 ELnDERRERLAEKRE 634
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
438-502 |
7.26e-05 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 44.56 E-value: 7.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2388316540 438 SGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAESAQVIVVT---HLAQVA 502
Cdd:cd03272 160 SGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTfrpELLEVA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-368 |
7.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 2 IEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRAD---------SGAIRSGSEQALVEGRWRIAA 72
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEkeadelfkpQGRKPELNLKELKELEEELKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 73 DGAVAERVRDAGGDLDGDELLLAR------TLSTEGRSRAVVGGRSAPVAVLTELGEQLvvvhgQSDQLRLKSATAQREa 146
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEEleaeleELREELEKLEKLLQLLPLYQELEALEAEL-----AELPERLEELEERLE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 147 ldrfagpELARALTEYQAVHARWAQSQADLETLEADRD--------RRAREAEELRLAMEEIEQAApeRGEDDRLAERAD 218
Cdd:COG4717 157 -------ELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEEL--EEAQEELEELEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 219 RLANIEDLRLAAAQAHELIQAESLDEGRDAVSLIesarrtvdrvAGHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLD 298
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAAALLAL----------LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2388316540 299 SDGGRELETVQE-------RRAELAALVRKYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDRRA 368
Cdd:COG4717 298 ASLGKEAEELQAlpaleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-497 |
7.59e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 118 LTELGEQLVVVHGQSDQLRLKSATAQREALDrfAGPELARALTEYQAVHARWAQSQADLETLEADRDRRAREAEELRLAM 197
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKA--LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 198 ----EEIEQAAPERGE-DDRLAERADRLANIEDLRLAAAQAHELIQAEsLDEGRDAVSLIESARRTVDRVAGHDAqlvpv 272
Cdd:TIGR02168 848 eelsEDIESLAAEIEElEELIEELESELEALLNERASLEEALALLRSE-LEELSEELRELESKRSELRRELEELR----- 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 273 vEALANAGFVLGEAAMQLSSYLASLDSDGGRELETVQER-----------RAELAALVRK---YGPSLDDVIDHLEQGST 338
Cdd:TIGR02168 922 -EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeeeaRRRLKRLENKikeLGPVNLAAIEEYEELKE 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 339 RLLELDQDGDRILELRASVDADLAELDRRASAltalreaaadRLSTAVTAELAALAMPTARLSVAVETRDEFTA------ 412
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEIDREARE----------RFKDTFDQVNENFQRVFPKLFGGGEAELRLTDpedlle 1070
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 413 TGRDQVAlllQPhPGSEPRALgKGASGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAESAQV 492
Cdd:TIGR02168 1071 AGIEIFA---QP-PGKKNQNL-SLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQF 1145
|
....*
gi 2388316540 493 IVVTH 497
Cdd:TIGR02168 1146 IVITH 1150
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1-159 |
8.03e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 1 MIEEISIRHLGVI-GEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDRADSGA------IRSGSEQALVE-------G 66
Cdd:COG0419 1 KLLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSklrsdlINVGSEEASVElefehggK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 67 RWRIA-ADGAVAERVRDAGGDLdgdELLLARTLSTEGRSRAvvggrsapVAVLTELGEQLVVVHGQSDQLRlksaTAQRE 145
Cdd:COG0419 81 RYRIErRQGEFAEFLEAKPSER---KEALKRLLGLEIYEEL--------KERLKELEEALESALEELAELQ----KLKQE 145
|
170
....*....|....
gi 2388316540 146 ALDRFAGPELARAL 159
Cdd:COG0419 146 ILAQLSGLDPIETL 159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
157-383 |
1.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 157 RALTEYQAVHARWAQSQADLETLEADRDRRAREAEELRLAMEEIEQAApERGEDDRLAERADRL-ANIEDLRLAAAQAHE 235
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE-LRAELARLEAELERLeARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 236 LIQAESLDEGRDAVSLIESARRTVDRVAghdaqlvpvvealanagfvlgEAAMQLSSYLASLDSDGGRELETVQERRAEL 315
Cdd:COG4913 331 QIRGNGGDRLEQLEREIERLERELEERE---------------------RRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2388316540 316 AALVRKYGPSLDDVIDHLEQGSTRLLELDQDgdrilelRASVDADLAELDRRAS----ALTALREAAADRLS 383
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRE-------LRELEAEIASLERRKSnipaRLLALRDALAEALG 454
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
222-393 |
3.28e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 222 NIEDLRLAAAQA---HELIQAESLDEGRDAVSLIESARrtvDRVAGHDAQLVPVVEALANAGFVLGEAAMQLSSY--LAS 296
Cdd:PHA02562 203 NIEEQRKKNGENiarKQNKYDELVEEAKTIKAEIEELT---DELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkVIK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 297 LDSDGG------RELETVQERRAELAALVRKYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASV---DADLAELDRR 367
Cdd:PHA02562 280 MYEKGGvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIstnKQSLITLVDK 359
|
170 180
....*....|....*....|....*....
gi 2388316540 368 ASALtalrEAAADRLSTAV---TAELAAL 393
Cdd:PHA02562 360 AKKV----KAAIEELQAEFvdnAEELAKL 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
176-421 |
3.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 176 LETLEADRDRRAREAEELRLAMEEIEQAAPERGEDDRLAERADRL--------ANIEDLRLAAAQAHEliQAESLD---- 243
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLeeliaerrETIEEKRERAEELRE--RAAELEaeae 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 244 ----EGRDAVSLIESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAmqlssylasldsDGGRELETVQERRAELAALV 319
Cdd:PRK02224 555 ekreAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA------------DAEDEIERLREKREALAELN 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 320 rkygpslDDVIDHLEQGSTRLLELDQ--DGDRILELRASVDADLAELDRRASALTALREAAADRLST--AVTAELAALAM 395
Cdd:PRK02224 623 -------DERRERLAEKRERKRELEAefDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigAVENELEELEE 695
|
250 260
....*....|....*....|....*.
gi 2388316540 396 PTARLsVAVETRDEFTATGRDQVALL 421
Cdd:PRK02224 696 LRERR-EALENRVEALEALYDEAEEL 720
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-63 |
1.30e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2388316540 1 MIEEISIRHLGVIGEARLPLGPgFTALTGETGAGKTMVVTALGLLlgdradSGAIRSGSEQAL 63
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFL------SDAARGGLQDAL 56
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
368-536 |
2.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 368 ASALTALREAAADRLStAVTAELAaLAMPTARLSVAVETRDeftatgrDQVALLLQpHPGSEPRALGKGASGGELsrVML 447
Cdd:COG4637 200 AAVLATLRETHPERFE-RILEALR-DAFPGFEDIEVEPDED-------GRVLLEFR-EKGLDRPFPARELSDGTL--RFL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 448 ALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAESAQVIVVTHLAQ-VAAFATNHLSVV-KDVDGAVTASSVR 525
Cdd:COG4637 268 ALLAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPAlLDALEPEEVLVLeREDDGETRIRRLS 347
|
170
....*....|.
gi 2388316540 526 QLQGEERIAEM 536
Cdd:COG4637 348 DLELPEWLEGY 358
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-377 |
3.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 156 ARALTEYQAVHARWAQSQADLETLEAdrdrrarEAEELRlamEEIEQAAPERGE-DDRLAERADRLANIEDLRLAAAQAH 234
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELETLEA-------EIEDLR---ETIAETEREREElAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 235 EL--IQAESLDEGRDAVS-LIESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAMQLSSYLASLDSD---GGRELETV 308
Cdd:PRK02224 303 GLddADAEAVEARREELEdRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEleeAREAVEDR 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2388316540 309 QERRAELAALVRKYGPSLDDVIDHLEQGSTRLLELDQDGDRILELRASVDADLAELDRRASALTALREA 377
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
438-497 |
3.86e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.44 E-value: 3.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2388316540 438 SGGELSRVMLALEVVVAGSDPVPTFIFDEVDAGVGGASAIEIGRRLARLAES-AQVIVVTH 497
Cdd:cd03239 96 SGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITL 156
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-317 |
5.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 136 RLKSATAQREALDRFAGP-ELARALTEYQAVHARWAQSQADLETLEADRDRRAREAEELRLAMEEIEQAAPERGEDD--- 211
Cdd:COG4913 263 RYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleq 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 212 ---RLAERADRLANIEDLRLAAAQAHELIQAESLDEGRDAVSLIESARRTVDRVAGHDAQLVPVVEALANAGFVLGEAAM 288
Cdd:COG4913 343 lerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180
....*....|....*....|....*....
gi 2388316540 289 QLSSYLASLDSDGGRELETVQERRAELAA 317
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
2-165 |
7.57e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 38.43 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 2 IEEISIRHLGVIGEARLPLGPGFTALTGETGAGKTMVVTALGLLLGDR-----ADSGAIRSGSEQALVEgrwriaadgAV 76
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKshrtsRDKELIRWGAEEAKIS---------AV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 77 AERvrdaggdlDGDELLLARTLSTEGRSRAVVGGRSAPvaVLTELGEQLVVVHGQSDQLRL--KSATAQREALDRFAG-- 152
Cdd:cd03242 72 LER--------QGGELALELTIRSGGGRKARLNGIKVR--RLSDLLGVLNAVWFAPEDLELvkGSPADRRRFLDRLLGql 141
|
170
....*....|....
gi 2388316540 153 -PELARALTEYQAV 165
Cdd:cd03242 142 ePAYAHVLSEYQKA 155
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-269 |
7.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 118 LTELGEQLVVVHGQSDQLR--LKSATAQREALDRFAG--------PELARALTEYQAVHARWAQSQADLETLEADRDRRA 187
Cdd:COG4913 619 LAELEEELAEAEERLEALEaeLDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2388316540 188 REAEELRlamEEIEQAAPERGE-DDRLAERADRLANIEDLRLAAAQAHELIQAESLDEGRDAVSLIESARRTVDRVAGHD 266
Cdd:COG4913 699 AELEELE---EELDELKGEIGRlEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
...
gi 2388316540 267 AQL 269
Cdd:COG4913 776 DAL 778
|
|
| |
