|
Name |
Accession |
Description |
Interval |
E-value |
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-545 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 608.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 1 MLTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVRYGSDKADITAVFTYQNNSPEAKWL 80
Cdd:COG0497 1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 81 QDHELDDDSGEIHLRRVIFATGRSKAWVNGRPSSLSELKELGRLLVQLYSQHSQQQLLEPPYPKHWLDRYNNFYAEANDV 160
Cdd:COG0497 81 EENGLDLDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 161 REAYSTWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEV-IQTD-YKEIEQEFDRLSHHEHIMQDCSYSLNVLDEAEQ 238
Cdd:COG0497 161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAaLQPGeEEELEEERRRLSNAEKLREALQEALEALSGGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 239 NITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLARKYRTQPE 318
Cdd:COG0497 241 GALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 319 TLKEEYEAWQSELEQLHQL-EDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLTEQVKPLALPEAHFEFKFEPL 397
Cdd:COG0497 321 ELLAYAEELRAELAELENSdERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 398 EQPTAEGLSFIQLLFTANKGIPPQPLARVASGGELSRIALVMQVMNAEKTEAEVLVFDEIDVGISGGTAEVVGRLLADLA 477
Cdd:COG0497 401 EEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLARLA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503974228 478 QHVQLLCITHQAQVAAQSDQHLLVKKQQTDP-ASSTIVELDENQIIFELARMSGGVEINETTLQHAKQL 545
Cdd:COG0497 481 RNHQVLCVTHLPQVAAMADHHFRVSKEVDGGrTVTRVRPLDEEERVEEIARMLGGAEITEAALAHAREL 549
|
|
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-545 |
2.01e-150 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 442.83 E-value: 2.01e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 1 MLTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVRYGSDKADITAVFTYQNNSPEAKWL 80
Cdd:PRK10869 1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 81 QDHELDDDSgEIHLRRVIFATGRSKAWVNGRPSSLSELKELGRLLVQLYSQHSQQQLLEPPYPKHWLDRYNNFYAEANDV 160
Cdd:PRK10869 81 EDNQLEDGN-ECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 161 REAYSTW---QRTIRLHQAAldaQATRLQRIGTLEHQIEELEEV-IQTD-YKEIEQEFDRLSHHEHIMQDCSYSLNVLDE 235
Cdd:PRK10869 160 RAAYQLWhqsCRDLAQHQQQ---SQERAARKQLLQYQLKELNEFaPQPGeFEQIDEEYKRLANSGQLLTTSQNALQLLAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 236 AE-QNITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLARKYR 314
Cdd:PRK10869 237 GEeVNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 315 TQPETLKEEYEAWQSELEQL-HQLEDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLTEQVKPLALPEAHF--E 391
Cdd:PRK10869 317 VSPEELPQHHQQLLEEQQQLdDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFtiD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 392 FKFEPlEQPTAEGLSFIQLLFTANKGIPPQPLARVASGGELSRIALVMQVMNAEKTEAEVLVFDEIDVGISGGTAEVVGR 471
Cdd:PRK10869 397 VKFDP-EHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGK 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503974228 472 LLADLAQHVQLLCITHQAQVAAQSDQHLLVKKqQTDPASS--TIVELDENQIIFELARMSGGVEINETTLQHAKQL 545
Cdd:PRK10869 476 LLRQLGESTQVMCVTHLPQVAGCGHQHFFVSK-ETDGGMTetHMQPLDKKARLQELARLLGGSEVTRNTLANAKEL 550
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
1-545 |
6.07e-126 |
|
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: 380.62 E-value: 6.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 1 MLTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVRYGSDKADITAVFTYQN-NSPEAKW 79
Cdd:TIGR00634 1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESlDDADYPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 80 LQDHEL--DDDSGEIHLRRVIFATGRSKAWVNGRPSSLSELKELGRLLVQLYSQHSQQQLLEPPYPKHWLDRYNNFYAEA 157
Cdd:TIGR00634 81 LQAIELeeEDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 158 NDVREAYSTWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTD--YKEIEQEFDRLSHHEHIMQDCSYSLNVL-- 233
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPgeDEALEAEQQRLSNLEKLRELSQNALAALrg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 234 --DEAEQNITQEMSSIIRRLESHAgrSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLAR 311
Cdd:TIGR00634 241 dvDVQEGSLLEGLGEAQLALASVI--DGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 312 KYRTQPETLKEEYEAWQSELEQLHQL-EDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLTEQVKPLALPEAHF 390
Cdd:TIGR00634 319 KYGASVEEVLEYAEKIKEELDQLDDSdESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 391 EFKFE------PLEQPTAEGLSFIQLLFTANKGIPPQPLARVASGGELSRIALVMQVMNAEKTEAEVLVFDEIDVGISGG 464
Cdd:TIGR00634 399 TVEIKtslpsgAKARAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 465 TAEVVGRLLADLAQHVQLLCITHQAQVAAQSDQHLLVKKQQTDPASSTIV-ELDENQIIFELARMSGGVEINETTLQHAK 543
Cdd:TIGR00634 479 TAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVrPLSGEERVAELARMLAGLEKSDLTLAHAQ 558
|
..
gi 503974228 544 QL 545
Cdd:TIGR00634 559 EL 560
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
2-531 |
4.91e-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: 176.24 E-value: 4.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 2 LTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVRYGSDKADITAVFtyqnnspeakwlq 81
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVF------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 82 dheldddsgeihlrrvifatgrskawvngrpsSLSELKELGRLLvqlysqhsqqqlleppypkhwldrynnfyaeandvr 161
Cdd:cd03241 68 --------------------------------DISDEEEAKALL------------------------------------ 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 162 eaystwqrtirlhqaaldaqatrlqrigtLEHQIEELEEVIqtdykeieqefdrlshhehimqdcsyslnvldeaeqnit 241
Cdd:cd03241 80 -----------------------------LELGIEDDDDLI--------------------------------------- 91
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 242 qemssiIRRLESHAGRSeqlseiyNSLLNAQSeiddATANLrqfidrqsfdperMEELNSKLEVFHrlarkyrtqpetlk 321
Cdd:cd03241 92 ------IRREISRKGRS-------RYFINGQS----VTLKL-------------LRELGSLLVDIH-------------- 127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 322 eeyeaWQSEleqlHQLEdpetlaeqveksheefLEKAQHLDNIRResaaplakqlteqvkplalpeahfefkfepleqpt 401
Cdd:cd03241 128 -----GQHD----HQNL----------------LNPERQLDLLDG----------------------------------- 147
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 402 aeGLSFIQLLFTANKGIPPQPLARVASGGELSRIALVMQVMNAEKTEAEVLVFDEIDVGISGGTAEVVGRLLADLAQHVQ 481
Cdd:cd03241 148 --GLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQ 225
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 503974228 482 LLCITHQAQVAAQSDQHLLVKKQQTDPA-SSTIVELDENQIIFELARMSGG 531
Cdd:cd03241 226 VLCITHLPQVAAMADNHFLVEKEVEGGRtVTKVRELDKEERVEEIARMLSG 276
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1-193 |
2.29e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 63.11 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 1 MLTHLTLINF-ALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDT------NYVRYGSDKADITAVFTYQNN 73
Cdd:COG0419 1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSrsklrsDLINVGSEEASVELEFEHGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 74 SPEAKWLQdheldddsgeihlrrvifatGRSKAWVNGRPSSLSELkeLGRLLVqlysqhsqqqlleppypkhwLDRYNNF 153
Cdd:COG0419 81 RYRIERRQ--------------------GEFAEFLEAKPSERKEA--LKRLLG--------------------LEIYEEL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503974228 154 YAEANDVREAYstwQRTIRLHQAALDAQATRLQRIGTLEH 193
Cdd:COG0419 119 KERLKELEEAL---ESALEELAELQKLKQEILAQLSGLDP 155
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-379 |
6.26e-11 |
|
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: 65.38 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 1 MLTHLTLINF-ALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNY------------VRYGSDKADITAV 67
Cdd:pfam02463 1 YLKRIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLrserlsdlihskSGAFVNSAEVEIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 68 FtyqNNSpeakwlqDHELDDDSGEIHLRRVIFATGRSKAWVNGRPSSLSELKELGRlLVQLYSQH---------SQQQLL 138
Cdd:pfam02463 81 F---DNE-------DHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLE-SQGISPEAynflvqggkIEIIAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 139 EPPYPKHWLDRYNNFYAEANDVREAYS-TWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLS 217
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRLKRKKKEALKkLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 218 HHEHIMQDCSYSLNVLDEAEQNITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERME 297
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 298 ELNSKLEVFHrlarkyRTQPETLKEEYEAWQSELEQLHQLEDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLT 377
Cdd:pfam02463 310 VDDEEKLKES------EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
..
gi 503974228 378 EQ 379
Cdd:pfam02463 384 ER 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
18-367 |
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 503974228 18 IDIEQGFNVLTGETGAGKSLLLDALSACLG---------ER-TDTNYVRYGSDKADITAVFTYQNNspeakwlqDHELDD 87
Cdd:TIGR02169 19 IPFSKGFTVISGPNGSGKSNIGDAILFALGlssskamraERlSDLISNGKNGQSGNEAYVTVTFKN--------DDGKFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 88 DSGEIHLRRVIFATGR-SKAWVNGRPSSLSELKE-LGRLLV--QLYS---QHSQQQLLE--PPYPKHWLDRY---NNFYA 155
Cdd:TIGR02169 91 DELEVVRRLKVTDDGKySYYYLNGQRVRLSEIHDfLAAAGIypEGYNvvlQGDVTDFISmsPVERRKIIDEIagvAEFDR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 156 EANDVREAYSTWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEvIQTDYKEIEQeFDRLSHHEHIMQDCSYSLNVLDE 235
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEG-YELLKEKEALERQKEAIERQLAS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 236 AEQNITQ----------EMSSIIRRLESHAGRSEQLSEiyNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEV 305
Cdd:TIGR02169 249 LEEELEKlteeiselekRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503974228 306 FHRLARKYRTQPETLKEEYEAWQSELEQL--------HQLEDPETLAEQVEKSH----EEFLEKAQHLDNIRRE 367
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLteeyaelkEELEDLRAELEEVDKEFaetrDELKDYREKLEKLKRE 400
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
428-501 |
1.39e-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: 51.09 E-value: 1.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503974228 428 SGGELSRIALVMQVMNaektEAEVLVFDEIDVGISGGTAEVVGRLLADLAQH-VQLLCITHQAQVAAQSDQHLLV 501
Cdd:cd00267 82 SGGQRQRVALARALLL----NPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIV 152
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-506 |
3.45e-07 |
|
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: 50.05 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 427 ASGGELSRIALVMQVMNAEKTEAEVLVFDEIDVGISGGTAEVVGRLLADLAQHV-QLLCITHQAQVAAQSDQHLLVKKQQ 505
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLIHIKKVI 157
|
.
gi 503974228 506 T 506
Cdd:cd03227 158 T 158
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-379 |
8.05e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 155 AEANDVREAYSTWQRTIRLHQAALDAQATRLQRigtLEHQIEELEEVIQTDYKEIEQEFDRLSHHEhimqdcsyslNVLD 234
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAE----------EELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 235 EAEQNITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLARKYR 314
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503974228 315 TQPETLKEEYEAWQSELEQLHQLEdpETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLTEQ 379
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
5-71 |
8.67e-07 |
|
ATP-binding cassette domain of eukaryotic SM6 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: 213243 [Multi-domain] Cd Length: 198 Bit Score: 49.52 E-value: 8.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503974228 5 LTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGER-TDTN-------YVRYGSDKADITAVFTYQ 71
Cdd:cd03276 4 ITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKaSDTNrgsslkdLIKDGESSAKITVTLKNQ 78
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
2-128 |
2.09e-06 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 50.16 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 2 LTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSAC-LGE----RTDTNYVRYGSDKADITAvftyqnnspe 76
Cdd:PRK00064 3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLaPGRshrtARDKELIRFGAEAAVIHG---------- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 503974228 77 akwlqdhELDDDSGEIHLRRVIFATGRSKAWVNGRP-SSLSELkeLGRLLVQL 128
Cdd:PRK00064 73 -------RVEKGGRELPLGLEIDKKGGRKVRINGEPqRKLAEL--AGLLNVVL 116
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-50 |
5.13e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 47.11 E-value: 5.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503974228 5 LTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERT 50
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKT 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-379 |
5.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 168 QRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLSHHEHIMQDCSYSLNVLDEAEQNITQEMSSI 247
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 248 IRRLESHAGRSEQLS----EIYNSLLNAQSEIDDATANL-RQFIDRQSFDPERMEELNSKLEVFHRLARKYRTQPETLKE 322
Cdd:COG1196 301 EQDIARLEERRRELEerleELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503974228 323 EYEAWQSELEQLHQLEDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLTEQ 379
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
2-72 |
1.18e-05 |
|
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: 47.29 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503974228 2 LTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACL---GERT--DTNYVRYGSDKADITAVFTYQN 72
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLAtgkSHRTsrDKELIRWGAEEAKISAVLERQG 76
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
2-46 |
4.49e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.43 E-value: 4.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503974228 2 LTHLTLINFALADHLAIDIEQGFNVL-TGETGAGKSLLLDALSACL 46
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLlTGPSGSGKSTLLDAIQTLL 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-367 |
5.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 2 LTHLTLINFALAD-HLAIDIEQGFNVLTGETGAGKSLLLDALSACL-----------------GERTDTNYVR--YGSDK 61
Cdd:COG4913 3 LQRLQLINWGTFDgVHTIDFDGRGTLLTGDNGSGKSTLLDAIQTLLvpakrprfnkaandagkSDRTLLSYVRgkYGSER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 62 ADITAVFTY-----------------------------------QNNSPEAKW-------LQDHELDDDSGEIHLRRVIF 99
Cdd:COG4913 83 DEAGTRPVYlrpgdtwsaiaatfandgsgqtvtlaqvfwlkgdaSSLGDVKRFfviadgpLDLEDFEEFAHGFDIRALKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 100 ATGRSKAWVNGRPSSLSE--LKELG-------RLLVQLYSQHS--------QQQLLEPPypkhwldrynNFYAEANDVRE 162
Cdd:COG4913 163 RLKKQGVEFFDSFSAYLArlRRRLGigsekalRLLHKTQSFKPigdlddfvREYMLEEP----------DTFEAADALVE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 163 AYSTWQRTirlHQAALDAQAtrlqrigtlehQIEELEEvIQTDYKEIEQEFDRLSHHEHIMQDCSY-----SLNVLDEAE 237
Cdd:COG4913 233 HFDDLERA---HEALEDARE-----------QIELLEP-IRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 238 QNITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEID-DATANLRQFIDRQSfdpERMEELNSKLEVFHRLARKYRTQ 316
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLE---RELEERERRRARLEALLAALGLP 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 503974228 317 PETLKEEYEA----WQSELEQLHQLEdpETLAEQVEKSHEEFLEKAQHLDNIRRE 367
Cdd:COG4913 375 LPASAEEFAAlraeAAALLEALEEEL--EALEEALAEAEAALRDLRRELRELEAE 427
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
2-50 |
7.92e-05 |
|
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: 43.99 E-value: 7.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503974228 2 LTHLTLINF-ALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERT 50
Cdd:cd03278 1 LKKLELKGFkSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQS 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-387 |
9.17e-05 |
|
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: 45.44 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 82 DHELDDDSGEIhlrrvifaTGRSKAWVNGRPSSLSELKELGRLLVQLYSQHSQQQLLeppypKHWLDRYNNFYAEANDVR 161
Cdd:TIGR02169 645 EGELFEKSGAM--------TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL-----QSELRRIENRLDELSQEL 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 162 EAYSTWQRTIRLHQAALDAQATRLQRigtlehQIEELEEVIQTDYKEIEQEFDRLSHHEHIMQDCSYSLNVLDEAE---- 237
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKE------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndle 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 238 --------QNITQEMSSI---IRRLESHAGRSEQ-LSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEV 305
Cdd:TIGR02169 786 arlshsriPEIQAELSKLeeeVSRIEARLREIEQkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 306 FHRLARKYRTQPETLKEEYEAWQSELEQL-HQLEDPETLAEQVEKSheefLEKAQHLDNIRRESAAPLAKQLTEQVKPLA 384
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELeAQLRELERKIEELEAQ----IEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
...
gi 503974228 385 LPE 387
Cdd:TIGR02169 942 EDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
113-383 |
9.34e-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: 45.43 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 113 SSLSELKELGRLLVQLYSQHSQQQLLEppypkhwLDRYNNFYAEANDVREAYSTWQRTIRLHQAALDAQATRL----QRI 188
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISAL-------RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 189 GTLEHQIEELEEVIQTDYKEIEQEFDRLSHHEHIMQDCSYSLNVLDEAEQNITQEMSSIIRRLE----SHAGRSEQLSEI 264
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdleeQIEELSEDIESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 265 YNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLARKYRTQPETLKEEYEAWQSELEQLHQ-------- 336
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELrleglevr 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 503974228 337 -LEDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLaKQLTEQVKPL 383
Cdd:TIGR02168 938 iDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL-KRLENKIKEL 984
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-69 |
1.05e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503974228 2 LTHLTLINF-ALADHLAIDIEQGFNVLTGETGAGKSLLLDALS-ACLGE--------RTDTNYVRYGSDKADITAVFT 69
Cdd:cd03240 1 IDKLSIRNIrSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKyALTGElppnskggAHDPKLIREGEVRAQVKLAFE 78
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-379 |
1.67e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 146 WLDRYNNFYAEANDVREAYSTWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLShhehimQD 225
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE------QD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 226 CSYSLNVLDEAEQNITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSfdpermEELNSKLEV 305
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL------EAEAELAEA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503974228 306 FHRLARKYRTQPETLKEEYEAWQSELEQLHQLEDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAKQLTEQ 379
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
158-349 |
4.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 158 NDVREAYSTWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLSHHEHIMQDCSYSLNVLD--E 235
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 236 AEQNITQEMSSIIRRLESHAGRSEQLSEIYNSLLNAQSEIDDATANLRQFIDRQSFD-PERMEELNSKLEVFHRLARKYR 314
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|....*
gi 503974228 315 TQPETLKEEYEAWQSELEQLHQLEDPETLAEQVEK 349
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-92 |
4.47e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 2 LTHLTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVR----YGSDKADITAVFTYQNNSPEA 77
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEedfyLGDDPDLPEIEIELTFGSLLS 82
|
90
....*....|....*
gi 503974228 78 KWLQDHELDDDSGEI 92
Cdd:COG3593 83 RLLRLLLKEEDKEEL 97
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
24-128 |
6.00e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 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: 213240 [Multi-domain] Cd Length: 251 Bit Score: 41.90 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 24 FNVLTGETGAGKSLLLDALSACLGeRTDTNYVR-------------YGSDKADITAVFtyqNNSPEAKWLQDHElddDSG 90
Cdd:cd03273 27 FNAITGLNGSGKSNILDAICFVLG-ITNLSTVRasnlqdliykrgqAGITKASVTIVF---DNSDKSQSPIGFE---NYP 99
|
90 100 110
....*....|....*....|....*....|....*...
gi 503974228 91 EIHLRRVIFATGRSKAWVNGRPSSLSELKELGRlLVQL 128
Cdd:cd03273 100 EITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQ-SVQL 136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-403 |
6.79e-04 |
|
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: 42.74 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 2 LTHLTLINF-ALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGER-----------------TDTnyvRYGSDKAD 63
Cdd:TIGR02168 2 LKKLELAGFkSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQsakalrggkmedvifngSET---RKPLSLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 64 ITAVFtyqNNSpeakwlqDHELD-DDSGEIHLRRVIFATGRSKAWVNGRPSSLSE------------------------- 117
Cdd:TIGR02168 79 VELVF---DNS-------DGLLPgADYSEISITRRLYRDGESEYFINGQPCRLKDiqdlfldtglgkrsysiieqgkise 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 118 ----------------------------------------------LKELGRLLVQLYSQHSQ-QQLLEppypKH----- 145
Cdd:TIGR02168 149 iieakpeerraifeeaagiskykerrketerklertrenldrlediLNELERQLKSLERQAEKaERYKE----LKaelre 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 146 -----WLDRYNNFYAEANDVREAYSTWQRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLSHHe 220
Cdd:TIGR02168 225 lelalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 221 himqdcsysLNVLDEAEQNITQEMSSIIRRLESHAGRSEQLSEIYNSLlnaQSEIDDATANLRQFidrqsfdPERMEELN 300
Cdd:TIGR02168 304 ---------KQILRERLANLERQLEELEAQLEELESKLDELAEELAEL---EEKLEELKEELESL-------EAELEELE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 301 SKLEVFHRLARKYRTQPETLKEEYEAWQSELEQLH-QLEDPETLAEQVEKSHEEFL-EKAQHLDNIRRESAAPLAKQLTE 378
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNnEIERLEARLERLEDRRERLQqEIEELLKKLEEAELKELQAELEE 444
|
490 500
....*....|....*....|....*
gi 503974228 379 QVKPLALPEAHFEFKFEPLEQPTAE 403
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREE 469
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
186-367 |
1.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 186 QRIGTLEHQIEELEEVIQTDYKEIEQEFDRLSHHEHIMQDCSYSLNVLDEAEQNITQEMSSIIRRLESHAGRSE------ 259
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptctq 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 260 QLSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLARKYRTQPETLK---EEYEAWQSELEQLHq 336
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLItlvDKAKKVKAAIEELQ- 371
|
170 180 190
....*....|....*....|....*....|.
gi 503974228 337 lEDPETLAEQVEKSHEEFLEKAQHLDNIRRE 367
Cdd:PHA02562 372 -AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
175-374 |
1.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 175 QAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLSHHEHIMQDCSYSLN-VLDEAEQNiTQEMSSIIRRLES 253
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDdLLAEAGLD-DADAEAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 254 HAGRSEQ----LSEIYNSLLNAQSEIDDATANLRQFIDRQSFDPERMEELNSKLEVFHRLARKYRTQPETLKEEYEAWQS 329
Cdd:PRK02224 319 LEDRDEElrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503974228 330 ELEQLH-QLEDPETLAEQVEKSHEEFLEKAQHLDNIRRESAAPLAK 374
Cdd:PRK02224 399 RFGDAPvDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
428-505 |
1.22e-03 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 41.67 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 428 SGGELSRIAL---VMQvmnaektEAEVLVFDEIDVGISGGTAEVVGRLLADLAQHVQLLCITHQAQVAAQSDQHLLVKKQ 504
Cdd:COG4988 475 SGGQAQRLALaraLLR-------DAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
.
gi 503974228 505 Q 505
Cdd:COG4988 548 R 548
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
24-120 |
1.82e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 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: 213242 [Multi-domain] Cd Length: 247 Bit Score: 40.25 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 24 FNVLTGETGAGKSLLLDALSACLGERtdTNYVR--------YG-------SDKADITAVFTyqnnspeakwlqdheldDD 88
Cdd:cd03275 24 FTCIIGPNGSGKSNLMDAISFVLGEK--SSHLRsknlkdliYRarvgkpdSNSAYVTAVYE-----------------DD 84
|
90 100 110
....*....|....*....|....*....|..
gi 503974228 89 SGEIHLRRVIFATGRSKAWVNGRPSSLSELKE 120
Cdd:cd03275 85 DGEEKTFRRIITGGSSSYRINGKVVSLKEYNE 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
5-263 |
2.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 5 LTLINFALADHLAIDIEQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVRYgsdkaditavFTYQNNSPEakwLQDHE 84
Cdd:COG4717 6 LEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEADEL----------FKPQGRKPE---LNLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 85 LDDDSGEIHLRRVIFATGRSKawvngrpssLSELKELGRLLVQLysqhsQQQLLEppypkhwLDRYNNFYAEANDVREAY 164
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL---------QEELEELEEELEEL-----EAELEE-------LREELEKLEKLLQLLPLY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 165 STW---QRTIRLHQAALDAQATRLQRIGTLEHQIEELEEVIQTDYKEIEQEFDRLS-HHEHIMQDCSYSLNVLDEAEQNI 240
Cdd:COG4717 132 QELealEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL 211
|
250 260
....*....|....*....|...
gi 503974228 241 TQEMSSIIRRLESHAGRSEQLSE 263
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLEN 234
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
361-529 |
2.49e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 361 LDNIRRESAAPLaKQLTEQVKpLALPEAHfEFKFEPLEQPTaeglsfIQLLFTANKGIPPQPlARVASGGELSRIALVMQ 440
Cdd:COG4637 203 LATLRETHPERF-ERILEALR-DAFPGFE-DIEVEPDEDGR------VLLEFREKGLDRPFP-ARELSDGTLRFLALLAA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 441 VMNAEktEAEVLVFDEIDVGISGGTAEVVGRLLADLAQHVQLLCITHQAQVAAQ--SDQHLLVKKQqtDPASSTIVELDE 518
Cdd:COG4637 273 LLSPR--PPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDAlePEEVLVLERE--DDGETRIRRLSD 348
|
170
....*....|.
gi 503974228 519 NQIIFELARMS 529
Cdd:COG4637 349 LELPEWLEGYS 359
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
428-497 |
2.72e-03 |
|
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: 39.37 E-value: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503974228 428 SGGE--LSRIALVMQVMNAEKteAEVLVFDEIDVGISGGTAEVVGRLLADLAQHVQLLCITHQAQVAAQSDQ 497
Cdd:cd03278 115 SGGEkaLTALALLFAIFRVRP--SPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADR 184
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-354 |
7.30e-03 |
|
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: 39.28 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 148 DRYNNFYAEANDVREAYSTWQRTIRLHQAAL-DAQATRLQ---RIGTLEHQIEELEEVIQTDYKEIEQEFDRLSHHEHIM 223
Cdd:TIGR02169 287 EEQLRVKEKIGELEAEIASLERSIAEKERELeDAEERLAKleaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 224 QDCSYSLNVLDEAEQ--------------NITQEMSSIIRRLESHAGRSEQLSEiynSLLNAQSEIDDATANLRQFIDRQ 289
Cdd:TIGR02169 367 EDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSE---ELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503974228 290 SFDPERMEELNSKLEVFHRLARKYRTQPETLKEEYEAWQSELEQLH-QLEDPETLAEQVEKSHEEF 354
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrELAEAEAQARASEERVRGG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-367 |
8.38e-03 |
|
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: 39.27 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 147 LDRYNNFYAEANDVREAYSTWQR-------TIRLHQAALDAQATRLQ--------RIGTLEHQIEELEEVIQTDYKEIEQ 211
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQeleekleELRLEVSELEEEIEELQkelyalanEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 212 EFDRLSHHEHIMQDCSYSLNVLDEAEQNITQEMSSIIRRLESHAGRSEQLSEIYNSL----LNAQSEIDDATANLRQFID 287
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqlETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503974228 288 RQSFDPERMEELNSKLEVFH-----RLARKYRTQPETLKEEYEAWQSELEQLhqLEDPETLAEQVEKSHEEFLEKAQHLD 362
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEEL--QEELERLEEALEELREELEEAEQALD 478
|
....*
gi 503974228 363 NIRRE 367
Cdd:TIGR02168 479 AAERE 483
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-70 |
9.19e-03 |
|
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: 37.34 E-value: 9.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503974228 21 EQGFNVLTGETGAGKSLLLDALSACLGERTDTNYVRY----GSDKADITAVFTY 70
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSgvkaGCIVAAVSAELIF 73
|
|
| |
