|
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 |
2.31e-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: 2.31e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351376 61 KDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASK 129
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-455 |
1.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 146 KEDARKKVQQVEELLTkRIHLLEEDVKAAQAELEKafagtETEKALR----------LSLESKLSAMKKMQEGDLEMTLA 215
Cdd:COG1196 174 KEEAERKLEATEENLE-RLEDILGELERQLEPLER-----QAEKAERyrelkeelkeLEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 216 LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASpdenvssgELRGLSATLREEKERDAEERQkERNHFEERIQALQEDL 295
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELEL--------ELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA---DSTQSREAPLKTQVSEFEESENCEAALAEK 372
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEallEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 373 EALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKA 452
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
...
gi 564351376 453 VEK 455
Cdd:COG1196 479 LAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-462 |
3.35e-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: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 138 GGSEIQRVKEDARKKVQQVEELLtKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLE----SKLSAMKKMQEGDLEMT 213
Cdd:TIGR02169 164 GVAEFDRKKEKALEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 214 LA--------LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLR------EEKERDAEERQK 279
Cdd:TIGR02169 243 ERqlasleeeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 280 ERNHFEERIQALQEDLREKEREIATEKKnslKRDKaiqgLTMALKSKEKEVEELNSIIKELTADSTQSREA--------- 350
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERK---RRDK----LTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyrekle 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 351 -------PLKTQVSEF--------EESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLE 415
Cdd:TIGR02169 396 klkreinELKRELDRLqeelqrlsEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564351376 416 RDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPG 462
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-613 |
1.32e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 97 EHIYKKNIELKVEVESLKRELQErdqlLVKASKAVESLAEGGGSEIQRVKEDARKkvqqveelLTKRIHLLEEDVKAAQA 176
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEK----FIKRTENIEELIKEKEKELEEVLREINE--------ISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 177 ELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELK------LSLKSKEALIQCLKEEKSQMASP 250
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelKELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 251 DENVS------SGELRGLSATL--REEKERDAEERQKERNHFEERIQALQEDLREKEReiATEKKNSLKRDKA------I 316
Cdd:PRK03918 309 LREIEkrlsrlEEEINGIEERIkeLEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKrltgltP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 317 QGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEESEN----CEAALAE--KEALLAKLHSenvtknt 388
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARigELKKEIKELKKAIEELKKAKGkcpvCGRELTEehRKELLEEYTA------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 389 ENHRLLRNVKKVTQELNDLKKEKLRLERDLEEaHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGES---S 465
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 466 SKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQNCYLmtaEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYE 545
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKELEPFYNEYLELKDAEKELE 615
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564351376 546 GLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRK--------QLEQDVLAYRNLQTALQEQLSEIRKREEE 613
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-446 |
2.27e-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: 65.85 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 160 LTKRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKKMQEgdlEMTLALEEKDRLIEELKLSLKSKEALIQC 239
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAE--------------LRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 240 LKEEKSQMASPDENV-----SSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDK 314
Cdd:TIGR02168 745 LEERIAQLSKELTELeaeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 315 AIQGLTMALKSKEKEVEELNSIIKELTADSTQSREaplktqvsefeESENCEAALAEKEALLAKLHSENVTKNTENHRLL 394
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAA-----------EIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564351376 395 RNVKKVTQELNDLKKEKLRLERDLEEAHREgnrgartIHDLRNEVEKLRKEV 446
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREK-------LAQLELRLEGLEVRI 938
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-613 |
3.51e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 85 EERIQQEFAGPTEHIYKKNIELKVE----VESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELL 160
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 161 TKRIHLLEEDVKAAQ-AELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEAliQC 239
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA--DE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 240 LKEEKSQMASPDENVSSGELRGLSAtlrEEKERDAEERQKERNHFEERIQALQEDLRE-KEREIATEKKNSLKRDKAiqg 318
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKA---DAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKA--- 1380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 319 ltMALKSKEKEVEELNSIIKEL-----TADSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRL 393
Cdd:PTZ00121 1381 --DAAKKKAEEKKKADEAKKKAeedkkKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 394 LRNVKKVTQELN--DLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKlRKEVCEREKAVEKHYKSLPGESSSKFHSQ 471
Cdd:PTZ00121 1459 AEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 472 E----QVVKGLTESASQEDLL----LQKSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSE 543
Cdd:PTZ00121 1538 EakkaEEKKKADELKKAEELKkaeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351376 544 YEGLTGDLKTEQNVyahlAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYRNLQTALQE---QLSEIRKREEE 613
Cdd:PTZ00121 1618 AKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkKAEEAKKAEED 1686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-432 |
3.76e-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: 65.46 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 142 IQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFagtETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDR 221
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 222 LIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRgLSATL------REEKERDAEERQKERNHFEERIQALQEDL 295
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-LEAQLeeleskLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEES------ENCEA 367
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARleRLEDRRERLQQEIEELLKKleeaelKELQA 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564351376 368 ALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE------KLRLERDLEEAHREGNRGARTI 432
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQENLEGFSEGVKAL 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-467 |
4.92e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 59 NMKDFENQITELKKENFNLKLRIYFLEERIQQ-EFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEG 137
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 138 GGSEIQRVKEDARKKVQQVEELLT-KRIHLLEEDVKAAQAELE---KAFAGTETEKalrlsLESKLSAMKKMQEgdlEMT 213
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEElEERHELYEEAKAKKEELErlkKRLTGLTPEK-----LEKELEELEKAKE---EIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 214 LALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKernhFEERIQALQE 293
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKE----IEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 294 DLREKEREIATEKKNSLKRDKAIQgltmaLKSKEKEVEELNsiIKELTADSTQSRE-----APLKTQVSEFEESENCEAA 368
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYN--LEELEKKAEEYEKlkeklIKLKGEIKSLKKELEKLEE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 369 L-AEKEALLAKLHSENVTKNTENHRLLR------------------------NVKKVTQELNDLKKEKLRLERDLEEAHR 423
Cdd:PRK03918 554 LkKKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKKLEEELDKAFE 633
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564351376 424 EGNRGARTIHDLRNEVEKLRKEVCERE-KAVEKHYKSLPGESSSK 467
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGL 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-571 |
1.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 101 KKNIELKVEVESLKRELQER---DQLLVKASKAVESLAEGGGSEIQRVKEDARKK----VQQVEELLTKRihllEEDVKA 173
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKkaeeKKKADEAKKKA----EEAKKA 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 174 AQAElEKAFAGTETEKALRLSLESKLS--AMKKMQEGDL--EMTLALEEKDRLIEELKlslKSKEAliqclKEEKSQMAS 249
Cdd:PTZ00121 1447 DEAK-KKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKadEAKKKAEEAKKKADEAK---KAAEA-----KKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 250 PDENVSSGELRGLSATLREEKERDAEERQKErnhfEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKE 329
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 330 VEELNSIIKEltadstqsrEAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKvTQELNDLKK 409
Cdd:PTZ00121 1594 IEEVMKLYEE---------EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK-AEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 410 EKLRleRDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVE---------KHYKSLPGESSSKFHSQEQVVKGLTE 480
Cdd:PTZ00121 1664 AEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeaeekKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 481 SASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSpdsklifskEKQQSEYEGLTGDLKT------- 553
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED---------EKRRMEVDKKIKDIFDnfaniie 1812
|
490 500
....*....|....*....|.
gi 564351376 554 ---EQNVYAHLAKNLQDTDSK 571
Cdd:PTZ00121 1813 ggkEGNLVINDSKEMEDSAIK 1833
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-610 |
1.19e-09 |
|
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: 63.54 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 59 NMKDFENQITELKKENFNLKLRIYFLEERIQQEfagptehiYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGG 138
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETL--------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 139 GSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEE 218
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 219 KDRLIEELKLSLKSKEALIQCLkeekSQMASPDENVSS------GELRGLSATLREEKERDAEERQKE----RNHFEE-- 286
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVL----SELISVDEGYEAaieaalGGRLQAVVVENLNAAKKAIAFLKQnelgRVTFLPld 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 287 -----RIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS---IIKELTAD--------------- 343
Cdd:TIGR02168 580 sikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNaleLAKKLRPGyrivtldgdlvrpgg 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 344 -STQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAH 422
Cdd:TIGR02168 660 vITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 423 REGNRGARTIHDLRNEVEKLRKEVCEREKAVEkhykslpgESSSKFHSQEQVVKGLTESA--SQEDLLLQKSNEKDLEAI 500
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLE--------EAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAE 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 501 qqncylMTAEELKFGSDGLITEKCSQQspdsklIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVL 580
Cdd:TIGR02168 812 ------LTLLNEEAANLRERLESLERR------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
570 580 590
....*....|....*....|....*....|
gi 564351376 581 ALRKQLEQDVLAYRNLQTALQEQLSEIRKR 610
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESK 909
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-727 |
1.87e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 101 KKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKV-QQVEELLTKRIHLLEEDVKAAQA--- 176
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIaRKAEDARKAEEARKAEDAKKAEAark 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 177 --------ELEKAFAGTETEKALRLSLESKLSAMKKMQEGD-LEMTLALEEKDRLIEELKLSLKSKE-ALIQCLKEEKSQ 246
Cdd:PTZ00121 1184 aeevrkaeELRKAEDARKAEAARKAEEERKAEEARKAEDAKkAEAVKKAEEAKKDAEEAKKAEEERNnEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 247 MASPDENVSSGELRGLSATLR--EEKERDAEERQKERNHFEERIQALQEDLR-----EKEREIATEKKNSLKR--DKAIQ 317
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeaKKKAEEAKKKADAAKKkaEEAKK 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 318 GLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNV 397
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 398 KKVTQElndlKKEKLRLERDLEEahregnrgARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKG 477
Cdd:PTZ00121 1424 KKKAEE----KKKADEAKKKAEE--------AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 478 LTESASQEDLLLQKSNEKDleaiqqncylmTAEELKFGSDGLITEKCSQQSPDSKlifSKEKQQSEYEGLTGDLKTEQNV 557
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKK-----------KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELKKAEEL 1557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 558 YAhlAKNLQDTDSKLQAELKRVLALRKQLEqdvlayrnLQTALQEQLSEIRKREEEPFSFYSDQTSYlsiclEEHSQFQL 637
Cdd:PTZ00121 1558 KK--AEEKKKAEEAKKAEEDKNMALRKAEE--------AKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKA 1622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 638 EHFSQ-EEIKKKVIDLIQLVKDLHADNQHLKKTIFDISCMGVQGNDRLESTKQAELMASKADEDTLKFKADDENHFQSDQ 716
Cdd:PTZ00121 1623 EELKKaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
650
....*....|.
gi 564351376 717 HLEQSREIMED 727
Cdd:PTZ00121 1703 KAEELKKKEAE 1713
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-607 |
2.89e-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: 62.39 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 268 EEKERDAEERQKERNHfEERIQALQEDLREKEREIATEKKNSLKRDKA------------IQGLTMALKSKEKEVEELNS 335
Cdd:TIGR02169 194 DEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaierqlasleeeLEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 336 IIKELTA---DSTQSREAPLKTQVSEFE-ESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK 411
Cdd:TIGR02169 273 LLEELNKkikDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 412 LRLERDLEEahregnrgartihdLRNEVEKLRKEVCErekaVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQK 491
Cdd:TIGR02169 353 DKLTEEYAE--------------LKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 492 SNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNvyahlakNLQDTDSK 571
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-------RVEKELSK 487
|
330 340 350
....*....|....*....|....*....|....*.
gi 564351376 572 LQAELKRVLALRKQLEQDVLAYRNLQTALQEQLSEI 607
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-503 |
4.98e-09 |
|
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: 61.61 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 203 KKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRglsatlREEKERDAEERQKERN 282
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE------VSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 283 HFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTadstqsreaplktqvsefEES 362
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK------------------EEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 363 ENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDL-----RN 437
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEA 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351376 438 EVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKD-LEAIQQN 503
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDsLERLQEN 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-348 |
8.02e-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: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEgggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAG 184
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 185 TETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSA 264
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 265 TLREEKER-DAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:COG1196 406 EEAEEALLeRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
....*
gi 564351376 344 STQSR 348
Cdd:COG1196 486 LAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-516 |
1.27e-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: 60.08 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 217 EEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdeNVSSGELRGLSATLREeKERDAEERQKERNHFEERIQALQEDLR 296
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRL-----DELSQELSDASRKIGE-IEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 297 EKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEEL-----NSIIKELTADSTQsreapLKTQVSEFEES-ENCEAALA 370
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK-----LEEEVSRIEARlREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 371 EKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREgnrgartIHDLRNEVEKLRKEVCERE 450
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351376 451 K---AVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQK--------SNEKDLEAIQQNCYLMTAEELKFGS 516
Cdd:TIGR02169 896 AqlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgedeeipEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
61-455 |
1.90e-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: 59.26 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 61 KDFENQITELKKENFNLKLRIyfleERIQQEFAGPTEHIYKKN---IELKVEVESLKRELQERDQLLVKASKAVESLAEg 137
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNI----EKKQQEINEKTTEISNTQtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 138 ggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFagTETEKALRlSLESKLSAMKKMQEG----DLEMT 213
Cdd:TIGR04523 289 ---QLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI--SQNNKIIS-QLNEQISQLKKELTNseseNSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 214 LALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsatlreekERDAEERQKERNHFEERIQALQE 293
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-----------------------ESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 294 DLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEltadstqsreapLKTQVSEFEES--------ENC 365
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES------------LETQLKVLSRSinkikqnlEQK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 366 EAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRgartiHDLRNEVEKLRKE 445
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKE 562
|
410
....*....|
gi 564351376 446 VCEREKAVEK 455
Cdd:TIGR04523 563 IDEKNKEIEE 572
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
141-418 |
6.53e-08 |
|
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: 57.83 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 141 EIQRVKEDARKKVQQVEelltkRIHLLEEDVKAAQAELEKAFA--------GTETEKAL-RLSLESKLSAMKKMQEGDLE 211
Cdd:pfam17380 297 EQERLRQEKEEKAREVE-----RRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELeRIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 212 MTLaleEKDRLIEELKLSLKSKE---------ALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEE---RQK 279
Cdd:pfam17380 372 MEI---SRMRELERLQMERQQKNervrqeleaARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEeraREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 280 ERNHFEERIQALQ-EDLREKEREiatEKKNSLKRDKAiqgltmalKSKEKEVEELNSII--KELTADSTQSREAPLKTQV 356
Cdd:pfam17380 449 ERVRLEEQERQQQvERLRQQEEE---RKRKKLELEKE--------KRDRKRAEEQRRKIleKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564351376 357 SEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLkkEKLRLERDL 418
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL--EAMEREREM 577
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-446 |
1.22e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 60 MKDFENQITELKKENFNLKLRIYFLEERIQQ--EFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEG 137
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 138 GGSEIQRVK------EDARKKVQQVEELLTKRIHLLE---EDVKAAQAELEKAFAGTETEKALrLSLESKLSAMKKMQeg 208
Cdd:PRK03918 382 TGLTPEKLEkeleelEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAKGKCPVCGRE-LTEEHRKELLEEYT-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 209 dLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKS-----QMASPDENVSSgELRGLSATLREEKERDAEERQKERNH 283
Cdd:PRK03918 459 -AELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE-KLKKYNLEELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 284 FEERIQALQEDLR-----EKEREIATEKKNSLKRDKAiQGLTMALKSKEKEVEELNSIIKELTA---------DSTQSRE 349
Cdd:PRK03918 537 LKGEIKSLKKELEkleelKKKLAELEKKLDELEEELA-ELLKELEELGFESVEELEERLKELEPfyneylelkDAEKELE 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 350 APLKTQVSEFEESENCEAALAEKEALLAKLHSE----NVTKNTENHRLLRN-----------VKKVTQELNDLKKEKLRL 414
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREeylelsrelagLRAELEELEKRREEIKKT 695
|
410 420 430
....*....|....*....|....*....|....*
gi 564351376 415 ERDLEEAHREGNRGARTIHDL---RNEVEKLRKEV 446
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLekaLERVEELREKV 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-446 |
1.29e-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: 57.00 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 84 LEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGG--SEIQRVKEDARKKVQQVEellt 161
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELE---- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 162 KRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKkmqegdlemtlaLEEKDRLIEELKLSLKSKEALIQCLk 241
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALND--------------LEARLSHSR------------IPEIQAELSKLEEEVSRIEARLREI- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 242 EEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERN------HFEERIQALQEDLREKEREIATEKKNSLKRDKA 315
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 316 IQGLTMALKSKEKEVEELNSIIKELTA--DSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRL 393
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAklEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564351376 394 LRNVKKVTQELNDLKKEKLRLERDLEEahregnrgartIHDLRNEVEKLRKEV 446
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKRAKLEEERKA-----------ILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-668 |
2.17e-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: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 57 ARNMKDFENQITELKKENFNLKLRIyfleERIQQEFagptehiYKKNIELKvEVESLKRELQERDQLLVKASKAVESLAE 136
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEI----EELQKEL-------YALANEIS-RLEQQKQILRERLANLERQLEELEAQLE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 137 GGGSEIQRVKEDARKKVQQVEELLtKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKkmqegdLEMTLAL 216
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------LQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 217 EEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELrglsatlrEEKERDAEERQKERNHFEERIQALQEDLR 296
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--------EELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 297 EKEREIaTEKKNSLKRdkaIQGLTMALKSKEKEVEELNSIIKELTADstQSREAPLKTQVSEFEESEN-----CEAALAE 371
Cdd:TIGR02168 472 EAEQAL-DAAERELAQ---LQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSELISVDEgyeaaIEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 372 --------------------KEALLAKLH-----SENVTKNTENHRLLRN------------------------------ 396
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflKQNELGRVTflpldSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 397 --VKKVTQELNDLKKEKL----------------------------RLERD--LEEAHREGNRGARTIHDLRNEVEKLRK 444
Cdd:TIGR02168 626 lvVDDLDNALELAKKLRPgyrivtldgdlvrpggvitggsaktnssILERRreIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 445 EVCEREKAVEKHYKSLPgESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQncyLMTAEELKFGSDGLITEKC 524
Cdd:TIGR02168 706 ELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IEELEERLEEAEEELAEAE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 525 SQQSPDSKLIfskEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQdvlayrnlqtaLQEQL 604
Cdd:TIGR02168 782 AEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-----------LEEQI 847
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 605 SEIRKREEEpfsfYSDQTSYLSICLEEHSQfQLEHFS------QEEIKKKVIDLIQLVKDLHADNQHLKK 668
Cdd:TIGR02168 848 EELSEDIES----LAAEIEELEELIEELES-ELEALLneraslEEALALLRSELEELSEELRELESKRSE 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-454 |
5.65e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 61 KDFENQITELKKENFNLKLRIYFLEERIQQEfagpTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVEslaegggs 140
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 141 EIQRVKEDARKKVQQVEELLTKRIhLLEEDVKAAQAELEKAfagTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKD 220
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEA---EEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 221 RLIEELKLSLKSKEALIQCLKEEKSQMASPDENVssgelrglsATLREEKERDAEERQKERNHFEERIQALQEDLREKER 300
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAEL---------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 301 EIATEKKNSLKRDKAIQGLTM---ALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESEncEAALAEKEALLA 377
Cdd:COG1196 471 EAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY--EAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 378 klhsenvtknteNHRLLRNVKKVTQELNDLKKEK------LRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREK 451
Cdd:COG1196 549 ------------QNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
...
gi 564351376 452 AVE 454
Cdd:COG1196 617 VLG 619
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
102-493 |
2.29e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 102 KNIELKVEVESLKRELQERDQLLVKAS---KAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAEL 178
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 179 EKAFAGTETEKALRLSLESKLSAMKKMQEGDLEmtlalEEKDRLIEELKLSLKSKEALIQCLKEEKSQmASPDENVSSGE 258
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-----EEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKE 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 259 lrglsatlrEEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIK 338
Cdd:PTZ00121 1712 ---------AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 339 E-LTADSTQSREAPLKTQVSEFEESENCEAALAE----------------KEALLAKLHSENVTKNTENHRLLRNVK--K 399
Cdd:PTZ00121 1783 EeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnlvindskemedsaiKEVADSKNMQLEEADAFEKHKFNKNNEngE 1862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 400 VTQELNDLKKEKLRLERDLEEAHREgnrgartihdlrNEVEKLRKEVCEREKAvEKHYKSLPGESSSKFHSQEQVVKGLT 479
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEA------------DEIEKIDKDDIEREIP-NNNMAGKNNDIIDDKLDKDEYIKRDA 1929
|
410
....*....|....
gi 564351376 480 ESASQEDLLLQKSN 493
Cdd:PTZ00121 1930 EETREEIIKISKKD 1943
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-456 |
2.37e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 146 KEDARKKVQQVEELLTKRIHLLEE--DVKAAQAELEKAFAGTETEK-----------ALRLSLESKLSAMKKMQE-GDLE 211
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREEleTLEAEIEDLRETIAETEREReelaeevrdlrERLEELEEERDDLLAEAGlDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 212 MTLALEEKDRL---IEELKLSLKSKEALIQclkEEKSQMASPDENVSsgELRGLSATLREEKERDAEERQKERNHFEERi 288
Cdd:PRK02224 309 AEAVEARREELedrDEELRDRLEECRVAAQ---AHNEEAESLREDAD--DLEERAEELREEAAELESELEEAREAVEDR- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 289 qalQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQV-----------S 357
Cdd:PRK02224 383 ---REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 358 EFEES------ENCEAALAEKEALLAKLHSEnVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGART 431
Cdd:PRK02224 460 PVEGSphvetiEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
330 340
....*....|....*....|....*.
gi 564351376 432 IHDLRNEVEKLRKEVCE-REKAVEKH 456
Cdd:PRK02224 539 AEELRERAAELEAEAEEkREAAAEAE 564
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-424 |
2.41e-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: 52.75 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 58 RNMKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEH------IYKKNIELKVEVESLKRELQERDQLLVKASKAV 131
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 132 ESLAEGGGSEIQRVKEDARKKVQQVEEL--LTKRIHLLEEDVKAAQAELekafagteteKALRLSLESKLSAMKKMQEgd 209
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAEL----------TLLNEEAANLRERLESLER-- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 210 lemtlALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsATLREEKERDAEERQKERNHFEERIQ 289
Cdd:TIGR02168 832 -----RIAATERRLEDLEEQIEELSEDIESLAAEIEEL----------------EELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 290 ALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEEL----NSIIKELTADSTQSREAPLKTQVSEFEESENC 365
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351376 366 EAALAEKEALLAKLHSENVTKNTEnhrlLRNVKK----VTQELNDLKKEKLRLERDLEEAHRE 424
Cdd:TIGR02168 971 RRRLKRLENKIKELGPVNLAAIEE----YEELKErydfLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-375 |
2.60e-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: 52.75 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 58 RNMKDFENQITELKKENFNLKLRIYFLEERIQQefagptehiykknIELKV-EVESLKRELQERDQLLVKASKAVESLAE 136
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEE-------------LRLEVsELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 137 GGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEdvkaaQAELEKAFAGTETEKAlrlSLESKLSAMKKMQEgdlEMTLAL 216
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEE-----LAELEEKLEELKEELE---SLEAELEELEAELE---ELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 217 EEKDRLIEELklslksKEALIQCLKEEKSQMAspdenvssgELRglsaTLREEKERDAEERQKERNHFEERIQALQE-DL 295
Cdd:TIGR02168 375 EELEEQLETL------RSKVAQLELQIASLNN---------EIE----RLEARLERLEDRRERLQQEIEELLKKLEEaEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFE-ESENCEAALAEK 372
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQENLEgFSEGVKALLKNQ 515
|
...
gi 564351376 373 EAL 375
Cdd:TIGR02168 516 SGL 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-455 |
3.20e-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: 52.43 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 107 KVEVESLKRELQERDQLLVKASKAVESLaeggGSEIQRVKEDARKKVQQVEELLTKRIHLleedvKAAQAELEK-AFAGT 185
Cdd:pfam15921 488 KMTLESSERTVSDLTASLQEKERAIEAT----NAEITKLRSRVDLKLQELQHLKNEGDHL-----RNVQTECEAlKLQMA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 186 ETEKA---LRLSLE--SKLSAMKKMQEGDLEMTLALEEK---DRLIE--ELKLSLKSKEALIQCLKEEKSQMASPDENVS 255
Cdd:pfam15921 559 EKDKVieiLRQQIEnmTQLVGQHGRTAGAMQVEKAQLEKeinDRRLElqEFKILKDKKDAKIRELEARVSDLELEKVKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 256 SGELRGLSATLREEKERD-----AEERQKERNHFEERIQALQEDLREKEREIATeKKNSLKrdkaiqgltMALKSKEKEV 330
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDqllneVKTSRNELNSLSEDYEVLKRNFRNKSEEMET-TTNKLK---------MQLKSAQSEL 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 331 EELNSIIKELTADSTQSREAPLKTQvsefeesENCEAALAEKEALLAKLHSenvtkntenhrLLRNVKKVTQELNDLKKE 410
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQ-------KQITAKRGQIDALQSKIQF-----------LEEAMTNANKEKHFLKEE 770
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 564351376 411 KLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEK 455
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| 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 564351376 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLEKGSKE------- 1477
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELRAELEAQKEElaellra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1478 --KQKENEKLR-----ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQ 1550
Cdd:COG4942 113 lyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|....*
gi 564351376 1551 LLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
87-668 |
4.94e-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: 51.65 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 87 RIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKR--I 164
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 165 HLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMqegdLEMTLALEEKDRLieELKLSLKSKEALIQCLKEEK 244
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA----FEELRVQAENARL--EMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 245 SQMASPDENVSSgeLRGLSATLREEKERD----AEERQKERNHFEERIQALQEDLR---EKEREIATEK---KNSLKRDK 314
Cdd:pfam05483 232 KKEINDKEKQVS--LLLIQITEKENKMKDltflLEESRDKANQLEEKTKLQDENLKeliEKKDHLTKELediKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 315 AIQgltmalKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALAEKEALLaKLHSENVTKNTENHRLL 394
Cdd:pfam05483 310 STQ------KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL-RTEQQRLEKNEDQLKII 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 395 R-NVKKVTQELNDLKKEKLRLERDLEEAHREGNRgARTIHDLRNEVEKLRKEVcereKAVEKHYKSLPGESSSKFHSQEQ 473
Cdd:pfam05483 383 TmELQKKSSELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIAEEL----KGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 474 VVKGLTESASQ-----EDLLLQKSNEKdleaiqqncylMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQseyEGLT 548
Cdd:pfam05483 458 QLTAIKTSEEHylkevEDLKTELEKEK-----------LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---EDII 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 549 GDLKTEQNVYAHLaKNLQDTDSKLQAELKRVlalRKQLEQDvlayrnlqtaLQEQLSEIRKREEEPFSFYSDqtsylsiC 628
Cdd:pfam05483 524 NCKKQEERMLKQI-ENLEEKEMNLRDELESV---REEFIQK----------GDEVKCKLDKSEENARSIEYE-------V 582
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 564351376 629 LEEHSQFQLEHFSQEEIKKKVIDLIQLVKDLHADNQHLKK 668
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
61-455 |
8.12e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.13 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 61 KDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVE-SLKRELQERDQLLVKASKAVESLAEGGG 139
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvEGILKDTELTKLKESAKAKESGLRKGVS 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 140 SEIqrvKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEK 219
Cdd:pfam02463 654 LEE---GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 220 DRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVssgelrgLSATLREEKERDAEERQKERNHFEERiqaLQEDLREKE 299
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE-------KSELSLKEKELAEEREKTEKLKVEEE---KEEKLKAQE 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 300 REIatEKKNSLKRDKAIQGLTMALKsKEKEVEELNSIIKELTADSTQSreaplKTQVSEFEESENCEAALAEKEALLAKL 379
Cdd:pfam02463 801 EEL--RALEEELKEEAELLEEEQLL-IEQEEKIKEEELEELALELKEE-----QKLEKLAEEELERLEEEITKEELLQEL 872
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351376 380 HSENVTKNTENHR--LLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEK 455
Cdd:pfam02463 873 LLKEEELEEQKLKdeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-491 |
8.43e-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: 50.15 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 273 DAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREApL 352
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 353 KTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQE-LNDLKKEKLRLERDLEEAHREGNRGART 431
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 432 IHDLRNEVEKLRKEVCEREKAVEKHYKSLPgessskfhSQEQVVKGLTESASQEDLLLQK 491
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELA--------ELAAELAELQQEAEELEALIAR 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
64-613 |
8.75e-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: 50.89 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 64 ENQITELKKENFN-LKLRIYFLEERIQQ-------EFAGPTEHIYKKNIE---LKVEVESLKRELQERDQLLVKASKAVE 132
Cdd:pfam15921 244 EDQLEALKSESQNkIELLLQQHQDRIEQlisehevEITGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 133 SLAEGGGSEIQRVKEDARKKVQQVE-ELLTKRIHLLEEDVKAAQAELEKAFAGTETEKAL--------RLSLESKLSamK 203
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEkQLVLANSELTEARTERDQFSQESGNLDDQLQKLLadlhkrekELSLEKEQN--K 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 204 KMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEE-----KSQMAS-PDENVSSGELRGLSATLREEKERdaeer 277
Cdd:pfam15921 402 RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmERQMAAiQGKNESLEKVSSLTAQLESTKEM----- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 278 qkernhfeeriqalqedLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA--DSTQSREAPLKTQ 355
Cdd:pfam15921 477 -----------------LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 356 VSEFEESE-NCEA---ALAEKEALLAKLHS--ENVTKNTENH-----RLLRNVKKVTQELND--LKKEKLRLERDLEEAH 422
Cdd:pfam15921 540 GDHLRNVQtECEAlklQMAEKDKVIEILRQqiENMTQLVGQHgrtagAMQVEKAQLEKEINDrrLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 423 -RE------------------GNRGARTIHDLRNEVEKLRKEV--CERE-KAVEKHYKSLPGESSSKFHSQEQVVKGLTE 480
Cdd:pfam15921 620 iRElearvsdlelekvklvnaGSERLRAVKDIKQERDQLLNEVktSRNElNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 481 S--ASQEDLLLQKSNEKDLEAIQQNcylmtAEELKFGSDGLITEKCSQ-QSPDSKLIFSKEKQQSEYEGlTGDLKTEQNV 557
Cdd:pfam15921 700 QlkSAQSELEQTRNTLKSMEGSDGH-----AMKVAMGMQKQITAKRGQiDALQSKIQFLEEAMTNANKE-KHFLKEEKNK 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351376 558 YAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVlayRNLQTALQE---QLSE----IRKREEE 613
Cdd:pfam15921 774 LSQELSTVATEKNKMAGELEVLRSQERRLKEKV---ANMEVALDKaslQFAEcqdiIQRQEQE 833
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-670 |
1.17e-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: 50.40 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 56 RARNMKDFENQITELKKENFNLKLRIYFLEERIQQ-----EFAGPTEHIYKKNI-ELKVEVESLKRELQERDQLLVKASK 129
Cdd:TIGR04523 66 DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsdlSKINSEIKNDKEQKnKLEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 130 AVESLAegggSEIQRVKEDARKKVQQVEELLTKRiHLLEEDVKAAQAELEKAfagteteKALRLSLESKLSAMKKMQEGD 209
Cdd:TIGR04523 146 EIKKKE----KELEKLNNKYNDLKKQKEELENEL-NLLEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKKKIQKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 210 LEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgelrglsatLREEKERDAEERQKERNHFEERIQ 289
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD---------EQNKIKKQLSEKQKELEQNNKKIK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 290 ALQEDLREKEREIatEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEfEESENCE- 366
Cdd:TIGR04523 285 ELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqiSQLKKELTN-SESENSEk 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 367 -AALAEKEALLAKLHSENVTKNTENHRL----------LRNVKKVTQELND----LKKEKLRLERDLEEAHREGNRGART 431
Cdd:TIGR04523 362 qRELEEKQNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEqikkLQQEKELLEKEIERLKETIIKNNSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 432 IHDLRNEV---EKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLlqKSNEKDLEaiQQNCYLMT 508
Cdd:TIGR04523 442 IKDLTNQDsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--NEEKKELE--EKVKDLTK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 509 -AEELKFGSDGLITEKCSQQSPDSKLifSKEKQQSEYEGLTGDLKTEQNVY-------AHLAKNLQDTDSKLQAELKRVL 580
Cdd:TIGR04523 518 kISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKnkeieelKQTQKSLKKKQEEKQELIDQKE 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 581 ALRKQLEQDVLAYRNLQTALQEQLSEIRKREEEPFSFYSDQTSYLSICLEEHSQFQLE-----------HFSQEEIKKKV 649
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETikeirnkwpeiIKKIKESKTKI 675
|
650 660
....*....|....*....|..
gi 564351376 650 IDLIQLVKD-LHADNQHLKKTI 670
Cdd:TIGR04523 676 DDIIELMKDwLKELSLHYKKYI 697
|
|
| 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 564351376 1422 EKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALstmlEKGSKEKQKENEKLRESLARKTESLEHLQL 1501
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1502 EYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQ 1581
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
.
gi 564351376 1582 D 1582
Cdd:COG1196 390 E 390
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-460 |
2.14e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 266 LREEKERDAEERQKERNHFEERIQALQEDLREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA- 342
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAr 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 343 -DSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLhSENVTKNTENHRLLRNVKkvtQELNDLKKE-KLRLERDLEE 420
Cdd:COG3206 242 lAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAEL-AELSARYTPNHPDVIALR---AQIAALRAQlQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564351376 421 AHREGNRGARTIHDLRNEVEKLRKEVcEREKAVEKHYKSL 460
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRL 356
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-606 |
2.20e-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: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 221 RLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQED---LRE 297
Cdd:pfam02463 123 ELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqeLKL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 298 KEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALAEKEALLA 377
Cdd:pfam02463 203 KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 378 KLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHY 457
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 458 KSLpGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQqncylmtaeelkfgSDGLITEKCSQQSPDSKLIFSK 537
Cdd:pfam02463 363 KLQ-EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--------------EAQLLLELARQLEDLLKEEKKE 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351376 538 EKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLSE 606
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| 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 564351376 1397 QDLLMEHIQEIRTL---RKHLEESIKTNEKLRKQLERQGCETDQGSTNVSA-----------YSSELHNSLTSEIQFLRK 1462
Cdd:COG1196 287 QAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELEELEEeleeleeeleeAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1463 QNEALSTMLEKGSKEKQKENEKLRE--SLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcssLQELSR 1540
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---EEEEEA 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564351376 1541 VQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-351 |
4.40e-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: 47.84 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 105 ELKVEVESLKRELQERDQLLVKASKAVESLaegggseiqrvkEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAfag 184
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKAL------------LKQLAALERRIAALARRIRALEQELAALEAELAEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 185 TETEKALRLSLESK-------LSAMKKMQEGDLEMTLA----LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMAspden 253
Cdd:COG4942 89 EKEIAELRAELEAQkeelaelLRALYRLGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAELA----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 254 vssgELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKEVEEL 333
Cdd:COG4942 164 ----ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--------------ELAELQQEAEEL 225
|
250
....*....|....*...
gi 564351376 334 NSIIKELTADSTQSREAP 351
Cdd:COG4942 226 EALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-502 |
5.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 113 LKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELlTKRIHLLEEDVKAAQAELEKAfagtETEKALR 192
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEEL----REELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 193 LSLESKLSAMKKMQEGDLEMTL------ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATL 266
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 267 rEEKERDAEERQKERNHFEERIQALQEDLREKEREI-ATEKKNSLKRDK----------AIQGLTMALKSKEKEVEELNS 335
Cdd:COG4717 202 -EELQQRLAELEEELEEAQEELEELEEELEQLENELeAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 336 IIKELTAD--STQSREAPLKTQVSEFEESENCEAALAEKE--ALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK 411
Cdd:COG4717 281 LVLGLLALlfLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 412 LRLERDLEEAHRE---GNRGARTIHDLRNEVEKLRKEVcEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLL 488
Cdd:COG4717 361 EELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEE 439
|
410
....*....|....
gi 564351376 489 LQKSNEKDLEAIQQ 502
Cdd:COG4717 440 ELEELEEELEELRE 453
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1397-1585 |
5.75e-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: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEA-----LSTML 1471
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL-NQLKSEISDLNNQKEQdwnkeLKSEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1472 EKGSKEKQKENEKLRES---LARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSR 1548
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564351376 1549 QQLLLQKDELLQSLQMELKV----YEKLAEEHQKLQQDVNK 1585
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKlqqeKELLEKEIERLKETIIK 437
|
|
| 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 564351376 1453 LTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVC 1532
Cdd:COG1196 244 LEAELEELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564351376 1533 SSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEK-LAEEHQKLQQDV 1583
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAeLAEAEEALLEAE 371
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1397-1595 |
6.00e-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: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHN------SLTSEIQFLRKQNEALSTM 1470
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaaNLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1471 LEKGSKEKQKENE----------KLRESLARKTESLEHLQLEYASVREENERLR-------RDISEKERQNQQLTQEvcs 1533
Cdd:TIGR02168 840 LEDLEEQIEELSEdieslaaeieELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRE--- 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564351376 1534 sLQELSRVQEEAKSRQQLLLQKdelLQSLQmelkvyEKLAEEHQKLQQDVNKCPEASDNSFD 1595
Cdd:TIGR02168 917 -LEELREKLAQLELRLEGLEVR---IDNLQ------ERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
46-372 |
6.08e-05 |
|
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: 48.09 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 46 IMSEEKVSPTRARNMK--DFENQITELKKENFNlklRIYFLEERIQQEFAGPTEHiykkniELKVEVESLKRELQERDQL 123
Cdd:NF033838 70 ILSEIQKSLDKRKHTQnvALNKKLSDIKTEYLY---ELNVLKEKSEAELTSKTKK------ELDAAFEQFKKDTLEPGKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 124 LVKASKAVEslaEGGGSEIQRVKEDARKKVQQVEEllTKRIHLLEEDVKAAQAELE------KAFAGTETEKALRLSLES 197
Cdd:NF033838 141 VAEATKKVE---EAEKKAKDQKEEDRRNYPTNTYK--TLELEIAESDVEVKKAELElvkeeaKEPRDEEKIKQAKAKVES 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 198 KLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKS--------QMASPD--EN------VSSGELRG 261
Cdd:NF033838 216 KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRrakrgvlgEPATPDkkENdakssdSSVGEETL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 262 LSATLREEKErdAEERQKERNHFEERIQALQEdlrEKEREIATEKKNSLKRDKAiqglTMALKSKEKEVEelnsIIKElt 341
Cdd:NF033838 296 PSPSLKPEKK--VAEAEKKVEEAKKKAKDQKE---EDRRNYPTNTYKTLELEIA----ESDVKVKEAELE----LVKE-- 360
|
330 340 350
....*....|....*....|....*....|.
gi 564351376 342 aDSTQSREAPLKTQVSEFEESENCEAALAEK 372
Cdd:NF033838 361 -EAKEPRNEEKIKQAKAKVESKKAEATRLEK 390
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-613 |
6.65e-05 |
|
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: 47.86 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 141 EIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAA---QAELEkAFAGTETEKAlRLS-----LESKLSAMKKMQEGDLEM 212
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQeqlQAETE-LCAEAEEMRA-RLAarkqeLEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 213 TLALE-EKDRL---IEELKLSLKSKEALIQCLKEEKsqmASPDENVSSGELRGLsaTLREEKERdaeeRQKERNHFEERI 288
Cdd:pfam01576 91 SQQLQnEKKKMqqhIQDLEEQLDEEEAARQKLQLEK---VTTEAKIKKLEEDIL--LLEDQNSK----LSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 289 QALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEFeesencE 366
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiAELQAQIAEL------R 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 367 AALAEKE----ALLAKLHSENVTKNTenhrLLRNVKKVTQELNDLKKeklrlerDLEEAHREGNRGARTIHDLRNEVEKL 442
Cdd:pfam01576 236 AQLAKKEeelqAALARLEEETAQKNN----ALKKIRELEAQISELQE-------DLESERAARNKAEKQRRDLGEELEAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 443 RKEV--------------CEREKAVEKHYKSLpgESSSKFHSQE---------QVVKGLTESASQedlllQKSNEKDLEA 499
Cdd:pfam01576 305 KTELedtldttaaqqelrSKREQEVTELKKAL--EEETRSHEAQlqemrqkhtQALEELTEQLEQ-----AKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 500 IQQNCYLMTAE---ELKFGSDGLIT-----EKCSQQSPDSKLIFSK------------EKQQSEYEGLTGDLKTEQNVYA 559
Cdd:pfam01576 378 AKQALESENAElqaELRTLQQAKQDsehkrKKLEGQLQELQARLSEserqraelaeklSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351376 560 HLAKN-------LQDTDSKLQAELKRVLA--------------LRKQLEQDVLAYRNLQ---TALQEQLSEIRKREEE 613
Cdd:pfam01576 458 KLSKDvsslesqLQDTQELLQEETRQKLNlstrlrqledernsLQEQLEEEEEAKRNVErqlSTLQAQLSDMKKKLEE 535
|
|
| 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 564351376 1399 LLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAysselhnsLTSEIQFLRKQNEALSTMLEKGSKEK 1478
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1479 QKENEKLR-ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLT-QEVCSSLQELSRVQEEAKSRQQLLLQKD 1556
Cdd:COG4717 140 ELAELPERlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 564351376 1557 ELLQSLQMELKVYEKLAEEHQKLQQ 1581
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1448-1581 |
6.88e-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: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1448 ELHNSLTSEIQFLRKQNEALSTMLEKGSKEKQKENEKLRESLARKTES-------LEHLQLEYASVREENERLRRDISEK 1520
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdpteLDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564351376 1521 ERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDellqslQMELKVYEKLAEEHQKLQQ 1581
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR------GFTFKEIEKLKEQLKLLQS 285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-428 |
6.92e-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: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 215 ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgELRGLSATLRE-EKERDAEERQKERNhfEERIQALQE 293
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRAlEQELAALEAELAEL--EKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 294 DLREKEREIA---------------------TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPL 352
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564351376 353 KTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRG 428
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-612 |
9.77e-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: 47.37 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 285 EERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEFE-- 360
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErlEELEEDLSSLEqe 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 361 ------ESENCEAALAEKEALLAKLHSEnvTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNR---GART 431
Cdd:TIGR02169 753 ienvksELKELEARIEELEEDLHKLEEA--LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 432 IHDLRNEVEKLRKEVCEREKAVEKhykslpgessskfhsqeqvvkgltesasQEDLLlqksnEKDLEAIQQNcylmtAEE 511
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEK----------------------------EIENL-----NGKKEELEEE-----LEE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 512 LKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEgltgDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQD-- 589
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIE----ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpe 948
|
330 340
....*....|....*....|....
gi 564351376 590 -VLAYRNLQTALQEQLSEIRKREE 612
Cdd:TIGR02169 949 eELSLEDVQAELQRVEEEIRALEP 972
|
|
| 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 564351376 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSEIQFLRKQNEALSTMLEKGSKEKQKENEK 1484
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1485 LRE---------SLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKsrQQLLLQK 1555
Cdd:COG1196 389 LEAlraaaelaaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE--ALLELLA 466
|
170 180
....*....|....*....|....*.
gi 564351376 1556 DELLQSLQMELKVYEKLAEEHQKLQQ 1581
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAAR 492
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1458-1575 |
1.31e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1458 QFLRKQNEalstmLEKGSKEKQKENEKL-------RESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQE 1530
Cdd:PRK12704 65 EIHKLRNE-----FEKELRERRNELQKLekrllqkEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564351376 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 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 126 KASKAVESLAEgggSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEkAFAgtETEKALRLSLESKLSAMKkm 205
Cdd:COG3206 149 LAAAVANALAE---AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE-EFR--QKNGLVDLSEEAKLLLQQ-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 206 qegdlemtlaLEEKDRLIEELKLSLKSKEALIQCLKEE-KSQMASPDENVSSGELRGLSATLRE-EKERDAEERQKERNH 283
Cdd:COG3206 221 ----------LSELESQLAEARAELAEAEARLAALRAQlGSGPDALPELLQSPVIQQLRAQLAElEAELAELSARYTPNH 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351376 284 feERIQALQEDLREKEREIATEKKNSL-KRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE 349
Cdd:COG3206 291 --PDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-421 |
1.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 144 RVKEDARKKVQQVEELltKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLEsKLSAMKKMqegdlemtLALEEKDRLI 223
Cdd:COG4913 222 DTFEAADALVEHFDDL--ERAHEALEDAREQIELLEPIRELAERYAAARERLA-ELEYLRAA--------LRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 224 EELklslkskEALIQCLKEEKSQMAspdenvssGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIA 303
Cdd:COG4913 291 ELL-------EAELEELRAELARLE--------AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 304 TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAplktqvsefeesenCEAALAEKEALLaklhsen 383
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAAL------- 414
|
250 260 270
....*....|....*....|....*....|....*...
gi 564351376 384 vtkntenHRLLRNVKKVTQELNDLKKEKLRLERDLEEA 421
Cdd:COG4913 415 -------RDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
86-333 |
1.88e-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: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 86 ERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGS----------EIQRVKEDARK---- 151
Cdd:pfam10174 460 EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKkdsklksleiAVEQKKEECSKlenq 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 152 --KVQQVEEL------LTKRIHLLEEDVK-------AAQAELEK---AFAGTETEKALRLSLESKLSAMKKMQEGDLEMT 213
Cdd:pfam10174 540 lkKAHNAEEAvrtnpeINDRIRLLEQEVArykeesgKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 214 LA------LEEKDRLIEELKLSLKSKEALIQC-----LKEEKSQMASPDENVSSGELRgLSATLREEKERDA---EERQK 279
Cdd:pfam10174 620 VAnikhgqQEMKKKGAQLLEEARRREDNLADNsqqlqLEELMGALEKTRQELDATKAR-LSSTQQSLAEKDGhltNLRAE 698
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 564351376 280 ERNHFEERIQALQEDL----REKEREIATEKKNSLKRDKAiQGLTMALK-SKEKEVEEL 333
Cdd:pfam10174 699 RRKQLEEILEMKQEALlaaiSEKDANIALLELSSSKKKKT-QEEVMALKrEKDRLVHQL 756
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
211-593 |
2.72e-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: 46.12 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 211 EMTLALEEKDRLIEELKLSLKSKEaliqclKEEKSQMaspdenvssgELRGLSATLREEKERDAEERQkeRNHFEERIQA 290
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLK------EQAKKAL----------EYYQLKEKLELEEEYLLYLDY--LKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 291 LQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALA 370
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 371 EKEALLAKLhsENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGnrgartiHDLRNEVEKLRKEVCERE 450
Cdd:pfam02463 322 EKKKAEKEL--KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE-------LLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 451 KAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLitEKCSQQSPD 530
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL--KDELELKKS 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351376 531 SKLIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAY 593
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
215-432 |
2.92e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 215 ALEEKDRLIEELKLSLKS--KEALIQcLKEEKSQmaspdenvssgelrglsatLREEKERDAEERQKERNHFEERIQALQ 292
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAikKEALLE-AKEEIHK-------------------LRNEFEKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 293 EDLREKEREIAtekknslKRDKAIQGLTMALKSKEKEVEELNSIIKELTADstqsreaplktQVSEFEESenceAALAEK 372
Cdd:PRK12704 96 ENLDRKLELLE-------KREEELEKKEKELEQKQQELEKKEEELEELIEE-----------QLQELERI----SGLTAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564351376 373 EAllaklhsenvtknteNHRLLRNVKKvtqelnDLKKEKLRLERDLE-EAHREGNRGARTI 432
Cdd:PRK12704 154 EA---------------KEILLEKVEE------EARHEAAVLIKEIEeEAKEEADKKAKEI 193
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-503 |
3.50e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 101 KKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEK 180
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 181 AFAGTETEKALRLSLEsKLSAMKKMQEGDLEMTLALEEKDRLIEELKlslksKEALIQCLKEEKSQMASPDENVSSGELR 260
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELK-----KAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 261 GlsatlREEKERDAEERQKERNhfEERIQAlqEDLREKEREiatEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEL 340
Cdd:PTZ00121 1682 K-----AEEDEKKAAEALKKEA--EEAKKA--EELKKKEAE---EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 341 TADSTQSReaplKTQVSEFEESENCEAALAEKEALLaklhSENVTKNTENHRLlrNVKKVTQELNDlkkeklrlerDLEE 420
Cdd:PTZ00121 1750 KKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVI----EEELDEEDEKRRM--EVDKKIKDIFD----------NFAN 1809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 421 AHREGNRGARTIHDLRNEVEKLRKEVC-------EREKAVEKH---YKSLPGESSSK---FHSQEQVVKGLTESASQEDl 487
Cdd:PTZ00121 1810 IIEGGKEGNLVINDSKEMEDSAIKEVAdsknmqlEEADAFEKHkfnKNNENGEDGNKeadFNKEKDLKEDDEEEIEEAD- 1888
|
410
....*....|....*.
gi 564351376 488 LLQKSNEKDLEAIQQN 503
Cdd:PTZ00121 1889 EIEKIDKDDIEREIPN 1904
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-381 |
3.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 54 PTRARNMKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVES 133
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 134 L-AEGGGSEIQRVKEDARKKVQQVEELL------------TKRIHLLEEDVKAAQAEL-------------EKAFAGTET 187
Cdd:COG4717 225 LeEELEQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 188 EKALRLSLESKLSAMKKMQ-------EGDLEMTLALEEKDRlIEELKLSLKS-----KEALIQCLKEEKSQMASPDENVS 255
Cdd:COG4717 305 EELQALPALEELEEEELEEllaalglPPDLSPEELLELLDR-IEELQELLREaeeleEELQLEELEQEIAALLAEAGVED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 256 SGELRglsatlreEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKrdKAIQGLTMALKSKEKEVEELns 335
Cdd:COG4717 384 EEELR--------AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEEL-- 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564351376 336 iikeltadstQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHS 381
Cdd:COG4717 452 ----------REELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-449 |
3.98e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEGG-----------------GSEIQRVKEDARKKVQQVEELlTKRIHLL 167
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleeraeelreeaaelESELEEAREAVEDRREEIEEL-EEEIEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 168 EEDVKAAQAELEKAF-----------AGTETEKALRLSLESKLSAMKKMQE--------------GDLEMTLALEEKDRL 222
Cdd:PRK02224 397 RERFGDAPVDLGNAEdfleelreerdELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 223 IEELKLSLKSKEALIQCLKEE----KSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREK 298
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 299 eREIATEK---------------------KNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQ 355
Cdd:PRK02224 557 -REAAAEAeeeaeeareevaelnsklaelKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRErlAEKRER 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 356 VSEFEES---ENCEAALAEKEAllAKLHSENVTKNTENHRLLRN--------VKKVTQELNDLKKEKLRLE---RDLEEA 421
Cdd:PRK02224 636 KRELEAEfdeARIEEAREDKER--AEEYLEQVEEKLDELREERDdlqaeigaVENELEELEELRERREALEnrvEALEAL 713
|
410 420
....*....|....*....|....*...
gi 564351376 422 HREGNRGARTIHDLRNEVEKLRKEVCER 449
Cdd:PRK02224 714 YDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-494 |
4.62e-04 |
|
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: 45.34 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 64 ENQITELKKENFNLKLRIYFLEERIQQEfaGPTEHIYKKNIELKVEVESLKRELQERDQLLVK-----ASKAVESLAEGG 138
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNPGP 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 139 GSEIQRVKEDARKKVQQVEE-------LLTKRIHLLEEDVKAAQAELEKAfagTETEKALRLSLESKLSAMKKMQEgdlE 211
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEdvyhqltSERKQRASLKEQMQEIQQSFSIL---TQCDNRSKEDIPNLQNITVRLQD---L 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 212 MTLALEEKDRLIEELKLSLKSKEALI-------------QCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQ 278
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQdlqdvrlhlqqcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 279 KERNHFEERIQALQEDLR------EKEREIATEKKNSLKRDKAIQGLTMALKSK-EKEVEELNSIIKELtadstqSREAP 351
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEmlaqcqTLLRELETHIEEYDREFNEIENASSSLGSDlAAREDALNQSLKEL------MHQAR 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 352 LKTQVSEFEESENCEAALAEKEALlaklhsenvtkntenhrllrnvkkvtQELNDLKKEKLRLERDLEEAHREGNRGART 431
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTG--------------------------AELSHLAAEIQFFNRLREEDTHLLKTLEAE 807
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351376 432 IHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNE 494
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| 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 564351376 1405 QEIRTLRKHLEESIKTNEKLRKQLERQgcETDQGSTNVSAYSSELHNSLT------------SEIQFLRKQNEALSTMLE 1472
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQ--KEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 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 |
5.45e-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: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 86 ERIQQEFAGP------TEHIYKKNIELKVEVESLKRELQERDQllvkasKAVESLAEGGGSEIQRVKEDARKKVQQVEel 159
Cdd:pfam17380 392 ERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQ------REVRRLEEERAREMERVRLEEQERQQQVE-- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 160 ltkRIHLLEEDVKAAQAELEKafagtETEKALRLSLESKLSAMKKMQegdlemtlalEEKDRLIEElklslKSKEALIQC 239
Cdd:pfam17380 464 ---RLRQQEEERKRKKLELEK-----EKRDRKRAEEQRRKILEKELE----------ERKQAMIEE-----ERKRKLLEK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 240 LKEEKSqmaspdenvssgelrglSATLREEKERDAEERQKERNHFEERIQaLQEDLRekereIATEKKNSLKRDKAIQGL 319
Cdd:pfam17380 521 EMEERQ-----------------KAIYEEERRREAEEERRKQQEMEERRR-IQEQMR-----KATEERSRLEAMEREREM 577
|
250
....*....|....
gi 564351376 320 TMALKSKEKEVEEL 333
Cdd:pfam17380 578 MRQIVESEKARAEY 591
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1397-1568 |
5.72e-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: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAysSELHNSLTSEIQFLRKQNEALSTMLEKGS- 1475
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHp 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1476 --KEKQKENEKLRESLARKTES-LEHLQLEYASVREENERLRRDISEKERQNQQLTQevcsSLQELSRVQEEAKSRQQLL 1552
Cdd:COG3206 292 dvIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELY 367
|
170
....*....|....*.
gi 564351376 1553 lqkDELLQSLQmELKV 1568
Cdd:COG3206 368 ---ESLLQRLE-EARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-453 |
7.71e-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: 43.98 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 263 SATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA 342
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 343 DStQSREAPLKTQV------------------SEFEES--------------ENCEAALAEKEALLAKLHSENVTKNTEN 390
Cdd:COG4942 98 EL-EAQKEELAELLralyrlgrqpplalllspEDFLDAvrrlqylkylaparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351376 391 HRLLRNVKKVTQELNDLKKEKL----RLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAV 453
Cdd:COG4942 177 EALLAELEEERAALEALKAERQkllaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-452 |
7.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 64 ENQITELKKENFNLKLRIYFLEERIQqefagptehiykkNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGgSEIQ 143
Cdd:COG4717 101 EEELEELEAELEELREELEKLEKLLQ-------------LLPLYQELEALEAELAELPERLEELEERLEELRELE-EELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 144 RVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKmQEGDLEMTLALEEKDRLI 223
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 224 EELKLSLKSKEALIQCLKEEKSQMASPDEN------VSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQ----- 292
Cdd:COG4717 246 KEARLLLLIAAALLALLGLGGSLLSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleell 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 293 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKE--VEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALA 370
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 371 EKEALLAKLHSENVTK---------NTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGnrgarTIHDLRNEVEK 441
Cdd:COG4717 406 ELEEQLEELLGELEELlealdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEE 480
|
410
....*....|.
gi 564351376 442 LRKEVCEREKA 452
Cdd:COG4717 481 LKAELRELAEE 491
|
|
| 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 564351376 1390 TIASRFPQDLLMEHIQEirTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSEIQFLRKQNEalst 1469
Cdd:pfam17380 283 AVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1470 mlekgskEKQKENEKLR-ESLA---RKTESLEHLQLEYasvREENERLRRD--------ISEKERQNQQLTQEVcsSLQE 1537
Cdd:pfam17380 357 -------ERKRELERIRqEEIAmeiSRMRELERLQMER---QQKNERVRQEleaarkvkILEEERQRKIQQQKV--EMEQ 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564351376 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 564351376 1397 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgcetdqgSTNVSAYSSELHNSLTSEIQFLRKQNEALSTMLEKGSK 1476
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ--------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1477 EKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKD 1556
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564351376 1557 ELLQSLQ---MELKVYEKLAEEHQKLQQDVNKCPEASDNSFDLFESTQA 1602
Cdd:TIGR02169 938 DPKGEDEeipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
|
| 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 564351376 1476 KEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQ-EEAKSRQQLLLQ 1554
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQ 102
|
....*....
gi 564351376 1555 KDELLQSLQ 1563
Cdd:COG4942 103 KEELAELLR 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1400-1585 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1400 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLekgsKEKQ 1479
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREAL----DELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1480 KENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELL 1559
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180
....*....|....*....|....*.
gi 564351376 1560 QSLQMElkvYEKLAEEHQKLQQDVNK 1585
Cdd:TIGR02168 890 ALLRSE---LEELSEELRELESKRSE 912
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-658 |
1.23e-03 |
|
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: 43.94 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 144 RVKEDaRKKVQQVEELLTKRIHLLEEDVKAAQAELekafagteTEKalrlslESKLSAMKKMQEGDLEMTLALEEKDRLI 223
Cdd:pfam05483 216 KLKED-HEKIQHLEEEYKKEINDKEKQVSLLLIQI--------TEK------ENKMKDLTFLLEESRDKANQLEEKTKLQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 224 EE-LKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSAT-----LREEKERDAEERQKERN--------------H 283
Cdd:pfam05483 281 DEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticqLTEEKEAQMEELNKAKAahsfvvtefeattcS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 284 FEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIK------------ELTADSTQSREAP 351
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAedeklldekkqfEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 352 --------------LKTQVSEFEESEncEAALAEKEALLAKLHSENVtKNTE----NHRLLRNVKKVTQELNDLKKEKLR 413
Cdd:pfam05483 441 lifllqarekeihdLEIQLTAIKTSE--EHYLKEVEDLKTELEKEKL-KNIEltahCDKLLLENKELTQEASDMTLELKK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 414 LERDLEEAHREGNRGARTIH-------DLRNEVEKLRKEVCEREKAVE-KHYKSLPGESSSKFHSQEQVVKGLTESASQE 485
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIEnleekemNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 486 DLLLQKSNE-KDLEAIQQNCYLM----TAE-------ELKFGSDGLITEKCSQQSPDSKLIFSKE---KQQSEyEGLTGD 550
Cdd:pfam05483 598 NLKKQIENKnKNIEELHQENKALkkkgSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEiedKKISE-EKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 551 LKTEQNVYAHLAKNLQDTDSKLQAELKRVLALrkqLEQDVLAYRNLQTALQEQLSEIRKREEEPFSFYSDQTSYLSICLE 630
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVAL---MEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKA 753
|
570 580 590
....*....|....*....|....*....|..
gi 564351376 631 E----HSQFQLEHFSQEEIKKKVIDLIQLVKD 658
Cdd:pfam05483 754 EllslKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-445 |
1.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 56 RARNMKDFENQITELKKENFNLKLRIYFLEERIQQEFagptehiyKKNIELKVEVESLKRELQERDQLLVKASKAVESLA 135
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALL--------ERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 136 EGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAfAGTETEKALRLSLESKLSAMKKMQEGDLEMTLA 215
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 216 LEEKD----------------------------RLIEELKLSLKSKEALIQCLKEEKSqmASPDENVSSGELRGLSATLR 267
Cdd:COG1196 528 VLIGVeaayeaaleaalaaalqnivveddevaaAAIEYLKAAKAGRATFLPLDKIRAR--AALAAALARGAIGAAVDLVA 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 268 EEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQS 347
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 348 REaplktqvsEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNR 427
Cdd:COG1196 686 ER--------LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
410
....*....|....*...
gi 564351376 428 GARTIHDLRNEVEKLRKE 445
Cdd:COG1196 758 EPPDLEELERELERLERE 775
|
|
| 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 564351376 1453 LTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVC 1532
Cdd:COG1196 237 LEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564351376 1533 SSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-444 |
1.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 264 ATLREEKER-DAEERQKERNHFEERIQALQEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKEVEELnsiiKELTA 342
Cdd:COG4913 272 AELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEA--------------RLDALREELDEL----EAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 343 DSTQSREAPLKTQVSEFEES-ENCEAALAEKEALLAKLHsenVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEA 421
Cdd:COG4913 334 GNGGDRLEQLEREIERLERElEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
170 180
....*....|....*....|...
gi 564351376 422 HREGNRGARTIHDLRNEVEKLRK 444
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLER 433
|
|
| 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 564351376 64 ENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNiELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQ 143
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 144 RVKEDARKKVQQVEEL--LTKRIHLLEEDVKAAQAELE-----------------KAFAGTETE-KALRLSLESKLSAMK 203
Cdd:TIGR02168 825 RLESLERRIAATERRLedLEEQIEELSEDIESLAAEIEeleelieeleseleallNERASLEEAlALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 204 KMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEeksqmaspdenvssgelrglsaTLREEKERDAEERQKERNH 283
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE----------------------RLSEEYSLTLEEAEALENK 962
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564351376 284 FEERIQALQEDLREKEREIA----------TEKKNSLKR----DKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERydflTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-410 |
1.74e-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: 43.09 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 55 TRARNMKDFENQITELKKENFNLKLRIYFLEERIqQEFAGPTEHIYKKNIELKVEVESLKRELQERDQllvkaskavesl 134
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK------------ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 135 aegggsEIQRVKEDARKKVQQVEElLTKRIHLLEEDVKaaqaELEKafagtetekaLRLSLESKLSAMKKmqegdlemtl 214
Cdd:TIGR04523 427 ------EIERLKETIIKNNSEIKD-LTNQDSVKELIIK----NLDN----------TRESLETQLKVLSR---------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 215 ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsatlrEEKERDAEERQKErnhFEERIQALQED 294
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKEL--------------------EEKVKDLTKKISS---LKEKIEKLESE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 295 LREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQsreapLKTQVSEFE-ESENCEAALAE 371
Cdd:TIGR04523 533 KKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE-----KQELIDQKEkEKKDLIKEIEE 607
|
330 340 350
....*....|....*....|....*....|....*....
gi 564351376 372 KEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE 410
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| 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 564351376 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSeiqflRKQNEALSTMLEKGSKEKQKENEK 1484
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1485 LRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQM 1564
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
170
....*....|....*..
gi 564351376 1565 ElKVYEKLAEEHQKLQQ 1581
Cdd:TIGR02168 436 K-ELQAELEELEEELEE 451
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
78-344 |
1.81e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 78 KLRIYFLEERIQQEFagptEHIYKKNIelkVEVESLKRELQ-ERDQ----LLVKASKAVESL-----AEGGGSEIQRVKE 147
Cdd:PRK05771 8 KVLIVTLKSYKDEVL----EALHELGV---VHIEDLKEELSnERLRklrsLLTKLSEALDKLrsylpKLNPLREEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 148 DARKK--VQQVEELLTKrihlLEEDVKAAQAELEKAfagtETEKAlrlSLESKLSAMKKMQEGDLEMTLALEEKDRLIEE 225
Cdd:PRK05771 81 VKSLEelIKDVEEELEK----IEKEIKELEEEISEL----ENEIK---ELEQEIERLEPWGNFDLDLSLLLGFKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 226 LKLSLKSKEALIQ--------CLKEEKSQM------ASPDENVSSGELR------------GLSATLREEKERDAEERQK 279
Cdd:PRK05771 150 GTVPEDKLEELKLesdvenveYISTDKGYVyvvvvvLKELSDEVEEELKklgferleleeeGTPSELIREIKEELEEIEK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564351376 280 ERNHFEERIQALQEdlREKEREIATEKKNSLKRDKAiQGLTMALKSK----------EKEVEELNSIIKELTADS 344
Cdd:PRK05771 230 ERESLLEELKELAK--KYLEELLALYEYLEIELERA-EALSKFLKTDktfaiegwvpEDRVKKLKELIDKATGGS 301
|
|
| DUF445 |
pfam04286 |
Protein of unknown function (DUF445); Predicted to be a membrane protein. |
144-379 |
1.95e-03 |
|
Protein of unknown function (DUF445); Predicted to be a membrane protein.
Pssm-ID: 427840 [Multi-domain] Cd Length: 368 Bit Score: 42.61 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 144 RVKEDARKKVQQVEELLTKRIHLLEEDvkAAQAELEKAFAGTETEKALRLSLESKLSAMkkMQEGDLEMTLaleekDRLI 223
Cdd:pfam04286 77 ADPTNAERLAREVAKLLAEILEDLDDE--RVQRLLKKALRRRLEEIDLAPLLGKLLELL--LAEGRHQALL-----DDLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 224 EELKLSLKSKEA------LIQCLKEEKSQMASPDENVSSGELRGLSATLRE-EKERDAEERQKERNHFEERIQALQEDlr 296
Cdd:pfam04286 148 DRLRDWLRSEEGkqriaeMIDEFLEEWGPLVALLGGIAEMILRALSSLLDEvQADPDHPLRLAFDRAVRELITDLLND-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 297 EKEREIATEKKNSLKRDKAIQGLTMALkskekeVEELNSIIKELTADSTQSREAPLKTQVSEFEEsenceaALAEKEALL 376
Cdd:pfam04286 226 PELRAEVEELKQKLLADPAVQDYVKAL------WESLRSLLLDDLSDPDSALRRRISELLAEFGE------RLAEDPELR 293
|
...
gi 564351376 377 AKL 379
Cdd:pfam04286 294 DKL 296
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-613 |
2.13e-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: 43.09 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 277 RQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS-------IIKELTADSTQ--S 347
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDklkknkdKINKLNSDLSKinS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 348 REAPLKTQVSEFE-ESENCEAALAEKEALLAKLhsenvtkNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGN 426
Cdd:TIGR04523 111 EIKNDKEQKNKLEvELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 427 RGARTIHDLRNEVEKLRKEVCEREKAVEKHyKSLpgesSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQncyL 506
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL----ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---L 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 507 MTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKT--EQNVYAHLAKNLQDTDSKLQ----------- 573
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEeiqnqisqnnk 335
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 564351376 574 --AELKRVLA-LRKQLEQDVLAYRNLQTALQEQLSEIRKREEE 613
Cdd:TIGR04523 336 iiSQLNEQISqLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
|
| 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 564351376 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEgggsEIQRVKEDARKKVQQVEELlTKRIHLLEEDVKAAQAELEKAFAG 184
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKL-QAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 185 TETEKALRLSLE------------SKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKsqmaspde 252
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 253 nvssgelrglsatlrEEKERDAEERQKERnhfeeriQALQEDLREKEREiATEKKNSLKRDKAIQGLTMALKSKEKEVEE 332
Cdd:COG3883 167 ---------------EAAKAELEAQQAEQ-------EALLAQLSAEEAA-AEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*....
gi 564351376 333 LNSIIKELTADSTQSREAP 351
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAA 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
58-662 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 58 RNMKDFENQITELKKENFNLKLRIYFLE-ERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVES--- 133
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPlAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrl 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 134 ----LAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQeGD 209
Cdd:TIGR00618 347 lqtlHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ-GQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 210 LEMTLALEEKDRLIEELKLSLKSKEAliQCLKEEKSqmaspdenvssgELRGLSATLREEKERDA---------EERQKE 280
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKI------------HLQESAQSLKEREQQLQtkeqihlqeTRKKAV 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 281 RNHFEERIQALQEDLREKEREIATEKKNSL-------KRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLK 353
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARQDIDnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 354 TQV------SEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLR------NVKKVTQELNDLKKEKLRLERDLEEA 421
Cdd:TIGR00618 572 FSIltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqpeqDLQDVRLHLQQCSQELALKLTALHAL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 422 HREGNRGARTIHDLRNEVEKLRK--EVCEREKAVEKHYKSLPG------ESSSKFHSQEQVVKGL--------------- 478
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELlaSRQLALQKMQSEKEQLTYwkemlaQCQTLLRELETHIEEYdrefneienassslg 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 479 TESASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNVY 558
Cdd:TIGR00618 732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 559 A------------HLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLS--------------EIRKREE 612
Cdd:TIGR00618 812 IpsdedilnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiqlsdklnginqiKIQFDGD 891
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 564351376 613 EPFSFYSDQTSYLSICL--EEHSQFQLEHFSQEEIKKKVIDLIQLVKDLHAD 662
Cdd:TIGR00618 892 ALIKFLHEITLYANVRLanQSEGRFHGRYADSHVNARKYQGLALLVADAYTG 943
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
218-340 |
2.66e-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: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 218 EKDRLIEELKLSL---KSKEALIQCLKEEksqmASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQED 294
Cdd:COG2433 360 PPDVDRDEVKARVirgLSIEEALEELIEK----ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564351376 295 LREKEREIA----------TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEL 340
Cdd:COG2433 436 LEEKDERIErlerelsearSEERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
60-355 |
3.62e-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: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 60 MKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQER-DQLLVKASKAVESLAEG- 137
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTENl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 138 -----------GGSEIQRVKEDARKKVQQVE----ELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAM 202
Cdd:COG5185 357 eaikeeienivGEVELSKSSEELDSFKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 203 KKMQEGDLEMTLALEEKDRLIEELKLSlKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERN 282
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQS-RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351376 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 564351376 1400 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgcetdqgstnVSAYSSELhNSLTSEIQFLRKQNEALSTML---EKGSK 1476
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKE-----------LEELKEEI-EELEKELESLEGSKRKLEEKIrelEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1477 EKQKENEKLRESLARkTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcSSLQELSRVQEEAKSRQQLLLQKD 1556
Cdd:PRK03918 270 ELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI-NGIEERIKELEEKEERLEELKKKL 347
|
170 180
....*....|....*....|....*....
gi 564351376 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 |
4.08e-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: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1405 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHnSLTSEIQFLRKQNEALSTMLEKGSKEK---QKE 1481
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIaqlSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1482 NEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKS----RQQLLLQKDE 1557
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlrerLESLERRIAA 835
|
170 180 190
....*....|....*....|....*....|....*.
gi 564351376 1558 LLQSLQMELKVYEKLAEEHQKLQQDVNKCPEASDNS 1593
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-427 |
4.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 258 ELRGLSATLREEKERdAEERQKERNHFEERIQALQE---------DLREKEREIA--TEKKNSLKR-DKAIQGLTMALKS 325
Cdd:COG4913 618 ELAELEEELAEAEER-LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAelEAELERLDAsSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 326 KEKEVEELNSIIKELTADSTQsreapLKTQVSEFEES-ENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQEL 404
Cdd:COG4913 697 LEAELEELEEELDELKGEIGR-----LEKELEQAEEElDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
170 180
....*....|....*....|....*..
gi 564351376 405 ND----LKKEKLRLERDLEEAHREGNR 427
Cdd:COG4913 772 EEridaLRARLNRAEEELERAMRAFNR 798
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
105-613 |
4.30e-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: 42.12 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 105 ELKVEVESLKRELQERDQLLVKASK--AVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLE---EDVKaaQAELE 179
Cdd:pfam10174 203 QKEKENIHLREELHRRNQLQPDPAKtkALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEdreEEIK--QMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 180 KA---FAGTETEKaLRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEksqmaspdenVSS 256
Cdd:pfam10174 281 KShskFMKNKIDQ-LKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTE----------VDA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 257 GELR-GLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIatekkNSLKrdKAIQGLTMALKSKEKEVEELNS 335
Cdd:pfam10174 350 LRLRlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKI-----NVLQ--KKIENLQEQLRDKDKQLAGLKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 336 IIKELTADSTQSREApLKTqvsefeesenCEAALAEKEALLAKLHSEnvtKNTENHRLLRNVKKVTQELNDLKKEKLRLE 415
Cdd:pfam10174 423 RVKSLQTDSSNTDTA-LTT----------LEEALSEKERIIERLKEQ---REREDRERLEELESLKKENKDLKEKVSALQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 416 RDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSS--KFHSQEQVVKGLTESASQEDLLLQKSN 493
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQlkKAHNAEEAVRTNPEINDRIRLLEQEVA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 494 EKDLEAIQQNCYLmtaEELKfgsdGLITEKCSQQSpdsklifSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQ 573
Cdd:pfam10174 569 RYKEESGKAQAEV---ERLL----GILREVENEKN-------DKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKG 634
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564351376 574 AELKrVLALRkqlEQDVLAYRNLQTALQEQLSEIRKREEE 613
Cdd:pfam10174 635 AQLL-EEARR---REDNLADNSQQLQLEELMGALEKTRQE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
140-392 |
4.58e-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: 41.29 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 140 SEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKKmQEGDLEMTLALEEK 219
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------------LERRIAALAR-RIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 220 DrlIEELKLSLKSKEALIQCLKEEKSQMAspDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKE 299
Cdd:COG4942 84 E--LAELEKEIAELRAELEAQKEELAELL--RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 300 REIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAdSTQSREAPLKTQVSEFEESE-NCEAALAEKEALLAK 378
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAeELEALIARLEAEAAA 238
|
250
....*....|....
gi 564351376 379 LHSENVTKNTENHR 392
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
275-509 |
4.90e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 275 EERQKERNHFEERIQALQEDlREKEREIATEKKNSLKRDKA-----IQGLTMALKSKEKEVEELNSIIKELTAdstqSRE 349
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQ-REKEKERYKRDREQWERQRRelesrVAELKEELRQSREKHEELEEKYKELSA----SSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 350 APLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGA 429
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 430 RTIHDLRN-------EVEKLRKEVCE-REKAVEKHYKSLPGESSSK--------FHSQEQVVKGLTES----ASQEDLLL 489
Cdd:pfam07888 192 KEFQELRNslaqrdtQVLQLQDTITTlTQKLTTAHRKEAENEALLEelrslqerLNASERKVEGLGEElssmAAQRDRTQ 271
|
250 260
....*....|....*....|
gi 564351376 490 QKSNEKDLEAIQQNCYLMTA 509
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADA 291
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
230-374 |
5.04e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 230 LKSKEAliQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNS 309
Cdd:PRK12705 30 RLAKEA--ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564351376 310 LKRDKAIQGLTMALKSKEKEVEELNSIIKELTADstQSREAPLKTQVSEFEESENCEAALAEKEA 374
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAELEEEKAQRVKKIEEEA 170
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
258-358 |
5.42e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 258 ELRGLSATLRE-EKERDAEERQKERNHFEeRIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSI 336
Cdd:COG0542 412 ELDELERRLEQlEIEKEALKKEQDEASFE-RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....
gi 564351376 337 IKELTADSTQSREAP--LKTQVSE 358
Cdd:COG0542 491 EKELAELEEELAELAplLREEVTE 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1362-1597 |
5.63e-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: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1362 HALSDDEMSEKSFLSREPKPDSETEKYPTIASrfpqdlLMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgCETDQGSTn 1441
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTY------WKEMLAQCQTLLRELETHIEEYDREFNEIEN--ASSSLGSD- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1442 vSAYSSELHNSLTSEIQFLRKqnealsTMLEKGSKEKQKENEKLRESLARKTEsLEHLQLEYASVREENERLRRDISEKE 1521
Cdd:TIGR00618 734 -LAAREDALNQSLKELMHQAR------TVLKARTEAHFNNNEEVTAALQTGAE-LSHLAAEIQFFNRLREEDTHLLKTLE 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351376 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 |
5.82e-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: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1465 EALSTMLEKGSKEKQKENEKLRES----LARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcsslqelsr 1540
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEREL--------- 450
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564351376 1541 vqEEAKSRQQLLLQKDELLQSLQMELKVYEK-LAEEHQKLQQ 1581
Cdd:COG2433 451 --SEARSEERREIRKDREISRLDREIERLEReLEEERERIEE 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
275-455 |
7.69e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 275 EERQKERNHFEERIQALQEDLrekeREIATEKKNSLKRDKAIQGLTMA------LKSKEKEVEELNSIIKELTADSTQSR 348
Cdd:COG4913 613 AALEAELAELEEELAEAEERL----EALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 349 EapLKTQVSEfeesenCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK-----LRLERDLEEAHR 423
Cdd:COG4913 689 A--LEEQLEE------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|..
gi 564351376 424 EgNRGARTIHDLRNEVEKLRKEVCEREKAVEK 455
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAEEELER 791
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-342 |
8.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 56 RARNMKDFENQITELKKenfnlKLRIYFLE--ERIQQEFagptEHIYKKNIELKVEVESLKRELqERDQLLVKASKAVES 133
Cdd:PRK03918 494 ELIKLKELAEQLKELEE-----KLKKYNLEelEKKAEEY----EKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 134 laegggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKaaqaELEKAFAGTETEKALRLSLESKLSAMKKMQEgDLEMT 213
Cdd:PRK03918 564 -------KLDELEEELAELLKELEELGFESVEELEERLK----ELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 214 LA-LEEKDRLIEELKLSLkskealiqclkEEKSQMASPDENvssgelrglsatlrEEKERDAEERQKERNHFEERIQALQ 292
Cdd:PRK03918 632 FEeLAETEKRLEELRKEL-----------EELEKKYSEEEY--------------EELREEYLELSRELAGLRAELEELE 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 564351376 293 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKeVEELNSIIKELTA 342
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKA 735
|
|
| 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 564351376 1402 EHIQEIRTLRKHLEESIKtneklrkqlerqgcetdqgstnvsaysselhnsltSEIQFLRKQNEALSTMLEKGSKEKQKE 1481
Cdd:pfam09311 154 EELIEVRTAADHMEEKLK-----------------------------------AEILFLKEQIQAEQCLKENLEETLQAE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1482 NEKLRESLArkteSLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQS 1561
Cdd:pfam09311 199 IENCKEEIA----SISSLKVELERIKAEKEQLENGLTEKIRQLEDLQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQR 274
|
170 180
....*....|....*....|
gi 564351376 1562 LQMELKVYEKLAEEHQKLQQ 1581
Cdd:pfam09311 275 LQTELDVSEQVQRDFVKLSQ 294
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1451-1585 |
8.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351376 1451 NSLTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQE 1530
Cdd:COG4372 48 EQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564351376 1531 VCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQDVNK 1585
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| |
