|
Name |
Accession |
Description |
Interval |
E-value |
| Cnn_1N |
pfam07989 |
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ... |
61-129 |
2.26e-19 |
|
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.
Pssm-ID: 462333 [Multi-domain] Cd Length: 69 Bit Score: 83.72 E-value: 2.26e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281599321 61 KDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASK 129
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-464 |
3.55e-11 |
|
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: 68.56 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 138 GGSEIQRVKEDARKKVQQVEELLtKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLE----SKLSAMKKMQEGDLEMT 213
Cdd:TIGR02169 164 GVAEFDRKKEKALEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 214 LA--------LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLR------EEKERDAEERQK 279
Cdd:TIGR02169 243 ERqlasleeeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 280 ERNHFEERIQALQEDLREKEREIATEKKnslKRDKaiqgLTMALKSKEKEVEELNSIIKELTADSTQSREA--------- 350
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERK---RRDK----LTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyrekle 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 351 -------PLKTQVSEFEVR------ESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLE 417
Cdd:TIGR02169 396 klkreinELKRELDRLQEElqrlseELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 281599321 418 RDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPG 464
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-729 |
8.33e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 101 KKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKV-QQVEELLTKRIHLLEEDVKAAQA--- 176
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIaRKAEDARKAEEARKAEDAKKAEAark 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 177 --ELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKlslKSKEALIQCLKEEKSQMASPDENV 254
Cdd:PTZ00121 1184 aeEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK---KDAEEAKKAEEERNNEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 255 SSGELRGLSATLREEKERDAEERQKErnhfEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELN 334
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 335 SIIKELTADSTQSREAPLKTQVSEF--EVRESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE 412
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAaeEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 413 KLRLE---------RDLEEAHREGNRgARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTES 483
Cdd:PTZ00121 1417 KKKADeakkkaeekKKADEAKKKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 484 ASQEDLLLQKSNEKDleaiqqncylmTAEELKFGSDGLITEKCSQQSPDSKlifSKEKQQSEYEGLTGDLKTEQNVYAhl 563
Cdd:PTZ00121 1496 KKKADEAKKAAEAKK-----------KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELKKAEELKK-- 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 564 AKNLQDTDSKLQAELKRVLALRKQLEqdvlayrnLQTALQEQLSEIRKREEEPFSFYSDQTSYlsiclEEHSQFQLEHFS 643
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEE--------AKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELK 1626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 644 Q-EEIKKKVIDLIQLVKDLHADNQHLKKTIFDISCMGVQGNDRLESTKQAELMASKADEDTLKFKADDENHFQSDQHLEQ 722
Cdd:PTZ00121 1627 KaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
....*..
gi 281599321 723 SREIMED 729
Cdd:PTZ00121 1707 LKKKEAE 1713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-434 |
1.50e-10 |
|
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: 66.62 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 142 IQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFagtETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDR 221
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 222 LIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRgLSATL------REEKERDAEERQKERNHFEERIQALQEDL 295
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-LEAQLeeleskLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEVRESEN----CEA 369
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARleRLEDRRERLQQEIEELLKKLEEAelkeLQA 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281599321 370 ALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE------KLRLERDLEEAHREGNRGARTI 434
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQENLEGFSEGVKAL 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-445 |
1.53e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 147 EDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKmqegdlemtlALEEKDRLIEEL 226
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA----------ELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 227 KLSLKSKEALIQCLKEEKSQMASpDENVSSGELRGLSATLREEKERDAEERQKERNHfEERIQALQEDLREKEREIATEK 306
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAELEEELEEL-EEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 307 KNSLKRDKAIQGLTMALKSKEKEVEELNSiiKELTADSTQSREAPLKTQVSEFEVRESENCEAALAEKEALLAKLHSENV 386
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 281599321 387 TKNTENHRLLrnvkKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLR 445
Cdd:COG1196 436 EEEEEEEALE----EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-448 |
3.86e-10 |
|
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: 65.08 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 160 LTKRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKKMQEgdlEMTLALEEKDRLIEELKLSLKSKEALIQC 239
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAE--------------LRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 240 LKEEKSQMASPDENV-----SSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDK 314
Cdd:TIGR02168 745 LEERIAQLSKELTELeaeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 315 AIQGLTMALKSKEKEVEELNSIIKELTADSTQSREaplktqvsefevrESENCEAALAEKEALLAKLHSENVTKNTENHR 394
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAA-------------EIEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 281599321 395 LLRNVKKVTQELNDLKKEKLRLERDLEEAHREgnrgartIHDLRNEVEKLRKEV 448
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREK-------LAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-612 |
4.45e-10 |
|
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: 65.08 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 59 NMKDFENQITELKKENFNLKLRIYFLEERIQQEfagptehiYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGG 138
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETL--------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 139 GSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEE 218
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 219 KDRLIEELKLSLKSKEALIQCLkeekSQMASPDENVSS------GELRGLSATLREEKERDAEERQKE----RNHFEE-- 286
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVL----SELISVDEGYEAaieaalGGRLQAVVVENLNAAKKAIAFLKQnelgRVTFLPld 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 287 -----RIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS---IIKEL-------TADSTQSRE-- 349
Cdd:TIGR02168 580 sikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNaleLAKKLrpgyrivTLDGDLVRPgg 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 350 ----APLKTQVSEFEVR-ESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAH 424
Cdd:TIGR02168 660 vitgGSAKTNSSILERRrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 425 REGNRGARTIHDLRNEVEKLRKEVCEREKAVEkhykslpgESSSKFHSQEQVVKGLTESA--SQEDLLLQKSNEKDLEAI 502
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLE--------EAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAE 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 503 qqncylMTAEELKFGSDGLITEKCSQQspdsklIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVL 582
Cdd:TIGR02168 812 ------LTLLNEEAANLRERLESLERR------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
570 580 590
....*....|....*....|....*....|
gi 281599321 583 ALRKQLEQDVLAYRNLQTALQEQLSEIRKR 612
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESK 909
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-615 |
7.27e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 97 EHIYKKNIELKVEVESLKRELQErdqlLVKASKAVESLAEGGGSEIQRVKEDARKkvqqveelLTKRIHLLEEDVKAAQA 176
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEK----FIKRTENIEELIKEKEKELEEVLREINE--------ISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 177 ELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELK------LSLKSKEALIQCLKEEKSQMASP 250
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelKELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 251 DENVS------SGELRGLSATL--REEKERDAEERQKERNHFEERIQALQEDLREKEReiATEKKNSLKRDKA------I 316
Cdd:PRK03918 309 LREIEkrlsrlEEEINGIEERIkeLEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKrltgltP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 317 QGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEVRESE--NCEAALAE--KEALLAKLHSenvtknt 390
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARigELKKEIKELKKAIEELKKAKGKcpVCGRELTEehRKELLEEYTA------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 391 ENHRLLRNVKKVTQELNDLKKEKLRLERDLEEaHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGES---S 467
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 468 SKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQNCYLmtaEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYE 547
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKELEPFYNEYLELKDAEKELE 615
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281599321 548 GLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRK--------QLEQDVLAYRNLQTALQEQLSEIRKREEE 615
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-469 |
7.71e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 59 NMKDFENQITELKKENFNLKLRIYFLEERIQQ-EFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEG 137
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 138 GGSEIQRVKEDARKKVQQVEELLT-KRIHLLEEDVKAAQAELE---KAFAGTETEKalrlsLESKLSAMKKMQEgdlEMT 213
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEElEERHELYEEAKAKKEELErlkKRLTGLTPEK-----LEKELEELEKAKE---EIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 214 LALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKernhFEERIQALQE 293
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKE----IEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 294 DLREKEREIATEKKNSLKRDKA--IQGLTMALKS--------KEKEVEELNSIIKELTAD-----STQSREAPLKTQVSE 358
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAeqLKELEEKLKKynleelekKAEEYEKLKEKLIKLKGEikslkKELEKLEELKKKLAE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 359 FEvRESENCEAALAEKEALLAKLHSENVTKNTENHRLLR-------NVKKVTQELNDLKKEKLRLERDLEEAHREGNRGA 431
Cdd:PRK03918 561 LE-KKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
410 420 430
....*....|....*....|....*....|....*....
gi 281599321 432 RTIHDLRNEVEKLRKEVCERE-KAVEKHYKSLPGESSSK 469
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGL 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-615 |
1.62e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 85 EERIQQEFAGPTEHIYKknIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARK--KVQQVEELLTK 162
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARK--AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKaeAARKAEEVRKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 163 RIHLLEEDVKAAQaELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALE-EKDRLIEELKLSLKSKEALIQ--- 238
Cdd:PTZ00121 1191 EELRKAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaEEERNNEEIRKFEEARMAHFArrq 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 239 -CLKEEKSQMAS----------PDENVSSGELRGL-SATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEK 306
Cdd:PTZ00121 1270 aAIKAEEARKADelkkaeekkkADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 307 KNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREA-PLKTQVSEFEVRESENCEAALAEKEALLAKLHSEN 385
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 386 V-------------------TKNTENHRLLRNVKKVTQELN--DLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKl 444
Cdd:PTZ00121 1430 KkkadeakkkaeeakkadeaKKKAEEAKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA- 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 445 RKEVCEREKAVEKHYKSLPGESSSKFHSQE----QVVKGLTESASQEDLL----LQKSNEKDLEAIQQNCYLMTAEELKF 516
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEakkaEEKKKADELKKAEELKkaeeKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 517 GSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNVyahlAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYR 596
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
570 580
....*....|....*....|..
gi 281599321 597 NLQTALQE---QLSEIRKREEE 615
Cdd:PTZ00121 1665 EEAKKAEEdkkKAEEAKKAEED 1686
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-609 |
2.25e-09 |
|
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: 62.78 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 268 EEKERDAEERQKERNHfEERIQALQEDLREKEREIATEKKNSLKRDKA------------IQGLTMALKSKEKEVEELNS 335
Cdd:TIGR02169 194 DEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaierqlasleeeLEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 336 IIKELTA---DSTQSREAPLKTQVSEFEVrESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE 412
Cdd:TIGR02169 273 LLEELNKkikDLGEEEQLRVKEKIGELEA-EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 413 KLRLERDLEEahregnrgartihdLRNEVEKLRKEVCErekaVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQ 492
Cdd:TIGR02169 352 RDKLTEEYAE--------------LKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 493 KSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNvyahlakNLQDTDS 572
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-------RVEKELS 486
|
330 340 350
....*....|....*....|....*....|....*..
gi 281599321 573 KLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLSEI 609
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
49-453 |
3.31e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 49 EEKVSPTRAR--NMKDFENQITELKKENFNLKLRIYFLEERIQQ------EFAGPTEHIYKKNIELK---------VEVE 111
Cdd:PRK03918 220 REELEKLEKEvkELEELKEEIEELEKELESLEGSKRKLEEKIREleerieELKKEIEELEEKVKELKelkekaeeyIKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 112 SLKRELQERDQLLVKASKAVESLAEGggseIQRVKEDARKKVQQVEELLTKRI------------HLLEEDVKAAQAELE 179
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEING----IEERIKELEEKEERLEELKKKLKelekrleeleerHELYEEAKAKKEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 180 ---KAFAGTETEKalrlsLESKLSAMKKMQEgdlEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSS 256
Cdd:PRK03918 376 rlkKRLTGLTPEK-----LEKELEELEKAKE---EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 257 GELRGLSATLREEKERDAEERQKernhFEERIQALQEDLREKEREIATEKKNSLKRDKA--IQGLTMALKS--------K 326
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKynleelekK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 327 EKEVEELNSIIKELTAD-----STQSREAPLKTQVSEFEvRESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKK 401
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEikslkKELEKLEELKKKLAELE-KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 281599321 402 VTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREK 453
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-348 |
7.88e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEgggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAG 184
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 185 TETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSA 264
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 265 TLREEKER-DAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:COG1196 406 EEAEEALLeRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
....*
gi 281599321 344 STQSR 348
Cdd:COG1196 486 LAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-518 |
1.15e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 217 EEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdeNVSSGELRGLSATLREeKERDAEERQKERNHFEERIQALQEDLR 296
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRL-----DELSQELSDASRKIGE-IEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 297 EKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEEL-----NSIIKELTADSTQsreapLKTQVSEFEVRESEnCEAAL 371
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK-----LEEEVSRIEARLRE-IEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 372 AEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREgnrgartIHDLRNEVEKLRKEVCER 451
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281599321 452 EK---AVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQK--------SNEKDLEAIQQNCYLMTAEELKFGS 518
Cdd:TIGR02169 895 EAqlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgedeeipEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
61-457 |
1.19e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 61 KDFENQITELKKENFNLKLRIyfleERIQQEFAGPTEHIYKKN---IELKVEVESLKRELQERDQLLVKASKAVESLAEg 137
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNI----EKKQQEINEKTTEISNTQtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 138 ggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFagTETEKALRlSLESKLSAMKKMQEG----DLEMT 213
Cdd:TIGR04523 289 ---QLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI--SQNNKIIS-QLNEQISQLKKELTNseseNSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 214 LALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsatlreekERDAEERQKERNHFEERIQALQE 293
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-----------------------ESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 294 DLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEltadstqsreapLKTQVSEFEV------RESENC 367
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES------------LETQLKVLSRsinkikQNLEQK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 368 EAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRgartiHDLRNEVEKLRKE 447
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKE 562
|
410
....*....|
gi 281599321 448 VCEREKAVEK 457
Cdd:TIGR04523 563 IDEKNKEIEE 572
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-505 |
1.27e-08 |
|
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: 60.07 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 203 KKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRglsatlREEKERDAEERQKERN 282
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE------VSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 283 HFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAdstqsreaplktqvsefevr 362
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE-------------------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 363 ESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDL----- 437
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkle 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281599321 438 RNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKD-LEAIQQN 505
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDsLERLQEN 500
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
141-420 |
1.26e-07 |
|
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: 56.67 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 141 EIQRVKEDARKKVQQVEelltkRIHLLEEDVKAAQAELEKAFA--------GTETEKAL-RLSLESKLSAMKKMQEGDLE 211
Cdd:pfam17380 297 EQERLRQEKEEKAREVE-----RRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELeRIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 212 MTLaleEKDRLIEELKLSLKSKE---------ALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEE---RQK 279
Cdd:pfam17380 372 MEI---SRMRELERLQMERQQKNervrqeleaARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEeraREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 280 ERNHFEERIQALQ-EDLREKEREiatEKKNSLKRDKAiqgltmalKSKEKEVEELNSII--KELTADSTQSREAPLKTQV 356
Cdd:pfam17380 449 ERVRLEEQERQQQvERLRQQEEE---RKRKKLELEKE--------KRDRKRAEEQRRKIleKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281599321 357 SEFEVRESENceAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLkkEKLRLERDL 420
Cdd:pfam17380 518 LEKEMEERQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL--EAMEREREM 577
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-373 |
1.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 61 KDFENQITELKKENFNLKLRIYFLEERIQQEfagpTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVEslaegggs 140
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 141 EIQRVKEDARKKVQQVEELLTKRIhLLEEDVKAAQAELEKAfagTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKD 220
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEA---EEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 221 RLIEELKLSLKSKEALIQCLKEEKSQMASPDENVssgelrglsATLREEKERDAEERQKERNHFEERIQALQEDLREKER 300
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAEL---------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281599321 301 EIATEKKNSLKRDKAIQGLTM---ALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEVRESENCEAALAE 373
Cdd:COG1196 471 EAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-670 |
1.95e-07 |
|
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: 56.22 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 57 ARNMKDFENQITELKKENFNLKLRIyfleERIQQEFagptehiYKKNIELKvEVESLKRELQERDQLLVKASKAVESLAE 136
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEI----EELQKEL-------YALANEIS-RLEQQKQILRERLANLERQLEELEAQLE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 137 GGGSEIQRVKEDARKKVQQVEELLtKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKkmqegdLEMTLAL 216
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------LQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 217 EEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELrglsatlrEEKERDAEERQKERNHFEERIQALQEDLR 296
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--------EELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 297 EKEREIaTEKKNSLKRdkaIQGLTMALKSKEKEVEELNSIIKELTADstQSREAPLKTQVSE-FEVRES-ENC-EAALAE 373
Cdd:TIGR02168 472 EAEQAL-DAAERELAQ---LQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSElISVDEGyEAAiEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 374 --------------------KEALLAKLH-----SENVTKNTENHRLLRN------------------------------ 398
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflKQNELGRVTflpldSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 399 --VKKVTQELNDLKKEKL----------------------------RLERD--LEEAHREGNRGARTIHDLRNEVEKLRK 446
Cdd:TIGR02168 626 lvVDDLDNALELAKKLRPgyrivtldgdlvrpggvitggsaktnssILERRreIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 447 EVCEREKAVEKHYKSLPgESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQncyLMTAEELKFGSDGLITEKC 526
Cdd:TIGR02168 706 ELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IEELEERLEEAEEELAEAE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 527 SQQSPDSKLIfskEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQdvlayrnlqtaLQEQL 606
Cdd:TIGR02168 782 AEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-----------LEEQI 847
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 607 SEIRKREEEpfsfYSDQTSYLSICLEEHSQfQLEHFS------QEEIKKKVIDLIQLVKDLHADNQHLKK 670
Cdd:TIGR02168 848 EELSEDIES----LAAEIEELEELIEELES-ELEALLneraslEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-448 |
3.48e-07 |
|
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: 55.46 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 84 LEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGG--SEIQRVKEDARKKVQQVEellt 161
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELE---- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 162 KRIHLLEEDVKAAQAELEKAFAGTETEKalrlsLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLK 241
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 242 EE----KSQMASPDENVSSGELRgLSATLREEKERDAEERQ--KERNHFEERIQALQEDLREKEREIATEKknsLKRDKA 315
Cdd:TIGR02169 840 EQridlKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDleSRLGDLKKERDELEAQLRELERKIEELE---AQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 316 IQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVsefevreSENCEAALAEKEALlaklhsENVtknteNHRL 395
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-------QAELQRVEEEIRAL------EPV-----NMLA 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 281599321 396 LRNVKKVTQELNDLKKEKLRLERDLEEahregnrgartIHDLRNEVEKLRKEV 448
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKRAKLEEERKA-----------ILERIEEYEKKKREV 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
108-457 |
6.77e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 108 VEVESLKRELQERD---QLLVKASKAVESLAEG----------GGSE-IQRVK------EDARKKVQQVEELLTKRIHLL 167
Cdd:pfam15921 412 ITIDHLRRELDDRNmevQRLEALLKAMKSECQGqmerqmaaiqGKNEsLEKVSsltaqlESTKEMLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 168 E------EDVKAAQAELEKAFAGTETE-KALRLSLESKLSAMKKMQ-EGDL---------EMTLALEEKDRLIEELKLSL 230
Cdd:pfam15921 492 EssertvSDLTASLQEKERAIEATNAEiTKLRSRVDLKLQELQHLKnEGDHlrnvqteceALKLQMAEKDKVIEILRQQI 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 231 KSKEALIQ-------CLKEEKSQMASP--DENVSSGELRGLS----ATLREEKERDAE---ERQKERNHFEERIQALQED 294
Cdd:pfam15921 572 ENMTQLVGqhgrtagAMQVEKAQLEKEinDRRLELQEFKILKdkkdAKIRELEARVSDlelEKVKLVNAGSERLRAVKDI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 295 LREKER---EIATEKK--NSLKRDKAIqgLTMALKSKEKEVEELNSIIKeLTADSTQSREAPLKTQVSEFEVRESENCEA 369
Cdd:pfam15921 652 KQERDQllnEVKTSRNelNSLSEDYEV--LKRNFRNKSEEMETTTNKLK-MQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 370 ALAEKEALLAKLHSENVTKnTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVC 449
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQ-SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVA 807
|
....*...
gi 281599321 450 EREKAVEK 457
Cdd:pfam15921 808 NMEVALDK 815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
102-495 |
6.88e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 102 KNIELKVEVESLKRELQERDQLLVKAS---KAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAEL 178
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 179 EKAFAGTETEKALRLSLESKLSAMKKMQEGDLEmtlalEEKDRLIEELKLSLKSKEALIQCLKEEKSQmASPDENVSSGE 258
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-----EEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKE 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 259 lrglsatlrEEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIK 338
Cdd:PTZ00121 1712 ---------AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 339 ELTADSTQSR----EAPLKTQVSEFEVRESENCEAAL-----------AEKEALLAKLHSENVTKNTENHRLLRNVK--K 401
Cdd:PTZ00121 1783 EELDEEDEKRrmevDKKIKDIFDNFANIIEGGKEGNLvindskemedsAIKEVADSKNMQLEEADAFEKHKFNKNNEngE 1862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 402 VTQELNDLKKEKLRLERDLEEAHREgnrgartihdlrNEVEKLRKEVCEREKAvEKHYKSLPGESSSKFHSQEQVVKGLT 481
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEA------------DEIEKIDKDDIEREIP-NNNMAGKNNDIIDDKLDKDEYIKRDA 1929
|
410
....*....|....
gi 281599321 482 ESASQEDLLLQKSN 495
Cdd:PTZ00121 1930 EETREEIIKISKKD 1943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
266-615 |
1.34e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 266 LREEKERDAE--ERQKERnhfEERIQALQEDLREKEREIATEKKNSLKRDkaiqgltmaLKSKEKEVEELNSIIKELTAd 343
Cdd:COG1196 194 ILGELERQLEplERQAEK---AERYRELKEELKELEAELLLLKLRELEAE---------LEELEAELEELEAELEELEA- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 344 stqsreaplktqvsefevrESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEA 423
Cdd:COG1196 261 -------------------ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 424 HREGNRGARTIHDLRNEVEKLRKEVCEREKAVEkhykslpgESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQ 503
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELE--------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 504 QncylmtAEELKfgsdglitekcSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLA 583
Cdd:COG1196 394 A------AAELA-----------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350
....*....|....*....|....*....|..
gi 281599321 584 LRKQLEQDVLAYRNLQTALQEQLSEIRKREEE 615
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
87-670 |
2.57e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 87 RIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKR--I 164
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 165 HLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMqegdLEMTLALEEKDRLieELKLSLKSKEALIQCLKEEK 244
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA----FEELRVQAENARL--EMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 245 SQMASPDENVSSgeLRGLSATLREEKERD----AEERQKERNHFEERIQALQEDLR---EKEREIATEK---KNSLKRDK 314
Cdd:pfam05483 232 KKEINDKEKQVS--LLLIQITEKENKMKDltflLEESRDKANQLEEKTKLQDENLKeliEKKDHLTKELediKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 315 AIQgltmalKSKEKEVEELNSIIKELTAD-STQSREAPLKTQVSEFEVRESENCEAALAEkealLAKLHSENVTKNTENH 393
Cdd:pfam05483 310 STQ------KALEEDLQIATKTICQLTEEkEAQMEELNKAKAAHSFVVTEFEATTCSLEE----LLRTEQQRLEKNEDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 394 RLLR-NVKKVTQELNDLKKEKLRLERDLEEAHREGNRgARTIHDLRNEVEKLRKEVcereKAVEKHYKSLPGESSSKFHS 472
Cdd:pfam05483 380 KIITmELQKKSSELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIAEEL----KGKEQELIFLLQAREKEIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 473 QEQVVKGLTESASQ-----EDLLLQKSNEKdleaiqqncylMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQseyE 547
Cdd:pfam05483 455 LEIQLTAIKTSEEHylkevEDLKTELEKEK-----------LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---E 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 548 GLTGDLKTEQNVYAHLaKNLQDTDSKLQAELKRVlalRKQLEQDvlayrnlqtaLQEQLSEIRKREEEPFSFYSDqtsyl 627
Cdd:pfam05483 521 DIINCKKQEERMLKQI-ENLEEKEMNLRDELESV---REEFIQK----------GDEVKCKLDKSEENARSIEYE----- 581
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 281599321 628 siCLEEHSQFQLEHFSQEEIKKKVIDLIQLVKDLHADNQHLKK 670
Cdd:pfam05483 582 --VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-448 |
3.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 60 MKDFENQITELKKENFNLKLRIYFLEERIQQ--EFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEG 137
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 138 GGSEIQRVK------EDARKKVQQVEELLTKRIHLLE---EDVKAAQAELEKAFAGTETEKALrLSLESKLSAMKKMQeg 208
Cdd:PRK03918 382 TGLTPEKLEkeleelEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAKGKCPVCGRE-LTEEHRKELLEEYT-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 209 dLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKS-----QMASPDENVSSgELRGLSATLREEKERDAEERQKERNH 283
Cdd:PRK03918 459 -AELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE-KLKKYNLEELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 284 FEERIQALQEDLR-----EKEREIATEKKNSLKRDKAiQGLTMALKSKEKEVEELNSIIKELTA---------DSTQSRE 349
Cdd:PRK03918 537 LKGEIKSLKKELEkleelKKKLAELEKKLDELEEELA-ELLKELEELGFESVEELEERLKELEPfyneylelkDAEKELE 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 350 APLKTQvsEFEVRESENCEAALAEKEALLAKLHSE----NVTKNTENHRLLRN-----------VKKVTQELNDLKKEKL 414
Cdd:PRK03918 616 REEKEL--KKLEEELDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREeylelsrelagLRAELEELEKRREEIK 693
|
410 420 430
....*....|....*....|....*....|....*..
gi 281599321 415 RLERDLEEAHREGNRGARTIHDL---RNEVEKLRKEV 448
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKLekaLERVEELREKV 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-360 |
3.32e-06 |
|
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: 52.37 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 58 RNMKDFENQITELKKENFNLKLRIYFLEERIQQefagptehiykknIELKV-EVESLKRELQERDQLLVKASKAVESLAE 136
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEE-------------LRLEVsELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 137 GGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEdvkaaQAELEKAFAGTETEKAlrlSLESKLSAMKKMQEgdlEMTLAL 216
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEE-----LAELEEKLEELKEELE---SLEAELEELEAELE---ELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 217 EEKDRLIEELklslksKEALIQCLKEEKSQMAspdenvssgELRglsaTLREEKERDAEERQKERNHFEERIQALQE-DL 295
Cdd:TIGR02168 375 EELEEQLETL------RSKVAQLELQIASLNN---------EIE----RLEARLERLEDRRERLQQEIEELLKKLEEaEL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281599321 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFE 360
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQENLE 502
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
64-615 |
3.76e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 64 ENQITELKKENFN-LKLRIYFLEERIQQ-------EFAGPTEHIYKKNIE---LKVEVESLKRELQERDQLLVKASKAVE 132
Cdd:pfam15921 244 EDQLEALKSESQNkIELLLQQHQDRIEQlisehevEITGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 133 SLAEGGGSEIQRVKEDARKKVQQVE-ELLTKRIHLLEEDVKAAQAELEKAFAGTETEKAL--------RLSLESKLSamK 203
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEkQLVLANSELTEARTERDQFSQESGNLDDQLQKLLadlhkrekELSLEKEQN--K 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 204 KMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEE-----KSQMAS-PDENVSSGELRGLSATLREEKERdaeer 277
Cdd:pfam15921 402 RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmERQMAAiQGKNESLEKVSSLTAQLESTKEM----- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 278 qkernhfeeriqalqedLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA--DSTQSREAPLKTQ 355
Cdd:pfam15921 477 -----------------LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 356 VSEFEVRESEnCEA---ALAEKEALLAKLHS--ENVTKNTENH-----RLLRNVKKVTQELND--LKKEKLRLERDLEEA 423
Cdd:pfam15921 540 GDHLRNVQTE-CEAlklQMAEKDKVIEILRQqiENMTQLVGQHgrtagAMQVEKAQLEKEINDrrLELQEFKILKDKKDA 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 424 H-RE------------------GNRGARTIHDLRNEVEKLRKEV--CERE-KAVEKHYKSLPGESSSKFHSQEQVVKGLT 481
Cdd:pfam15921 619 KiRElearvsdlelekvklvnaGSERLRAVKDIKQERDQLLNEVktSRNElNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 482 ES--ASQEDLLLQKSNEKDLEAIQQNcylmtAEELKFGSDGLITEKCSQ-QSPDSKLIFSKEKQQSEYEGlTGDLKTEQN 558
Cdd:pfam15921 699 MQlkSAQSELEQTRNTLKSMEGSDGH-----AMKVAMGMQKQITAKRGQiDALQSKIQFLEEAMTNANKE-KHFLKEEKN 772
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281599321 559 VYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVlayRNLQTALQE---QLSE----IRKREEE 615
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKV---ANMEVALDKaslQFAEcqdiIQRQEQE 833
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-458 |
4.51e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 146 KEDARKKVQQVEELLTKRIHLLEE--DVKAAQAELEKAFAGTETEK-----------ALRLSLESKLSAMKKMQE-GDLE 211
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREEleTLEAEIEDLRETIAETEREReelaeevrdlrERLEELEEERDDLLAEAGlDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 212 MTLALEEKDRL---IEELKLSLKSKEALIQclkEEKSQMASPDENVSsgELRGLSATLREEKERDAEERQKERNHFEERi 288
Cdd:PRK02224 309 AEAVEARREELedrDEELRDRLEECRVAAQ---AHNEEAESLREDAD--DLEERAEELREEAAELESELEEAREAVEDR- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 289 qalQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQV---------SEF 359
Cdd:PRK02224 383 ---REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpeCGQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 360 EVRES------ENCEAALAEKEALLAKLHSEnVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGART 433
Cdd:PRK02224 460 PVEGSphvetiEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
330 340
....*....|....*....|....*.
gi 281599321 434 IHDLRNEVEKLRKEVCE-REKAVEKH 458
Cdd:PRK02224 539 AEELRERAAELEAEAEEkREAAAEAE 564
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1405-1585 |
4.66e-06 |
|
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: 50.92 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLEKGSKE------- 1477
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELRAELEAQKEElaellra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1478 --KQKENEKLR-----ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQ 1550
Cdd:COG4942 113 lyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|....*
gi 281599321 1551 LLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-340 |
5.06e-06 |
|
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: 51.60 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 58 RNMKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEH------IYKKNIELKVEVESLKRELQERDQLLVKASKAV 131
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 132 ESLAEGGGSEIQRVKEDARKKVQQVEEL--LTKRIHLLEEDVKAAQAEL--EKAFAGTETEKALRL---------SLESK 198
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAELtlLNEEAANLRERLESLerriaaterRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 199 LSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgELRGLSATLReEKERDAEERQ 278
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE-ELRELESKRS-ELRRELEELR 921
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281599321 279 KERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQ-GLTMALKSKEKEVEELNSIIKEL 340
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-672 |
1.58e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 56 RARNMKDFENQITELKKENFNLKLRIYFLEERIQQ-----EFAGPTEHIYKKNI-ELKVEVESLKRELQERDQLLVKASK 129
Cdd:TIGR04523 66 DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsdlSKINSEIKNDKEQKnKLEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 130 AVESLAegggSEIQRVKEDARKKVQQVEELLTKRiHLLEEDVKAAQAELEKAfagteteKALRLSLESKLSAMKKMQEGD 209
Cdd:TIGR04523 146 EIKKKE----KELEKLNNKYNDLKKQKEELENEL-NLLEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKKKIQKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 210 LEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgelrglsatLREEKERDAEERQKERNHFEERIQ 289
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD---------EQNKIKKQLSEKQKELEQNNKKIK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 290 ALQEDLREKEREIatEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEfevRESENC 367
Cdd:TIGR04523 285 ELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqiSQLKKELTN---SESENS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 368 E--AALAEKEALLAKLHSENVTKNTENHRL----------LRNVKKVTQELND----LKKEKLRLERDLEEAHREGNRGA 431
Cdd:TIGR04523 360 EkqRELEEKQNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEqikkLQQEKELLEKEIERLKETIIKNN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 432 RTIHDLRNEV---EKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLlqKSNEKDLEaiQQNCYL 508
Cdd:TIGR04523 440 SEIKDLTNQDsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--NEEKKELE--EKVKDL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 509 MT-AEELKFGSDGLITEKCSQQSPDSKLifSKEKQQSEYEGLTGDLKTEQNVY-------AHLAKNLQDTDSKLQAELKR 580
Cdd:TIGR04523 516 TKkISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKnkeieelKQTQKSLKKKQEEKQELIDQ 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 581 VLALRKQLEQDVLAYRNLQTALQEQLSEIRKREEEPFSFYSDQTSYLSICLEEHSQFQLE-----------HFSQEEIKK 649
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETikeirnkwpeiIKKIKESKT 673
|
650 660
....*....|....*....|....
gi 281599321 650 KVIDLIQLVKD-LHADNQHLKKTI 672
Cdd:TIGR04523 674 KIDDIIELMKDwLKELSLHYKKYI 697
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-504 |
1.67e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 113 LKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELlTKRIHLLEEDVKAAQAELEKAfagtETEKALR 192
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEEL----REELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 193 LSLESKLSAMKKMQEGDLEMTL------ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATL 266
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 267 rEEKERDAEERQKERNHFEERIQALQEDLREKEREI-ATEKKNSLKRDK----------AIQGLTMALKSKEKEVEELNS 335
Cdd:COG4717 202 -EELQQRLAELEEELEEAQEELEELEEELEQLENELeAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 336 IIKELTADSTQSREAPLKTQVSEFEVRESENCEAALAEKE--ALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK 413
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 414 LRLERDLEEAHRE---GNRGARTIHDLRNEVEKLRKEVcEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLL 490
Cdd:COG4717 361 EELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEE 439
|
410
....*....|....
gi 281599321 491 LQKSNEKDLEAIQQ 504
Cdd:COG4717 440 ELEELEEELEELRE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1422-1582 |
1.69e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1422 EKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALstmlEKGSKEKQKENEKLRESLARKTESLEHLQL 1501
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1502 EYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQ 1581
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
.
gi 281599321 1582 D 1582
Cdd:COG1196 390 E 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-493 |
2.16e-05 |
|
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: 48.99 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 273 DAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREApL 352
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 353 KTQVSEFEVRESENCEAALAEKEALLakLHSENVTKNTENHRLLRNVKKVTQE-LNDLKKEKLRLERDLEEAHREGNRGA 431
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281599321 432 RTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPgessskfhSQEQVVKGLTESASQEDLLLQK 493
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELA--------ELAAELAELQQEAEELEALIAR 231
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
61-457 |
2.54e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 61 KDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVE-SLKRELQERDQLLVKASKAVESLAEGGG 139
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvEGILKDTELTKLKESAKAKESGLRKGVS 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 140 SEIqrvKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEK 219
Cdd:pfam02463 654 LEE---GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 220 DRLIEELKLSLKSKEALIQCLKEEKSQMAspdenvssgelrglsatlREEKERDAEERQKERNHFEERIQALQEDLREKE 299
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKK------------------EEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 300 REIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEVRESENCEAALAEKEALLA 379
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281599321 380 KLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEK 457
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1397-1585 |
3.08e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1397 QDLLMEHIQEIRTL---RKHLEESIKTNEKLRKQLERQGCETDQGSTNVSA-----------YSSELHNSLTSEIQFLRK 1462
Cdd:COG1196 287 QAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELEELEEeleeleeeleeAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1463 QNEALSTMLEKGSKEKQKENEKLRE--SLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcssLQELSR 1540
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---EEEEEA 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 281599321 1541 VQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-614 |
3.52e-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: 48.91 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 285 EERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEFEV- 361
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErlEELEEDLSSLEQe 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 362 -----RESENCEAALAEKEALLAKLHSEnvTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNR---GART 433
Cdd:TIGR02169 753 ienvkSELKELEARIEELEEDLHKLEEA--LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 434 IHDLRNEVEKLRKEVCEREKAVEKhykslpgessskfhsqeqvvkgltesasQEDLLlqksnEKDLEAIQQNcylmtAEE 513
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEK----------------------------EIENL-----NGKKEELEEE-----LEE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 514 LKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEgltgDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQD-- 591
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIE----ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpe 948
|
330 340
....*....|....*....|....
gi 281599321 592 -VLAYRNLQTALQEQLSEIRKREE 614
Cdd:TIGR02169 949 eELSLEDVQAELQRVEEEIRALEP 972
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-462 |
4.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 266 LREEKERDAEERQKERNHFEERIQALQEDLREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 344 STQSREAPLKTQVSEFEVRESENCEAALAEKEALLAKLhSENVTKNTENHRLLRNVKkvtQELNDLKKE-KLRLERDLEE 422
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAEL-AELSARYTPNHPDVIALR---AQIAALRAQlQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 281599321 423 AHREGNRGARTIHDLRNEVEKLRKEVcEREKAVEKHYKSL 462
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRL 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-381 |
4.49e-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: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 144 RVKEDARKKVQQVEELltKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLEsKLSAMKKMqegdlemtLALEEKDRLI 223
Cdd:COG4913 222 DTFEAADALVEHFDDL--ERAHEALEDAREQIELLEPIRELAERYAAARERLA-ELEYLRAA--------LRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 224 EELklslkskEALIQCLKEEKSQMAspdenvssGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIA 303
Cdd:COG4913 291 ELL-------EAELEELRAELARLE--------AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281599321 304 TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREApLKTQVSEFEVRESEnCEAALAEKEALLAKL 381
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA-LEEALAEAEAALRD-LRRELRELEAEIASL 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1397-1585 |
5.11e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEA-----LSTML 1471
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL-NQLKSEISDLNNQKEQdwnkeLKSEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1472 EKGSKEKQKENEKLRES---LARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSR 1548
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 281599321 1549 QQLLLQKDELLQSLQMELKV----YEKLAEEHQKLQQDVNK 1585
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKlqqeKELLEKEIERLKETIIK 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1397-1595 |
5.85e-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: 48.13 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHN------SLTSEIQFLRKQNEALSTM 1470
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaaNLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1471 LEKGSKEKQKENE----------KLRESLARKTESLEHLQLEYASVREENERLR-------RDISEKERQNQQLTQEvcs 1533
Cdd:TIGR02168 840 LEDLEEQIEELSEdieslaaeieELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRE--- 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281599321 1534 sLQELSRVQEEAKSRQQLLLQKdelLQSLQmelkvyEKLAEEHQKLQQDVNKCPEASDNSFD 1595
Cdd:TIGR02168 917 -LEELREKLAQLELRLEGLEVR---IDNLQ------ERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1453-1583 |
5.91e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1453 LTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVC 1532
Cdd:COG1196 244 LEAELEELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 281599321 1533 SSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEK-LAEEHQKLQQDV 1583
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAeLAEAEEALLEAE 371
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-351 |
6.56e-05 |
|
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: 47.45 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 105 ELKVEVESLKRELQERDQLLVKASKAVESLaegggseiqrvkEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAfag 184
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKAL------------LKQLAALERRIAALARRIRALEQELAALEAELAEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 185 TETEKALRLSLESKLSAMKKM--------QEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMAspdenvss 256
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 257 gELRGLSATLREEKERDAEERQKErnhfEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLtmalkskEKEVEELNSI 336
Cdd:COG4942 161 -ELAALRAELEAERAELEALLAEL----EEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEAL 228
|
250
....*....|....*
gi 281599321 337 IKELTADSTQSREAP 351
Cdd:COG4942 229 IARLEAEAAAAAERT 243
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1448-1581 |
6.82e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.93 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1448 ELHNSLTSEIQFLRKQNEALSTMLEKGSKEKQKENEKLRESLARKTES-------LEHLQLEYASVREENERLRRDISEK 1520
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdpteLDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281599321 1521 ERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDellqslQMELKVYEKLAEEHQKLQQ 1581
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR------GFTFKEIEKLKEQLKLLQS 285
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1399-1581 |
6.85e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1399 LLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAysselhnsLTSEIQFLRKQNEALSTMLEKGSKEK 1478
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1479 QKENEKLR-ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLT-QEVCSSLQELSRVQEEAKSRQQLLLQKD 1556
Cdd:COG4717 140 ELAELPERlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 281599321 1557 ELLQSLQMELKVYEKLAEEHQKLQQ 1581
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1405-1581 |
1.05e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSEIQFLRKQNEALSTMLEKGSKEKQKENEK 1484
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1485 LRE---------SLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKsrQQLLLQK 1555
Cdd:COG1196 389 LEAlraaaelaaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE--ALLELLA 466
|
170 180
....*....|....*....|....*.
gi 281599321 1556 DELLQSLQMELKVYEKLAEEHQKLQQ 1581
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAAR 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-615 |
1.10e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 141 EIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAA---QAELEkAFAGTETEKAlRLS-----LESKLSAMKKMQEGDLEM 212
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQeqlQAETE-LCAEAEEMRA-RLAarkqeLEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 213 TLALE-EKDRL---IEELKLSLKSKEALIQCLKEEKsqmASPDENVSSGELRGLsaTLREEKERdaeeRQKERNHFEERI 288
Cdd:pfam01576 91 SQQLQnEKKKMqqhIQDLEEQLDEEEAARQKLQLEK---VTTEAKIKKLEEDIL--LLEDQNSK----LSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 289 QALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEFEVRESEN 366
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 367 CEaalaEKEALLAKLHSENVTKNTenhrLLRNVKKVTQELNDLKKeklrlerDLEEAHREGNRGARTIHDLRNEVEKLRK 446
Cdd:pfam01576 242 EE----ELQAALARLEEETAQKNN----ALKKIRELEAQISELQE-------DLESERAARNKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 447 EV--------------CEREKAVEKHYKSLpgESSSKFHSQE---------QVVKGLTESASQedlllQKSNEKDLEAIQ 503
Cdd:pfam01576 307 ELedtldttaaqqelrSKREQEVTELKKAL--EEETRSHEAQlqemrqkhtQALEELTEQLEQ-----AKRNKANLEKAK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 504 QNCYLMTAE---ELKFGSDGLIT-----EKCSQQSPDSKLIFSK------------EKQQSEYEGLTGDLKTEQNVYAHL 563
Cdd:pfam01576 380 QALESENAElqaELRTLQQAKQDsehkrKKLEGQLQELQARLSEserqraelaeklSKLQSELESVSSLLNEAEGKNIKL 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281599321 564 AKN-------LQDTDSKLQAELKRVLA--------------LRKQLEQDVLAYRNLQ---TALQEQLSEIRKREEE 615
Cdd:pfam01576 460 SKDvsslesqLQDTQELLQEETRQKLNlstrlrqledernsLQEQLEEEEEAKRNVErqlSTLQAQLSDMKKKLEE 535
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1458-1575 |
1.33e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1458 QFLRKQNEalstmLEKGSKEKQKENEKL-------RESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQE 1530
Cdd:PRK12704 65 EIHKLRNE-----FEKELRERRNELQKLekrllqkEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 281599321 1531 vcsSLQELSRV----QEEAKsrqQLLLQ--KDELLQSLQMELKVYEKLAEE 1575
Cdd:PRK12704 140 ---QLQELERIsgltAEEAK---EILLEkvEEEARHEAAVLIKEIEEEAKE 184
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
126-349 |
1.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 126 KASKAVESLAEgggSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEkAFAgtETEKALRLSLESKLSAMKkm 205
Cdd:COG3206 149 LAAAVANALAE---AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE-EFR--QKNGLVDLSEEAKLLLQQ-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 206 qegdlemtlaLEEKDRLIEELKLSLKSKEALIQCLKEE-KSQMASPDENVSSGELRGLSATLRE-EKERDAEERQKERNH 283
Cdd:COG3206 221 ----------LSELESQLAEARAELAEAEARLAALRAQlGSGPDALPELLQSPVIQQLRAQLAElEAELAELSARYTPNH 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281599321 284 feERIQALQEDLREKEREIATEKKNSL-KRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE 349
Cdd:COG3206 291 --PDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-608 |
1.67e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 221 RLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQED---LRE 297
Cdd:pfam02463 123 ELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqeLKL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 298 KEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEV-----RESENCEAALA 372
Cdd:pfam02463 203 KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaqvlKENKEEEKEKK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 373 EKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEahregnrgARTIHDLRNEVEKLRKEVCERE 452
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK--------EKEEIEELEKELKELEIKREAE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 453 KAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQqncylmtaeelkfgSDGLITEKCSQQSPD 532
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--------------EAQLLLELARQLEDL 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281599321 533 SKLIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLSE 608
Cdd:pfam02463 421 LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
86-333 |
1.84e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 86 ERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGS----------EIQRVKEDARK---- 151
Cdd:pfam10174 460 EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKkdsklksleiAVEQKKEECSKlenq 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 152 --KVQQVEEL------LTKRIHLLEEDVK-------AAQAELEK---AFAGTETEKALRLSLESKLSAMKKMQEGDLEMT 213
Cdd:pfam10174 540 lkKAHNAEEAvrtnpeINDRIRLLEQEVArykeesgKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 214 LA------LEEKDRLIEELKLSLKSKEALIQC-----LKEEKSQMASPDENVSSGELRgLSATLREEKERDA---EERQK 279
Cdd:pfam10174 620 VAnikhgqQEMKKKGAQLLEEARRREDNLADNsqqlqLEELMGALEKTRQELDATKAR-LSSTQQSLAEKDGhltNLRAE 698
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 281599321 280 ERNHFEERIQALQEDL----REKEREIATEKKNSLKRDKAiQGLTMALK-SKEKEVEEL 333
Cdd:pfam10174 699 RRKQLEEILEMKQEALlaaiSEKDANIALLELSSSKKKKT-QEEVMALKrEKDRLVHQL 756
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-429 |
2.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 258 ELRGLSATLREEKERdAEERQKERNHFEERIQALQE---------DLREKEREIA--TEKKNSLKR-DKAIQGLTMALKS 325
Cdd:COG4913 618 ELAELEEELAEAEER-LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAelEAELERLDAsSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 326 KEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEVRESENCEAALAEKEALLAKLHSENVTKNTENhRLLRNVkkvT 403
Cdd:COG4913 697 LEAELEELEEELDELKGEigRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER-ELRENL---E 772
|
170 180
....*....|....*....|....*.
gi 281599321 404 QELNDLKKEKLRLERDLEEAHREGNR 429
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-430 |
3.53e-04 |
|
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: 45.14 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 215 ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgELRGLSATLRE-EKERDAEERQKERNhfEERIQALQE 293
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRAlEQELAALEAELAEL--EKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 294 DLREKEREIA---------------------TEKKNSLKRDKAIQGLTMALKskeKEVEELNSIIKELTA--DSTQSREA 350
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAAlrAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 351 PLKTQVSEFEvRESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRG 430
Cdd:COG4942 175 ELEALLAELE-EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-660 |
4.81e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 144 RVKEDaRKKVQQVEELLTKRIHLLEEDVKAAQAELekafagteTEKalrlslESKLSAMKKMQEGDLEMTLALEEKDRLI 223
Cdd:pfam05483 216 KLKED-HEKIQHLEEEYKKEINDKEKQVSLLLIQI--------TEK------ENKMKDLTFLLEESRDKANQLEEKTKLQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 224 EE-LKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSAT-----LREEKERDAEERQKERN--------------H 283
Cdd:pfam05483 281 DEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticqLTEEKEAQMEELNKAKAahsfvvtefeattcS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 284 FEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIK------------ELTADSTQSREAP 351
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAedeklldekkqfEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 352 LK--TQVSEFEVRESE--------NCEAALAEKEALLAKLHSENVtKNTE----NHRLLRNVKKVTQELNDLKKEKLRLE 417
Cdd:pfam05483 441 LIflLQAREKEIHDLEiqltaiktSEEHYLKEVEDLKTELEKEKL-KNIEltahCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 418 RDLEEAHREGNRGARTIH-------DLRNEVEKLRKEVCEREKAVE-KHYKSLPGESSSKFHSQEQVVKGLTESASQEDL 489
Cdd:pfam05483 520 EDIINCKKQEERMLKQIEnleekemNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 490 LLQKSNE-KDLEAIQQNCYLM----TAE-------ELKFGSDGLITEKCSQQSPDSKLIFSKE---KQQSEyEGLTGDLK 554
Cdd:pfam05483 600 KKQIENKnKNIEELHQENKALkkkgSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEiedKKISE-EKLLEEVE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 555 TEQNVYAHLAKNLQDTDSKLQAELKRVLALrkqLEQDVLAYRNLQTALQEQLSEIRKREEEPFSFYSDQTSYLSICLEE- 633
Cdd:pfam05483 679 KAKAIADEAVKLQKEIDKRCQHKIAEMVAL---MEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEl 755
|
570 580 590
....*....|....*....|....*....|
gi 281599321 634 ---HSQFQLEHFSQEEIKKKVIDLIQLVKD 660
Cdd:pfam05483 756 lslKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1405-1552 |
5.22e-04 |
|
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: 44.37 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1405 QEIRTLRKHLEESIKTNEKLRKQLERQgcETDQGSTNVSAYSSELHNSLT------------SEIQFLRKQNEALSTMLE 1472
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQ--KEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1473 KgSKEKQKENEKLRESLARKTESLEHLQleyASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLL 1552
Cdd:COG4942 154 E-LRADLAELAALRAELEAERAELEALL---AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
86-333 |
5.40e-04 |
|
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: 44.73 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 86 ERIQQEFAGP------TEHIYKKNIELKVEVESLKRELQERDQllvkasKAVESLAEGGGSEIQRVKEDARKKVQQVEel 159
Cdd:pfam17380 392 ERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQ------REVRRLEEERAREMERVRLEEQERQQQVE-- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 160 ltkRIHLLEEDVKAAQAELEKafagtETEKALRLSLESKLSAMKKMQegdlemtlalEEKDRLIEElklslKSKEALIQC 239
Cdd:pfam17380 464 ---RLRQQEEERKRKKLELEK-----EKRDRKRAEEQRRKILEKELE----------ERKQAMIEE-----ERKRKLLEK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 240 LKEEKSqmaspdenvssgelrglSATLREEKERDAEERQKERNHFEERIQaLQEDLRekereIATEKKNSLKRDKAIQGL 319
Cdd:pfam17380 521 EMEERQ-----------------KAIYEEERRREAEEERRKQQEMEERRR-IQEQMR-----KATEERSRLEAMEREREM 577
|
250
....*....|....
gi 281599321 320 TMALKSKEKEVEEL 333
Cdd:pfam17380 578 MRQIVESEKARAEY 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-455 |
5.79e-04 |
|
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: 44.37 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 263 SATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA 342
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 343 DStQSREAPLKTQV------------------SEFE------------VRESENCEAALAEKEALLAKLHSENVTKNTEN 392
Cdd:COG4942 98 EL-EAQKEELAELLralyrlgrqpplalllspEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281599321 393 HRLLRNVKKVTQELNDLKKEKL----RLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAV 455
Cdd:COG4942 177 EALLAELEEERAALEALKAERQkllaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1397-1568 |
5.97e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAysSELHNSLTSEIQFLRKQNEALSTMLEKGS- 1475
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHp 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1476 --KEKQKENEKLRESLARKTES-LEHLQLEYASVREENERLRRDISEKERQNQQLTQevcsSLQELSRVQEEAKSRQQLL 1552
Cdd:COG3206 292 dvIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELY 367
|
170
....*....|....*.
gi 281599321 1553 lqkDELLQSLQmELKV 1568
Cdd:COG3206 368 ---ESLLQRLE-EARL 379
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
211-595 |
7.00e-04 |
|
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: 44.58 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 211 EMTLALEEKDRLIEELKLSLKSKEaliqclKEEKSQMaspdenvssgELRGLSATLREEKERDAEERQkeRNHFEERIQA 290
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLK------EQAKKAL----------EYYQLKEKLELEEEYLLYLDY--LKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 291 LQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEfevrESENCEAA 370
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK----VDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 371 LAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGnrgartiHDLRNEVEKLRKEVCE 450
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE-------LLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 451 REKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLitEKCSQQS 530
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL--KDELELK 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281599321 531 PDSKLIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAY 595
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1390-1582 |
8.76e-04 |
|
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: 44.34 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1390 TIASRFPQDLLMEHIQEirTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSEIQFLRKQNEalst 1469
Cdd:pfam17380 283 AVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1470 mlekgskEKQKENEKLR-ESLA---RKTESLEHLQLEYasvREENERLRRD--------ISEKERQNQQLTQEVcsSLQE 1537
Cdd:pfam17380 357 -------ERKRELERIRqEEIAmeiSRMRELERLQMER---QQKNERVRQEleaarkvkILEEERQRKIQQQKV--EMEQ 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 281599321 1538 LSRVQEEAKSRQqllLQKDELLQSLQMELKVYEKLAEEHQ--KLQQD 1582
Cdd:pfam17380 425 IRAEQEEARQRE---VRRLEEERAREMERVRLEEQERQQQveRLRQQ 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1397-1602 |
9.62e-04 |
|
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: 44.29 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgcetdqgSTNVSAYSSELHNSLTSEIQFLRKQNEALSTMLEKGSK 1476
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ--------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1477 EKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKD 1556
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 281599321 1557 ELLQSLQ---MELKVYEKLAEEHQKLQQDVNKCPEASDNSFDLFESTQA 1602
Cdd:TIGR02169 938 DPKGEDEeipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
215-376 |
9.75e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 215 ALEEKDRLIEELKLSLKS--KEALIQcLKEEKSQmaspdenvssgelrglsatLREEKERDAEERQKERNHFEERIQALQ 292
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAikKEALLE-AKEEIHK-------------------LRNEFEKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 293 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS-------IIKELTADSTQSR-----EAPLKTQVSEFe 360
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeqlqeleRISGLTAEEAKEIllekvEEEARHEAAVL- 174
|
170
....*....|....*..
gi 281599321 361 VRESENcEAAL-AEKEA 376
Cdd:PRK12704 175 IKEIEE-EAKEeADKKA 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1563 |
9.82e-04 |
|
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: 43.60 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1476 KEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQ-EEAKSRQQLLLQ 1554
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQ 102
|
....*....
gi 281599321 1555 KDELLQSLQ 1563
Cdd:COG4942 103 KEELAELLR 111
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-615 |
1.08e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 277 RQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS-------IIKELTADSTQ--S 347
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDklkknkdKINKLNSDLSKinS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 348 REAPLKTQVSEFEVrESENCEAALAEKEALLAKLhsenvtkNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREG 427
Cdd:TIGR04523 111 EIKNDKEQKNKLEV-ELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 428 NRGARTIHDLRNEVEKLRKEVCEREKAVEKHyKSLpgesSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQncy 507
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL----ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 508 LMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKT--EQNVYAHLAKNLQDTDSKLQ---------- 575
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEeiqnqisqnn 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 281599321 576 ---AELKRVLA-LRKQLEQDVLAYRNLQTALQEQLSEIRKREEE 615
Cdd:TIGR04523 335 kiiSQLNEQISqLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-451 |
1.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEGG-----------------GSEIQRVKEDARKKVQQVEELlTKRIHLL 167
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleeraeelreeaaelESELEEAREAVEDRREEIEEL-EEEIEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 168 EEDVKAAQAELEKAF-----------AGTETEKALRLSLESKLSAMKKMQE--------------GDLEMTLALEEKDRL 222
Cdd:PRK02224 397 RERFGDAPVDLGNAEdfleelreerdELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 223 IEELKLSLKSKEALIQCLKEE----KSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREK 298
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 299 eREIATEK---------------------KNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQ 355
Cdd:PRK02224 557 -REAAAEAeeeaeeareevaelnsklaelKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRErlAEKRER 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 356 VSEFEVR-ESENCEAALAEKEAllAKLHSENVTKNTENHRLLRN--------VKKVTQELNDLKKEKLRLE---RDLEEA 423
Cdd:PRK02224 636 KRELEAEfDEARIEEAREDKER--AEEYLEQVEEKLDELREERDdlqaeigaVENELEELEELRERREALEnrvEALEAL 713
|
410 420
....*....|....*....|....*...
gi 281599321 424 HREGNRGARTIHDLRNEVEKLRKEVCER 451
Cdd:PRK02224 714 YDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
46-376 |
1.20e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 46 IMSEEKVSPTRARNMK--DFENQITELKKENFNlklRIYFLEERIQQEFAGPTEHiykkniELKVEVESLKRELQERDQL 123
Cdd:NF033838 70 ILSEIQKSLDKRKHTQnvALNKKLSDIKTEYLY---ELNVLKEKSEAELTSKTKK------ELDAAFEQFKKDTLEPGKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 124 LVKASKAVEslaEGGGSEIQRVKEDARKKVQQVEEllTKRIHLLEEDVKAAQAELE------KAFAGTETEKALRLSLES 197
Cdd:NF033838 141 VAEATKKVE---EAEKKAKDQKEEDRRNYPTNTYK--TLELEIAESDVEVKKAELElvkeeaKEPRDEEKIKQAKAKVES 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 198 KLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKS--------QMASPD--EN------VSSGELRG 261
Cdd:NF033838 216 KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRrakrgvlgEPATPDkkENdakssdSSVGEETL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 262 LSATLREEK-----ERDAEERQKE---------RNH-------FEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLT 320
Cdd:NF033838 296 PSPSLKPEKkvaeaEKKVEEAKKKakdqkeedrRNYptntyktLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAK 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 281599321 321 MALKSKEKEVEELNSIIKEL-TADSTQSREAPLKTQVSEFEVRESENCEAALAEKEA 376
Cdd:NF033838 376 AKVESKKAEATRLEKIKTDRkKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPA 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1400-1585 |
1.21e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1400 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLekgsKEKQ 1479
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREAL----DELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1480 KENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELL 1559
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180
....*....|....*....|....*.
gi 281599321 1560 QSLQMElkvYEKLAEEHQKLQQDVNK 1585
Cdd:TIGR02168 890 ALLRSE---LEELSEELRELESKRSE 912
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-446 |
1.41e-03 |
|
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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 264 ATLREEKER-DAEERQKERNHFEERIQALQEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKEVEELnsiiKELTA 342
Cdd:COG4913 272 AELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEA--------------RLDALREELDEL----EAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 343 DSTQSREAPLKTQVSEFEvRESENCEAALAEKEALLAKLHsenVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEE 422
Cdd:COG4913 334 GNGGDRLEQLEREIERLE-RELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
|
170 180
....*....|....*....|....
gi 281599321 423 AHREGNRGARTIHDLRNEVEKLRK 446
Cdd:COG4913 410 AEAALRDLRRELRELEAEIASLER 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-412 |
1.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 55 TRARNMKDFENQITELKKENFNLKLRIYFLEERIqQEFAGPTEHIYKKNIELKVEVESLKRELQERDQllvkaskavesl 134
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK------------ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 135 aegggsEIQRVKEDARKKVQQVEElLTKRIHLLEEDVKaaqaELEKafagtetekaLRLSLESKLSAMKKmqegdlemtl 214
Cdd:TIGR04523 427 ------EIERLKETIIKNNSEIKD-LTNQDSVKELIIK----NLDN----------TRESLETQLKVLSR---------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 215 ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsatlrEEKERDAEERQKErnhFEERIQALQED 294
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKEL--------------------EEKVKDLTKKISS---LKEKIEKLESE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 295 LREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEVRESenceaaLA 372
Cdd:TIGR04523 533 KKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE------IE 606
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 281599321 373 EKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE 412
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1453-1585 |
1.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1453 LTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVC 1532
Cdd:COG1196 237 LEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 281599321 1533 SSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-343 |
1.73e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 64 ENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNiELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQ 143
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 144 RVKEDARKKVQQVEEL--LTKRIHLLEEDVKAAQAELE-----------------KAFAGTETE-KALRLSLESKLSAMK 203
Cdd:TIGR02168 825 RLESLERRIAATERRLedLEEQIEELSEDIESLAAEIEeleelieeleseleallNERASLEEAlALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 204 KMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEeksqmaspdenvssgelrglsaTLREEKERDAEERQKERNH 283
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE----------------------RLSEEYSLTLEEAEALENK 962
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281599321 284 FEERIQALQEDLREKEREIA----------TEKKNSLKR----DKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERydflTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1405-1581 |
1.77e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSeiqflRKQNEALSTMLEKGSKEKQKENEK 1484
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1485 LRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQM 1564
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
170
....*....|....*..
gi 281599321 1565 ElKVYEKLAEEHQKLQQ 1581
Cdd:TIGR02168 436 K-ELQAELEELEEELEE 451
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
78-344 |
1.92e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 78 KLRIYFLEERIQQEFagptEHIYKKNIelkVEVESLKRELQ-ERDQ----LLVKASKAVESL-----AEGGGSEIQRVKE 147
Cdd:PRK05771 8 KVLIVTLKSYKDEVL----EALHELGV---VHIEDLKEELSnERLRklrsLLTKLSEALDKLrsylpKLNPLREEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 148 DARKK--VQQVEELLTKrihlLEEDVKAAQAELEKAfagtETEKAlrlSLESKLSAMKKMQEGDLEMTLALEEKDRLIEE 225
Cdd:PRK05771 81 VKSLEelIKDVEEELEK----IEKEIKELEEEISEL----ENEIK---ELEQEIERLEPWGNFDLDLSLLLGFKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 226 LKLSLKSKEALIQ--------CLKEEKSQM------ASPDENVSSGELR------------GLSATLREEKERDAEERQK 279
Cdd:PRK05771 150 GTVPEDKLEELKLesdvenveYISTDKGYVyvvvvvLKELSDEVEEELKklgferleleeeGTPSELIREIKEELEEIEK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281599321 280 ERNHFEERIQALQEdlREKEREIATEKKNSLKRDKAiQGLTMALKSK----------EKEVEELNSIIKELTADS 344
Cdd:PRK05771 230 ERESLLEELKELAK--KYLEELLALYEYLEIELERA-EALSKFLKTDktfaiegwvpEDRVKKLKELIDKATGGS 301
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
105-351 |
2.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEgggsEIQRVKEDARKKVQQVEELlTKRIHLLEEDVKAAQAELEKAFAG 184
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKL-QAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 185 TETEKALRLSLE------------SKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKsqmaspde 252
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 253 nvssgelrglsatlrEEKERDAEERQKERnhfeeriQALQEDLREKEREiATEKKNSLKRDKAIQGLTMALKSKEKEVEE 332
Cdd:COG3883 167 ---------------EAAKAELEAQQAEQ-------EALLAQLSAEEAA-AEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*....
gi 281599321 333 LNSIIKELTADSTQSREAP 351
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAA 242
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
258-363 |
2.64e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 258 ELRGLSATLRE-EKERDAEERQKERNHFEeRIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSI 336
Cdd:COG0542 412 ELDELERRLEQlEIEKEALKKEQDEASFE-RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....*....
gi 281599321 337 IKELTADSTQSREAP--LKTQVSEFEVRE 363
Cdd:COG0542 491 EKELAELEEELAELAplLREEVTEEDIAE 519
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
218-340 |
2.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 218 EKDRLIEELKLSL---KSKEALIQCLKEEksqmASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQED 294
Cdd:COG2433 360 PPDVDRDEVKARVirgLSIEEALEELIEK----ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 281599321 295 LREKEREIA----------TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEL 340
Cdd:COG2433 436 LEEKDERIErlerelsearSEERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
96-664 |
2.96e-03 |
|
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: 42.65 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 96 TEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQvEELLTKRIHLLEE--DVKA 173
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAITCTaqCEKL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 174 AQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDEN 253
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 254 VSSGElrglsaTLREEKERDAEERQKERNHFEERIQALQEDLrekerEIATEKKNSLKR--DKAIQGLTMALKSKEKEVE 331
Cdd:TIGR00618 537 YAQLE------TSEEDVYHQLTSERKQRASLKEQMQEIQQSF-----SILTQCDNRSKEdiPNLQNITVRLQDLTEKLSE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 332 ELNSIIKELTADSTQSREAPLKTQVSEFEVRESENCEAALAEKEALLAKLHSENVTkntENHRLLRNVKKVTQELNDLKK 411
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR---EHALSIRVLPKELLASRQLAL 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 412 EKLRLERDLEEAHREG-NRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLL 490
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 491 LQKSNEKDLEAIQQNCYLMTAEelkfgsdGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNVyaHLAKNLQDT 570
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLA-------AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE--TLVQEEEQF 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 571 DSKLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLS--------------EIRKREEEPFSFYSDQTSYLSICL--EEH 634
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiqlsdklnginqiKIQFDGDALIKFLHEITLYANVRLanQSE 913
|
570 580 590
....*....|....*....|....*....|
gi 281599321 635 SQFQLEHFSQEEIKKKVIDLIQLVKDLHAD 664
Cdd:TIGR00618 914 GRFHGRYADSHVNARKYQGLALLVADAYTG 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
140-394 |
3.05e-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: 42.06 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 140 SEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKKmQEGDLEMTLALEEK 219
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------------LERRIAALAR-RIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 220 DrlIEELKLSLKSKEALIQCLKEEKSQMAspDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKE 299
Cdd:COG4942 84 E--LAELEKEIAELRAELEAQKEELAELL--RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 300 REIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAdSTQSREAPLKTQVSEFEvRESENCEAALAEKEALLA 379
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQ-QEAEELEALIARLEAEAA 237
|
250
....*....|....*
gi 281599321 380 KLHSENVTKNTENHR 394
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
60-355 |
3.50e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 60 MKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQER-DQLLVKASKAVESLAEG- 137
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTENl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 138 -----------GGSEIQRVKEDARKKVQQVE----ELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAM 202
Cdd:COG5185 357 eaikeeienivGEVELSKSSEELDSFKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 203 KKMQEGDLEMTLALEEKDRLIEELKLSlKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERN 282
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQS-RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281599321 283 HFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELT-----ADSTQSREAPLKTQ 355
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTqylstIESQQAREDPIPDQ 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1400-1585 |
3.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1400 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgcetdqgstnVSAYSSELhNSLTSEIQFLRKQNEALSTML---EKGSK 1476
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKE-----------LEELKEEI-EELEKELESLEGSKRKLEEKIrelEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1477 EKQKENEKLRESLARkTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcSSLQELSRVQEEAKSRQQLLLQKD 1556
Cdd:PRK03918 270 ELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI-NGIEERIKELEEKEERLEELKKKL 347
|
170 180
....*....|....*....|....*....
gi 281599321 1557 ELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEELER 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1405-1593 |
4.11e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHnSLTSEIQFLRKQNEALSTMLEKGSKEK---QKE 1481
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIaqlSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1482 NEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKS----RQQLLLQKDE 1557
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlrerLESLERRIAA 835
|
170 180 190
....*....|....*....|....*....|....*.
gi 281599321 1558 LLQSLQMELKVYEKLAEEHQKLQQDVNKCPEASDNS 1593
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-496 |
4.41e-03 |
|
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: 41.88 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 64 ENQITELKKENFNLKLRIYFLEERIQQEfaGPTEHIYKKNIELKVEVESLKRELQERDQLLVK-----ASKAVESLAEGG 138
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNPGP 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 139 GSEIQRVKEDARKKVQQVEELLTkriHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEE 218
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVY---HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 219 KDRliEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKE--------RNHFEERIQA 290
Cdd:TIGR00618 603 LSE--AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirvlPKELLASRQL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 291 LQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEVRESENCEAA 370
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKART 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 371 LAEKEALLAKLHSEnvtkntenhrllrnvkKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCE 450
Cdd:TIGR00618 761 EAHFNNNEEVTAAL----------------QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 281599321 451 REKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNE 496
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1362-1597 |
5.58e-03 |
|
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: 41.88 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1362 HALSDDEMSEKSFLSREPKPDSETEKYPTIASrfpqdlLMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgCETDQGSTn 1441
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTY------WKEMLAQCQTLLRELETHIEEYDREFNEIEN--ASSSLGSD- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1442 vSAYSSELHNSLTSEIQFLRKqnealsTMLEKGSKEKQKENEKLRESLARKTEsLEHLQLEYASVREENERLRRDISEKE 1521
Cdd:TIGR00618 734 -LAAREDALNQSLKELMHQAR------TVLKARTEAHFNNNEEVTAALQTGAE-LSHLAAEIQFFNRLREEDTHLLKTLE 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281599321 1522 RQNQQltqEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELK-VYEKLAEEHQKLQQDVNKCPEASDNSFDLF 1597
Cdd:TIGR00618 806 AEIGQ---EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIThQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1465-1581 |
5.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1465 EALSTMLEKGSKEKQKENEKLRES----LARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcsslqelsr 1540
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEREL--------- 450
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 281599321 1541 vqEEAKSRQQLLLQKDELLQSLQMELKVYEK-LAEEHQKLQQ 1581
Cdd:COG2433 451 --SEARSEERREIRKDREISRLDREIERLEReLEEERERIEE 490
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
263-569 |
6.46e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 263 SATLREEKERDAEERQKERNHFEERIQALQEDLREK--EREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEL 340
Cdd:COG5185 262 NTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKiaEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 341 TADSTQSREAPLKTQVSEFEVRESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELND-LKKEKLRLERD 419
Cdd:COG5185 342 TAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 420 LEEAHREGNRG-------ARTIHDLRNEVEKLRKEVCEREKA-VEKHYKSLP-------GESSSKFHSQEQVVKGLTESA 484
Cdd:COG5185 422 IEELQRQIEQAtssneevSKLLNELISELNKVMREADEESQSrLEEAYDEINrsvrskkEDLNEELTQIESRVSTLKATL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 485 SQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGsDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNVYAHLA 564
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARG-YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTI 580
|
....*
gi 281599321 565 KNLQD 569
Cdd:COG5185 581 ESQQA 585
|
|
| DUF445 |
pfam04286 |
Protein of unknown function (DUF445); Predicted to be a membrane protein. |
144-381 |
6.66e-03 |
|
Protein of unknown function (DUF445); Predicted to be a membrane protein.
Pssm-ID: 427840 [Multi-domain] Cd Length: 368 Bit Score: 41.07 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 144 RVKEDARKKVQQVEELLTKRIHLLEEDvkAAQAELEKAFAGTETEKALRLSLESKLSAMkkMQEGDLEMTLaleekDRLI 223
Cdd:pfam04286 77 ADPTNAERLAREVAKLLAEILEDLDDE--RVQRLLKKALRRRLEEIDLAPLLGKLLELL--LAEGRHQALL-----DDLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 224 EELKLSLKSKEA------LIQCLKEEKSQMASPDENVSSGELRGLSATLRE-EKERDAEERQKERNHFEERIQALQEDlr 296
Cdd:pfam04286 148 DRLRDWLRSEEGkqriaeMIDEFLEEWGPLVALLGGIAEMILRALSSLLDEvQADPDHPLRLAFDRAVRELITDLLND-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 297 EKEREIATEKKNSLKRDKAIQGLTMALkskekeVEELNSIIKELTADSTQSREAPLKTQVSEFevresencEAALAEKEA 376
Cdd:pfam04286 226 PELRAEVEELKQKLLADPAVQDYVKAL------WESLRSLLLDDLSDPDSALRRRISELLAEF--------GERLAEDPE 291
|
....*
gi 281599321 377 LLAKL 381
Cdd:pfam04286 292 LRDKL 296
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
105-615 |
7.21e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 105 ELKVEVESLKRELQERDQLLVKASK--AVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLE---EDVKaaQAELE 179
Cdd:pfam10174 203 QKEKENIHLREELHRRNQLQPDPAKtkALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEdreEEIK--QMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 180 KA---FAGTETEKaLRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEksqmaspdenVSS 256
Cdd:pfam10174 281 KShskFMKNKIDQ-LKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTE----------VDA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 257 GELR-GLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIatekkNSLKrdKAIQGLTMALKSKEKEVEELNS 335
Cdd:pfam10174 350 LRLRlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKI-----NVLQ--KKIENLQEQLRDKDKQLAGLKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 336 IIKELTADSTQSREApLKTqvsefevresenCEAALAEKEALLAKLHSEnvtKNTENHRLLRNVKKVTQELNDLKKEKLR 415
Cdd:pfam10174 423 RVKSLQTDSSNTDTA-LTT------------LEEALSEKERIIERLKEQ---REREDRERLEELESLKKENKDLKEKVSA 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 416 LERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSS--KFHSQEQVVKGLTESASQEDLLLQK 493
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQlkKAHNAEEAVRTNPEINDRIRLLEQE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 494 SNEKDLEAIQQNCYLmtaEELKfgsdGLITEKCSQQSpdsklifSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSK 573
Cdd:pfam10174 567 VARYKEESGKAQAEV---ERLL----GILREVENEKN-------DKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 281599321 574 LQAELKrVLALRkqlEQDVLAYRNLQTALQEQLSEIRKREEE 615
Cdd:pfam10174 633 KGAQLL-EEARR---REDNLADNSQQLQLEELMGALEKTRQE 670
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-342 |
8.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 56 RARNMKDFENQITELKKenfnlKLRIYFLE--ERIQQEFagptEHIYKKNIELKVEVESLKRELqERDQLLVKASKAVES 133
Cdd:PRK03918 494 ELIKLKELAEQLKELEE-----KLKKYNLEelEKKAEEY----EKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 134 laegggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKaaqaELEKAFAGTETEKALRLSLESKLSAMKKMQEgDLEMT 213
Cdd:PRK03918 564 -------KLDELEEELAELLKELEELGFESVEELEERLK----ELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 214 LA-LEEKDRLIEELKLSLkskealiqclkEEKSQMASPDENvssgelrglsatlrEEKERDAEERQKERNHFEERIQALQ 292
Cdd:PRK03918 632 FEeLAETEKRLEELRKEL-----------EELEKKYSEEEY--------------EELREEYLELSRELAGLRAELEELE 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 281599321 293 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKeVEELNSIIKELTA 342
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKA 735
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
97-615 |
8.14e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 97 EHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKrihlleedvkaAQA 176
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD-----------CQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 177 ELEKafagtetekalrLSLESKLsamkkmqegdlemtLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdENVSS 256
Cdd:TIGR00606 327 ELEK------------LNKERRL--------------LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ----SLATR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 257 GELRGLSATLREEKE-RDAEERQKERNHFEER-IQALQEDLREKEReIATEKKNSLKRDKAIQGLTMALKSK--EKEVEE 332
Cdd:TIGR00606 377 LELDGFERGPFSERQiKNFHTLVIERQEDEAKtAAQLCADLQSKER-LKQEQADEIRDEKKGLGRTIELKKEilEKKQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 333 LNSIIKELTADSTQSREAPLKTQvsefEVRESENcEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE 412
Cdd:TIGR00606 456 LKFVIKELQQLEGSSDRILELDQ----ELRKAER-ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 413 KLRLERDLEEAhregnrgartiHDLRNEVEKLRKEVCEREKAVEKHYKSLPGES--SSKFHSQEQVVKGLTESASQEDLL 490
Cdd:TIGR00606 531 TTTRTQMEMLT-----------KDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKqlEDWLHSKSKEINQTRDRLAKLNKE 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 491 LQKSnEKDLEAIQQNCYLMTAEELKFGSDglITEKCSQQSPDSKLIFSKEKQQSEYEGLtGDLKTEQNVYAHLAKNLQDT 570
Cdd:TIGR00606 600 LASL-EQNKNHINNELESKEEQLSSYEDK--LFDVCGSQDEESDLERLKEEIEKSSKQR-AMLAGATAVYSQFITQLTDE 675
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 281599321 571 DS----------KLQAELKRVLalrKQLEQDVLAYRNLQTALQEQLSEIRKREEE 615
Cdd:TIGR00606 676 NQsccpvcqrvfQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1451-1585 |
8.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1451 NSLTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQE 1530
Cdd:COG4372 48 EQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 281599321 1531 VCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1402-1581 |
8.74e-03 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 40.34 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1402 EHIQEIRTLRKHLEESIKtneklrkqlerqgcetdqgstnvsaysselhnsltSEIQFLRKQNEALSTMLEKGSKEKQKE 1481
Cdd:pfam09311 154 EELIEVRTAADHMEEKLK-----------------------------------AEILFLKEQIQAEQCLKENLEETLQAE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 1482 NEKLRESLArkteSLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQS 1561
Cdd:pfam09311 199 IENCKEEIA----SISSLKVELERIKAEKEQLENGLTEKIRQLEDLQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQR 274
|
170 180
....*....|....*....|
gi 281599321 1562 LQMELKVYEKLAEEHQKLQQ 1581
Cdd:pfam09311 275 LQTELDVSEQVQRDFVKLSQ 294
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
230-377 |
9.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 230 LKSKEAliQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNS 309
Cdd:PRK12705 30 RLAKEA--ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281599321 310 LKRDKAIQGLTMALKSKEKEVEELNSIIKELTADstQSREAPLKTQVSEFE------VRESENCEAALAEKEAL 377
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAELEeekaqrVKKIEEEADLEAERKAQ 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-457 |
9.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 279 KERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAplktqvse 358
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281599321 359 fevRESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAhregnrgartIHDLR 438
Cdd:COG1579 89 ---KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE----------LAELE 155
|
170
....*....|....*....
gi 281599321 439 NEVEKLRKevcEREKAVEK 457
Cdd:COG1579 156 AELEELEA---EREELAAK 171
|
|
| |
