|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-696 |
5.81e-128 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 403.16 E-value: 5.81e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAGDRKPLGRAEV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 81 TLTIDNSDGKLPIEYSEVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSGIGREMHIIVGQGKLSEILESRPEERRAY 160
Cdd:COG1196 81 SLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 161 IEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIVTLRAE 240
Cdd:COG1196 161 IEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 241 WEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERARTSGHEVpy 320
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 321 sgadpEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAA 400
Cdd:COG1196 319 -----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 401 TARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHEREVY 480
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 481 TLESRIETLRQAAPRASASELLSGQ---GWRGLSGEVHPDPGCEAAVAAALGAHAEAVVGPASEEALRGLLGAEVERTVV 557
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEaeaDYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 558 MEDAGRESRWRLEAELPEGAQWLL-------DRLSVEPSVAVAINRLLADVALVPDWEAARAAVEADpRVRAVTPEGDLV 630
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLpldkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGD-TLLGRTLVAARL 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2713584088 631 GQGWAQVGHAAASSVEVAGAIARAEEELAAARARLGELSGTVEGAGLAAQEARIEAASATAALREH 696
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-638 |
3.06e-114 |
|
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: 370.93 E-value: 3.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAGDRKPLGRAEVTL 82
Cdd:TIGR02168 2 LKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 83 TIDNSDGKLP-IEYSEVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSGIGREMHIIVGQGKLSEILESRPEERRAYI 161
Cdd:TIGR02168 82 VFDNSDGLLPgADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRAIF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 162 EEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIVTLRAEW 241
Cdd:TIGR02168 162 EEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 242 EDADLQAEALKERVAALTEEAEERGAEqmgWEEDLARIVPREE---AAQKLWFRLSTLAERVHATSRIAAERARtsghev 318
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEK---LEELRLEVSELEEeieELQKELYALANEISRLEQQKQILRERLA------ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 319 pYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVA---QREDTARRAEREHLAQIKALADHREGVVRLLAAE 395
Cdd:TIGR02168 313 -NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsleAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 396 ENHAATARGAAEELERQRGAEAEAQARLRQ---------AEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLE 466
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQeieellkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 467 QVRAEQREHEREVYTLESRIETLR------QAAPRASASELLSGQGWRGLSGEV----HPDPGCEAAVAAALGAHAEAVV 536
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLErlqenlEGFSEGVKALLKNQSGLSGILGVLseliSVDEGYEAAIEAALGGRLQAVV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 537 GPASEEALRG---LLGAEVERTVVME------DAGRESRWRLEAELPEGAQWLLDRLSVEPSVAVAINRLLADVALVPDW 607
Cdd:TIGR02168 552 VENLNAAKKAiafLKQNELGRVTFLPldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL 631
|
650 660 670
....*....|....*....|....*....|..
gi 2713584088 608 -EAARAAVEADPRVRAVTPEGDLVGQGWAQVG 638
Cdd:TIGR02168 632 dNALELAKKLRPGYRIVTLDGDLVRPGGVITG 663
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-505 |
3.12e-68 |
|
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: 242.96 E-value: 3.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 2 HLKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAGdrKPLGRAEVT 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSG--AFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 82 LTIDNSDGKLPIEYSEVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSGIGREMHIIVGQGKLSEILESRPEERRAYI 161
Cdd:pfam02463 79 ITFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 162 EEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIVTLRAEW 241
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 242 EDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERARTSGHEVpys 321
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 322 gadPEALELRAQEADAQFEALEEAAEIARERLEVL----LEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEen 397
Cdd:pfam02463 316 ---LKESEKEKKKAEKELKKEKEEIEELEKELKELeikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 398 haataRGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHER 477
Cdd:pfam02463 391 -----KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
490 500
....*....|....*....|....*...
gi 2713584088 478 EVYTLESRIETLRQAAPRASASELLSGQ 505
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-93 |
1.93e-52 |
|
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: 179.58 E-value: 1.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAGDRKPLGRAEVTL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90
....*....|.
gi 2713584088 83 TIDNSDGKLPI 93
Cdd:cd03278 81 TFDNSDGRYSI 91
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-514 |
4.00e-46 |
|
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: 177.18 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 2 HLKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAGDRKPlGRAEVT 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSG-NEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 82 LTIDNSDGKLPIEYsEVSVTRRMFRDG-ASEYEINGAKARLMDIQELLSDSGIGREMHIIVGQGKLSEILESRPEERRAY 160
Cdd:TIGR02169 80 VTFKNDDGKFPDEL-EVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 161 IEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIVTLRAE 240
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 241 WEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPR------EEAAQKLWFRLSTLAERVHATSRI-------- 306
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeEEQLRVKEKIGELEAEIASLERSIaekerele 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 307 -AAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHR 385
Cdd:TIGR02169 319 dAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 386 EGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERL 465
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2713584088 466 EQVRAEQREHEREVYTLESRIETLRQAAPRASASELLSGQGWRGLSGEV 514
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-150 |
1.22e-24 |
|
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: 103.53 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATTL-KFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAG--AGDRKplgr 77
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRgqAGITK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2713584088 78 AEVTLTIDNSD-GKLPIEYS---EVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSGIGRE-MHIIVGQGKLSEIL 150
Cdd:cd03273 77 ASVTIVFDNSDkSQSPIGFEnypEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNnPHFLIMQGRITKVL 154
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-133 |
9.09e-18 |
|
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: 83.39 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEqGAKTLRGGKMQDVIFAGAGDRKPLGRAEVTL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGE-KSSHLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2713584088 83 TIDNSDGklpieysEVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSGI 133
Cdd:cd03275 80 VYEDDDG-------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINI 123
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-197 |
3.13e-17 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 80.23 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 6 LTLKGFKSFASaTTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQ--GAKTLRGGKMQDVIFAGAGDRKPLGRAEVTLT 83
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKtsRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 84 IDNSDGKLPIEYSEVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSGIGREMHIIVGQGKLSEILESRPEERRAYIEE 163
Cdd:pfam13476 80 NNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180 190
....*....|....*....|....*....|....
gi 2713584088 164 AagvLKHRRRKEKAQRKLAGMQGNLDRLRDLTEE 197
Cdd:pfam13476 160 A---LEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-149 |
5.82e-16 |
|
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: 78.07 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLK-FEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKtLRGGKMQDVIFAGAGdrKPLGRAEVT 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEpFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTH-LREEQRQALLHEGSG--PSVMSAYVE 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2713584088 82 LTIDNSDGKLPIEYSEVSVtRRMFRDGASEYEINGAKARLMDIQELLSDSGIGRE-MHIIVGQGKLSEI 149
Cdd:cd03272 78 IIFDNSDNRFPIDKEEVRL-RRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSnPYYIVPQGKINSL 145
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-87 |
7.02e-15 |
|
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: 73.11 E-value: 7.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVifaGAGDRKPLGRAEVTL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLA---GGGVKAGINSASVEI 77
|
....*
gi 2713584088 83 TIDNS 87
Cdd:cd03239 78 TFDKS 82
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-205 |
8.94e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 70.81 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 2 HLKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEqgaKTLRGGKMQDVIFagagdRKPLGRAEVT 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYG---KARSRSKLRSDLI-----NVGSEEASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 82 LTIDNSDGKLpieysevSVTRRmfrdgaseyeingakarlmdiqellsdsgigremhiivgQGKLSEILESRPEERRAYI 161
Cdd:COG0419 73 LEFEHGGKRY-------RIERR---------------------------------------QGEFAEFLEAKPSERKEAL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2713584088 162 EEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPL 205
Cdd:COG0419 107 KRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQL 150
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-131 |
2.43e-12 |
|
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: 68.88 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASaTTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGgkmQDviFAGAGDRKPLgRAEV 80
Cdd:COG3593 1 MKLEKIKIKNFRSIKD-LSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDE---ED--FYLGDDPDLP-EIEI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2713584088 81 TLTIDnsdgklpieysevSVTRRMFRDGASEYEINGAKARLMDIQELLSDS 131
Cdd:COG3593 74 ELTFG-------------SLLSRLLRLLLKEEDKEELEEALEELNEELKEA 111
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-107 |
1.25e-11 |
|
ATP-binding cassette domain of eukaryotic SMC4 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: 213241 [Multi-domain] Cd Length: 212 Bit Score: 64.62 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLK-FEPGICAVVGPNGSGKSNVVDALAWVMGEQgAKTLRGGKMQDVIFagagdrkplgraevt 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGpFHKSFSAIVGPNGSGKSNVIDSMLFVFGFR-ASKMRQKKLSDLIH--------------- 66
|
90 100
....*....|....*....|....*.
gi 2713584088 82 ltidNSDGKLPIEYSEVSVTRRMFRD 107
Cdd:cd03274 67 ----NSAGHPNLDSCSVEVHFQEIID 88
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-487 |
1.64e-11 |
|
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: 67.77 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 171 RRRKEKAQRKLAGMQGNLDRLrdltEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIVTLRAEWEDADLQAEA 250
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 251 LKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERARTSGHEVPYSGADPEALEL 330
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 331 RAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARgaaeelE 410
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS------E 947
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713584088 411 RQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIE 487
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-104 |
1.64e-10 |
|
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: 61.08 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATTLKFEPGICAVVGPNGSGKSNVVDALAWVM-GEQGAKTLRGGKMQDVIFAGAgdrkplGRAEVT 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGE------VRAQVK 74
|
90 100
....*....|....*....|...
gi 2713584088 82 LTIDNSDGKlpieysEVSVTRRM 104
Cdd:cd03240 75 LAFENANGK------KYTITRSL 91
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-103 |
2.95e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 62.64 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATtLKFEPgICAVVGPNGSGKSNVVDALAWV--MGEQGAKT---LRGGkMQDVIFAGAGDRKPlgR 77
Cdd:COG4637 2 ITRIRIKNFKSLRDLE-LPLGP-LTVLIGANGSGKSNLLDALRFLsdAARGGLQDalaRRGG-LEELLWRGPRTITE--P 76
|
90 100
....*....|....*....|....*.
gi 2713584088 78 AEVTLTIDNSDGKlPIEYsEVSVTRR 103
Cdd:COG4637 77 IRLELEFAEEDER-DLRY-ELELGLP 100
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-161 |
3.19e-10 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 62.48 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 2 HLKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALaWVMGeqGAKTLRGGKMQDVIFAGAgdrkplGRAEVT 81
Cdd:COG1195 1 RLKRLSLTNFRNYESLE-LEFSPGINVLVGPNGQGKTNLLEAI-YLLA--TGRSFRTARDAELIRFGA------DGFRVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 82 LTIDNSDGKLPIEYSevsvtrrMFRDGASEYEINGAKA-RLMDIQELLSDSGIGREMHIIVGQGklseilesrPEERRAY 160
Cdd:COG1195 71 AEVERDGREVRLGLG-------LSRGGKKRVRINGKPVrRLSDLAGLLPVVLFSPEDLRLVKGG---------PSERRRF 134
|
.
gi 2713584088 161 I 161
Cdd:COG1195 135 L 135
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-49 |
5.30e-10 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 60.78 E-value: 5.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASAT-TLKFEPGICAVVGPNGSGKSNVVDALAWVMG 49
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEiDFDNPPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-85 |
1.20e-09 |
|
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: 57.75 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 5 SLTLKGFKSFASATTLKF-EPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGkmqdviFAGAGDRKPLGRAEVTLT 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFgEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS------GVKAGCIVAAVSAELIFT 74
|
..
gi 2713584088 84 ID 85
Cdd:cd03227 75 RL 76
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-120 |
2.82e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 59.40 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALaWVMGEqgAKTLRGGKMQDVIFAGAgdrkplGRAEV 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELD-LELSPGVNVLVGENGQGKTNLLEAI-YLLAP--GRSHRTARDKELIRFGA------EAAVI 70
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2713584088 81 TLTIDNSDGKLPIEYSEVSVTRRMFRdgaseyeINGAKAR 120
Cdd:PRK00064 71 HGRVEKGGRELPLGLEIDKKGGRKVR-------INGEPQR 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
148-492 |
3.94e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 148 EILESRPEERRAYIEEAAGVLKHRRRKEKAQRKLAgmQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARL 227
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 228 RLAGDRIVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIA 307
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 308 AERA------RTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEE--VAQREDTARRAEREHLAQIK 379
Cdd:COG1196 568 AAKAgratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlVAARLEAALRRAVTLAGRLR 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 380 ALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEgewEEAKDRQEQARRQRAPLEEAGERAGAEQR 459
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAEEERLEEELEEE 724
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2713584088 460 AAEERLEQVRAEQREHEREVY------------------TLESRIETLRQA 492
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEelleeealeelpeppdleELERELERLERE 775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-492 |
6.11e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALAWVMgeqgAKTLRggKMQDVIFAGAGDRKPLGRAEV 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRT-IEFSPGLNVIYGPNEAGKSTLLAFIRAML----LERLE--KEADELFKPQGRKPELNLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 81 tltidnsdgklpieysevsvtrrmfrdGASEYEINGAKARLMDIQELLsdsgigREMHIIVGQGKLSEILESRPEERRAY 160
Cdd:COG4717 74 ---------------------------KELEEELKEAEEKEEEYAELQ------EELEELEEELEELEAELEELREELEK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 161 IEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIVTLRAE 240
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 241 WEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLS-------------------------T 295
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiagvlF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 296 LAERVHATSRIAAERARTSGHEVPYSGADPEALE-LRAQEADAQFEALEEAAEIARERLEVLLEEVAQ-REDTARRAERE 373
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEeLEEEELEELLAALGLPPDLSPEELLELLDRIEElQELLREAEELE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 374 HLAQIKALADHREGVVRLLAAEENHAATARG-AAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARrqrapLEEAGE 452
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAALeQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELE 435
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2713584088 453 RAGAEQRAAEERLEQVRAEQREHEREVYTLES--RIETLRQA 492
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQE 477
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-607 |
1.01e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.83 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATTLKF--EPGICAVVGPNGSGKSNVVDALAWVM-GEQGAKTlrggkmQDVIFAGAGDRKPLGR 77
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYALyGKLPRRS------EVIRSLNSLYAAPSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 78 AEVTLTIDnSDGKLPIEYSEVSVTRRmFRDGASEYEI---------NGAKARLMDIQELLSD-SGIGREMH---IIVGQG 144
Cdd:TIGR00618 75 AFAELEFS-LGTKIYRVHRTLRCTRS-HRKTEQPEQLyleqkkgrgRILAAKKSETEEVIHDlLKLDYKTFtrvVLLPQG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 145 KLSEILESRPEERRAYIEEAAGVLKHRRR--KEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATV-QAT 221
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLalMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELkHLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 222 LRDARLRLAGDRIVTLRAEWEDADLQAEALKERVAALTE-EAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERV 300
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 301 HATSRIA-AERARTSGHevpYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREdtarRAEREHLAQIK 379
Cdd:TIGR00618 313 HTELQSKmRSRAKLLMK---RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ----HTLTQHIHTLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 380 ALADHREGVVRLLAA------EENHAATARGAAEELERQRGAEAEAQARLRQaegeweEAKDRQEQARRQRAPLEEAGER 453
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKeldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQ------RYAELCAAAITCTAQCEKLEKI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 454 AGAE-QRAAEERLEQVRAEQREHEREVytlesrietlRQAAPRASASELLSGQgwrglsgevhPDPGCEAAVAAALGAHA 532
Cdd:TIGR00618 460 HLQEsAQSLKEREQQLQTKEQIHLQET----------RKKAVVLARLLELQEE----------PCPLCGSCIHPNPARQD 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 533 EAVVGPASEEALRGL-----LGAEVERTVVMEDAGRESRWRLEAELPEGAQWLLDRLSVEPSVAVAINRLLADVALVPDW 607
Cdd:TIGR00618 520 IDNPGPLTRRMQRGEqtyaqLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL 599
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-489 |
3.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 155 EERRAYIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRI 234
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 235 VTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERARTS 314
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 315 GHEVPYSGADP---EALELRAQEADAQFEALEEAAEIARERLEVLLE--EVAQREDTARRAEREHLAQIKALADHREGVV 389
Cdd:COG1196 606 SDLREADARYYvlgDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgeGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 390 RLLAAEENHAATARGAAEELERQRgaeAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVR 469
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEEREL---AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
330 340
....*....|....*....|
gi 2713584088 470 AEQrehEREVYTLESRIETL 489
Cdd:COG1196 763 EEL---ERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-493 |
5.46e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALawVMGEQGAKTLrGGKMQDVIFAGAGDrkplgrAEV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADAD-LRLEDGVTVIHGVNGSGKSSLLEAC--FFALYGSKAL-DDTLDDVITIGAEE------AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 81 TLTIDNSDGKLPIEysevsvtRRMFRDGAS-----------EYEINGAKARLMDIQELLSDSGIGREMHIIVGQGKLSEI 149
Cdd:PRK02224 71 ELWFEHAGGEYHIE-------RRVRLSGDRattakcvletpEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEVNKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 150 LESRPEERRAYIEEAAGVLKHRRRKEKA-------QRKLAGMQGNLDRLRDLTEE------------LSRQLKPLARQ-A 209
Cdd:PRK02224 144 INATPSDRQDMIDDLLQLGKLEEYRERAsdarlgvERVLSDQRGSLDQLKAQIEEkeekdlherlngLESELAELDEEiE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 210 EAAQRAATVQATLRDARLRLAG-----DRIVTLRAEWED-------ADLQAEALKERVAALTEEAEERGAEQMGWEEDLA 277
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEheerrEELETLEAEIEDlretiaeTEREREELAEEVRDLRERLEELEEERDDLLAEAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 278 RIVPREEAAQKlwfRLSTLAERVHAT-SRIAAERARTSGHEVPYSGADPEALELRAQEADAQFEALEeaaeiarerlevl 356
Cdd:PRK02224 304 LDDADAEAVEA---RREELEDRDEELrDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE------------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 357 LEEVAQREDTARRAEREHLAQI-KALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKD 435
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELeEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 436 RQEQARRQRA--PLEEAGERAGAEQRaaEERLEQVRAEQREHEREVYTLESRIETLRQAA 493
Cdd:PRK02224 448 LLEAGKCPECgqPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERAEDLV 505
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-47 |
7.48e-08 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 54.66 E-value: 7.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2713584088 2 HLKSLTLKGFKSFASATTLKFEPGIC------AVVGPNGSGKSNVVDALAWV 47
Cdd:COG1106 1 MLISFSIENFRSFKDELTLSMVASGLrllrvnLIYGANASGKSNLLEALYFL 52
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
202-698 |
1.18e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 55.26 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 202 LKPLARQAEAAQRAATVQATLRD------------ARLRLAG-------------DRIVTLRA---EWEDADLQAEALKE 253
Cdd:COG3321 803 LTGLVRQCLAAAGDAVVLPSLRRgedelaqlltalAQLWVAGvpvdwsalypgrgRRRVPLPTypfQREDAAAALLAAAL 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 254 RVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERARTS--GHEVPYSGADPEALELR 331
Cdd:COG3321 883 AAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLalAAAAAAAAAALAAAEAG 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 332 AQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARGAAEELER 411
Cdd:COG3321 963 ALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAA 1042
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 412 QRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETLRQ 491
Cdd:COG3321 1043 AAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAA 1122
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 492 AAPRASASELLSGQGWRGLSGEVHPDPGCEAAVAAALGAHAEAVVGPASEEALRGLLGAE---VERTVVMEDAGRESRWR 568
Cdd:COG3321 1123 ALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAaalAAALAGLAALLLAALLA 1202
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 569 LEAELPEGAQWLLDRLSVEPSVAVAINRLLADVALVPDWEAARAAVEADPRVRAVTPEGDLVGQGWAQVGHAAASSVEVA 648
Cdd:COG3321 1203 ALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAA 1282
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2713584088 649 GAIARAEEELAAARARLGELSGTVEGAGLAAQEARIEAASATAALREHDG 698
Cdd:COG3321 1283 AALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAA 1332
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-87 |
2.67e-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: 51.44 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGF---KSFasatTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAgdrkplGRAE 79
Cdd:cd03276 1 IESITLKNFmchRHL----QIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGE------SSAK 70
|
....*...
gi 2713584088 80 VTLTIDNS 87
Cdd:cd03276 71 ITVTLKNQ 78
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-505 |
3.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 352 RLEVLLEEVAQREDTARRAEREhLAQIKALADHREGVVRLLAAEENHA------ATARGAAEELERQRGAEAEAQARLRQ 425
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER-LEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 426 AEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVR-----AEQREHEREVYTLESRIETLRQAAPRASASE 500
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaAEDLARLELRALLEERFAAALGDAVERELRE 769
|
....*
gi 2713584088 501 LLSGQ 505
Cdd:COG4913 770 NLEER 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-492 |
3.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASaTTLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAgdrkplGRAEV 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGG------SGTEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 81 TLTIDNSDGKLPIeysevsvTRRMFRDGASEYEINGAKArlmdiqELLSDSGIGREMH-----------IIVGQGKLSEI 149
Cdd:PRK03918 74 ELKFEKNGRKYRI-------VRSFNRGESYLKYLDGSEV------LEEGDSSVREWVErlipyhvflnaIYIRQGEIDAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 150 LESRpEERRAYIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDL---TEELSRQLKplarqaeaaQRAATVQATLRdaR 226
Cdd:PRK03918 141 LESD-ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrTENIEELIK---------EKEKELEEVLR--E 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 227 LRLAGDRIVTLRAEWEDAD---LQAEALKERVAALTEEAEERGAEQMGWEEdlaRIVPREEAAQKLWFRLSTLAERVhat 303
Cdd:PRK03918 209 INEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEE---KIRELEERIEELKKEIEELEEKV--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 304 sriaaerartsghevpysgADPEALELRAQEadaqfealeeaaeiaRERLEVLLEEVAQREdtaRRAEREhlaqIKALAD 383
Cdd:PRK03918 283 -------------------KELKELKEKAEE---------------YIKLSEFYEEYLDEL---REIEKR----LSRLEE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 384 HREGVVRLLAAEENHAATargaAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLE-EAGERAGAEQRAAE 462
Cdd:PRK03918 322 EINGIEERIKELEEKEER----LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELE 397
|
490 500 510
....*....|....*....|....*....|
gi 2713584088 463 ERLEQVRAEQREHEREVYTLESRIETLRQA 492
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKA 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-500 |
5.29e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 247 QAEALKERVAALTEEAEERGAEQMGWEEDLARIvprEEAAQKLWFRLSTLAERVHATSRIA----AERARTS-----GHE 317
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKA---EEARKAEDAKRVEIARKAEDARKAEearkAEDAKKAeaarkAEE 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 318 VPYSGADPEALELR----AQEADAQFEALEEAAEIARERLEVL--LEEVAQREDTARRAEREHLAQI-----KALADHRE 386
Cdd:PTZ00121 1187 VRKAEELRKAEDARkaeaARKAEEERKAEEARKAEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEirkfeEARMAHFA 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 387 GVVRLLAAEENHAATARGAAEEL---------ERQRGAE-----AEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGE 452
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKkkadeakkaEEKKKADeakkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2713584088 453 RAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETLRQAAPRASASE 500
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-500 |
6.45e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 144 GKLSEILEsRPEERRAYIEE-AAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATL 222
Cdd:PRK02224 237 DEADEVLE-EHEERREELETlEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 223 RD---ARLRLAGDRIVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLarivprEEAAQKLWFRLSTLAEr 299
Cdd:PRK02224 316 REeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL------EEAREAVEDRREEIEE- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 300 vhATSRIAAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARER-----LEVLLEE---------VAQRED 365
Cdd:PRK02224 389 --LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeAEALLEAgkcpecgqpVEGSPH 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 366 TARRAE-REHLAQIKALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQR 444
Cdd:PRK02224 467 VETIEEdRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2713584088 445 APLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETLRQAAPRASASE 500
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA 602
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-44 |
7.02e-06 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 48.75 E-value: 7.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2713584088 1 MHLKSLTLKGFKSFaSATTLKFEPGICAVVGPNGSGKSNVVDAL 44
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEIDLDEDLTVLIGKNNSGKSSILEAL 43
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-158 |
1.11e-05 |
|
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: 47.58 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALAWVMGEQG-AKTLRGGKMQDVIFA--GAGDRKPLGRAE 79
Cdd:cd03241 1 LLELSIKNFALIEELE-LDFEEGLTVLTGETGAGKSILLDALSLLLGGRAsADLIRSGAEKAVVEGvfDISDEEEAKALL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2713584088 80 VTLTIDNSDgklpieysEVSVTRRMFRDGASEYEINGAKARLMDIQEllsdsgIGREMHIIVGQGKlsEILESRPEERR 158
Cdd:cd03241 80 LELGIEDDD--------DLIIRREISRKGRSRYFINGQSVTLKLLRE------LGSLLVDIHGQHD--HQNLLNPERQL 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-492 |
1.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 283 EEAAQKLWFRLSTLAERVHATSRIAAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQ 362
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 363 REDTARRAEREHLA----QIKALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRqaegewEEAKDRQE 438
Cdd:COG4913 321 LREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR------AEAAALLE 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2713584088 439 QARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETLRQA 492
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-120 |
1.38e-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: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 3 LKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALAWVmgeQGAKTLRGGKMQDVIFAGAgdrkplGRAEVTL 82
Cdd:cd03242 1 LKSLELRNFRNYAELE-LEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELIRWGA------EEAKISA 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 2713584088 83 TIDNSDGKLPIEYSEVSVTRRMFRdgaseyeINGAKAR 120
Cdd:cd03242 71 VLERQGGELALELTIRSGGGRKAR-------LNGIKVR 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-500 |
1.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 247 QAEALKERVAALTEEAEE-RGAEQMGWEEDLARivPREEAAQKLWFRLSTLAERVHATSRIAAERARTSGHEvpysGADP 325
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEkKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE----AKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 326 EALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARGA 405
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 406 AEElerQRGAEAEAQARLRQAegewEEAKDRQEQARRQRAPLEEAGERAGAEQ--RAAEERL--EQVRAEQREHEREVYT 481
Cdd:PTZ00121 1566 AEE---AKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIkaEELKKAEEEKKKVEQL 1638
|
250
....*....|....*....
gi 2713584088 482 LESRIETLRQAAPRASASE 500
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEE 1657
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
155-494 |
2.26e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 155 EERRAYIEEAagvLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAAT-VQATLRDArlrlagDR 233
Cdd:COG3096 278 NERRELSERA---LELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNlVQTALRQQ------EK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 234 IVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRiAAERART 313
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 314 SGHEVPYSgadPEALELRAQEADAQFEALEEAAEIARERLEVlleevaqrEDTARRAEREHLAQIKALADhreGVVRLLA 393
Cdd:COG3096 428 LCGLPDLT---PENAEDYLAAFRAKEQQATEEVLELEQKLSV--------ADAARRQFEKAYELVCKIAG---EVERSQA 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 394 AEenhaaTARGAAEELERQRgAEAEAQARLRQAEGEWEEAKDRQEQARRQ--------------RAPLEEAGERAGAEQR 459
Cdd:COG3096 494 WQ-----TARELLRRYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLleefcqrigqqldaAEELEELLAELEAQLE 567
|
330 340 350
....*....|....*....|....*....|....*
gi 2713584088 460 AAEERLEQVRAEQREHEREVYTLESRIETLRQAAP 494
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP 602
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-44 |
3.35e-05 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 46.58 E-value: 3.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2713584088 1 MHLKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDAL 44
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVD-LELSPGVNVIVGPNGQGKTNLLEAI 43
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
232-492 |
3.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 232 DRIVTLRAEWEDADLQAEALKERVAALTEEA----EERGAEQMGWEEDLARIvprEEAAQKLWFRLSTLAERVHATSRIA 307
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDAKKAEAArkaeEVRKAEELRKAEDARKA---EAARKAEEERKAEEARKAEDAKKAE 1227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 308 ----AERARTSGHEvpysgadpealelrAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALAD 383
Cdd:PTZ00121 1228 avkkAEEAKKDAEE--------------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 384 HREGvvrllAAEENHAATARGAAEElerQRGAEaEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEE 463
Cdd:PTZ00121 1294 EAKK-----AEEKKKADEAKKKAEE---AKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
250 260
....*....|....*....|....*....
gi 2713584088 464 RLEQVRAEQREHEREVYTLESRIETLRQA 492
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
6-94 |
3.43e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 45.34 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 6 LTLKGFKSFASATTLKFEP----GICAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMQDVIFAGAgdrkplGRAEVT 81
Cdd:cd03279 6 LELKNFGPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGE------DTAEVS 79
|
90
....*....|...
gi 2713584088 82 LTIDNSDGKLPIE 94
Cdd:cd03279 80 FTFQLGGKKYRVE 92
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-499 |
3.62e-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: 47.36 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 352 RLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWE 431
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2713584088 432 EAKDRQEQARRQRAPLEEAGERAGAE-------QRAAEERLEQVRAEQREHEREVYTLESRIETLRQAAPRASAS 499
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAEltllneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-275 |
4.80e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.84 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 28 AVVGPNGSGKSNVVDALAWVmgeqgaktlrGGKMQDVIFAGAGDRKPLGRAEVTLTIDNSDGKLPIEYSEvsvtrRMFRD 107
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFL----------ADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEI-----SEFLE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 108 GASEYEInGAKARLMDIQELLSDSGIGREMHIIvgqgkLSEILESRPEERRAYIEEAAGVLKHRRRKEKAQRKLAGMQgN 187
Cdd:pfam13304 68 DGVRYRY-GLDLEREDVEEKLSSKPTLLEKRLL-----LREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLI-S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 188 LDRLRDLTEELSRQLKPLARQAEAAqraatvQATLRDARLRLAGDRIVTLRAE----WEDADLQAEALKERVAALTEEAE 263
Cdd:pfam13304 141 GLLLLSIISPLSFLLLLDEGLLLED------WAVLDLAADLALFPDLKELLQRlvrgLKLADLNLSDLGEGIEKSLLVDD 214
|
250
....*....|..
gi 2713584088 264 ERGAEQMGWEED 275
Cdd:pfam13304 215 RLRERGLILLEN 226
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-479 |
5.51e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 145 KLSEILESRPEERRAyiEEAAGVLKHRRRKEKAQRKlAGMQGNLDRLRDLTEElSRQLKPLARQAEAAQRAATVQATLRD 224
Cdd:PTZ00121 1406 KADELKKAAAAKKKA--DEAKKKAEEKKKADEAKKK-AEEAKKADEAKKKAEE-AKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 225 ARlrlagdRIVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQklwfrLSTLAERVHATS 304
Cdd:PTZ00121 1482 AK------KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-----AKKAEEKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 305 RIAAERARTSgHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLA--QIKALA 382
Cdd:PTZ00121 1551 LKKAEELKKA-EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKAE 1629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 383 DHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARR-QRAPLEEAGERAGAEQRAA 461
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaAEALKKEAEEAKKAEELKK 1709
|
330
....*....|....*...
gi 2713584088 462 EERLEQVRAEQREHEREV 479
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEE 1727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-484 |
6.45e-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: 46.60 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 160 YIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRqlkplarqaeaaqraatvqatlrdaRLRLAGDRIVTLRA 239
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ-------------------------ELSDASRKIGEIEK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 240 EWEDADLQAEALKERVAALTEE----AEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLaervhatsriaaeRARTSG 315
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDL-------------EARLSH 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 316 HEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVA-----QREDTARRAEREhlAQIKALADHREGVVR 390
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQelqeqRIDLKEQIKSIE--KEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 391 LLAAEENHAATARGAAEELERQR-GAEA---EAQARLRQAEGEWEEAKDRQEQARRQRAPLE------EAGERAGAEQRA 460
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERdELEAqlrELERKIEELEAQIEKKRKRLSELKAKLEALEeelseiEDPKGEDEEIPE 948
|
330 340
....*....|....*....|....
gi 2713584088 461 AEERLEQVRAEQREHEREVYTLES 484
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEP 972
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-501 |
1.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 151 ESRPEERRAYIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQlkplarqaeaaqraatvqATLRDARLRLA 230
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA------------------AEAAKAEAEAA 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 231 GDRIVTLRAEWEDADLQAEALKERVAALTEEAEE-RGAEQMG--WEEDL--ARIVPREEAAQKLWFRLSTLAERVHATSR 305
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKkkAEEDKkkADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 306 IA--AERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVL---LEEVAQREDTARRAEREhlaqiKA 380
Cdd:PTZ00121 1436 AKkkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEA-----KK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 381 LADHREGVVRLLAAEENHAATARGAAEELerQRGAEAEAQARLRQAEgeweEAKDRQEQARRQRAPLEEagERAGAEQRA 460
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADELKKAE----ELKKAEEKKKAEEAKKAE--EDKNMALRK 1582
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2713584088 461 AEErLEQVRAEQREHEREVYTLESRI--ETLRQA-APRASASEL 501
Cdd:PTZ00121 1583 AEE-AKKAEEARIEEVMKLYEEEKKMkaEEAKKAeEAKIKAEEL 1625
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-506 |
1.72e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 1 MHLKSLTLKGFKSFASATtLKFEPGICAVVGPNGSGKSNVVDALAWVM-GEQgaktlRGGKMQDVIFAGAGD-------R 72
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSE-IEFDTGINIITGKNGAGKSSIVDAIRFALfTDK-----RTEKIEDMIKKGKNNlevelefR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 73 KPLGRAEVTLTIDNSdGKLPIEYSEVSVTRRMFRDGASEYEINGAKARLMDIQELLSDSgigremhIIVGQGKLSEILES 152
Cdd:PRK01156 75 IGGHVYQIRRSIERR-GKGSRREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDVFLNS-------IFVGQGEMDSLISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 153 RPEERRAYIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEaaqraatvQATLRDARLRLAGD 232
Cdd:PRK01156 147 DPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK--------QIADDEKSHSITLK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 233 RIVTLRAEWEDADLQAEALKE---RVAALTEEAEErgaeqmgWEEDLARIVPREEAAQKLWFRLSTLAERVhatSRIAAE 309
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSalnELSSLEDMKNR-------YESEIKTAESDLSMELEKNNYYKELEERH---MKIIND 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 310 RARTSGHEVPYSGADPEALELRAQeadaqfealeeaaeiareRLEVLLEEVAQREDTARRAEREHlaqikalADHREGVV 389
Cdd:PRK01156 289 PVYKNRNYINDYFKYKNDIENKKQ------------------ILSNIDAEINKYHAIIKKLSVLQ-------KDYNDYIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 390 RLLAAEE-NHaatargaaeELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQV 468
Cdd:PRK01156 344 KKSRYDDlNN---------QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
490 500 510
....*....|....*....|....*....|....*....
gi 2713584088 469 RAEQREHEREVYTLESRIETLRQAAPRASAS-ELLSGQG 506
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNmEMLNGQS 453
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
285-650 |
1.83e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 285 AAQKLWFRLSTLAERVHATSRI-------AAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLL 357
Cdd:COG3903 550 ALAPFWFLRGLLREGRRWLERAlaaageaAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAAL 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 358 EEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQ 437
Cdd:COG3903 630 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 438 EQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETLRQAAPRASASELLSGQGWRGLSGEVHPD 517
Cdd:COG3903 710 ALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAA 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 518 PGCEAAVAAALGAHAEAVVGPASEEALRGLLGAEVERTVVMEDAGRESRWRLEAELPEGAQWLLDRLSVEPSVAVAINRL 597
Cdd:COG3903 790 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAA 869
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2713584088 598 LADVALVPDWEAARAAVEADPRVRAVTPEGDLVGQGWAQVGHAAASSVEVAGA 650
Cdd:COG3903 870 LAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAA 922
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-493 |
3.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 389 VRLLAAEENHAATARGAAEELERQRgaEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQV 468
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELE--YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100
....*....|....*....|....*.
gi 2713584088 469 RAEQREHE-REVYTLESRIETLRQAA 493
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLEREL 354
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-500 |
3.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 145 KLSEILESRPEERRAyIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELsRQLKPLARQAEAAQRAATVQATLRD 224
Cdd:PTZ00121 1378 KKADAAKKKAEEKKK-ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 225 ARlrlagdRIVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARivpREEAAQKLWFRLSTLAERVHATS 304
Cdd:PTZ00121 1456 AK------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADE 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 305 RIAAERARTSgHEVPYSGADPEALELRaqEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAERehlAQIKALADH 384
Cdd:PTZ00121 1527 AKKAEEAKKA-DEAKKAEEKKKADELK--KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 385 REGVVRLLAAEENHAATARGAAEEL----------ERQRGAEAEAQARLRQAEGEWEEAKDRQEQARR---------QRA 445
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELkkaeeekkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeedkkkaEEA 1680
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2713584088 446 PLEEAGERAGAEQ--RAAEE--RLEQVRAEQREHEREVYTLESRIETLRQAAPRASASE 500
Cdd:PTZ00121 1681 KKAEEDEKKAAEAlkKEAEEakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
153-566 |
3.51e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.85 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 153 RPEERRAYIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGD 232
Cdd:COG3903 520 RLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAA 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 233 RIVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERAR 312
Cdd:COG3903 600 AAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAA 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 313 TSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLL 392
Cdd:COG3903 680 AAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAA 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 393 AAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQ 472
Cdd:COG3903 760 AAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAA 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 473 REHEREVYTLESRIETLRQAAPRASASELLSGQGWRGLSGEVHPDPGCEAAVAAALGAHAEAVVGPASEEALRGLLGAEV 552
Cdd:COG3903 840 AAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAA 919
|
410
....*....|....
gi 2713584088 553 ERTVVMEDAGRESR 566
Cdd:COG3903 920 AAAAAAAAAAAAAA 933
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
357-496 |
4.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 357 LEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATA-------------RGAAEELERQRGAEAEAQARL 423
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelerldassddlAALEEQLEELEAELEELEEEL 708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2713584088 424 RQAEGEWEEAKDRQEQARRQ----RAPLEEAGERAGAEQRA-AEERLEQVRAEQREhEREVYTLESRIETLRQAAPRA 496
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEEldelQDRLEAAEDLARLELRAlLEERFAAALGDAVE-RELRENLEERIDALRARLNRA 785
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-501 |
5.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 151 ESRPEERRAY-----IEEAAGVLKHRRRKEKAQRklagmqgnldrlrdlTEELSRQLKPLARQAEAAQRAATVQATLRDA 225
Cdd:PTZ00121 1211 ERKAEEARKAedakkAEAVKKAEEAKKDAEEAKK---------------AEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 226 RLRLAGDriVTLRAEWEDADlqaEALKERVAALTEEAEERGAEQMGWEEdlarIVPREEAAQKLWFRLSTLAERVHATSR 305
Cdd:PTZ00121 1276 EARKADE--LKKAEEKKKAD---EAKKAEEKKKADEAKKKAEEAKKADE----AKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 306 IAAERARTSGHEVPYSGADPEALELRAQEADAQFEALE--EAAEIARERLEVLLEEVAQREDTARRAEREHL----AQIK 379
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadeAKKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 380 ALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARlRQAEgeweEAKDRQEQARRQraplEEAGERAGAEQR 459
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA-KKAD----EAKKKAEEAKKA----DEAKKKAEEAKK 1497
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2713584088 460 AAEERLEQVRAEQREHEREVYTLESRIETLRQAAPRASASEL 501
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-396 |
5.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 156 ERRAYIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRAATVQATLRDARLRLAGDRIV 235
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 236 TLRAEWEDADLQAEALKERVAALteEAEERGAEQMGWEEDLARIvprEEAAQKLWFRLSTLAERVHATSRiAAERARTSG 315
Cdd:COG4913 299 ELRAELARLEAELERLEARLDAL--REELDELEAQIRGNGGDRL---EQLEREIERLERELEERERRRAR-LEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 316 HEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEvAQREDTARRAEREHLAQIKALADHREGVVRLLAAE 395
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-LRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
.
gi 2713584088 396 E 396
Cdd:COG4913 452 A 452
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
240-635 |
6.54e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.08 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 240 EWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLWFRLSTLAERVHATSRIAAERARTSGHEVP 319
Cdd:COG3903 533 RWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 320 YSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHA 399
Cdd:COG3903 613 AAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAA 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 400 ATARGAAEELERQRGAEAEAQARLRQAEGEWEEA-KDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHERE 478
Cdd:COG3903 693 ALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAAlLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAAL 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 479 VYTLESRIETLRQAAPRASASELLSGQGWRGLSGEVHPDPGCEAAVAAALGAHAEAVVGPASEEALRGLLGAEVERTVVM 558
Cdd:COG3903 773 AALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAA 852
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713584088 559 EDAGRESRWRLEAELPEGAQWLLDRLSVEPSVAVAINRLLADVALVPDWEAARAAVEADPRVRAVTPEGDLVGQGWA 635
Cdd:COG3903 853 ALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAA 929
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
306-478 |
6.74e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.97 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 306 IAAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHR 385
Cdd:PRK12678 52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 386 EGVVRllAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEwEEAKDRQEQARRQRAPLEEAGER-AGAEQRAAEER 464
Cdd:PRK12678 132 ERGEA--ARRGAARKAGEGGEQPATEARADAAERTEEEERDERR-RRGDREDRQAEAERGERGRREERgRDGDDRDRRDR 208
|
170
....*....|....
gi 2713584088 465 LEQVRAEQREHERE 478
Cdd:PRK12678 209 REQGDRREERGRRD 222
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-48 |
9.75e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 9.75e-04
10 20 30
....*....|....*....|....*....|.
gi 2713584088 19 TLKFEP-GICAVVGPNGSGKSNVVDALAWVM 48
Cdd:pfam13555 16 TIPIDPrGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-501 |
1.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 354 EVLLEEVAQREDTARRAEREHLAQI-KALADHREGVVRLLAAEENHAATARGA-----AEELERQRGAEAEAQARLRQAE 427
Cdd:PTZ00121 1132 EARKAEDARKAEEARKAEDAKRVEIaRKAEDARKAEEARKAEDAKKAEAARKAeevrkAEELRKAEDARKAEAARKAEEE 1211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2713584088 428 GEWEEAKdRQEQARRQRA--PLEEAGERAGAEQRAAEERLEQvraEQREHEREVYTLESRIETLRQAAPRASASEL 501
Cdd:PTZ00121 1212 RKAEEAR-KAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNE---EIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
167-491 |
1.24e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 167 VLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQL---KPLARQAEAAQRAATVQATLRDARLRLAGDRIVTL-RAEWE 242
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVerrRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELeRIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 243 DADLQAEALK-ERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLwfrlstlaervhatSRIAAERARTSGHEVPys 321
Cdd:pfam17380 357 ERKRELERIRqEEIAMEISRMRELERLQMERQQKNERVRQELEAARKV--------------KILEEERQRKIQQQKV-- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 322 gadpEALELRAQEADAQFEALEEAAEIARERLE-VLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAA 400
Cdd:pfam17380 421 ----EMEQIRAEQEEARQREVRRLEEERAREMErVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 401 TARgaaeELERQRGAEAEAQARLRQAEGEWEEakdrqeqarRQRAPLEEAGERAGAEQRAAEERLEQVRAEQrEHEREVY 480
Cdd:pfam17380 497 LEK----ELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEERRRIQ-EQMRKAT 562
|
330
....*....|.
gi 2713584088 481 TLESRIETLRQ 491
Cdd:pfam17380 563 EERSRLEAMER 573
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
252-490 |
1.93e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 252 KERVAALTEEAEERGAEQmgweEDLARIVPREEAAQKLWFRLSTLAERVH-ATSRIAAERARTSGHEVPYSGADPEALEL 330
Cdd:PRK02224 474 RERVEELEAELEDLEEEV----EEVEERLERAEDLVEAEDRIERLEERREdLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 331 RAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKAL-ADHREGVVRLlaaeenhaATARGAAEEL 409
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiADAEDEIERL--------REKREALAEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 410 ERQRGAE-AEAQARLRQAEGEWEEakDRQEQARRQRAPLEEAGERagaeqraAEERLEQVRAEQREHEREVYTLESRIET 488
Cdd:PRK02224 622 NDERRERlAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQ-------VEEKLDELREERDDLQAEIGAVENELEE 692
|
..
gi 2713584088 489 LR 490
Cdd:PRK02224 693 LE 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-489 |
2.01e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 143 QGKLSEILESRPEERRAyIEEAAGVLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSR--QLKPLARQAEAAQRAATVQA 220
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 221 TLRDaRLRLAGDriVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIvprEEAAQKLWFRLSTLAERV 300
Cdd:PTZ00121 1534 KKAD-EAKKAEE--KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA---EEARIEEVMKLYEEEKKM 1607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 301 HATSRIAAERARTSGHEV---------PYSGADPEALELRAQEADAQFEALEEAAEIARERLEvllEEVAQREDTARRAE 371
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELkkaeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAE 1684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 372 REHlaQIKALADHREgvvrllaAEEnhaataRGAAEELERQRGAEAEAQARLRQAEgewEEAKDRQEQARRQraplEEAG 451
Cdd:PTZ00121 1685 EDE--KKAAEALKKE-------AEE------AKKAEELKKKEAEEKKKAEELKKAE---EENKIKAEEAKKE----AEED 1742
|
330 340 350
....*....|....*....|....*....|....*...
gi 2713584088 452 ERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETL 489
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
155-497 |
2.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 155 EERRAYIEEAagvLKHRRRKEKAQRKLAGMQGNLDRLRDLTEELSRQLKPLARQAEAAQRA-ATVQATLRDArlrlagDR 233
Cdd:PRK04863 279 NERRVHLEEA---LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHlNLVQTALRQQ------EK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 234 IVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEED-------LARIVPREEAAQKlwfRLSTLAERVHATsri 306
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEvdelksqLADYQQALDVQQT---RAIQYQQAVQAL--- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 307 aaERARTSGHEVPYsgaDPEALELRAQEADAQFEALEEAAEIARERLEVLlEEVAQREDTARRAEREHLAQIKALADHRE 386
Cdd:PRK04863 424 --ERAKQLCGLPDL---TADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSEAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 387 GVVRLLAAEENHAATARGAA-----EELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAA 461
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQlrmrlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350
....*....|....*....|....*....|....*.
gi 2713584088 462 EERLEQVRAEQREHEREVYTLESRIETLRQAAPRAS 497
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA 613
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-49 |
2.19e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 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: 213244 [Multi-domain] Cd Length: 213 Bit Score: 39.89 E-value: 2.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2713584088 5 SLTLKGFKSFaSATTLKFEPGICAVVGPNGSGKSNVVDALAWVMG 49
Cdd:cd03277 5 RIKLENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLG 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-498 |
2.89e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 327 ALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARGAA 406
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 407 EELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQrapLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRI 486
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
170
....*....|..
gi 2713584088 487 ETLRQAAPRASA 498
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-496 |
3.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 147 SEILESRPEERRAYIEEAAGVLKHRRRKEKAQRKLA-GMQGNLDRLRDLTEELSRQLKPLARQAEaaqraaTVQATLRDA 225
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAeSLREDADDLEERAEELREEAAELESELE------EAREAVEDR 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 226 RLRLAG--DRIVTLRAEWEDADLQAEALKERVAALTEEAEERGAEQMGWEEDLARIVPREEAAQKLwfrlstlaervhat 303
Cdd:PRK02224 383 REEIEEleEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-------------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 304 srIAAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIAR-----ERLEVLLEEVAQREDTARRAER--EHLA 376
Cdd:PRK02224 449 --LEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEveerlERAEDLVEAEDRIERLEERREDleELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 377 QIKA-LADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQR---APLEEAGE 452
Cdd:PRK02224 527 ERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtllAAIADAED 606
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2713584088 453 RAGA--EQRAA--------EERLEQVRAEQREHEREVYtlESRIETLRQAAPRA 496
Cdd:PRK02224 607 EIERlrEKREAlaelnderRERLAEKRERKRELEAEFD--EARIEEAREDKERA 658
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
299-474 |
5.14e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 39.96 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 299 RVHATSRIAAERARTSGHEVPYSGADPEALELRAQEADAQFEALEEAAEIARERLEVLLEEVAQREDTA---RRAEREHL 375
Cdd:PRK07735 23 RKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAkakAKAAAAAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 376 AQIKALADHREGVVRLLAAEENHAATARGAAEEleRQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAG 455
Cdd:PRK07735 103 AKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA--KAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAAL 180
|
170
....*....|....*....
gi 2713584088 456 AEQRAAEERLEQVRAEQRE 474
Cdd:PRK07735 181 AKQKAAEAGEGTEEVTEEE 199
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
390-479 |
6.75e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 390 RLLAAEENHAA----TARGAAEELERQRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERL 465
Cdd:COG0542 419 RLEQLEIEKEAlkkeQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELE 498
|
90
....*....|....
gi 2713584088 466 EQVRAEQREHEREV 479
Cdd:COG0542 499 EELAELAPLLREEV 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-511 |
7.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 352 RLEVLLEEVAQREDTARRAER--EHLAQIKALADHREGVVRLLAAEENHAATARGAAEELERQRGAEAEAQARLRQAEGE 429
Cdd:COG4717 106 ELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 430 WEEAKDRQ-EQARRQRAPLEEAGERAGAEQRAAEERLEQVRAE--QREHEREVYTLESRIETLRQAAPRASASELLSGQG 506
Cdd:COG4717 186 LSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
....*
gi 2713584088 507 WRGLS 511
Cdd:COG4717 266 GSLLS 270
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-44 |
7.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.80 E-value: 7.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2713584088 3 LKSLTLKGFKSFASATtLKFEPgICAVVGPNGSGKSNVVDAL 44
Cdd:COG4938 1 IKSISIKNFGPFKEAE-LELKP-LTLLIGPNGSGKSTLIQAL 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-491 |
8.20e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 412 QRGAEAEAQARLRQAEGEWEEAKDRQEQARRQRAPLEEAGERAGAEQRAAEERLEQVRAEQREHEREVYTLESRIETLRQ 491
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-47 |
8.45e-03 |
|
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: 37.61 E-value: 8.45e-03
10 20 30
....*....|....*....|....*....|
gi 2713584088 19 TLKFEPG-ICAVVGPNGSGKSNVVDALAWV 47
Cdd:cd00267 19 SLTLKAGeIVALVGPNGSGKSTLLRAIAGL 48
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
361-474 |
9.39e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713584088 361 AQREDTARRAEREHLAQIKALADHREGVVRLLAAEENHAATARgaAEELERQRGAEAEAQArlrqaegEWEEAKDRQEQA 440
Cdd:COG2268 208 AERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKK--AEERREAETARAEAEA-------AYEIAEANAERE 278
|
90 100 110
....*....|....*....|....*....|....
gi 2713584088 441 RRQRAPLEEAGERAGAEQRAAEERLEQVRAEQRE 474
Cdd:COG2268 279 VQRQLEIAEREREIELQEKEAEREEAELEADVRK 312
|
|
| |
