|
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 |
2.03e-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: 2.03e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351372 61 KDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASK 129
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-455 |
1.49e-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: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 146 KEDARKKVQQVEELLTkRIHLLEEDVKAAQAELEKafagtETEKALR----------LSLESKLSAMKKMQEGDLEMTLA 215
Cdd:COG1196 174 KEEAERKLEATEENLE-RLEDILGELERQLEPLER-----QAEKAERyrelkeelkeLEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 216 LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASpdenvssgELRGLSATLREEKERDAEERQkERNHFEERIQALQEDL 295
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELEL--------ELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA---DSTQSREAPLKTQVSEFEESENCEAALAEK 372
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEallEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 373 EALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKA 452
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
...
gi 564351372 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 |
2.73e-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: 68.94 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 138 GGSEIQRVKEDARKKVQQVEELLtKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLE----SKLSAMKKMQEGDLEMT 213
Cdd:TIGR02169 164 GVAEFDRKKEKALEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 214 LA--------LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLR------EEKERDAEERQK 279
Cdd:TIGR02169 243 ERqlasleeeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 280 ERNHFEERIQALQEDLREKEREIATEKKnslKRDKaiqgLTMALKSKEKEVEELNSIIKELTADSTQSREA--------- 350
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERK---RRDK----LTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyrekle 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 351 -------PLKTQVSEF--------EESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLE 415
Cdd:TIGR02169 396 klkreinELKRELDRLqeelqrlsEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564351372 416 RDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPG 462
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-613 |
7.74e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 97 EHIYKKNIELKVEVESLKRELQErdqlLVKASKAVESLAEGGGSEIQRVKEDARKkvqqveelLTKRIHLLEEDVKAAQA 176
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEK----FIKRTENIEELIKEKEKELEEVLREINE--------ISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 177 ELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELK------LSLKSKEALIQCLKEEKSQMASP 250
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelKELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 251 DENVS------SGELRGLSATL--REEKERDAEERQKERNHFEERIQALQEDLREKEReiATEKKNSLKRDKA------I 316
Cdd:PRK03918 309 LREIEkrlsrlEEEINGIEERIkeLEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKrltgltP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 317 QGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEESEN----CEAALAE--KEALLAKLHSenvtknt 388
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARigELKKEIKELKKAIEELKKAKGkcpvCGRELTEehRKELLEEYTA------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 389 ENHRLLRNVKKVTQELNDLKKEKLRLERDLEEaHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGES---S 465
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 466 SKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQNCYLmtaEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYE 545
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKELEPFYNEYLELKDAEKELE 615
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564351372 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 |
2.24e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 160 LTKRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKKMQEgdlEMTLALEEKDRLIEELKLSLKSKEALIQC 239
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAE--------------LRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 240 LKEEKSQMASPDENV-----SSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDK 314
Cdd:TIGR02168 745 LEERIAQLSKELTELeaeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 315 AIQGLTMALKSKEKEVEELNSIIKELTADSTQSREaplktqvsefeESENCEAALAEKEALLAKLHSENVTKNTENHRLL 394
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAA-----------EIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564351372 395 RNVKKVTQELNDLKKEKLRLERDLEEAHREgnrgartIHDLRNEVEKLRKEV 446
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREK-------LAQLELRLEGLEVRI 938
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-613 |
2.38e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 85 EERIQQEFAGPTEHIYKKNIELKVE----VESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELL 160
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 161 TKRIHLLEEDVKAAQ-AELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEAliQC 239
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA--DE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 240 LKEEKSQMASPDENVSSGELRGLSAtlrEEKERDAEERQKERNHFEERIQALQEDLRE-KEREIATEKKNSLKRDKAiqg 318
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKA---DAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKA--- 1380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 319 ltMALKSKEKEVEELNSIIKEL-----TADSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRL 393
Cdd:PTZ00121 1381 --DAAKKKAEEKKKADEAKKKAeedkkKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 394 LRNVKKVTQELN--DLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKlRKEVCEREKAVEKHYKSLPGESSSKFHSQ 471
Cdd:PTZ00121 1459 AEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 472 E----QVVKGLTESASQEDLL----LQKSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSE 543
Cdd:PTZ00121 1538 EakkaEEKKKADELKKAEELKkaeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351372 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 |
3.54e-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: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 142 IQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFagtETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDR 221
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 222 LIEELKLSLKSKEALIQCLKEEKsQMASPDENVSSGELRGLSATL------REEKERDAEERQKERNHFEERIQALQEDL 295
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQLeeleskLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFEES------ENCEA 367
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARleRLEDRRERLQQEIEELLKKleeaelKELQA 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564351372 368 ALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE------KLRLERDLEEAHREGNRGARTI 432
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQENLEGFSEGVKAL 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-467 |
3.78e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 59 NMKDFENQITELKKENFNLKLRIYFLEERIQQ-EFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEG 137
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 138 GGSEIQRVKEDARKKVQQVEELLT-KRIHLLEEDVKAAQAELE---KAFAGTETEKalrlsLESKLSAMKKMQEgdlEMT 213
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEElEERHELYEEAKAKKEELErlkKRLTGLTPEK-----LEKELEELEKAKE---EIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 214 LALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKernhFEERIQALQE 293
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKE----IEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 294 DLREKEREIATEKKNSLKRDKAIQgltmaLKSKEKEVEELNsiIKELTADSTQSRE-----APLKTQVSEFEESENCEAA 368
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYN--LEELEKKAEEYEKlkeklIKLKGEIKSLKKELEKLEE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 369 L-AEKEALLAKLHSENVTKNTENHRLLR------------------------NVKKVTQELNDLKKEKLRLERDLEEAHR 423
Cdd:PRK03918 554 LkKKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKKLEEELDKAFE 633
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564351372 424 EGNRGARTIHDLRNEVEKLRKEVCERE-KAVEKHYKSLPGESSSK 467
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGL 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-571 |
7.54e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 101 KKNIELKVEVESLKRELQER---DQLLVKASKAVESLAEGGGSEIQRVKEDARKK----VQQVEELLTKRihllEEDVKA 173
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKkaeeKKKADEAKKKA----EEAKKA 1446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 174 AQAElEKAFAGTETEKALRLSLESKLS--AMKKMQEGDL--EMTLALEEKDRLIEELKlslKSKEAliqclKEEKSQMAS 249
Cdd:PTZ00121 1447 DEAK-KKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKadEAKKKAEEAKKKADEAK---KAAEA-----KKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 250 PDENVSSGELRGLSATLREEKERDAEERQKErnhfEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKE 329
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 330 VEELNSIIKEltadstqsrEAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKvTQELNDLKK 409
Cdd:PTZ00121 1594 IEEVMKLYEE---------EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK-AEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 410 EKLRleRDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVE---------KHYKSLPGESSSKFHSQEQVVKGLTE 480
Cdd:PTZ00121 1664 AEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeaeekKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 481 SASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSpdsklifskEKQQSEYEGLTGDLKT------- 553
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED---------EKRRMEVDKKIKDIFDnfaniie 1812
|
490 500
....*....|....*....|.
gi 564351372 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 |
1.11e-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: 63.92 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 59 NMKDFENQITELKKENFNLKLRIYFLEERIQQEfagptehiYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGG 138
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETL--------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 139 GSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEE 218
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 219 KDRLIEELKLSLKSKEALIQCLkeekSQMASPDENVSS------GELRGLSATLREEKERDAEERQKE----RNHFEE-- 286
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVL----SELISVDEGYEAaieaalGGRLQAVVVENLNAAKKAIAFLKQnelgRVTFLPld 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 287 -----RIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS---IIKELTAD--------------- 343
Cdd:TIGR02168 580 sikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNaleLAKKLRPGyrivtldgdlvrpgg 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 344 -STQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAH 422
Cdd:TIGR02168 660 vITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 423 REGNRGARTIHDLRNEVEKLRKEVCEREKAVEkhykslpgESSSKFHSQEQVVKGLTESA--SQEDLLLQKSNEKDLEAI 500
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLE--------EAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAE 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 501 qqncylMTAEELKFGSDGLITEKCSQQspdsklIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVL 580
Cdd:TIGR02168 812 ------LTLLNEEAANLRERLESLERR------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
570 580 590
....*....|....*....|....*....|
gi 564351372 581 ALRKQLEQDVLAYRNLQTALQEQLSEIRKR 610
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESK 909
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-607 |
2.50e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 268 EEKERDAEERQKERNHfEERIQALQEDLREKEREIATEKKNSLKRDKA------------IQGLTMALKSKEKEVEELNS 335
Cdd:TIGR02169 194 DEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaierqlasleeeLEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 336 IIKELTA---DSTQSREAPLKTQVSEFE-ESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK 411
Cdd:TIGR02169 273 LLEELNKkikDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 412 LRLERDLEEahregnrgartihdLRNEVEKLRKEVCErekaVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQK 491
Cdd:TIGR02169 353 DKLTEEYAE--------------LKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 492 SNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNvyahlakNLQDTDSK 571
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-------RVEKELSK 487
|
330 340 350
....*....|....*....|....*....|....*.
gi 564351372 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 |
4.85e-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: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 203 KKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRglsatlREEKERDAEERQKERN 282
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE------VSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 283 HFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTadstqsreaplktqvsefEES 362
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK------------------EEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 363 ENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDL-----RN 437
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEA 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351372 438 EVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKD-LEAIQQN 503
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDsLERLQEN 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-348 |
8.28e-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: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEgggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAG 184
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 185 TETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSA 264
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 265 TLREEKER-DAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:COG1196 406 EEAEEALLeRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
....*
gi 564351372 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 |
9.92e-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: 60.47 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 217 EEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdeNVSSGELRGLSATLREeKERDAEERQKERNHFEERIQALQEDLR 296
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRL-----DELSQELSDASRKIGE-IEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 297 EKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEEL-----NSIIKELTADSTQsreapLKTQVSEFEES-ENCEAALA 370
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK-----LEEEVSRIEARlREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 371 EKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREgnrgartIHDLRNEVEKLRKEVCERE 450
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351372 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 |
1.49e-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: 59.65 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 61 KDFENQITELKKENFNLKLRIyfleERIQQEFAGPTEHIYKKN---IELKVEVESLKRELQERDQLLVKASKAVESLAEg 137
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNI----EKKQQEINEKTTEISNTQtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 138 ggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFagTETEKALRlSLESKLSAMKKMQEG----DLEMT 213
Cdd:TIGR04523 289 ---QLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI--SQNNKIIS-QLNEQISQLKKELTNseseNSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 214 LALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsatlreekERDAEERQKERNHFEERIQALQE 293
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-----------------------ESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 294 DLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEltadstqsreapLKTQVSEFEES--------ENC 365
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES------------LETQLKVLSRSinkikqnlEQK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 366 EAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRgartiHDLRNEVEKLRKE 445
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKE 562
|
410
....*....|
gi 564351372 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 |
4.60e-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: 58.21 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 141 EIQRVKEDARKKVQQVEelltkRIHLLEEDVKAAQAELEKAFA--------GTETEKAL-RLSLESKLSAMKKMQEGDLE 211
Cdd:pfam17380 297 EQERLRQEKEEKAREVE-----RRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELeRIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 212 MTLaleEKDRLIEELKLSLKSKE---------ALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEE---RQK 279
Cdd:pfam17380 372 MEI---SRMRELERLQMERQQKNervrqeleaARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEeraREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 280 ERNHFEERIQALQ-EDLREKEREiatEKKNSLKRDKAiqgltmalKSKEKEVEELNSII--KELTADSTQSREAPLKTQV 356
Cdd:pfam17380 449 ERVRLEEQERQQQvERLRQQEEE---RKRKKLELEKE--------KRDRKRAEEQRRKIleKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564351372 357 SEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLkkEKLRLERDL 418
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL--EAMEREREM 577
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-668 |
5.06e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 101 KKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKV-QQVEELLTKRIHLLEEDVKAAQA--- 176
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIaRKAEDARKAEEARKAEDAKKAEAark 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 177 --------ELEKAFAGTETEKALRLSLESKLSAMKKMQEGD-LEMTLALEEKDRLIEELKLSLKSKE-ALIQCLKEEKSQ 246
Cdd:PTZ00121 1184 aeevrkaeELRKAEDARKAEAARKAEEERKAEEARKAEDAKkAEAVKKAEEAKKDAEEAKKAEEERNnEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 247 MASPDENVSSGELRGLSATLR--EEKERDAEERQKERNHFEERIQALQEDLR-----EKEREIATEKKNSLKR--DKAIQ 317
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeaKKKAEEAKKKADAAKKkaEEAKK 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 318 GLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNV 397
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 398 KKVTQElndlKKEKLRLERDLEEahregnrgARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKG 477
Cdd:PTZ00121 1424 KKKAEE----KKKADEAKKKAEE--------AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 478 LTESASQEDLLLQKSNEKDleaiqqncylmTAEELKFGSDGLITEKCSQQSPDSKlifSKEKQQSEYEGLTGDLKTEQNV 557
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKK-----------KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELKKAEEL 1557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 558 YAhlAKNLQDTDSKLQAELKRVLALRKQLEqdvlayrnLQTALQEQLSEIRKREEEPFSFYSDQTSYlsiclEEHSQFQL 637
Cdd:PTZ00121 1558 KK--AEEKKKAEEAKKAEEDKNMALRKAEE--------AKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKA 1622
|
570 580 590
....*....|....*....|....*....|..
gi 564351372 638 EHFSQ-EEIKKKVIDLIQLVKDLHADNQHLKK 668
Cdd:PTZ00121 1623 EELKKaEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-503 |
8.04e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 49 EEKVSPTRARNMKDFENQITELKK-ENFNLKLriyflEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQErdqlLVKA 127
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKaEEAKKKA-----EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE----AKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 128 SKAVESLAEGGGSEIQRVKEDARK--KVQQVEELLTKRIHLLEEDVKAAQaELEKAFAGTETEKALRLSlESKLSAMKKM 205
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAE-EDKNMALRKA 1583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 206 QEgdlemtLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLR---EEKERDAEERQKERN 282
Cdd:PTZ00121 1584 EE------AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKkkeAEEKKKAEELKKAEE 1657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 283 hfEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKE-KEVEELNSIIKELTADSTQSREAplktqvsefEE 361
Cdd:PTZ00121 1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEaKKAEELKKKEAEEKKKAEELKKA---------EE 1726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 362 SENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKK---------------VTQELNDLKKEKLRLERD--------- 417
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKeeekkaeeirkekeaVIEEELDEEDEKRRMEVDkkikdifdn 1806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 418 LEEAHREGNRGARTIHDLRNEVEKLRKEVC-------EREKAVEKH---YKSLPGESSSK---FHSQEQVVKGLTESASQ 484
Cdd:PTZ00121 1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVAdsknmqlEEADAFEKHkfnKNNENGEDGNKeadFNKEKDLKEDDEEEIEE 1886
|
490
....*....|....*....
gi 564351372 485 EDlLLQKSNEKDLEAIQQN 503
Cdd:PTZ00121 1887 AD-EIEKIDKDDIEREIPN 1904
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-446 |
9.08e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 60 MKDFENQITELKKENFNLKLRIYFLEERIQQ--EFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEG 137
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 138 GGSEIQRVK------EDARKKVQQVEELLTKRIHLLE---EDVKAAQAELEKA-----FAGTETEKALRLSLESKLSA-M 202
Cdd:PRK03918 382 TGLTPEKLEkeleelEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAeL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 203 KKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQcLKEEKSQMASPDEnvssgELRGLSATLREEKERDAEERQKERN 282
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKELEE-----KLKKYNLEELEKKAEEYEKLKEKLI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 283 HFEERIQALQEDLR-----EKEREIATEKKNSLKRDKAiQGLTMALKSKEKEVEELNSIIKELTA---------DSTQSR 348
Cdd:PRK03918 536 KLKGEIKSLKKELEkleelKKKLAELEKKLDELEEELA-ELLKELEELGFESVEELEERLKELEPfyneylelkDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 349 EAPLKTQVSEFEESENCEAALAEKEALLAKLHSE----NVTKNTENHRLLRN-----------VKKVTQELNDLKKEKLR 413
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREeylelsrelagLRAELEELEKRREEIKK 694
|
410 420 430
....*....|....*....|....*....|....*.
gi 564351372 414 LERDLEEAHREGNRGARTIHDL---RNEVEKLRKEV 446
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEKLekaLERVEELREKV 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-446 |
1.07e-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: 57.39 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 84 LEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGG--SEIQRVKEDARKKVQQVEellt 161
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELE---- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 162 KRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKkmqegdlemtlaLEEKDRLIEELKLSLKSKEALIQCLk 241
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALND--------------LEARLSHSR------------IPEIQAELSKLEEEVSRIEARLREI- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 242 EEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERN------HFEERIQALQEDLREKEREIATEKKNSLKRDKA 315
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 316 IQGLTMALKSKEKEVEELNSIIKELTA--DSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRL 393
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAklEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564351372 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 |
1.78e-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: 56.60 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 57 ARNMKDFENQITELKKENFNLKLRIyfleERIQQEFagptehiYKKNIELKvEVESLKRELQERDQLLVKASKAVESLAE 136
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEI----EELQKEL-------YALANEIS-RLEQQKQILRERLANLERQLEELEAQLE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 137 GGGSEIQRVKEDARKKVQQVEELLtKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKkmqegdLEMTLAL 216
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------LQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 217 EEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELrglsatlrEEKERDAEERQKERNHFEERIQALQEDLR 296
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--------EELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 297 EKEREIaTEKKNSLKRdkaIQGLTMALKSKEKEVEELNSIIKELTADstQSREAPLKTQVSEFEESEN-----CEAALAE 371
Cdd:TIGR02168 472 EAEQAL-DAAERELAQ---LQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSELISVDEgyeaaIEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 372 --------------------KEALLAKLH-----SENVTKNTENHRLLRN------------------------------ 396
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflKQNELGRVTflpldSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 397 --VKKVTQELNDLKKEKL----------------------------RLERD--LEEAHREGNRGARTIHDLRNEVEKLRK 444
Cdd:TIGR02168 626 lvVDDLDNALELAKKLRPgyrivtldgdlvrpggvitggsaktnssILERRreIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 445 EVCEREKAVEKHYKSLPgESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQncyLMTAEELKFGSDGLITEKC 524
Cdd:TIGR02168 706 ELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IEELEERLEEAEEELAEAE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 525 SQQSPDSKLIfskEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQdvlayrnlqtaLQEQL 604
Cdd:TIGR02168 782 AEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-----------LEEQI 847
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 605 SEIRKREEEpfsfYSDQTSYLSICLEEHSQfQLEHFS------QEEIKKKVIDLIQLVKDLHADNQHLKK 668
Cdd:TIGR02168 848 EELSEDIES----LAAEIEELEELIEELES-ELEALLneraslEEALALLRSELEELSEELRELESKRSE 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1390-1616 |
3.39e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1390 EKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALstmlEKGSKEKQKENEKLRESLARKTESLEHLQL 1469
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1470 EYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQ 1549
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351372 1550 ESRGEAcgggQKGQDPFSNLHGLLKEIQVLRDQAERSIQTNNTLKSKLEKQLSQGSKQAQEGALTLA 1616
Cdd:COG1196 390 EALRAA----AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-454 |
5.22e-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: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 61 KDFENQITELKKENFNLKLRIYFLEERIQQEfagpTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVEslaegggs 140
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 141 EIQRVKEDARKKVQQVEELLTKRIhLLEEDVKAAQAELEKAfagTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEKD 220
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEA---EEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 221 RLIEELKLSLKSKEALIQCLKEEKSQMASPDENVssgelrglsATLREEKERDAEERQKERNHFEERIQALQEDLREKER 300
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAEL---------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 301 EIATEKKNSLKRDKAIQGLTM---ALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESEncEAALAEKEALLA 377
Cdd:COG1196 471 EAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY--EAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 378 klhsenvtknteNHRLLRNVKKVTQELNDLKKEK------LRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREK 451
Cdd:COG1196 549 ------------QNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
...
gi 564351372 452 AVE 454
Cdd:COG1196 617 VLG 619
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
102-493 |
1.65e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 102 KNIELKVEVESLKRELQERDQLLVKAS---KAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAEL 178
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 179 EKAFAGTETEKALRLSLESKLSAMKKMQEGDLEmtlalEEKDRLIEELKLSLKSKEALIQCLKEEKSQmASPDENVSSGE 258
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-----EEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKE 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 259 lrglsatlrEEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIK 338
Cdd:PTZ00121 1712 ---------AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 339 E-LTADSTQSREAPLKTQVSEFEESENCEAALAE----------------KEALLAKLHSENVTKNTENHRLLRNVK--K 399
Cdd:PTZ00121 1783 EeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnlvindskemedsaiKEVADSKNMQLEEADAFEKHKFNKNNEngE 1862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 400 VTQELNDLKKEKLRLERDLEEAHREgnrgartihdlrNEVEKLRKEVCEREKAvEKHYKSLPGESSSKFHSQEQVVKGLT 479
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEA------------DEIEKIDKDDIEREIP-NNNMAGKNNDIIDDKLDKDEYIKRDA 1929
|
410
....*....|....
gi 564351372 480 ESASQEDLLLQKSN 493
Cdd:PTZ00121 1930 EETREEIIKISKKD 1943
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-456 |
1.73e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 146 KEDARKKVQQVEELLTKRIHLLEE--DVKAAQAELEKAFAGTETEK-----------ALRLSLESKLSAMKKMQE-GDLE 211
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREEleTLEAEIEDLRETIAETEREReelaeevrdlrERLEELEEERDDLLAEAGlDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 212 MTLALEEKDRL---IEELKLSLKSKEALIQclkEEKSQMASPDENVSsgELRGLSATLREEKERDAEERQKERNHFEERi 288
Cdd:PRK02224 309 AEAVEARREELedrDEELRDRLEECRVAAQ---AHNEEAESLREDAD--DLEERAEELREEAAELESELEEAREAVEDR- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 289 qalQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQV-----------S 357
Cdd:PRK02224 383 ---REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 358 EFEES------ENCEAALAEKEALLAKLHSEnVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGART 431
Cdd:PRK02224 460 PVEGSphvetiEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
330 340
....*....|....*....|....*.
gi 564351372 432 IHDLRNEVEKLRKEVCE-REKAVEKH 456
Cdd:PRK02224 539 AEELRERAAELEAEAEEkREAAAEAE 564
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-455 |
2.06e-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: 53.20 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 107 KVEVESLKRELQERDQLLVKASKAVESLaeggGSEIQRVKEDARKKVQQVEELLTKRIHLleedvKAAQAELEK-AFAGT 185
Cdd:pfam15921 488 KMTLESSERTVSDLTASLQEKERAIEAT----NAEITKLRSRVDLKLQELQHLKNEGDHL-----RNVQTECEAlKLQMA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 186 ETEKA---LRLSLE--SKLSAMKKMQEGDLEMTLALEEK---DRLIE--ELKLSLKSKEALIQCLKEEKSQMASPDENVS 255
Cdd:pfam15921 559 EKDKVieiLRQQIEnmTQLVGQHGRTAGAMQVEKAQLEKeinDRRLElqEFKILKDKKDAKIRELEARVSDLELEKVKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 256 SGELRGLSATLREEKERD-----AEERQKERNHFEERIQALQEDLREKEREIATeKKNSLKrdkaiqgltMALKSKEKEV 330
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDqllneVKTSRNELNSLSEDYEVLKRNFRNKSEEMET-TTNKLK---------MQLKSAQSEL 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 331 EELNSIIKELTADSTQSREAPLKTQvsefeesENCEAALAEKEALLAKLHSenvtkntenhrLLRNVKKVTQELNDLKKE 410
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQ-------KQITAKRGQIDALQSKIQF-----------LEEAMTNANKEKHFLKEE 770
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 564351372 411 KLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEK 455
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-424 |
2.26e-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: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 58 RNMKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEH------IYKKNIELKVEVESLKRELQERDQLLVKASKAV 131
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 132 ESLAEGGGSEIQRVKEDARKKVQQVEEL--LTKRIHLLEEDVKAAQAELekafagteteKALRLSLESKLSAMKKMQEgd 209
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAEL----------TLLNEEAANLRERLESLER-- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 210 lemtlALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsATLREEKERDAEERQKERNHFEERIQ 289
Cdd:TIGR02168 832 -----RIAATERRLEDLEEQIEELSEDIESLAAEIEEL----------------EELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 290 ALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEEL----NSIIKELTADSTQSREAPLKTQVSEFEESENC 365
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351372 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 |
2.42e-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: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 58 RNMKDFENQITELKKENFNLKLRIYFLEERIQQefagptehiykknIELKV-EVESLKRELQERDQLLVKASKAVESLAE 136
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEE-------------LRLEVsELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 137 GGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEdvkaaQAELEKAFAGTETEKAlrlSLESKLSAMKKMQEgdlEMTLAL 216
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEE-----LAELEEKLEELKEELE---SLEAELEELEAELE---ELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 217 EEKDRLIEELklslksKEALIQCLKEEKSQMAspdenvssgELRglsaTLREEKERDAEERQKERNHFEERIQALQE-DL 295
Cdd:TIGR02168 375 EELEEQLETL------RSKVAQLELQIASLNN---------EIE----RLEARLERLEDRRERLQQEIEELLKKLEEaEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 296 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAD--STQSREAPLKTQVSEFE-ESENCEAALAEK 372
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQENLEgFSEGVKALLKNQ 515
|
...
gi 564351372 373 EAL 375
Cdd:TIGR02168 516 SGL 518
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
87-668 |
3.23e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 87 RIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKR--I 164
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 165 HLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMqegdLEMTLALEEKDRLieELKLSLKSKEALIQCLKEEK 244
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA----FEELRVQAENARL--EMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 245 SQMASPDENVSSgeLRGLSATLREEKERD----AEERQKERNHFEERIQALQEDLR---EKEREIATEK---KNSLKRDK 314
Cdd:pfam05483 232 KKEINDKEKQVS--LLLIQITEKENKMKDltflLEESRDKANQLEEKTKLQDENLKeliEKKDHLTKELediKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 315 AIQgltmalKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALAEKEALLaKLHSENVTKNTENHRLL 394
Cdd:pfam05483 310 STQ------KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL-RTEQQRLEKNEDQLKII 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 395 R-NVKKVTQELNDLKKEKLRLERDLEEAHREGNRgARTIHDLRNEVEKLRKEVcereKAVEKHYKSLPGESSSKFHSQEQ 473
Cdd:pfam05483 383 TmELQKKSSELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIAEEL----KGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 474 VVKGLTESASQ-----EDLLLQKSNEKdleaiqqncylMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQseyEGLT 548
Cdd:pfam05483 458 QLTAIKTSEEHylkevEDLKTELEKEK-----------LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---EDII 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 549 GDLKTEQNVYAHLaKNLQDTDSKLQAELKRVlalRKQLEQDvlayrnlqtaLQEQLSEIRKREEEPFSFYSDqtsylsiC 628
Cdd:pfam05483 524 NCKKQEERMLKQI-ENLEEKEMNLRDELESV---REEFIQK----------GDEVKCKLDKSEENARSIEYE-------V 582
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 564351372 629 LEEHSQFQLEHFSQEEIKKKVIDLIQLVKDLHADNQHLKK 668
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1365-1621 |
4.32e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1365 QDLLMEHIQEIRTL---RKHLEESIKTNEKLRKQLERQGCETDqgstnvsayssELHNSLTSEIQFLRKQNEALSTMLEk 1441
Cdd:COG1196 287 QAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELE- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1442 gskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLL 1521
Cdd:COG1196 355 ---EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1522 QKDELLQSLQMELkvyEKLAEEHQKLQQESRGEAcgggqkgqdpfSNLHGLLKEIQVLRDQAERSIQTNNTLKSKLEKQL 1601
Cdd:COG1196 432 ELEEEEEEEEEAL---EEAAEEEAELEEEEEALL-----------ELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
250 260
....*....|....*....|
gi 564351372 1602 SQGSKQAQEGALTLAVQALS 1621
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLA 517
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
64-613 |
4.37e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 64 ENQITELKKENFN-LKLRIYFLEERIQQ-------EFAGPTEHIYKKNIE---LKVEVESLKRELQERDQLLVKASKAVE 132
Cdd:pfam15921 244 EDQLEALKSESQNkIELLLQQHQDRIEQlisehevEITGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 133 SLAEGGGSEIQRVKEDARKKVQQVE-ELLTKRIHLLEEDVKAAQAELEKAFAGTETEKAL--------RLSLESKLSamK 203
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEkQLVLANSELTEARTERDQFSQESGNLDDQLQKLLadlhkrekELSLEKEQN--K 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 204 KMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEE-----KSQMAS-PDENVSSGELRGLSATLREEKERdaeer 277
Cdd:pfam15921 402 RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmERQMAAiQGKNESLEKVSSLTAQLESTKEM----- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 278 qkernhfeeriqalqedLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA--DSTQSREAPLKTQ 355
Cdd:pfam15921 477 -----------------LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 356 VSEFEESE-NCEA---ALAEKEALLAKLHS--ENVTKNTENH-----RLLRNVKKVTQELND--LKKEKLRLERDLEEAH 422
Cdd:pfam15921 540 GDHLRNVQtECEAlklQMAEKDKVIEILRQqiENMTQLVGQHgrtagAMQVEKAQLEKEINDrrLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 423 -RE------------------GNRGARTIHDLRNEVEKLRKEV--CERE-KAVEKHYKSLPGESSSKFHSQEQVVKGLTE 480
Cdd:pfam15921 620 iRElearvsdlelekvklvnaGSERLRAVKDIKQERDQLLNEVktSRNElNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 481 S--ASQEDLLLQKSNEKDLEAIQQNcylmtAEELKFGSDGLITEKCSQ-QSPDSKLIFSKEKQQSEYEGlTGDLKTEQNV 557
Cdd:pfam15921 700 QlkSAQSELEQTRNTLKSMEGSDGH-----AMKVAMGMQKQITAKRGQiDALQSKIQFLEEAMTNANKE-KHFLKEEKNK 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351372 558 YAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVlayRNLQTALQE---QLSE----IRKREEE 613
Cdd:pfam15921 774 LSQELSTVATEKNKMAGELEVLRSQERRLKEKV---ANMEVALDKaslQFAEcqdiIQRQEQE 833
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
61-455 |
5.63e-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: 51.51 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 61 KDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVE-SLKRELQERDQLLVKASKAVESLAEGGG 139
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvEGILKDTELTKLKESAKAKESGLRKGVS 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 140 SEIqrvKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQEGDLEMTLALEEK 219
Cdd:pfam02463 654 LEE---GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 220 DRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVssgelrgLSATLREEKERDAEERQKERNHFEERiqaLQEDLREKE 299
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE-------KSELSLKEKELAEEREKTEKLKVEEE---KEEKLKAQE 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 300 REIatEKKNSLKRDKAIQGLTMALKsKEKEVEELNSIIKELTADSTQSreaplKTQVSEFEESENCEAALAEKEALLAKL 379
Cdd:pfam02463 801 EEL--RALEEELKEEAELLEEEQLL-IEQEEKIKEEELEELALELKEE-----QKLEKLAEEELERLEEEITKEELLQEL 872
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351372 380 HSENVTKNTENHR--LLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEK 455
Cdd:pfam02463 873 LLKEEELEEQKLKdeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-670 |
8.64e-06 |
|
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: 50.79 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 56 RARNMKDFENQITELKKENFNLKLRIYFLEERIQQ-----EFAGPTEHIYKKNI-ELKVEVESLKRELQERDQLLVKASK 129
Cdd:TIGR04523 66 DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsdlSKINSEIKNDKEQKnKLEVELNKLEKQKKENKKNIDKFLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 130 AVESLAegggSEIQRVKEDARKKVQQVEELLTKRiHLLEEDVKAAQAELEKAfagteteKALRLSLESKLSAMKKMQEGD 209
Cdd:TIGR04523 146 EIKKKE----KELEKLNNKYNDLKKQKEELENEL-NLLEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKKKIQKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 210 LEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgelrglsatLREEKERDAEERQKERNHFEERIQ 289
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD---------EQNKIKKQLSEKQKELEQNNKKIK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 290 ALQEDLREKEREIatEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEfEESENCE- 366
Cdd:TIGR04523 285 ELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqiSQLKKELTN-SESENSEk 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 367 -AALAEKEALLAKLHSENVTKNTENHRL----------LRNVKKVTQELND----LKKEKLRLERDLEEAHREGNRGART 431
Cdd:TIGR04523 362 qRELEEKQNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEqikkLQQEKELLEKEIERLKETIIKNNSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 432 IHDLRNEV---EKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLlqKSNEKDLEaiQQNCYLMT 508
Cdd:TIGR04523 442 IKDLTNQDsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--NEEKKELE--EKVKDLTK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 509 -AEELKFGSDGLITEKCSQQSPDSKLifSKEKQQSEYEGLTGDLKTEQNVY-------AHLAKNLQDTDSKLQAELKRVL 580
Cdd:TIGR04523 518 kISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKnkeieelKQTQKSLKKKQEEKQELIDQKE 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 581 ALRKQLEQDVLAYRNLQTALQEQLSEIRKREEEPFSFYSDQTSYLSICLEEHSQFQLE-----------HFSQEEIKKKV 649
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETikeirnkwpeiIKKIKESKTKI 675
|
650 660
....*....|....*....|..
gi 564351372 650 IDLIQLVKD-LHADNQHLKKTI 670
Cdd:TIGR04523 676 DDIIELMKDwLKELSLHYKKYI 697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-491 |
1.00e-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: 50.15 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 273 DAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREApL 352
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 353 KTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQE-LNDLKKEKLRLERDLEEAHREGNRGART 431
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 432 IHDLRNEVEKLRKEVCEREKAVEKHYKSLPgessskfhSQEQVVKGLTESASQEDLLLQK 491
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELA--------ELAAELAELQQEAEELEALIAR 231
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1416-1551 |
1.99e-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: 48.86 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1416 ELHNSLTSEIQFLRKQNEALSTMLEKGSKEKQKENEKLRESLARKTES-------LEHLQLEYASVREENERLRRDISEK 1488
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdpteLDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351372 1489 ERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDellqslQMELKVYEKLAEEHQKLQQES 1551
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR------GFTFKEIEKLKEQLKLLQSLT 287
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-606 |
2.12e-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: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 221 RLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQED---LRE 297
Cdd:pfam02463 123 ELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqeLKL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 298 KEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALAEKEALLA 377
Cdd:pfam02463 203 KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 378 KLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHY 457
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 458 KSLpGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQqncylmtaeelkfgSDGLITEKCSQQSPDSKLIFSK 537
Cdd:pfam02463 363 KLQ-EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--------------EAQLLLELARQLEDLLKEEKKE 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351372 538 EKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLSE 606
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1373-1610 |
2.60e-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: 49.28 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1373 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHnSLTSEIQFLRKQNEALSTMLEKGSKEK---QKE 1449
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIaqlSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1450 NEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKS----RQQLLLQKDE 1525
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlrerLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1526 LLQSLQMELKVYEKLAEEHQKLQQESRgeacgggqKGQDPFSNLHGLLKEIQVLRDQAERSIQTNNTLKSKLEKQLSQGS 1605
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIE--------ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
....*
gi 564351372 1606 KQAQE 1610
Cdd:TIGR02168 908 SKRSE 912
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-460 |
2.68e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 266 LREEKERDAEERQKERNHFEERIQALQEDLREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA- 342
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAr 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 343 -DSTQSREAPLKTQVSEFEESENCEAALAEKEALLAKLhSENVTKNTENHRLLRNVKkvtQELNDLKKE-KLRLERDLEE 420
Cdd:COG3206 242 lAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAEL-AELSARYTPNHPDVIALR---AQIAALRAQlQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564351372 421 AHREGNRGARTIHDLRNEVEKLRKEVcEREKAVEKHYKSL 460
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRL 356
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1373-1606 |
4.49e-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: 48.51 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1373 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSeiqflRKQNEALSTMLEKGSKEKQKENEK 1452
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1453 LRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVC---SSLQELSRVQEEAKSRQQLLLQKDELLQS 1529
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErleARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351372 1530 LQMELKVYEKLAEEHQKLQQESRGEAcgggqkgqdPFSNLHGLLKEIQVLRDQAERSIQTNNTLKSKLEKQLSQGSK 1606
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEE---------ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-613 |
4.50e-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: 48.63 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 141 EIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAA---QAELEkAFAGTETEKAlRLS-----LESKLSAMKKMQEGDLEM 212
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQeqlQAETE-LCAEAEEMRA-RLAarkqeLEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 213 TLALE-EKDRL---IEELKLSLKSKEALIQCLKEEKsqmASPDENVSSGELRGLsaTLREEKERdaeeRQKERNHFEERI 288
Cdd:pfam01576 91 SQQLQnEKKKMqqhIQDLEEQLDEEEAARQKLQLEK---VTTEAKIKKLEEDIL--LLEDQNSK----LSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 289 QALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEFeesencE 366
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiAELQAQIAEL------R 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 367 AALAEKE----ALLAKLHSENVTKNtenhrllrNVKKVTQELNDLKKEklrLERDLEEAHREGNRGARTIHDLRNEVEKL 442
Cdd:pfam01576 236 AQLAKKEeelqAALARLEEETAQKN--------NALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 443 RKEV--------------CEREKAVEKHYKSLpgESSSKFHSQE---------QVVKGLTESASQedlllQKSNEKDLEA 499
Cdd:pfam01576 305 KTELedtldttaaqqelrSKREQEVTELKKAL--EEETRSHEAQlqemrqkhtQALEELTEQLEQ-----AKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 500 IQQNCYLMTAE---ELKFGSDGLIT-----EKCSQQSPDSKLIFSK------------EKQQSEYEGLTGDLKTEQNVYA 559
Cdd:pfam01576 378 AKQALESENAElqaELRTLQQAKQDsehkrKKLEGQLQELQARLSEserqraelaeklSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351372 560 HLAKN-------LQDTDSKLQAELKRVLA--------------LRKQLEQDVLAYRNLQ---TALQEQLSEIRKREEE 613
Cdd:pfam01576 458 KLSKDvsslesqLQDTQELLQEETRQKLNlstrlrqledernsLQEQLEEEEEAKRNVErqlSTLQAQLSDMKKKLEE 535
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-502 |
4.70e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 113 LKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELlTKRIHLLEEDVKAAQAELEKAfagtETEKALR 192
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEEL----REELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 193 LSLESKLSAMKKMQEGDLEMTL------ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATL 266
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 267 rEEKERDAEERQKERNHFEERIQALQEDLREKEREI-ATEKKNSLKRDK----------AIQGLTMALKSKEKEVEELNS 335
Cdd:COG4717 202 -EELQQRLAELEEELEEAQEELEELEEELEQLENELeAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 336 IIKELTAD--STQSREAPLKTQVSEFEESENCEAALAEKE--ALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK 411
Cdd:COG4717 281 LVLGLLALlfLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 412 LRLERDLEEAHRE---GNRGARTIHDLRNEVEKLRKEVcEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLL 488
Cdd:COG4717 361 EELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEE 439
|
410
....*....|....
gi 564351372 489 LQKSNEKDLEAIQQ 502
Cdd:COG4717 440 ELEELEEELEELRE 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1368-1550 |
5.54e-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: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1368 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERQgceTDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLEKGSKE-- 1445
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQEL-AALEAELAELEKEIAELRAELEAQKEEla 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1446 -------KQKENEKLR-----ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEA 1513
Cdd:COG4942 108 ellralyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 564351372 1514 KSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQE 1550
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
46-372 |
5.86e-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: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 46 IMSEEKVSPTRARNMK--DFENQITELKKENFNlklRIYFLEERIQQEFAGPTEHiykkniELKVEVESLKRELQERDQL 123
Cdd:NF033838 70 ILSEIQKSLDKRKHTQnvALNKKLSDIKTEYLY---ELNVLKEKSEAELTSKTKK------ELDAAFEQFKKDTLEPGKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 124 LVKASKAVEslaEGGGSEIQRVKEDARKKVQQVEEllTKRIHLLEEDVKAAQAELE------KAFAGTETEKALRLSLES 197
Cdd:NF033838 141 VAEATKKVE---EAEKKAKDQKEEDRRNYPTNTYK--TLELEIAESDVEVKKAELElvkeeaKEPRDEEKIKQAKAKVES 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 198 KLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKS--------QMASPD--EN------VSSGELRG 261
Cdd:NF033838 216 KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRrakrgvlgEPATPDkkENdakssdSSVGEETL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 262 LSATLREEKErdAEERQKERNHFEERIQALQEdlrEKEREIATEKKNSLKRDKAiqglTMALKSKEKEVEelnsIIKElt 341
Cdd:NF033838 296 PSPSLKPEKK--VAEAEKKVEEAKKKAKDQKE---EDRRNYPTNTYKTLELEIA----ESDVKVKEAELE----LVKE-- 360
|
330 340 350
....*....|....*....|....*....|.
gi 564351372 342 aDSTQSREAPLKTQVSEFEESENCEAALAEK 372
Cdd:NF033838 361 -EAKEPRNEEKIKQAKAKVESKKAEATRLEK 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-351 |
5.99e-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: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 105 ELKVEVESLKRELQERDQLLVKASKAVESLaegggseiqrvkEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAfag 184
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKAL------------LKQLAALERRIAALARRIRALEQELAALEAELAEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 185 TETEKALRLSLESK-------LSAMKKMQEGDLEMTLA----LEEKDRLIEELKLSLKSKEALIQCLKEEKSQMAspden 253
Cdd:COG4942 89 EKEIAELRAELEAQkeelaelLRALYRLGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAELA----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 254 vssgELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKEVEEL 333
Cdd:COG4942 164 ----ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--------------ELAELQQEAEEL 225
|
250
....*....|....*...
gi 564351372 334 NSIIKELTADSTQSREAP 351
Cdd:COG4942 226 EALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1367-1549 |
6.54e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1367 LLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAysselhnsLTSEIQFLRKQNEALSTMLEKGSKEK 1446
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1447 QKENEKLR-ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLT-QEVCSSLQELSRVQEEAKSRQQLLLQKD 1524
Cdd:COG4717 140 ELAELPERlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 564351372 1525 ELLQSLQMELKVYEKLAEEHQKLQQ 1549
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-612 |
7.89e-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: 47.76 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 285 EERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQVSEFE-- 360
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErlEELEEDLSSLEqe 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 361 ------ESENCEAALAEKEALLAKLHSEnvTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNR---GART 431
Cdd:TIGR02169 753 ienvksELKELEARIEELEEDLHKLEEA--LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 432 IHDLRNEVEKLRKEVCEREKAVEKhykslpgessskfhsqeqvvkgltesasQEDLLlqksnEKDLEAIQQNcylmtAEE 511
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEK----------------------------EIENL-----NGKKEELEEE-----LEE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 512 LKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEgltgDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQD-- 589
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIE----ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpe 948
|
330 340
....*....|....*....|....
gi 564351372 590 -VLAYRNLQTALQEQLSEIRKREE 612
Cdd:TIGR02169 949 eELSLEDVQAELQRVEEEIRALEP 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-428 |
9.09e-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: 47.07 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 215 ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMASPDENVSSgELRGLSATLRE-EKERDAEERQKERNhfEERIQALQE 293
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRAlEQELAALEAELAEL--EKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 294 DLREKEREIA---------------------TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPL 352
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564351372 353 KTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRG 428
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1426-1543 |
1.24e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1426 QFLRKQNEalstmLEKGSKEKQKENEKL-------RESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQE 1498
Cdd:PRK12704 65 EIHKLRNE-----FEKELRERRNELQKLekrllqkEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564351372 1499 vcsSLQELSRV----QEEAKsrqQLLLQ--KDELLQSLQMELKVYEKLAEE 1543
Cdd:PRK12704 140 ---QLQELERIsgltAEEAK---EILLEkvEEEARHEAAVLIKEIEEEAKE 184
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1365-1554 |
1.26e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1365 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHN------SLTSEIQFLRKQNEALSTM 1438
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaaNLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1439 LEKGSKEKQKENE----------KLRESLARKTESLEHLQLEYASVREENERLR-------RDISEKERQNQQLTQEVCS 1501
Cdd:TIGR02168 840 LEDLEEQIEELSEdieslaaeieELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRELEE 919
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564351372 1502 SLQELSRVQEE-AKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQESRGE 1554
Cdd:TIGR02168 920 LREKLAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-421 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 144 RVKEDARKKVQQVEELltKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLEsKLSAMKKMqegdlemtLALEEKDRLI 223
Cdd:COG4913 222 DTFEAADALVEHFDDL--ERAHEALEDAREQIELLEPIRELAERYAAARERLA-ELEYLRAA--------LRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 224 EELklslkskEALIQCLKEEKSQMAspdenvssGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIA 303
Cdd:COG4913 291 ELL-------EAELEELRAELARLE--------AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 304 TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAplktqvsefeesenCEAALAEKEALLaklhsen 383
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAAL------- 414
|
250 260 270
....*....|....*....|....*....|....*...
gi 564351372 384 vtkntenHRLLRNVKKVTQELNDLKKEKLRLERDLEEA 421
Cdd:COG4913 415 -------RDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
126-349 |
1.68e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 126 KASKAVESLAEgggSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEkAFAgtETEKALRLSLESKLSAMKkm 205
Cdd:COG3206 149 LAAAVANALAE---AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE-EFR--QKNGLVDLSEEAKLLLQQ-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 206 qegdlemtlaLEEKDRLIEELKLSLKSKEALIQCLKEE-KSQMASPDENVSSGELRGLSATLRE-EKERDAEERQKERNH 283
Cdd:COG3206 221 ----------LSELESQLAEARAELAEAEARLAALRAQlGSGPDALPELLQSPVIQQLRAQLAElEAELAELSARYTPNH 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351372 284 feERIQALQEDLREKEREIATEKKNSL-KRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE 349
Cdd:COG3206 291 --PDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
86-333 |
1.72e-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: 46.74 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 86 ERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGS----------EIQRVKEDARK---- 151
Cdd:pfam10174 460 EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKkdsklksleiAVEQKKEECSKlenq 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 152 --KVQQVEEL------LTKRIHLLEEDVK-------AAQAELEK---AFAGTETEKALRLSLESKLSAMKKMQEGDLEMT 213
Cdd:pfam10174 540 lkKAHNAEEAvrtnpeINDRIRLLEQEVArykeesgKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 214 LA------LEEKDRLIEELKLSLKSKEALIQC-----LKEEKSQMASPDENVSSGELRgLSATLREEKERDA---EERQK 279
Cdd:pfam10174 620 VAnikhgqQEMKKKGAQLLEEARRREDNLADNsqqlqLEELMGALEKTRQELDATKAR-LSSTQQSLAEKDGhltNLRAE 698
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 564351372 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 |
2.02e-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: 46.50 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 211 EMTLALEEKDRLIEELKLSLKSKEaliqclKEEKSQMaspdenvssgELRGLSATLREEKERDAEERQkeRNHFEERIQA 290
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLK------EQAKKAL----------EYYQLKEKLELEEEYLLYLDY--LKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 291 LQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALA 370
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 371 EKEALLAKLhsENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGnrgartiHDLRNEVEKLRKEVCERE 450
Cdd:pfam02463 322 EKKKAEKEL--KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE-------LLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 451 KAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLitEKCSQQSPD 530
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL--KDELELKKS 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351372 531 SKLIFSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAY 593
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
215-432 |
2.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 215 ALEEKDRLIEELKLSLKS--KEALIQcLKEEKSQmaspdenvssgelrglsatLREEKERDAEERQKERNHFEERIQALQ 292
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAikKEALLE-AKEEIHK-------------------LRNEFEKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 293 EDLREKEREIAtekknslKRDKAIQGLTMALKSKEKEVEELNSIIKELTADstqsreaplktQVSEFEESenceAALAEK 372
Cdd:PRK12704 96 ENLDRKLELLE-------KREEELEKKEKELEQKQQELEKKEEELEELIEE-----------QLQELERI----SGLTAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564351372 373 EAllaklhsenvtknteNHRLLRNVKKvtqelnDLKKEKLRLERDLE-EAHREGNRGARTI 432
Cdd:PRK12704 154 EA---------------KEILLEKVEE------EARHEAAVLIKEIEeEAKEEADKKAKEI 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1444-1616 |
2.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1444 KEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQ-EEAKSRQQLLLQ 1522
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1523 KDEL---LQSLQM---------------------ELKVYEKLAEEHQKLQQEsrgeacgggqkgqdpfsnLHGLLKEIQV 1578
Cdd:COG4942 103 KEELaelLRALYRlgrqpplalllspedfldavrRLQYLKYLAPARREQAEE------------------LRADLAELAA 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 564351372 1579 LRDQAERSIQTNNTLKSKLEKQLSQGSKQAQEGALTLA 1616
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-449 |
2.92e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEGG-----------------GSEIQRVKEDARKKVQQVEELlTKRIHLL 167
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleeraeelreeaaelESELEEAREAVEDRREEIEEL-EEEIEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 168 EEDVKAAQAELEKAF-----------AGTETEKALRLSLESKLSAMKKMQE--------------GDLEMTLALEEKDRL 222
Cdd:PRK02224 397 RERFGDAPVDLGNAEdfleelreerdELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 223 IEELKLSLKSKEALIQCLKEE----KSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREK 298
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 299 eREIATEK---------------------KNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSRE--APLKTQ 355
Cdd:PRK02224 557 -REAAAEAeeeaeeareevaelnsklaelKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRErlAEKRER 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 356 VSEFEES---ENCEAALAEKEAllAKLHSENVTKNTENHRLLRN--------VKKVTQELNDLKKEKLRLE---RDLEEA 421
Cdd:PRK02224 636 KRELEAEfdeARIEEAREDKER--AEEYLEQVEEKLDELREERDdlqaeigaVENELEELEELRERREALEnrvEALEAL 713
|
410 420
....*....|....*....|....*...
gi 564351372 422 HREGNRGARTIHDLRNEVEKLRKEVCER 449
Cdd:PRK02224 714 YDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1428-1588 |
3.04e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 45.75 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1428 LRKQNEALSTMLEKGS--KEKQKENEKLRESLARKTESLEhlqleyasvreenERLRRDISEKERQNQQLTQEVcsSLQE 1505
Cdd:pfam13779 491 LRAAQERLSEALERGAsdEEIAKLMQELREALDDYMQALA-------------EQAQQNPQDLQQPDDPNAQEM--TQQD 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1506 LS----RVQEEAKS-----RQQLLLQKDELLQSLQMelkvyeklaEEHQKLQQESRGEacggGQKGQDpfsNLHGLLKEI 1576
Cdd:pfam13779 556 LQrmldRIEELARSgrraeAQQMLSQLQQMLENLQA---------GQPQQQQQQGQSE----MQQAMD---ELGDLLREQ 619
|
170
....*....|..
gi 564351372 1577 QVLRDQAERSIQ 1588
Cdd:pfam13779 620 QQLLDETFRQLQ 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-381 |
3.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 54 PTRARNMKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVES 133
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 134 L-AEGGGSEIQRVKEDARKKVQQVEELL------------TKRIHLLEEDVKAAQAEL-------------EKAFAGTET 187
Cdd:COG4717 225 LeEELEQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 188 EKALRLSLESKLSAMKKMQ-------EGDLEMTLALEEKDRlIEELKLSLKS-----KEALIQCLKEEKSQMASPDENVS 255
Cdd:COG4717 305 EELQALPALEELEEEELEEllaalglPPDLSPEELLELLDR-IEELQELLREaeeleEELQLEELEQEIAALLAEAGVED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 256 SGELRglsatlreEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKrdKAIQGLTMALKSKEKEVEELns 335
Cdd:COG4717 384 EEELR--------AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEEL-- 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564351372 336 iikeltadstQSREAPLKTQVSEFEESENCEAALAEKEALLAKLHS 381
Cdd:COG4717 452 ----------REELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1384-1610 |
4.35e-04 |
|
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: 45.40 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1384 ESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHN---SLTSEIQFLRKQNEALSTMLEKGSKEKQKENEKLrESLARK 1460
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI-DKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1461 TESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQ-KDEL------LQSLQME 1533
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlKDEQnkikkqLSEKQKE 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351372 1534 LKVYEKLAEEHQKLQQESRGEACG-GGQKGQDPFSNLHGLLKEIQVLRDQAERSIQTNNTLKSKLEKQLSQGSKQAQE 1610
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
86-333 |
4.43e-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: 45.11 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 86 ERIQQEFAGP------TEHIYKKNIELKVEVESLKRELQERDQllvkasKAVESLAEGGGSEIQRVKEDARKKVQQVEel 159
Cdd:pfam17380 392 ERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQEEARQ------REVRRLEEERAREMERVRLEEQERQQQVE-- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 160 ltkRIHLLEEDVKAAQAELEKafagtETEKALRLSLESKLSAMKKMQegdlemtlalEEKDRLIEElklslKSKEALIQC 239
Cdd:pfam17380 464 ---RLRQQEEERKRKKLELEK-----EKRDRKRAEEQRRKILEKELE----------ERKQAMIEE-----ERKRKLLEK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 240 LKEEKSqmaspdenvssgelrglSATLREEKERDAEERQKERNHFEERIQaLQEDLRekereIATEKKNSLKRDKAIQGL 319
Cdd:pfam17380 521 EMEERQ-----------------KAIYEEERRREAEEERRKQQEMEERRR-IQEQMR-----KATEERSRLEAMEREREM 577
|
250
....*....|....
gi 564351372 320 TMALKSKEKEVEEL 333
Cdd:pfam17380 578 MRQIVESEKARAEY 591
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
64-494 |
5.10e-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: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 64 ENQITELKKENFNLKLRIYFLEERIQQEfaGPTEHIYKKNIELKVEVESLKRELQERDQLLVK-----ASKAVESLAEGG 138
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNPGP 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 139 GSEIQRVKEDARKKVQQVEE-------LLTKRIHLLEEDVKAAQAELEKAfagTETEKALRLSLESKLSAMKKMQEgdlE 211
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEdvyhqltSERKQRASLKEQMQEIQQSFSIL---TQCDNRSKEDIPNLQNITVRLQD---L 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 212 MTLALEEKDRLIEELKLSLKSKEALI-------------QCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQ 278
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQdlqdvrlhlqqcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 279 KERNHFEERIQALQEDLR------EKEREIATEKKNSLKRDKAIQGLTMALKSK-EKEVEELNSIIKELtadstqSREAP 351
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEmlaqcqTLLRELETHIEEYDREFNEIENASSSLGSDlAAREDALNQSLKEL------MHQAR 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 352 LKTQVSEFEESENCEAALAEKEALlaklhsenvtkntenhrllrnvkkvtQELNDLKKEKLRLERDLEEAHREGNRGART 431
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTG--------------------------AELSHLAAEIQFFNRLREEDTHLLKTLEAE 807
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564351372 432 IHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSSKFHSQEQVVKGLTESASQEDLLLQKSNE 494
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1373-1520 |
6.34e-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: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1373 QEIRTLRKHLEESIKTNEKLRKQLERQgcETDQGSTNVSAYSSELHNSLT------------SEIQFLRKQNEALSTMLE 1440
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQ--KEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1441 KgSKEKQKENEKLRESLARKTESLEHLQleyASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLL 1520
Cdd:COG4942 154 E-LRADLAELAALRAELEAERAELEALL---AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1404-1633 |
6.63e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1404 DQGSTNVSAYSSELHNsLTSEIQFLRKQNEALS---TMLEKGSKEKQKENEKLRESLARKTESLEHLQLEYASVREENER 1480
Cdd:TIGR02168 666 AKTNSSILERRREIEE-LEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1481 LRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQESRGEACGGGQ 1560
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1561 KGQDPFSNLHGLLKEIQVLRDQAER----------SIQTNNTLKSKLEKQLSQGSKQAQEGALTLAVQALSVTEWSLQLD 1630
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
...
gi 564351372 1631 KHD 1633
Cdd:TIGR02168 905 ELE 907
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-658 |
6.79e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 144 RVKEDaRKKVQQVEELLTKRIHLLEEDVKAAQAELekafagteTEKalrlslESKLSAMKKMQEGDLEMTLALEEKDRLI 223
Cdd:pfam05483 216 KLKED-HEKIQHLEEEYKKEINDKEKQVSLLLIQI--------TEK------ENKMKDLTFLLEESRDKANQLEEKTKLQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 224 EE-LKLSLKSKEALIQCLKEEKSQMASPDENVSSGELRGLSAT-----LREEKERDAEERQKER-------NHFEERIQA 290
Cdd:pfam05483 281 DEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticqLTEEKEAQMEELNKAKaahsfvvTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 291 LQEDLR-EKEREIATEKKNSL------KRDKAIQGLTMALKSKEKEVEELNSIIK------------ELTADSTQSREAP 351
Cdd:pfam05483 361 LEELLRtEQQRLEKNEDQLKIitmelqKKSSELEEMTKFKNNKEVELEELKKILAedeklldekkqfEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 352 --------------LKTQVSEFEESEncEAALAEKEALLAKLHSENVtKNTE----NHRLLRNVKKVTQELNDLKKEKLR 413
Cdd:pfam05483 441 lifllqarekeihdLEIQLTAIKTSE--EHYLKEVEDLKTELEKEKL-KNIEltahCDKLLLENKELTQEASDMTLELKK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 414 LERDLEEAHREGNRGARTIH-------DLRNEVEKLRKEVCEREKAVE-KHYKSLPGESSSKFHSQEQVVKGLTESASQE 485
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIEnleekemNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 486 DLLLQKSNE-KDLEAIQQNCYLM----TAE-------ELKFGSDGLITEKCSQQSPDSKLIFSKE---KQQSEyEGLTGD 550
Cdd:pfam05483 598 NLKKQIENKnKNIEELHQENKALkkkgSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEiedKKISE-EKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 551 LKTEQNVYAHLAKNLQDTDSKLQAELKRVLALrkqLEQDVLAYRNLQTALQEQLSEIRKREEEPFSFYSDQTSYLSICLE 630
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVAL---MEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKA 753
|
570 580 590
....*....|....*....|....*....|..
gi 564351372 631 E----HSQFQLEHFSQEEIKKKVIDLIQLVKD 658
Cdd:pfam05483 754 EllslKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1365-1531 |
7.11e-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: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1365 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAysSELHNSLTSEIQFLRKQNEALSTMLEKGS- 1443
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHp 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1444 --KEKQKENEKLRESLARKTES-LEHLQLEYASVREENERLRRDISEKERQNQQLTQevcsSLQELSRVQEEAKSRQQLL 1520
Cdd:COG3206 292 dvIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELY 367
|
170
....*....|.
gi 564351372 1521 lqkDELLQSLQ 1531
Cdd:COG3206 368 ---ESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-452 |
7.84e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 64 ENQITELKKENFNLKLRIYFLEERIQqefagptehiykkNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGgSEIQ 143
Cdd:COG4717 101 EEELEELEAELEELREELEKLEKLLQ-------------LLPLYQELEALEAELAELPERLEELEERLEELRELE-EELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 144 RVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKmQEGDLEMTLALEEKDRLI 223
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 224 EELKLSLKSKEALIQCLKEEKSQMASPDEN------VSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQ----- 292
Cdd:COG4717 246 KEARLLLLIAAALLALLGLGGSLLSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleell 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 293 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKE--VEELNSIIKELTADSTQSREAPLKTQVSEFEESENCEAALA 370
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 371 EKEALLAKLHSENVTK---------NTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGnrgarTIHDLRNEVEK 441
Cdd:COG4717 406 ELEEQLEELLGELEELlealdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEE 480
|
410
....*....|.
gi 564351372 442 LRKEVCEREKA 452
Cdd:COG4717 481 LKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1365-1552 |
8.24e-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: 44.67 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1365 QDLLMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgcetdqgSTNVSAYSSELHNSLTSEIQFLRKQNEALSTMLEKGSK 1444
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ--------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1445 EKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKD 1524
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
170 180 190
....*....|....*....|....*....|.
gi 564351372 1525 ELLQSLQ---MELKVYEKLAEEHQKLQQESR 1552
Cdd:TIGR02169 938 DPKGEDEeipEEELSLEDVQAELQRVEEEIR 968
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-453 |
9.20e-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: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 263 SATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTA 342
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 343 DStQSREAPLKTQV------------------SEFEES--------------ENCEAALAEKEALLAKLHSENVTKNTEN 390
Cdd:COG4942 98 EL-EAQKEELAELLralyrlgrqpplalllspEDFLDAvrrlqylkylaparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351372 391 HRLLRNVKKVTQELNDLKKEKL----RLERDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAV 453
Cdd:COG4942 177 EALLAELEEERAALEALKAERQkllaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1358-1545 |
1.15e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1358 TIASRFPQDLLMEHIQEirTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELHNSLTSEIQFLRKQNEalst 1437
Cdd:pfam17380 283 AVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1438 mlekgskEKQKENEKLR-ESLA---RKTESLEHLQLEYasvREENERLRRD--------ISEKERQNQQLTQEVcsSLQE 1505
Cdd:pfam17380 357 -------ERKRELERIRqEEIAmeiSRMRELERLQMER---QQKNERVRQEleaarkvkILEEERQRKIQQQKV--EMEQ 424
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564351372 1506 LSRVQEEAKSRQqllLQKDELLQSLQMELKVYEKLAEEHQ 1545
Cdd:pfam17380 425 IRAEQEEARQRE---VRRLEEERAREMERVRLEEQERQQQ 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-445 |
1.40e-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: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 56 RARNMKDFENQITELKKENFNLKLRIYFLEERIQQEFagptehiyKKNIELKVEVESLKRELQERDQLLVKASKAVESLA 135
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALL--------ERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 136 EGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAfAGTETEKALRLSLESKLSAMKKMQEGDLEMTLA 215
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 216 LEEKD----------------------------RLIEELKLSLKSKEALIQCLKEEKSqmASPDENVSSGELRGLSATLR 267
Cdd:COG1196 528 VLIGVeaayeaaleaalaaalqnivveddevaaAAIEYLKAAKAGRATFLPLDKIRAR--AALAAALARGAIGAAVDLVA 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 268 EEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQS 347
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 348 REaplktqvsEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNR 427
Cdd:COG1196 686 ER--------LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
410
....*....|....*...
gi 564351372 428 GARTIHDLRNEVEKLRKE 445
Cdd:COG1196 758 EPPDLEELERELERLERE 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-410 |
1.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 55 TRARNMKDFENQITELKKENFNLKLRIYFLEERIqQEFAGPTEHIYKKNIELKVEVESLKRELQERDQllvkaskavesl 134
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK------------ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 135 aegggsEIQRVKEDARKKVQQVEElLTKRIHLLEEDVKaaqaELEKafagtetekaLRLSLESKLSAMKKmqegdlemtl 214
Cdd:TIGR04523 427 ------EIERLKETIIKNNSEIKD-LTNQDSVKELIIK----NLDN----------TRESLETQLKVLSR---------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 215 ALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdenvssgelrglsatlrEEKERDAEERQKErnhFEERIQALQED 294
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKEL--------------------EEKVKDLTKKISS---LKEKIEKLESE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 295 LREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQsreapLKTQVSEFE-ESENCEAALAE 371
Cdd:TIGR04523 533 KKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE-----KQELIDQKEkEKKDLIKEIEE 607
|
330 340 350
....*....|....*....|....*....|....*....
gi 564351372 372 KEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKE 410
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
78-344 |
1.48e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 78 KLRIYFLEERIQQEFagptEHIYKKNIelkVEVESLKRELQ-ERDQ----LLVKASKAVESL-----AEGGGSEIQRVKE 147
Cdd:PRK05771 8 KVLIVTLKSYKDEVL----EALHELGV---VHIEDLKEELSnERLRklrsLLTKLSEALDKLrsylpKLNPLREEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 148 DARKK--VQQVEELLTKrihlLEEDVKAAQAELEKAfagtETEKAlrlSLESKLSAMKKMQEGDLEMTLALEEKDRLIEE 225
Cdd:PRK05771 81 VKSLEelIKDVEEELEK----IEKEIKELEEEISEL----ENEIK---ELEQEIERLEPWGNFDLDLSLLLGFKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 226 LKLSLKSKEALIQ--------CLKEEKSQM------ASPDENVSSGELR------------GLSATLREEKERDAEERQK 279
Cdd:PRK05771 150 GTVPEDKLEELKLesdvenveYISTDKGYVyvvvvvLKELSDEVEEELKklgferleleeeGTPSELIREIKEELEEIEK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564351372 280 ERNHFEERIQALQEdlREKEREIATEKKNSLKRDKAiQGLTMALKSK----------EKEVEELNSIIKELTADS 344
Cdd:PRK05771 230 ERESLLEELKELAK--KYLEELLALYEYLEIELERA-EALSKFLKTDktfaiegwvpEDRVKKLKELIDKATGGS 301
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-444 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 264 ATLREEKER-DAEERQKERNHFEERIQALQEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKEVEELnsiiKELTA 342
Cdd:COG4913 272 AELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEA--------------RLDALREELDEL----EAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 343 DSTQSREAPLKTQVSEFEES-ENCEAALAEKEALLAKLHsenVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEA 421
Cdd:COG4913 334 GNGGDRLEQLEREIERLERElEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
170 180
....*....|....*....|...
gi 564351372 422 HREGNRGARTIHDLRNEVEKLRK 444
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLER 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-613 |
1.62e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 277 RQKERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNS-------IIKELTADSTQ--S 347
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDklkknkdKINKLNSDLSKinS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 348 REAPLKTQVSEFE-ESENCEAALAEKEALLAKLhsenvtkNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGN 426
Cdd:TIGR04523 111 EIKNDKEQKNKLEvELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 427 RGARTIHDLRNEVEKLRKEVCEREKAVEKHyKSLpgesSSKFHSQEQVVKGLTESASQEDLLLQKSNEKDLEAIQQncyL 506
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL----ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---L 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 507 MTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKT--EQNVYAHLAKNLQDTDSKLQ----------- 573
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkEQDWNKELKSELKNQEKKLEeiqnqisqnnk 335
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 564351372 574 --AELKRVLA-LRKQLEQDVLAYRNLQTALQEQLSEIRKREEE 613
Cdd:TIGR04523 336 iiSQLNEQISqLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-343 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 64 ENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNiELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQ 143
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 144 RVKEDARKKVQQVEEL--LTKRIHLLEEDVKAAQAELE-----------------KAFAGTETE-KALRLSLESKLSAMK 203
Cdd:TIGR02168 825 RLESLERRIAATERRLedLEEQIEELSEDIESLAAEIEeleelieeleseleallNERASLEEAlALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 204 KMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEeksqmaspdenvssgelrglsaTLREEKERDAEERQKERNH 283
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE----------------------RLSEEYSLTLEEAEALENK 962
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564351372 284 FEERIQALQEDLREKEREIA----------TEKKNSLKR----DKAIQGLTMALKSKEKEVEELNSIIKELTAD 343
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERydflTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1368-1550 |
2.02e-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: 43.12 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1368 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLekgsKEKQ 1447
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREAL----DELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1448 KENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELL 1527
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180
....*....|....*....|...
gi 564351372 1528 QSLQMElkvYEKLAEEHQKLQQE 1550
Cdd:TIGR02168 890 ALLRSE---LEELSEELRELESK 909
|
|
| DUF445 |
pfam04286 |
Protein of unknown function (DUF445); Predicted to be a membrane protein. |
144-379 |
2.02e-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: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 144 RVKEDARKKVQQVEELLTKRIHLLEEDvkAAQAELEKAFAGTETEKALRLSLESKLSAMkkMQEGDLEMTLaleekDRLI 223
Cdd:pfam04286 77 ADPTNAERLAREVAKLLAEILEDLDDE--RVQRLLKKALRRRLEEIDLAPLLGKLLELL--LAEGRHQALL-----DDLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 224 EELKLSLKSKEA------LIQCLKEEKSQMASPDENVSSGELRGLSATLRE-EKERDAEERQKERNHFEERIQALQEDlr 296
Cdd:pfam04286 148 DRLRDWLRSEEGkqriaeMIDEFLEEWGPLVALLGGIAEMILRALSSLLDEvQADPDHPLRLAFDRAVRELITDLLND-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 297 EKEREIATEKKNSLKRDKAIQGLTMALkskekeVEELNSIIKELTADSTQSREAPLKTQVSEFEEsenceaALAEKEALL 376
Cdd:pfam04286 226 PELRAEVEELKQKLLADPAVQDYVKAL------WESLRSLLLDDLSDPDSALRRRISELLAEFGE------RLAEDPELR 293
|
...
gi 564351372 377 AKL 379
Cdd:pfam04286 294 DKL 296
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1368-1553 |
2.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1368 LMEHIQEIRTLRKHLEESIKTNEKLRKQLERqgcetdqgstnVSAYSSELhNSLTSEIQFLRKQNEALSTML---EKGSK 1444
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKE-----------LEELKEEI-EELEKELESLEGSKRKLEEKIrelEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1445 EKQKENEKLRESLARkTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcSSLQELSRVQEEAKSRQQLLLQKD 1524
Cdd:PRK03918 270 ELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI-NGIEERIKELEEKEERLEELKKKL 347
|
170 180
....*....|....*....|....*....
gi 564351372 1525 ELLQSLQMELKVYEKLAEEHQKLQQESRG 1553
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEELER 376
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
218-340 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 218 EKDRLIEELKLSL---KSKEALIQCLKEEksqmASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQED 294
Cdd:COG2433 360 PPDVDRDEVKARVirgLSIEEALEELIEK----ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564351372 295 LREKEREIA----------TEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKEL 340
Cdd:COG2433 436 LEEKDERIErlerelsearSEERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1433-1554 |
2.56e-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: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1433 EALSTMLEKGSKEKQKENEKLRES----LARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcsslqelsr 1508
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEREL--------- 450
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564351372 1509 vqEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQESRGE 1554
Cdd:COG2433 451 --SEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRK 494
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
58-662 |
2.69e-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: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 58 RNMKDFENQITELKKENFNLKLRIYFLE-ERIQQEFAGPTEHIYKKNIELKVEVESLKRELQERDQLLVKASKAVES--- 133
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPlAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrl 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 134 ----LAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAMKKMQeGD 209
Cdd:TIGR00618 347 lqtlHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ-GQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 210 LEMTLALEEKDRLIEELKLSLKSKEAliQCLKEEKSqmaspdenvssgELRGLSATLREEKERDA---------EERQKE 280
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKI------------HLQESAQSLKEREQQLQtkeqihlqeTRKKAV 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 281 RNHFEERIQALQEDLREKEREIATEKKNSL-------KRDKAIQGLTMALKSKEKEVEELNSIIKELTADSTQSREAPLK 353
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARQDIDnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 354 TQV------SEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLR------NVKKVTQELNDLKKEKLRLERDLEEA 421
Cdd:TIGR00618 572 FSIltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqpeqDLQDVRLHLQQCSQELALKLTALHAL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 422 HREGNRGARTIHDLRNEVEKLRK--EVCEREKAVEKHYKSLPG------ESSSKFHSQEQVVKGL--------------- 478
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELlaSRQLALQKMQSEKEQLTYwkemlaQCQTLLRELETHIEEYdrefneienassslg 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 479 TESASQEDLLLQKSNEKDLEAIQQNCYLMTAEELKFGSDGLITEKCSQQSPDSKLIFSKEKQQSEYEGLTGDLKTEQNVY 558
Cdd:TIGR00618 732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 559 A------------HLAKNLQDTDSKLQAELKRVLALRKQLEQDVLAYRNLQTALQEQLS--------------EIRKREE 612
Cdd:TIGR00618 812 IpsdedilnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiqlsdklnginqiKIQFDGD 891
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 564351372 613 EPFSFYSDQTSYLSICL--EEHSQFQLEHFSQEEIKKKVIDLIQLVKDLHAD 662
Cdd:TIGR00618 892 ALIKFLHEITLYANVRLanQSEGRFHGRYADSHVNARKYQGLALLVADAYTG 943
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1428-1613 |
2.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1428 LRKQNEALSTMLEKGSKEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEV--CSSLQE 1505
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1506 LSRVQEEAKSRQQLLLQKDELLQSLQMELKVY-------EKLAEEHQKLQQESRGEACGGGQKGQDPFSNLHGLLKEIQV 1578
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELreleeelEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*
gi 564351372 1579 LRDQAERSIQTNNTLKSKLEKQLSQGSKQAQEGAL 1613
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1305-1628 |
2.91e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1305 RRLRTEEDNLPYQHLLPESpEPSASHALSDDEMSEKSFLSrepKPDSETEKYPTIASRFPQDLlmehIQEIRTLRKHLEE 1384
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTG---KHQDVTAKYNRRRSKIKEQN----NRDIAGIKDKLAK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1385 SIKTNEKLR-------KQLERQ-GCETDQGSTNVSAYSSELHNSLtSEIQFLrkQNEALSTMLEKGSKE-KQKENEKLRE 1455
Cdd:pfam12128 402 IREARDRQLavaeddlQALESElREQLEAGKLEFNEEEYRLKSRL-GELKLR--LNQATATPELLLQLEnFDERIERARE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1456 SLARKTESLEHLQLEYASVReeneRLRRDISEKERQNQQLTQEVCSSLQELsrvqeeaksRQQLLLQKDELLQSLQMELK 1535
Cdd:pfam12128 479 EQEAANAEVERLQSELRQAR----KRRDQASEALRQASRRLEERQSALDEL---------ELQLFPQAGTLLHFLRKEAP 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1536 VYE----KLAEEHQKLQQESRGEACGGGQKGQDPFSNLHGLLKEIQV------------LRDQAERSIQTNNTLKSKLEK 1599
Cdd:pfam12128 546 DWEqsigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVpewaaseeelreRLDKAEEALQSAREKQAAAEE 625
|
330 340 350
....*....|....*....|....*....|.
gi 564351372 1600 QLSQGSKQ--AQEGALTLAVQALSVTEWSLQ 1628
Cdd:pfam12128 626 QLVQANGEleKASREETFARTALKNARLDLR 656
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
105-351 |
3.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 105 ELKVEVESLKRELQERDQLLVKASKAVESLAEgggsEIQRVKEDARKKVQQVEELlTKRIHLLEEDVKAAQAELEKAFAG 184
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKL-QAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 185 TETEKALRLSLE------------SKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEKsqmaspde 252
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 253 nvssgelrglsatlrEEKERDAEERQKERnhfeeriQALQEDLREKEREiATEKKNSLKRDKAIQGLTMALKSKEKEVEE 332
Cdd:COG3883 167 ---------------EAAKAELEAQQAEQ-------EALLAQLSAEEAA-AEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*....
gi 564351372 333 LNSIIKELTADSTQSREAP 351
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAA 242
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
60-355 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 60 MKDFENQITELKKENFNLKLRIYFLEERIQQEFAGPTEHIYKKNIELKVEVESLKRELQER-DQLLVKASKAVESLAEG- 137
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTENl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 138 -----------GGSEIQRVKEDARKKVQQVE----ELLTKRIHLLEEDVKAAQAELEKAFAGTETEKALRLSLESKLSAM 202
Cdd:COG5185 357 eaikeeienivGEVELSKSSEELDSFKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 203 KKMQEGDLEMTLALEEKDRLIEELKLSlKSKEALIQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERN 282
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQS-RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564351372 283 HFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELT-----ADSTQSREAPLKTQ 355
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTqylstIESQQAREDPIPDQ 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-427 |
3.80e-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: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 258 ELRGLSATLREEKERdAEERQKERNHFEERIQALQE---------DLREKEREIA--TEKKNSLKR-DKAIQGLTMALKS 325
Cdd:COG4913 618 ELAELEEELAEAEER-LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAelEAELERLDAsSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 326 KEKEVEELNSIIKELTADSTQsreapLKTQVSEFEES-ENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQEL 404
Cdd:COG4913 697 LEAELEELEEELDELKGEIGR-----LEKELEQAEEElDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
170 180
....*....|....*....|....*..
gi 564351372 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 |
3.84e-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: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 105 ELKVEVESLKRELQERDQLLVKASK--AVESLAEGGGSEIQRVKEDARKKVQQVEELLTKRIHLLE---EDVKaaQAELE 179
Cdd:pfam10174 203 QKEKENIHLREELHRRNQLQPDPAKtkALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEdreEEIK--QMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 180 KA---FAGTETEKaLRLSLESKLSAMKKMQEGDLEMTLALEEKDRLIEELKLSLKSKEALIQCLKEEksqmaspdenVSS 256
Cdd:pfam10174 281 KShskFMKNKIDQ-LKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTE----------VDA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 257 GELR-GLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIatekkNSLKrdKAIQGLTMALKSKEKEVEELNS 335
Cdd:pfam10174 350 LRLRlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKI-----NVLQ--KKIENLQEQLRDKDKQLAGLKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 336 IIKELTADSTQSREApLKTqvsefeesenCEAALAEKEALLAKLHSEnvtKNTENHRLLRNVKKVTQELNDLKKEKLRLE 415
Cdd:pfam10174 423 RVKSLQTDSSNTDTA-LTT----------LEEALSEKERIIERLKEQ---REREDRERLEELESLKKENKDLKEKVSALQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 416 RDLEEAHREGNRGARTIHDLRNEVEKLRKEVCEREKAVEKHYKSLPGESSS--KFHSQEQVVKGLTESASQEDLLLQKSN 493
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQlkKAHNAEEAVRTNPEINDRIRLLEQEVA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 494 EKDLEAIQQNCYLmtaEELKfgsdGLITEKCSQQSpdsklifSKEKQQSEYEGLTGDLKTEQNVYAHLAKNLQDTDSKLQ 573
Cdd:pfam10174 569 RYKEESGKAQAEV---ERLL----GILREVENEKN-------DKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKG 634
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564351372 574 AELkRVLALRkqlEQDVLAYRNLQTALQEQLSEIRKREEE 613
Cdd:pfam10174 635 AQL-LEEARR---REDNLADNSQQLQLEELMGALEKTRQE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1373-1573 |
4.33e-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: 41.67 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1373 QEIRTLRKHLEESIKTNEKLRKQLERQGCETDQGSTNVSAYSSELhNSLTSEIQFLRKQNEALSTMLEKGSKE------- 1445
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELRAELEAQKEElaellra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1446 --KQKENEKLR-----ESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVcSSLQELSRVQEEAK---- 1514
Cdd:COG4942 113 lyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER-AELEALLAELEEERaale 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564351372 1515 ----SRQQLLLQKDELLQSLQMELKVYEKLAEEHQKL-QQESRGEACGGGQKGQDPFSNLHGLL 1573
Cdd:COG4942 192 alkaERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
275-509 |
4.56e-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: 41.80 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 275 EERQKERNHFEERIQALQEDlREKEREIATEKKNSLKRDKA-----IQGLTMALKSKEKEVEELNSIIKELTAdstqSRE 349
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQ-REKEKERYKRDREQWERQRRelesrVAELKEELRQSREKHEELEEKYKELSA----SSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 350 APLKTQVSEFEESENCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEKLRLERDLEEAHREGNRGA 429
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 430 RTIHDLRN-------EVEKLRKEVCE-REKAVEKHYKSLPGESSSK--------FHSQEQVVKGLTES----ASQEDLLL 489
Cdd:pfam07888 192 KEFQELRNslaqrdtQVLQLQDTITTlTQKLTTAHRKEAENEALLEelrslqerLNASERKVEGLGEElssmAAQRDRTQ 271
|
250 260
....*....|....*....|
gi 564351372 490 QKSNEKDLEAIQQNCYLMTA 509
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADA 291
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
230-374 |
4.76e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 230 LKSKEAliQCLKEEKSQMASPDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKEREIATEKKNS 309
Cdd:PRK12705 30 RLAKEA--ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564351372 310 LKRDKAIQGLTMALKSKEKEVEELNSIIKELTADstQSREAPLKTQVSEFEESENCEAALAEKEA 374
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAELEEEKAQRVKKIEEEA 170
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
258-358 |
5.31e-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: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 258 ELRGLSATLRE-EKERDAEERQKERNHFEeRIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSI 336
Cdd:COG0542 412 ELDELERRLEQlEIEKEALKKEQDEASFE-RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....
gi 564351372 337 IKELTADSTQSREAP--LKTQVSE 358
Cdd:COG0542 491 EKELAELEEELAELAplLREEVTE 514
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1372-1615 |
5.42e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1372 IQEIRTLRKHLEESIKTNEKLRKQLERQGC-ETDQGSTNVSAYSSELHNSLTSEIQFLRKQNEALSTMLEKgsKEKQKEN 1450
Cdd:COG5185 288 IKQFENTKEKIAEYTKSIDIKKATESLEEQlAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEA--IKEEIEN 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1451 EKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQN-QQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQS 1529
Cdd:COG5185 366 IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEIlATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1530 LQMEL-KVYEKLAEEHQKLQQESRGEACGGGQkgqdpfSNLHGLLKEIQVLRDQAERSIQTNNTLKSKLEKQLSQGSKQA 1608
Cdd:COG5185 446 LISELnKVMREADEESQSRLEEAYDEINRSVR------SKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
....*..
gi 564351372 1609 QEGALTL 1615
Cdd:COG5185 520 DQVAESL 526
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-342 |
5.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 56 RARNMKDFENQITELKKenfnlKLRIYFLE--ERIQQEFagptEHIYKKNIELKVEVESLKRELqERDQLLVKASKAVES 133
Cdd:PRK03918 494 ELIKLKELAEQLKELEE-----KLKKYNLEelEKKAEEY----EKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 134 laegggsEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKaaqaELEKAFAGTETEKALRLSLESKLSAMKKMQEgDLEMT 213
Cdd:PRK03918 564 -------KLDELEEELAELLKELEELGFESVEELEERLK----ELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 214 LA-LEEKDRLIEELKLSLkskealiqclkEEKSQMASPDENvssgelrglsatlrEEKERDAEERQKERNHFEERIQALQ 292
Cdd:PRK03918 632 FEeLAETEKRLEELRKEL-----------EELEKKYSEEEY--------------EELREEYLELSRELAGLRAELEELE 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 564351372 293 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKeVEELNSIIKELTA 342
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKA 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
140-392 |
6.01e-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: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 140 SEIQRVKEDARKKVQQVEELLTKRIHLLEEDVKAAQAELEKafagtetekalrlsLESKLSAMKKmQEGDLEMTLALEEK 219
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------------LERRIAALAR-RIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 220 DrlIEELKLSLKSKEALIQCLKEEKSQMAspDENVSSGELRGLSATLREEKERDAEERQKERNHFEERIQALQEDLREKE 299
Cdd:COG4942 84 E--LAELEKEIAELRAELEAQKEELAELL--RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 300 REIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSIIKELTAdSTQSREAPLKTQVSEFEESE-NCEAALAEKEALLAK 378
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAeELEALIARLEAEAAA 238
|
250
....*....|....
gi 564351372 379 LHSENVTKNTENHR 392
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1419-1610 |
6.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1419 NSLTSEIQFLRKQNEALSTMLEkgskEKQKENEKLRESLARKTESLEHLQLEYASVREENERLRRDISEKERQNQQLTQE 1498
Cdd:COG4372 48 EQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1499 VCSSLQELSRVQEEAKSRQQLLLQKDELLQSLQMELKVYEKLAEEHQKLQQEsrgeacgggqkgqdpfSNLHGLLKEIQV 1578
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA----------------LSEAEAEQALDE 187
|
170 180 190
....*....|....*....|....*....|..
gi 564351372 1579 LRDQAERSIQTNNTLKSKLEKQLSQGSKQAQE 1610
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
275-455 |
7.22e-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: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 275 EERQKERNHFEERIQALQEDLrekeREIATEKKNSLKRDKAIQGLTMA------LKSKEKEVEELNSIIKELTADSTQSR 348
Cdd:COG4913 613 AALEAELAELEEELAEAEERL----EALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 349 EapLKTQVSEfeesenCEAALAEKEALLAKLHSENVTKNTENHRLLRNVKKVTQELNDLKKEK-----LRLERDLEEAHR 423
Cdd:COG4913 689 A--LEEQLEE------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|..
gi 564351372 424 EgNRGARTIHDLRNEVEKLRKEVCEREKAVEK 455
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAEEELER 791
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1370-1549 |
8.18e-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: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1370 EHIQEIRTLRKHLEESIKtneklrkqlerqgcetdqgstnvsaysselhnsltSEIQFLRKQNEALSTMLEKGSKEKQKE 1449
Cdd:pfam09311 154 EELIEVRTAADHMEEKLK-----------------------------------AEILFLKEQIQAEQCLKENLEETLQAE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 1450 NEKLRESLArkteSLEHLQLEYASVREENERLRRDISEKERQNQQLTQEVCSSLQELSRVQEEAKSRQQLLLQKDELLQS 1529
Cdd:pfam09311 199 IENCKEEIA----SISSLKVELERIKAEKEQLENGLTEKIRQLEDLQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQR 274
|
170 180
....*....|....*....|
gi 564351372 1530 LQMELKVYEKLAEEHQKLQQ 1549
Cdd:pfam09311 275 LQTELDVSEQVQRDFVKLSQ 294
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
97-613 |
8.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 97 EHIYKKNIELKVEVESLKRELQERDQLLVKASKAVESLAEGGGSEIQRVKEDARKKVQQVEELLTKrihlleedvkaAQA 176
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD-----------CQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 177 ELEKafagtetekalrLSLESKLsamkkmqegdlemtLALEEKDRLIEELKLSLKSKEALIQCLKEEKSQMaspdENVSS 256
Cdd:TIGR00606 327 ELEK------------LNKERRL--------------LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ----SLATR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 257 GELRGLSATLREEKE-RDAEERQKERNHFEER-IQALQEDLREKEReIATEKKNSLKRDKAIQGLTMALKSK--EKEVEE 332
Cdd:TIGR00606 377 LELDGFERGPFSERQiKNFHTLVIERQEDEAKtAAQLCADLQSKER-LKQEQADEIRDEKKGLGRTIELKKEilEKKQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 333 LNSIIKELtadstQSREAPLKTQVSEFEESENCEAALAEKEallaklhsenvtKNTENHRLLRNVKKVTQELNDLKKEKL 412
Cdd:TIGR00606 456 LKFVIKEL-----QQLEGSSDRILELDQELRKAERELSKAE------------KNSLTETLKKEVKSLQNEKADLDRKLR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 413 RLERDLEEAHREGNRGARTIHDLRNEV---EKLRKEVCEREKAVEKHYKSLPGES--SSKFHSQEQVVKGLTESASQEDL 487
Cdd:TIGR00606 519 KLDQEMEQLNHHTTTRTQMEMLTKDKMdkdEQIRKIKSRHSDELTSLLGYFPNKKqlEDWLHSKSKEINQTRDRLAKLNK 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 488 LLQKSnEKDLEAIQQNCYLMTAEELKFGSDglITEKCSQQSPDSKLIFSKEKQQSEYEGLtGDLKTEQNVYAHLAKNLQD 567
Cdd:TIGR00606 599 ELASL-EQNKNHINNELESKEEQLSSYEDK--LFDVCGSQDEESDLERLKEEIEKSSKQR-AMLAGATAVYSQFITQLTD 674
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 564351372 568 TDS----------KLQAELKRVLalrKQLEQDVLAYRNLQTALQEQLSEIRKREEE 613
Cdd:TIGR00606 675 ENQsccpvcqrvfQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-420 |
9.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 279 KERNHFEERIQALQEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKEVEELNSII-------------KELTA--- 342
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkyeeqlgnvrnnKEYEAlqk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351372 343 --DSTQSREAPLKTQVSEF-EESENCEAALAEKEALLAKLHSENVTKNTEnhrLLRNVKKVTQELNDLKKEKLRLERDLE 419
Cdd:COG1579 97 eiESLKRRISDLEDEILELmERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 564351372 420 E 420
Cdd:COG1579 174 P 174
|
|
| |
