|
Name |
Accession |
Description |
Interval |
E-value |
| PACT_coil_coil |
pfam10495 |
Pericentrin-AKAP-450 domain of centrosomal targeting protein; This domain is a coiled-coil ... |
1835-1913 |
3.00e-27 |
|
Pericentrin-AKAP-450 domain of centrosomal targeting protein; This domain is a coiled-coil region close to the C-terminus of centrosomal proteins that is directly responsible for recruiting AKAP-450 and pericentrin to the centrosome. Hence the suggested name for this region is a PACT domain (pericentrin-AKAP-450 centrosomal targeting). This domain is also present at the C-terminus of coiled-coil proteins from Drosophila and S. pombe, and that from the Drosophila protein is sufficient for targeting to the centrosome in mammalian cells. The function of these proteins is unknown but they seem good candidates for having a centrosomal or spindle pole body location. The final 22 residues of this domain in AKAP-450 appear specifically to be a calmodulin-binding domain indicating that this member at least is likely to contribute to centrosome assembly.
Pssm-ID: 463115 Cd Length: 77 Bit Score: 106.52 E-value: 3.00e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 1835 YLRAESFRKALIYQKKYLLLLIGGFQDSEQETLSMIAHLGVFPSKADKKvtaSRPFTRFRTAVRVVIAVLRLRFLVKKW 1913
Cdd:pfam10495 2 LLREESFRKDLAYQKKYLLLLLGGYQACNKADLRLLAQMGVTPPDDRPS---RKPRRKLKSAALAVIAIARMKRLAREW 77
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-645 |
9.45e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 141 QLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQ 220
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 221 QLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREAGTpVSAGREDAALQKEVESLTRDQWESRKQSEKD 300
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAEL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 301 RATLLSQMRVLESELEDQLVQHRGCAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQ 380
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 381 ATRPRPPGprDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQ 460
Cdd:COG1196 514 LLLAGLRG--LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 461 RRSTEELEVVNSRNSEIEELKAIIEHLQENQ--EQLQKAKAEEIEQLHEVIEKLQSELSLmgptvhEMSDLPPGSLHTEl 538
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTL------EGEGGSAGGSLTG- 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 539 scLQAEGMGGQALHNELQAAQAAKGAFGQLLADHGHSQALEALQERLQDAEAAAARHLTELEhcvALRQAEVEAMASRIQ 618
Cdd:COG1196 665 --GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE---ALEEQLEAEREELLE 739
|
490 500
....*....|....*....|....*..
gi 1958758604 619 EFEATLKAKEAIIVQRDLEIDAVNKWK 645
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-512 |
3.89e-12 |
|
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: 72.02 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 161 EEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQlivELEDLRKQLQQASREL 240
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE---RLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 241 LTLKEEnsvlwnqKETFTNEAKEREAgtpvsagrEDAALQKEVESLTRDQWESRKQS--------EKDRATLLSQMRVLE 312
Cdd:TIGR02169 754 ENVKSE-------LKELEARIEELEE--------DLHKLEEALNDLEARLSHSRIPEiqaelsklEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 313 SELEDQlvqHRGCAQLAEEVTTLKQQLATLDkhlrSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQAtrprppgprDS 392
Cdd:TIGR02169 819 QKLNRL---TLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKKEELEEELEELEAALRDL---------ES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 393 QCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLL-------IQEEEIKHLEETNENIQRQMA------QLQEELEK 459
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkakleALEEELSEIEDPKGEDEEIPEeelsleDVQAELQR 962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958758604 460 QRRSTEELEVVNsrNSEIEELKAIIEHLQENQEQLQKAKAEEiEQLHEVIEKL 512
Cdd:TIGR02169 963 VEEEIRALEPVN--MLAIQEYEEVLKRLDELKEKRAKLEEER-KAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-638 |
7.65e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 140 KQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESE 219
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 220 QQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREagtpvsagREDAALQKEVESLTRDQWESRKQSEK 299
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE--------AELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 300 DRATLLSQMRVLESELEDQLVQHRGCAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLR 379
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 380 QATRPRPPgprdsqcAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIkhleetneniqrQMAQLQEELEK 459
Cdd:COG1196 478 ALAELLEE-------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA------------VLIGVEAAYEA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 460 QRRSTEELEVVNSRNSEIEELKAIIEHLQENQ---------EQLQKAKAEEIEQLHEVIEKLQSELSLMGPTVHEMSDLP 530
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 531 PGSLHTELSCLQAEGMGGQAL------HNELQAAQAAKGAFGQLLADHGHSQALEALQERLQDAEAAAARHLTELEHCVA 604
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAvtlagrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510
....*....|....*....|....*....|....
gi 1958758604 605 LRQAEVEAMASRIQEFEATLKAKEAIIVQRDLEI 638
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-640 |
8.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 311 LESELEDQLVQHRGCAQLAEEVTTLKQQLATLDKHLRS-QRQFMDEQAAEREHEREEFQQEIKWLEGQLRQatrprppgp 389
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAE--------- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 390 rdsqcakLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEV 469
Cdd:COG1196 265 -------LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 470 VNSR-NSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSELSlmgptvhemsdlppgslhTELSCLQAEGMGG 548
Cdd:COG1196 338 ELEElEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE------------------ELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 549 QALHNELQAAQAAKGAFGQLLADhghSQALEALQERLQDAEAAAARHLTELEHCVALRQAEVEAMASRIQEFEATLKAKE 628
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330
....*....|..
gi 1958758604 629 AIIVQRDLEIDA 640
Cdd:COG1196 477 AALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-782 |
2.05e-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: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 140 KQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESE 219
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 220 QQLIVELEDLRKQLQQASRELLTLKEENSVLWNQ----KETFTNEAKEREAGTPVSAGREDAALQKEVESLTRdQWESRK 295
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 296 QSEKDRATLLSQMRVLESELEDQLvqhrgcAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEF--QQEIKW 373
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREEL------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLknQSGLSG 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 374 LEGQLRQATRPRP----------PGPRDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETN 443
Cdd:TIGR02168 521 ILGVLSELISVDEgyeaaieaalGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 444 ----------------------------ENIQRQMAQLQEELEKQRRSTEELEVVN-----------------SRNSEIE 478
Cdd:TIGR02168 601 lgvakdlvkfdpklrkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRpggvitggsaktnssilERRREIE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 479 ELKAIIEHLQENQEQLQKA---KAEEIEQLHEVIEKLQSELSLMGPTVHEMSDLPPGSLHTELSCL----QAEGMGGQAL 551
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKAlaeLRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriaQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 552 HNELQAAQAAKGAFGQLLADHGHSQALEALQERLQDAEAAAARHLTELEHCVALRQAEVEAMASRIQEFEATLKAKEAII 631
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 632 VQRDLEIDAVNK--WKVSHSVELEALLLALAHFQHAVEQQTSATPDEPPK-----LQQLLVQCARLSHQLHVLYRRFLRC 704
Cdd:TIGR02168 841 EDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALAllrseLEELSEELRELESKRSELRRELEEL 920
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758604 705 QVELGQHQPRVasvgcadppAEAQGKRDGELEQdgvssglALAPHSLVAQAKEEQPEDCHLGNTSLRAQLRQLEEKLD 782
Cdd:TIGR02168 921 REKLAQLELRL---------EGLEVRIDNLQER-------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-646 |
2.70e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 174 LERLREEsAAKDRLALELHTAEGLLEG--FKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLw 251
Cdd:COG1196 202 LEPLERQ-AEKAERYRELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 252 NQKEtftNEAKEREAgtpvSAGREDAALQKEVESLTrdqwESRKQSEKDRATLLSQMRVLESELEdqlvqhrgcaQLAEE 331
Cdd:COG1196 280 ELEL---EEAQAEEY----ELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELE----------ELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 332 VTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIkwlegqlrqatrprppgprdsqcAKLDEEVELLQEKLREk 411
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-----------------------EELEELAEELLEALRA- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 412 ldgfnELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQ 491
Cdd:COG1196 395 -----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 492 EQLQKAKAEEIEQLHEVIEKLQSELSLmgptvHEMSDLPPGSLHTELSCLQAEGMGGqaLHNELQAAQAAKGAFGQLLAD 571
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLL-----LEAEADYEGFLEGVKAALLLAGLRG--LAGAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758604 572 HGHSQALEALQERLQDAEAAAARHLTELEHCVALRQAEVEAMASRIQEFEATLKAKEAIIVQRDLEIDAVNKWKV 646
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-521 |
3.24e-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: 65.85 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 202 KVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEEnsvlWNQKETFTNEAKEREAgtpvSAGREDAALQK 281
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLA----RLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 282 EVESLTRDQWESRKQSEKdRATLLSQMRVLESELEDQLVQHRG-CAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAER 360
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEE-LEERLEEAEEELAEAEAEIEELEAqIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 361 EHER---EEFQQEIKWLEGQLRQATrprppgprdSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIK 437
Cdd:TIGR02168 827 ESLErriAATERRLEDLEEQIEELS---------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 438 HLEETNENIQRQMAQLQEELEKQRRSTEELEVvnsrnsEIEELKAIIEHLQ-----------ENQEQLQKAKAEEIEQLH 506
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLEL------RLEGLEVRIDNLQerlseeysltlEEAEALENKIEDDEEEAR 971
|
330
....*....|....*
gi 1958758604 507 EVIEKLQSELSLMGP 521
Cdd:TIGR02168 972 RRLKRLENKIKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1165-1678 |
1.01e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1165 YNSLVKKLEKVIQEQGDLQKVREHAclpdrSSLLAEIQALRAQLRMTHLQNQEKLQQLCAALTSTEARGSQREHQLRRQV 1244
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1245 ELLAY---KVEQEKCIANDLQKTLSKEQEAASDVRKRLMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEVLRLRYGH 1321
Cdd:COG1196 309 ERRREleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1322 VTwSYSGTSSASAGRAVLDGKENELKVVLEELECERGKGQVLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNNQ 1401
Cdd:COG1196 389 LE-ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1402 LCVALKHERAAKDNLQKELQIEASRCEALLAQEKGQLSELRKSLEAERSR---------SLELSEALQHERLLTEQLSRN 1472
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagavAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1473 AQEACARQDTQAQHA--LLRKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKE-------------- 1536
Cdd:COG1196 548 LQNIVVEDDEVAAAAieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryyvlgdtllgrtl 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1537 VSGNLRSAVDALQTHKQELGCCL-------EREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRV 1609
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTlegeggsAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 1610 KEKLRELELQRQRDEHKIEQLQRLVRELRWKEEAPGGNGPCRGSPCLGSLERDQFQEQQQELEKIRQQL 1678
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
108-521 |
2.45e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 108 ENTQECEQpIRKVYQSLSTAVEGLLDMALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRL 187
Cdd:COG1196 320 ELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 188 ALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEEN-SVLWNQKETFTNEAKEREA 266
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEeALLELLAELLEEAALLEAA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 267 GTPVSAGREDAALQKEVESLTRDQWESRKQSEKDRATLLSQMRVL---------ESELEDQLVQHRGcAQLAEEVTTLKQ 337
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavligvEAAYEAALEAALA-AALQNIVVEDDE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 338 QLATLDKHLRSQR----------------------------QFMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRPPGP 389
Cdd:COG1196 558 VAAAAIEYLKAAKagratflpldkiraraalaaalargaigAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 390 RDSQCAKLDEEVELLQEKLREKLDGF------NELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRS 463
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758604 464 TEELEVVNSRNSEIEELKAIIEHLQENQEQLQKAKAEE------IEQLHEVIEKLQSELSLMGP 521
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdLEELERELERLEREIEALGP 781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-515 |
3.24e-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: 62.38 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 108 ENTQECEQPIRKVyQSLSTAVEGLLDMALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRL 187
Cdd:TIGR02168 681 ELEEKIEELEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 188 ALELHTAEGLLEGfkvEKADLQEALGKKEESEQQlIvelEDLRKQLQQASRELLTLKEEnsvLWNQKETFTNEAKEREag 267
Cdd:TIGR02168 760 EAEIEELEERLEE---AEEELAEAEAEIEELEAQ-I---EQLKEELKALREALDELRAE---LTLLNEEAANLRERLE-- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 268 tpvSAGREDAALQKEVESLTRdQWESRKQSEKDRATLLSQMRVLESELEDQLvqhrgcaqlaEEVTTLKQQLATLDKHLR 347
Cdd:TIGR02168 828 ---SLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELEELIEELESEL----------EALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 348 SQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQAtrprppgprDSQCAKLDEEVELLQEKLREKLDgfnelvikkdladq 427
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQL---------ELRLEGLEVRIDNLQERLSEEYS-------------- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 428 qllIQEEEIKHLEETNENiqrQMAQLQEELEKQRRSTEELEVVNSRN-SEIEELKAIIEHLQENQEQLQKAKaeeiEQLH 506
Cdd:TIGR02168 951 ---LTLEEAEALENKIED---DEEEARRRLKRLENKIKELGPVNLAAiEEYEELKERYDFLTAQKEDLTEAK----ETLE 1020
|
....*....
gi 1958758604 507 EVIEKLQSE 515
Cdd:TIGR02168 1021 EAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-517 |
6.35e-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: 61.24 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 168 QKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIV-ELEDLRKQLQQASRELLTLKEE 246
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLkEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 247 nsvlwnqKETFTNEAKEREAgtpvsagrEDAALQKEVESLTRdqwESRKQSEKDRATLLSQMRVLESELEdqlvqhrgca 326
Cdd:TIGR02169 253 -------LEKLTEEISELEK--------RLEEIEQLLEELNK---KIKDLGEEEQLRVKEKIGELEAEIA---------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 327 QLAEEVTTLKQQLatldkhlrsqrQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRppgprdsqcAKLDEEVELLQE 406
Cdd:TIGR02169 305 SLERSIAEKEREL-----------EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR---------DKLTEEYAELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 407 KLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEEL------------EVVNSRN 474
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaiagieakinELEEEKE 444
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958758604 475 SEIEELKAIIEHLQENQEQLQKAKaEEIEQLHEVIEKLQSELS 517
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYE-QELYDLKEEYDRVEKELS 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1391-1643 |
1.06e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1391 SLEKQLAQNNQLCVALKHERaakdnlqKELQIEASRCEALLAQEKGQLSELRKSLEAERSRSLELSEAL----QHERLLT 1466
Cdd:TIGR02168 236 ELREELEELQEELKEAEEEL-------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1467 EQLSRNAQEACARQDTQAQhaLLRKLKAEKARALELEAMLEKVQKQAAHTQQqleaqaqerclELRREKEVSGNLRSAVD 1546
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEE--LESKLDELAEELAELEEKLEELKEELESLEA-----------ELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1547 ALQTHKQELGCCLEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRVKEKL----RELELQRQR 1622
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeeleEELEELQEE 455
|
250 260
....*....|....*....|.
gi 1958758604 1623 DEHKIEQLQRLVRELRWKEEA 1643
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQA 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-419 |
1.46e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 121 YQSLSTAVEGL-LDMALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRlalELHTAEGLLE 199
Cdd:TIGR02168 215 YKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE---EIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 200 GFKVEKADLQEALGKKEESEQQLI-------VELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREAGTPVSA 272
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLErqleeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 273 GREDaALQKEVESLTRDQWESRKQSEKDRATLlsqmRVLESELEdQLVQHRgcAQLAEEVTTLKQQLATLDKH-LRSQRQ 351
Cdd:TIGR02168 372 SRLE-ELEEQLETLRSKVAQLELQIASLNNEI----ERLEARLE-RLEDRR--ERLQQEIEELLKKLEEAELKeLQAELE 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758604 352 FMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRPpgPRDSQCAKLDEEVELLqEKLREKLDGFNELV 419
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALD--AAERELAQLQARLDSL-ERLQENLEGFSEGV 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-520 |
1.62e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 140 KQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLAL--ELHTAEGLLEGFKVEKADLQEalgkKEE 217
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEE----RLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 218 SEQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREAGTPVSAGREDAALQKEVESLTR--DQWESRK 295
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEelEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 296 QSEKDRATLLSQMRVLES-----ELEDQLVQHRGCAQLAEEVTTLKQQLATLDkHLRSQRQFMDEQAAEREHEREEFQQE 370
Cdd:COG4717 237 EAAALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGVLFLVLGLLALL-FLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 371 IKWLEGQLRQATRPRPPGPRDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQ--R 448
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaE 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958758604 449 QMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQEQLQkAKAEEIEQLHEVIEKLQSELSLMG 520
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE-ELEEELEELREELAELEAELEQLE 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1241-1595 |
1.67e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1241 RRQVELLAYKVEQEKCIANDLQKTLSKEQEAASDVRKRLMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEVLRLRyg 1320
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1321 hvtwsysgtssasAGRAVLDGKENELKVVLEELECERgkgqVLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNN 1400
Cdd:COG1196 302 -------------QDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1401 QLCVALKHERAAKDNLQKELQIEASRCEALLAQEKGQLSELRKSLEAERSRSLELSEALQhERLLTEQLSRNAQEACARQ 1480
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1481 DTQAQHALLRKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRR---EKEVSGNLRSAVDALQTHKQELGC 1557
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLleaEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958758604 1558 -CLEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRR 1595
Cdd:COG1196 524 gAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-516 |
3.40e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 140 KQLEDARQLHRCVEKEFrhrdEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEEse 219
Cdd:PRK03918 186 KRTENIEELIKEKEKEL----EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 220 qqLIVELEDLRKQLQQASRELltlkeensvlwnqketftnEAKEREagtpVSAGREDAALQKEVESLTRDQWESRKQSEK 299
Cdd:PRK03918 260 --KIRELEERIEELKKEIEEL-------------------EEKVKE----LKELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 300 DRATLLSQMRVLESELEDQLVQHRGCAQLAEEVTTLKQQLATLDKHLRSQrqfmdeqaaerehereefqQEIKWLEGQLR 379
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-------------------EEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 380 QATRPRPPGPRDSQCAKLD------EEVELLQEKLREKLDGFNELVIKKDLADQQL------------LIQEEEIKHL-- 439
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEelekakEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgrELTEEHRKELle 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 440 EETNE--NIQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSEL 516
Cdd:PRK03918 456 EYTAElkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-516 |
5.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 140 KQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLA-----LELHTAEGLLEGFKVEKADLQEALGK 214
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgreLTEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 215 KEESEQQLIVELEDLRKQLQQASR--ELLTLKEENSVLWNQKETFTNEAKEREAGTPVSAGREDAALQKEVESLTRDqWE 292
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 293 SRKQSEKDRATLLSQMRVLESELEDQLVQHRGCAQLAEEvttlkqqlaTLDKHLRSQRQFMDE--QAAEREHEREEFQQE 370
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE---------ELEERLKELEPFYNEylELKDAEKELEREEKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 371 IKWLEGQLRQATRprppgprdsQCAKLDEEVELLQEKLREKLDGFNE-----LVIKKDLADQQLLIQEEEIKHLEETNEN 445
Cdd:PRK03918 621 LKKLEEELDKAFE---------ELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREE 691
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758604 446 IQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKaiiehlqenqEQLQKAKAEEIEQLHEVIEKLQSEL 516
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELR----------EKVKKYKALLKERALSKVGEIASEI 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1392-1642 |
1.76e-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: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1392 LEKQLAQNNQLCVALKHERAAKDNLQKELQIEASRCEALLAQEKGQLSELRKSLEAERSR-----------SLELSEALQ 1460
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleeriaqlSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1461 HERLLTEQLSRNAQEACARQDTQAQhaLLRKLKAEKARALELEAMLEKVQKQAAHTQQqleaqaqerclELRREKEVSGN 1540
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNE-----------EAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1541 LRSAVDALQTHKQELGCCLEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRVK--EKLRELEL 1618
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElsEELRELES 908
|
250 260
....*....|....*....|....
gi 1958758604 1619 QRQRDEHKIEQLQRLVRELRWKEE 1642
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1162-1465 |
3.88e-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: 55.45 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1162 LGDYNSLVKKLEKVIQEQGDLQKVREHAclpdrSSLLAEIQALRAQLRMTHLQNQEKLQQLCAALTSTEARGSQREHQLR 1241
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEEL-----TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1242 RQVELLAYKVEQEKCIANDLQKTLSKEQEAA---SDVRKRLMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEVLRLR 1318
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1319 yghvtwsySGTSSASAGRAVLDGKENELKVVLEELECERGKGQVLQAQQEEQQLRHLQREgqSSRALEELKISLEKQLAQ 1398
Cdd:TIGR02168 386 --------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 1399 NNQLCVALKHERAAKDNLQKELQIEASRcealLAQEKGQLSELRKSLEAERSRSLELSEALQHERLL 1465
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERE----LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-515 |
5.28e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 169 KQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIV---ELEDLRKQLQQASRELLTLKE 245
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 246 ENSVLWNQKETFTNEAKEREAgtpvSAGREDAAlqKEVESLTRDQWESRKQSEKDRatlLSQMRVLESELEDQLVQHRGC 325
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLA----EAGLDDAD--AEAVEARREELEDRDEELRDR---LEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 326 A-QLAEEVTTLKQQLATLDKHLRSQRQFMDEQaaerehereefQQEIKWLEGQLRQATRPRPPGPRDSqcakldEEVELL 404
Cdd:PRK02224 351 AdDLEERAEELREEAAELESELEEAREAVEDR-----------REEIEELEEEIEELRERFGDAPVDL------GNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 405 QEKLREKLDGFNELV---------IKKDLADQQLLIQE----------EEIKHLEETNENIQRqMAQLQEELEKQRRSTE 465
Cdd:PRK02224 414 LEELREERDELREREaeleatlrtARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRER-VEELEAELEDLEEEVE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 466 ELEVVNSRNSEIEELKAIIEHLQENQEQLQK----------AKAEEIEQLHEVIEKLQSE 515
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERREDLEEliaerretieEKRERAEELRERAAELEAE 552
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
133-515 |
6.87e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 133 DMALDSSKQLEDARQLHRCVEKEFRHRDE-EMAQAVQKQQELLERLREESAAKDRL---ALELHTAEGLLEgfKVEKADL 208
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAkkkAEEAKKADEAKK--KAEEAKK 1458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 209 QEALGKKEESEQQLivelEDLRKQLQQASR--ELLTLKEENSVLWNQKETFTNEAKEREAGTPVSAGREDAALQKEVESL 286
Cdd:PTZ00121 1459 AEEAKKKAEEAKKA----DEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 287 TRDqwESRKQSEKDRATLLSQMRVLESELEDQLVQHrgcAQLAEEVTTLKQQLATLDKHLRSQRqfmdeqaaeREHEREE 366
Cdd:PTZ00121 1535 KAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEE---AKKAEEDKNMALRKAEEAKKAEEAR---------IEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 367 FQQEIKWLEGQLRQATRPRPPGPRDSQCAKLDEEVELLQEKLREKLDGFNELviKKdlADQQLLIQEEEIKHLEETNeni 446
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KK--AEEENKIKAAEEAKKAEED--- 1673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 447 QRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSE 515
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
112-489 |
8.00e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 112 ECEQPIRKVYQSLSTA---VEGLLDMALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLA 188
Cdd:PRK02224 325 ELRDRLEECRVAAQAHneeAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 189 LELHTAEGLLEGFKVEK-----------ADLQEALGKKEESEQQL----------------IVE-LEDLRKQLQQASREL 240
Cdd:PRK02224 405 VDLGNAEDFLEELREERdelrereaeleATLRTARERVEEAEALLeagkcpecgqpvegspHVEtIEEDRERVEELEAEL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 241 LTLKEENSVLwnqketftnEAKEREAGTPVSAGREDAALQKEVESLTRDQWESRKQSEKDRATLlSQMRVLESELEDQLV 320
Cdd:PRK02224 485 EDLEEEVEEV---------EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA-EELRERAAELEAEAE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 321 QHRGCAQLA--------EEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHereefqqeikwleGQLRQATRPRppgpRDS 392
Cdd:PRK02224 555 EKREAAAEAeeeaeearEEVAELNSKLAELKERIESLERIRTLLAAIADA-------------EDEIERLREK----REA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 393 QCAKLDEEVELLQEK------LREKLDG--FNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRST 464
Cdd:PRK02224 618 LAELNDERRERLAEKrerkreLEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
410 420
....*....|....*....|....*
gi 1958758604 465 EELEVVNSRNSEIEELKAIIEHLQE 489
Cdd:PRK02224 698 ERREALENRVEALEALYDEAEELES 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-515 |
1.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 171 QELLERLREEsaaKDRLALELHTAEGLLEGFKVEKADLQE---ALGKKEESEQQLIvELEDLRKQLQQASRELLTLKEEN 247
Cdd:COG4913 609 RAKLAALEAE---LAELEEELAEAEERLEALEAELDALQErreALQRLAEYSWDEI-DVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 248 SVLwnqketftneakereagtpvsagredAALQKEVESLtrdqWESRKQSEKDRATLLSQMRVLESELEdqlvqhrgcaQ 327
Cdd:COG4913 685 DDL--------------------------AALEEQLEEL----EAELEELEEELDELKGEIGRLEKELE----------Q 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 328 LAEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRprppgprdsqcakldeEVELLQEK 407
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA----------------RLNRAEEE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 408 LREKLDGFNE-------------------LVIKKDLADQQLLIQEEEIKHLEetNENIQRQMAQLQEELEKQRRSTEE-- 466
Cdd:COG4913 789 LERAMRAFNRewpaetadldadleslpeyLALLDRLEEDGLPEYEERFKELL--NENSIEFVADLLSKLRRAIREIKEri 866
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958758604 467 -------------------LEVVNSRNSEI----EELKAIIEHLQENQEQLQKAKAEEIEQLhevIEKLQSE 515
Cdd:COG4913 867 dplndslkripfgpgrylrLEARPRPDPEVrefrQELRAVTSGASLFDEELSEARFAALKRL---IERLRSE 935
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-507 |
1.35e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 155 EFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQ 234
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 235 QASRELLTLKEENSVLWNQKETFTNEAKEREagTPVSAGREDAA-LQKEVESlTRDQWESRkqsEKDRATLLSQMRVLES 313
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLE--ERAEELREEAAeLESELEE-AREAVEDR---REEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 314 ELEDQLVQHRGCA----QLAEEVTTLKQQLATLDKHLRSQRQFMDEqaaereheREEFQQEIKWLE-GQ-LRQATRPRPP 387
Cdd:PRK02224 399 RFGDAPVDLGNAEdfleELREERDELREREAELEATLRTARERVEE--------AEALLEAGKCPEcGQpVEGSPHVETI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 388 GPRDSQCAKLDEEVELLQ-------------EKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQ 454
Cdd:PRK02224 471 EEDRERVEELEAELEDLEeeveeveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 455 EELEKQRRSTEE----------------------------LEVVNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLH 506
Cdd:PRK02224 551 AEAEEKREAAAEaeeeaeeareevaelnsklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA 630
|
.
gi 1958758604 507 E 507
Cdd:PRK02224 631 E 631
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-514 |
1.46e-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: 53.49 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 168 QKQQELLERLREESAAKDRLalelhtaegllEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEEN 247
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEI-----------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 248 SVLWNQKETFTNeakereagtpvsagrEDAALQKEVESLTRdqweSRKQSEKDRATLLSQMRVLESELEdqlvqhrgcaQ 327
Cdd:TIGR04523 436 IKNNSEIKDLTN---------------QDSVKELIIKNLDN----TRESLETQLKVLSRSINKIKQNLE----------Q 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 328 LAEEVTTLKQQLatldKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEgqlrqatrprppgprdSQCAKLDEEVELLQEK 407
Cdd:TIGR04523 487 KQKELKSKEKEL----KKLNEEKKELEEKVKDLTKKISSLKEKIEKLE----------------SEKKEKESKISDLEDE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 408 LREKLDGFNELVIKKDLADQQlliqeEEIKHLEETNENIQRQMAQLQEELEKqrRSTEELEVvnsrNSEIEELKAIIEHL 487
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKN-----KEIEELKQTQKSLKKKQEEKQELIDQ--KEKEKKDL----IKEIEEKEKKISSL 615
|
330 340
....*....|....*....|....*..
gi 1958758604 488 qenQEQLQKAKAEEiEQLHEVIEKLQS 514
Cdd:TIGR04523 616 ---EKELEKAKKEN-EKLSSIIKNIKS 638
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-621 |
1.55e-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: 53.52 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 279 LQKEVESLTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHrgcAQLAEEVTTLKQQLATLDKHL---RSQRQFMDE 355
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL---KEAEEELEELTAELQELEEKLeelRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 356 QAAEREHEREEFQQEIkwlegqlrqatrprppgprdsqcAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEE 435
Cdd:TIGR02168 282 EIEELQKELYALANEI-----------------------SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 436 IKHLEETNENIQRQMAQLQEELEKqrrsteelevvnsRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQlhevIEKLQSE 515
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEE-------------LEAELEELESRLEELEEQLETLRSKVAQLELQ----IASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 516 LSLMGPTVhEMSDLPPGSLHTELSCLQAEgmggqALHNELQAAQAAKGAFGQLLAD-HGHSQALEALQERLQDAEAAAAR 594
Cdd:TIGR02168 402 IERLEARL-ERLEDRRERLQQEIEELLKK-----LEEAELKELQAELEELEEELEElQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*..
gi 1958758604 595 HLTELEHCVALRQAEVEAMASRIQEFE 621
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1373-1643 |
1.63e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1373 RHLQRegQSSRALEELKISLEKQLAQNNQLCVALKHERAAKDNLQKELQIEASRCEAL---LAQEKGQLSELRKSLEAER 1449
Cdd:COG1196 203 EPLER--QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELeaeLAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1450 srsLELSEALQHERLLTEQLSRnaqeacarqdtqaqhaLLRKLKAEKARALELEAMLEKvqkqaahtqqqleaQAqercL 1529
Cdd:COG1196 281 ---LELEEAQAEEYELLAELAR----------------LEQDIARLEERRRELEERLEE--------------LE----E 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1530 ELRREKEvsgnlrsavdALQTHKQElgccLEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDkRKWQRV 1609
Cdd:COG1196 324 ELAELEE----------ELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEEL 388
|
250 260 270
....*....|....*....|....*....|....
gi 1958758604 1610 KEKLRELELQRQRDEHKIEQLQRLVRELRWKEEA 1643
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1168-1643 |
1.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1168 LVKKLEKVIQEQGDLQKVREHAclpDRSSLLAEIQALRAQLRMTHLQNQEKLQQLCAALTSTEARGSQREHQLRRQVELL 1247
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1248 AYKVEQEKCIANDLQKTLSKEQEA------ASDVRKRLMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEVLRlrygh 1321
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKAdeakkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----- 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1322 vtwsysgtSSASAGRAVLDGKENELKVVLEElecERGKGQVLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNnq 1401
Cdd:PTZ00121 1472 --------ADEAKKKAEEAKKADEAKKKAEE---AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-- 1538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1402 lcvALKHERAAK-DNLQKELQI----EASRCEALLAQEKGQLSELRKsleAERSRSLELSEALQHERLLTEQLSRNAQEA 1476
Cdd:PTZ00121 1539 ---AKKAEEKKKaDELKKAEELkkaeEKKKAEEAKKAEEDKNMALRK---AEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1477 CARQDTQAQHALLRKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEVSGNLRSAVDALQTHKQELG 1556
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1557 CCLEREREKAAWLQAELEQLSARVKQQEARQDEK----RMDRRSSREDLDKRKwqrvKEKLRELELQRQRDEHKIEQLQR 1632
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEK 1768
|
490
....*....|.
gi 1958758604 1633 LVRELRWKEEA 1643
Cdd:PTZ00121 1769 KAEEIRKEKEA 1779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-512 |
1.78e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 122 QSLSTAVEGLLDMALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGF 201
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 202 KVEKADLQEALGKKEESE-QQLIVELEDLRKQLQQASRELLTLKEENSVLWN------QKETFTNEAKEREAGTPVSAGR 274
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGlAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDdevaaaAIEYLKAAKAGRATFLPLDKIR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 275 EDAALQKEVESLTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHRGCAQLAEEVTTLKQQLATLDKHLRSQRQFMD 354
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 355 EQAAEREHEREEFQQEIKWLEGQLRQATRPRPPGPRDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEE 434
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 435 EIKHLEETNENIQRQM---AQLQEELEKQRRSTEELEVVNSRnsEIEELKAIIEHLQENQEQLQKAKaEEIEQLHEVIEK 511
Cdd:COG1196 744 EEELLEEEALEELPEPpdlEELERELERLEREIEALGPVNLL--AIEEYEELEERYDFLSEQREDLE-EARETLEEAIEE 820
|
.
gi 1958758604 512 L 512
Cdd:COG1196 821 I 821
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-594 |
2.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 210 EALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREagtpvsAGREDAALQKEVESLtRD 289
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA------LEAELAELPERLEEL-EE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 290 QWESRKQSEKDRATLLSQMRVLESELEDQLVQ-----HRGCAQLAEEVTTLKQQLATLDKHLRSQRQFMDE-----QAAE 359
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEEleeelEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 360 REHEREEFQQEIKWLEGQLR--------QATRPRPPGPRDSQCAKLDEEVELL----QEKLREKLDGFNELVIKKDLADQ 427
Cdd:COG4717 234 NELEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLGLLallfLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 428 QLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEelkaIIEHLQENQEQLQKAKAEEIEQLHE 507
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----LEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 508 VIEK-------------LQSELSLMGPTVHE-MSDLPPGSLHTELSCLQAEgmgGQALHNELQAAQAAKGAFGQLLADHG 573
Cdd:COG4717 390 ALEQaeeyqelkeeleeLEEQLEELLGELEElLEALDEEELEEELEELEEE---LEELEEELEELREELAELEAELEQLE 466
|
410 420
....*....|....*....|.
gi 1958758604 574 HSQALEALQERLQDAEAAAAR 594
Cdd:COG4717 467 EDGELAELLQELEELKAELRE 487
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
168-492 |
2.56e-06 |
|
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: 52.82 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 168 QKQQELLERLREES--AAKDRLALELHTAEGLLEGFKVEKADL---------QEALGKKEESEQQLIvELEDLRKQLQQA 236
Cdd:pfam17380 287 RQQQEKFEKMEQERlrQEKEEKAREVERRRKLEEAEKARQAEMdrqaaiyaeQERMAMERERELERI-RQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 237 SRELLTLkEENSVLWNQKETFTNEAKEREAGTPVSAGREDAALQKE----VESLTRDQWESRKQSEKDRATllsQMRVLE 312
Cdd:pfam17380 366 RQEEIAM-EISRMRELERLQMERQQKNERVRQELEAARKVKILEEErqrkIQQQKVEMEQIRAEQEEARQR---EVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 313 SELEDQLVQHRgcaqlaEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRprppgprds 392
Cdd:pfam17380 442 EERAREMERVR------LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ--------- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 393 qcakldeevELLQEKLREKLdgfnelvIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNS 472
Cdd:pfam17380 507 ---------AMIEEERKRKL-------LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA 570
|
330 340
....*....|....*....|
gi 1958758604 473 RNSEIEELKAIIEHLQENQE 492
Cdd:pfam17380 571 MEREREMMRQIVESEKARAE 590
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
139-508 |
3.41e-06 |
|
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: 52.36 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 139 SKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEglLEGFKVEKADLQEALGKKEES 218
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE--VKSLQNEKADLDRKLRKLDQE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 219 EQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKE-----------REAGTPVSAGRED-AALQKEVESL 286
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqledwlHSKSKEINQTRDRlAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 287 TRDQWESRKQSEKDRATLLSqmrvleseLEDQLVQHRGC-------AQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAE 359
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSS--------YEDKLFDVCGSqdeesdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 360 RE------HEREEFQQEIKWLEGQLRQATRPRPpgprdsqcAKLDEEVELLQEKLREKldgfNELVIKKDLADQQLLIQE 433
Cdd:TIGR00606 676 NQsccpvcQRVFQTEAELQEFISDLQSKLRLAP--------DKLKSTESELKKKEKRR----DEMLGLAPGRQSIIDLKE 743
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758604 434 EEIKHLEETNENIQRQMAQLQEELEKQRRsteELEVVNSRNSEIEELK---AIIEHLQENQEQLQKAKAEEIEQLHEV 508
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQET---LLGTIMPEEESAKVCLtdvTIMERFQMELKDVERKIAQQAAKLQGS 818
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
131-544 |
4.08e-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: 52.03 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 131 LLDMALDS-SKQLEDARQLHRCVEKEFrhrdEEMAQAVQKQQELLErlreESAAKDRLALELHTAE----GLLEGFKVEK 205
Cdd:pfam05483 381 IITMELQKkSSELEEMTKFKNNKEVEL----EELKKILAEDEKLLD----EKKQFEKIAEELKGKEqeliFLLQAREKEI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 206 ADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEreagtpvsagredaaLQKEVES 285
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD---------------MTLELKK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 286 LTRDQWESRKQSEKdratLLSQMRVLEseledqlvqhrgcaqlaEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHERE 365
Cdd:pfam05483 518 HQEDIINCKKQEER----MLKQIENLE-----------------EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 366 EFQQEIKWLEGQLRQAtrprppgprDSQCAKLDEEVElLQEKLREKLDGFNELVIKKDLAD-QQLLIQEEEIKHLEETNE 444
Cdd:pfam05483 577 SIEYEVLKKEKQMKIL---------ENKCNNLKKQIE-NKNKNIEELHQENKALKKKGSAEnKQLNAYEIKVNKLELELA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 445 NIQRQMAQL----QEELEKQRRSTEELEvvnsrnSEIEELKAIIEHLQENQEQLQKAKAEEI-----------EQLHEVI 509
Cdd:pfam05483 647 SAKQKFEEIidnyQKEIEDKKISEEKLL------EEVEKAKAIADEAVKLQKEIDKRCQHKIaemvalmekhkHQYDKII 720
|
410 420 430
....*....|....*....|....*....|....*
gi 1958758604 510 EKLQSELSLMGPTVHEMSDLpPGSLHTELSCLQAE 544
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSA-KAALEIELSNIKAE 754
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
170-515 |
4.21e-06 |
|
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: 51.82 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 170 QQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSV 249
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 250 LWNQKETFTNEAKEREAGTPVSAGR----------------EDAALQKEVESLTRDQWESRKQSEKDRATLLSQMRVLES 313
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRvleretelermkerakKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 314 ELEDQLVQhrgCAQLAEEVTTLKQQLATLDKHlRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRPPGPRDSQ 393
Cdd:pfam07888 200 SLAQRDTQ---VLQLQDTITTLTQKLTTAHRK-EAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 394 CAKLdeEVELLQEKLREKldgfnELVIKKDLA----DQQLLIQEEEIKH--LEETNENIQRQMAQLQEE-LEKQRRSTE- 465
Cdd:pfam07888 276 QARL--QAAQLTLQLADA-----SLALREGRArwaqERETLQQSAEADKdrIEKLSAELQRLEERLQEErMEREKLEVEl 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758604 466 ------ELEVVNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSE 515
Cdd:pfam07888 349 grekdcNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-377 |
4.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 133 DMALDSSKQLEDARQLhrcvEKEFR--HRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKAdlQE 210
Cdd:COG4913 215 EYMLEEPDTFEAADAL----VEHFDdlERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA--QR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 211 ALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLwnqketftnEAKEREAGtpvsaGREDAALQKEVESLTRDq 290
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDEL---------EAQIRGNG-----GDRLEQLEREIERLERE- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 291 wesRKQSEKDRATLLSQMRVLESELEDQLvqhrgcAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEF--- 367
Cdd:COG4913 354 ---LEERERRRARLEALLAALGLPLPASA------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELrel 424
|
250
....*....|
gi 1958758604 368 QQEIKWLEGQ 377
Cdd:COG4913 425 EAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1377-1643 |
5.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1377 REGQSSRALEELKISLEKQLAQNNQLCVALKHERAAK-DNLQKELQIEASRcEALLAQEKGQLSELRKSLEaERSRSLEL 1455
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKAD-EAKKAEEKKKADEAKKKAE-EAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1456 SEALQHERLLTEQLSRNAQEACARQDTqaqhallrKLKAEKARALELEAMLEKvqKQAAHTQQQLEAQAQERCLELRREK 1535
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEA--------AKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKADAAKKKAEEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1536 EVSGNLRSAVDALQTHKQELGCClEREREKAAWLQAELEQL----SARVKQQEARQ--------DEKRMDRRSSREDLDK 1603
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEEKkkadEAKKKAEEAKKadeakkkaEEAKKAEEAKKKAEEA 1469
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958758604 1604 RKWQRVKEKLRElelQRQRDE--HKIEQLQRLVRELRWKEEA 1643
Cdd:PTZ00121 1470 KKADEAKKKAEE---AKKADEakKKAEEAKKKADEAKKAAEA 1508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-516 |
5.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 154 KEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALEL-HTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQ 232
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 233 LQQASRELLTLKEENSVLWNQ-----------KETFTNEAKEREAGTPVSAGREDAALQKEVESLTRDQWESRKqsEKDR 301
Cdd:COG4717 229 LEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK--EAEE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 302 ATLLSQMRVLESELEDQLVQHRG--CAQLAEEVTTLKQQLATLDKHLRSQRQFMDEqaaereHEREEFQQEIKWL----- 374
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGlpPDLSPEELLELLDRIEELQELLREAEELEEE------LQLEELEQEIAALlaeag 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 375 ---EGQLRQAtrprppGPRDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADqqlliQEEEIKHLEETNENIQRQMA 451
Cdd:COG4717 381 vedEEELRAA------LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELE 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758604 452 QLQEELEKQRRSTEELEvvnsRNSEIEELKAIIEHLQENQEQLQKAKAeEIEQLHEVIEKLQSEL 516
Cdd:COG4717 450 ELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWA-ALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
421-643 |
8.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 421 KKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELE-VVNSRNSEIEELKAIIEHLQENQEQLQKAKA 499
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 500 EEIEQLHEVIEKLQselsLMGPTVHEMSDLPPGSLHTELSCLQAEGMGGQALHNELQAAQAAKGAFGQLladhghSQALE 579
Cdd:COG4942 101 AQKEELAELLRALY----RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL------RAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758604 580 ALQERLQDAEAAAARHLTELEHCVALRQAEVEAMASRIQEFEATLKAKEAIIVQRDLEIDAVNK 643
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1343-1643 |
1.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1343 ENELKVVLEELECERGKGQVLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNNQ-LCVALKHERAAKDNLQKELQ 1421
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKrVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1422 iEASRCE-ALLAQEKGQLSELRKsleAERSRSLELSEALQHERLLTEqlSRNAQEAcaRQDTQAQHALLRKLKAEKARAL 1500
Cdd:PTZ00121 1174 -DAKKAEaARKAEEVRKAEELRK---AEDARKAEAARKAEEERKAEE--ARKAEDA--KKAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1501 ELEAMLEKVQK-QAAHTQQQLEAQAQERCLELRREKEV--SGNLRSAVDALQTHKQELGCCLEREREKA-----AWLQAE 1572
Cdd:PTZ00121 1246 EEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELkkAEEKKKADEAKKAEEKKKADEAKKKAEEAkkadeAKKKAE 1325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758604 1573 LEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRVKEKLRELELQRQRDEHKIEQLQRLVRELRWKEEA 1643
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
152-516 |
1.56e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 152 VEKEFRHRDEEMAQaVQKQQELLERLREESAAK-DRLALELHTAEGLLEGFKVEKADLQEALGK---KEESEQQLIVELE 227
Cdd:TIGR04523 129 LEKQKKENKKNIDK-FLTEIKKKEKELEKLNNKyNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 228 DLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREAgtpvsagrEDAALQKEVESLTRDQWESRKQSEkDRATLLSQ 307
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT--------EISNTQTQLNQLKDEQNKIKKQLS-EKQKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 308 MRVLESELEDQLvqhrgcAQLAEEVTTLKQQ-LATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRP 386
Cdd:TIGR04523 279 NNKKIKELEKQL------NQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 387 P-----GPRDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEE-------EIKHLEETNENIQRQMAQLQ 454
Cdd:TIGR04523 353 NsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqqkdeQIKKLQQEKELLEKEIERLK 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758604 455 EELEKQRRSTEELE-VVNSRNSEIEELKAIIEHLQENQEQLQKakaeEIEQLHEVIEKLQSEL 516
Cdd:TIGR04523 433 ETIIKNNSEIKDLTnQDSVKELIIKNLDNTRESLETQLKVLSR----SINKIKQNLEQKQKEL 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-642 |
1.57e-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: 50.45 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 137 DSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKE 216
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 217 ESEQQLIVELEDLRKQLQQASRELLTLKEEnsvLWNQKETFTNEAKEREagtpvSAGREDAALQKEVESLTRDQWESRKQ 296
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQE---LYDLKEEYDRVEKELS-----KLQRELAEAEAQARASEERVRGGRAV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 297 SEKDRAT------LLSQMRVLESE-----------------LEDQLVQHRgCAQLAEEVTTLKQQLATLDKHLRSQR--- 350
Cdd:TIGR02169 513 EEVLKASiqgvhgTVAQLGSVGERyataievaagnrlnnvvVEDDAVAKE-AIELLKRRKAGRATFLPLNKMRDERRdls 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 351 ------------QFMDEQAAEREHEREEFQQEI--------KWLEGQLRQATRP--------------RPPGPRDSQCAK 396
Cdd:TIGR02169 592 ilsedgvigfavDLVEFDPKYEPAFKYVFGDTLvvedieaaRRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 397 LDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEV-VNSRNS 475
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdLSSLEQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 476 EIEELKAIIEHLQENQEQLQKAKAEEIEQL--------HEVIEKLQSELSLMGPTVHEMS------DLPPGSLHTELSCL 541
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALndlearlsHSRIPEIQAELSKLEEEVSRIEarlreiEQKLNRLTLEKEYL 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 542 QAEGMGGQALHNELQAAQAAKGAfgQLLADHGHSQALEALQERLQDAEAAAARHLTELEHCVALRQAEVEAMASRIQEFE 621
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEK--EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
570 580
....*....|....*....|.
gi 1958758604 622 ATLKAKEAIIVQRDLEIDAVN 642
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALE 930
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1400-1643 |
1.63e-05 |
|
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: 50.12 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1400 NQLCVALKHERAAKDNLQKElQIEASRCEALLAQEKGQLSEL---RKSLEAERSRSLELSEAL----QHERLLTE---QL 1469
Cdd:pfam17380 272 NQLLHIVQHQKAVSERQQQE-KFEKMEQERLRQEKEEKAREVerrRKLEEAEKARQAEMDRQAaiyaEQERMAMErerEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1470 SRNAQEACARQDTQAQHallRKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEVSGNLRSAV---- 1545
Cdd:pfam17380 351 ERIRQEERKRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEqira 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1546 ---DALQTHKQELGCCLEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRVKEKLRELELQRQR 1622
Cdd:pfam17380 428 eqeEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260
....*....|....*....|.
gi 1958758604 1623 DEHKIEQLQRLVRELRWKEEA 1643
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKA 528
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-517 |
2.16e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 168 QKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEEN 247
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 248 SVLWNQ--KETFTNEAKE-REAGTPVSAGRED-AALQKEVESLTRDqwesRKQSEKDRATLLSQMRVLESELEDQLVQHr 323
Cdd:TIGR04523 305 EQDWNKelKSELKNQEKKlEEIQNQISQNNKIiSQLNEQISQLKKE----LTNSESENSEKQRELEEKQNEIEKLKKEN- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 324 gcAQLAEEVTTLKQQLATLDKHLRSQR---QFMDEQAAEREHEREEFQQEIKWLEgqlrqatrprppgprdSQCAKLDEE 400
Cdd:TIGR04523 380 --QSYKQEIKNLESQINDLESKIQNQEklnQQKDEQIKKLQQEKELLEKEIERLK----------------ETIIKNNSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 401 VELLQEKLREKLDGFNELVIKKDladqqllIQEEEIKHLEETNENIQRQMAQLQEELEKQrrsTEELEVVNSRNSEIEEL 480
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSK---EKELKKLNEEKKELEEK 511
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958758604 481 kaiIEHLQENQEQLQkakaEEIEQLHEVIEKLQSELS 517
Cdd:TIGR04523 512 ---VKDLTKKISSLK----EKIEKLESEKKEKESKIS 541
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
171-514 |
2.90e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.08 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 171 QELLERLR---EESAAKDRLALE--LHTAEGLLEGFKVEKA-------------------DLQEALGKKEESEQQLIVEL 226
Cdd:pfam06160 44 QEKFEEWRkkwDDIVTKSLPDIEelLFEAEELNDKYRFKKAkkaldeieellddieedikQILEELDELLESEEKNREEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 227 EDLRKQLQQASRELLT-----------LKEENSVLWNQKETFTNEAkerEAGTPVSAGREDAALQKEVESLtrdqwesrk 295
Cdd:pfam06160 124 EELKDKYRELRKTLLAnrfsygpaideLEKQLAEIEEEFSQFEELT---ESGDYLEAREVLEKLEEETDAL--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 296 qsEKDRATLLSQMRVLESELEDQLVQHR-GCAQLAEEvttlKQQLATLDkhlrsqrqfmdeqaaerehereeFQQEIKWL 374
Cdd:pfam06160 192 --EELMEDIPPLYEELKTELPDQLEELKeGYREMEEE----GYALEHLN-----------------------VDKEIQQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 375 EGQLRQATrprppgprdSQCAKLD-EEVELLQEKLREKLDGFNEL----VIKKDLADQQLLIQEEEIKHLEETNENIQRQ 449
Cdd:pfam06160 243 EEQLEENL---------ALLENLElDEAEEALEEIEERIDQLYDLlekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 450 MAQLQ-------EELEKQRRSTEELEVVNSRNSEIEELKA--------IIEHLQENQEQLqkakaEEIEQLH-EVIEKLQ 513
Cdd:pfam06160 314 LERVQqsytlneNELERVRGLEKQLEELEKRYDEIVERLEekevayseLQEELEEILEQL-----EEIEEEQeEFKESLQ 388
|
.
gi 1958758604 514 S 514
Cdd:pfam06160 389 S 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1142-1514 |
2.93e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1142 EVFAREQENAELQPRPYSSDLGDYNSLVKKLEKVIQEQGDLQKVREHAcLPDRSSLLAEIQALRAQLRMTHLQNQekLQQ 1221
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAE--LAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1222 LCAALTSTEARGSQREHQLRRQVELLAYKVEQEKCIANDLQKTLSKEQEAASDVRKRLMVEQGAVQDLKSELHACKQENT 1301
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1302 NLLESLDKVQQEVLRLRYGHVTWSYSGTSSASAGRAVLDGKENELK------------------VVLEELECERGKGQVL 1363
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvlgllaLLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1364 QAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNNQLCVALKH---ERAAKDNLQKELQIEAS--RCEALLAQEK-GQ 1437
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqeLLREAEELEEELQLEELeqEIAALLAEAGvED 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 1438 LSELRKSLEAERsrslELSEALQHERLLTEQLSRNAQEACARQDTQAQHALLRKLKAEKARALELEAMLEKVQKQAA 1514
Cdd:COG4717 384 EEELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1511 |
3.23e-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: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1199 AEIQALRAQLRMTHLQNQEKLQQLCAALTSTEARGSQ------REHQLRRQVELLAYKVEQEKCIANDLQKTLSKEQEAA 1272
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1273 SDVRKRLMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEvlrlryghvtwsysgtssASAGRAVLDGKENELKVVLEE 1352
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE------------------LKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1353 LecergkgqVLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNNQlcvALKHERAAKDNLQKELQI---EASRCEA 1429
Cdd:TIGR02168 819 A--------ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA---EIEELEELIEELESELEAllnERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1430 LLAQEKGQLSELRKSLEAERSRSLELSEALQHERLLTEQLSRNAQEACARQDTQAQHAllrklkAEKARaLELEAMLEKV 1509
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYS-LTLEEAEALE 960
|
..
gi 1958758604 1510 QK 1511
Cdd:TIGR02168 961 NK 962
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-600 |
3.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 131 LLDMALDSSKQLEDARQLHRCVEKEFRHRD--EEMAQAVQKQQELLERLREESAAKDRLAL-----ELHTAEGLLEGFKV 203
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 204 EKADLQEALGKKEESEQQLIVELEDLRKQLQQAS-RELLTLKEENSVLWNQKETFTNEAKE-----REAGTPVSAGRED- 276
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARleallAALGLPLPASAEEf 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 277 AALQKEVESLTRDQWESRKQSEKDRATLLSQMRVLESELEdqlvqhrgcaQLAEEVTTLKQQLATLDKHLRSQRQFMDEQ 356
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------ELEAEIASLERRKSNIPARLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 357 AAEREHE-----------------------------------REEFQQEIKW-----LEGQLR-QATRPRPPGPRDSQCA 395
Cdd:COG4913 453 LGLDEAElpfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAALRWvnrlhLRGRLVyERVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 396 K--LDEEVEL--------LQEKLREKLD-------------------------------------GFNELVI------KK 422
Cdd:COG4913 533 PdsLAGKLDFkphpfrawLEAELGRRFDyvcvdspeelrrhpraitragqvkgngtrhekddrrrIRSRYVLgfdnraKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 423 DLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEV---VNSRNSEIEELKAIIEHLQEN-------QE 492
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASsddlaalEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 493 QLQKAKAeEIEQLHEVIEKLQSELSLMGPTVHEMSDLPPgSLHTELSclQAEGMGGQALHNELQAaqaakgAFGQLLADH 572
Cdd:COG4913 693 QLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELD-ELQDRLE--AAEDLARLELRALLEE------RFAAALGDA 762
|
570 580
....*....|....*....|....*...
gi 1958758604 573 GHSQALEALQERLQDAEAAAARHLTELE 600
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELE 790
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
425-640 |
3.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 425 ADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVvnsrnsEIEELKAIIEHLQENQEQLQKAKAEEIEQ 504
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA------ELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 505 LHEVIEKLQSELSLMGPTVHEMSDLPPGSLHTELSCLQAEGMGGQALHNELQAAQAAKGAFGQLLADHGhsQALEALQER 584
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL--AELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758604 585 LQDAEAAAARHLTELEHCVALRQAEVEAMASRIQEFEATLKAKEAIIVQRDLEIDA 640
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
157-519 |
3.84e-05 |
|
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: 48.89 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 157 RHRDEEMAQA------VQKQQELLERLREESAAKDRLA---LELHTAEGLLEGFKVEKADLQEALGKKEE------SEQQ 221
Cdd:TIGR00606 557 RHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAklnKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQD 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 222 LIVELEDLRKQLQQASRELLTLKEENSVLwnqKETFTNEAKEREAGTPVSagREDAALQKEVESLTRDQWESRKQSEKDR 301
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVY---SQFITQLTDENQSCCPVC--QRVFQTEAELQEFISDLQSKLRLAPDKL 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 302 ATLLSQMRVLESELEDQLVQHRGCAQLAE----EVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQE------- 370
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdv 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 371 --IKWLEGQLRQATRPRPPGPRDSQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQR 448
Cdd:TIGR00606 792 tiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758604 449 QMAQLQEELEKQRRSTEELEV----VNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSELSLM 519
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVElsteVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1377-1631 |
4.71e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1377 REGQSSRALEELKISLEKQLAQNNQLCVALKHERAAKDNLQKELQI---EASRCEALLAQEKGQLSELRKSLEAERSRSL 1453
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQleqEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1454 ELSEALQ--HERLLTEQLSRNAQEA-CARQDTQAQHALLRKLKAE----KARALELEAMLEKVQkqaahtqqqleaqaqe 1526
Cdd:TIGR02169 762 ELEARIEelEEDLHKLEEALNDLEArLSHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLT---------------- 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1527 rcLELRREKEVSGNLRSAVDALQTHKQELGCCLEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKrkw 1606
Cdd:TIGR02169 826 --LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE--- 900
|
250 260
....*....|....*....|....*
gi 1958758604 1607 qrVKEKLRELELQRQRDEHKIEQLQ 1631
Cdd:TIGR02169 901 --LERKIEELEAQIEKKRKRLSELK 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-631 |
7.75e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 201 FKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELltlkeensvlwNQKETFTNEAKEREAgtpvsagREDAALQ 280
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER-----------EKAERYQALLKEKRE-------YEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 281 KEVESLTRdqweSRKQSEKDRATLLSQMRVLESELEDqlvqhrgcaqLAEEVTTLKQQLATLDKHLRSQRQfmDEQAAer 360
Cdd:TIGR02169 230 KEKEALER----QKEAIERQLASLEEELEKLTEEISE----------LEKRLEEIEQLLEELNKKIKDLGE--EEQLR-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 361 ehereeFQQEIKWLEGQLRQAtrprppgpRDSQCAKLDEeVELLQEKLREkldgfnelvikkdlADQQLLIQEEEIKHLE 440
Cdd:TIGR02169 292 ------VKEKIGELEAEIASL--------ERSIAEKERE-LEDAEERLAK--------------LEAEIDKLLAEIEELE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 441 ETNENIQRQMAQLQEELEKQRRSTEELEvvnsrnSEIEELKAIIEHLQENQEQLQkakaEEIEQLHEVIEKLQSELSLMG 520
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLR------AELEEVDKEFAETRDELKDYR----EKLEKLKREINELKRELDRLQ 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 521 PTVHEmsdlppgsLHTELSCLQAEGMGGQALHNELQAAQAAKGA--------FGQLLADHG-HSQALEALQERLQDAEaa 591
Cdd:TIGR02169 413 EELQR--------LSEELADLNAAIAGIEAKINELEEEKEDKALeikkqewkLEQLAADLSkYEQELYDLKEEYDRVE-- 482
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958758604 592 aaRHLTELEHCVALRQAEVEAMASRIQEFEATLKAKEAII 631
Cdd:TIGR02169 483 --KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
397-515 |
9.51e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 397 LDEEVELLQEKLREKLDGFNELVIKKDLADQQLLiqEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELE-------- 468
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEE--EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLErelsears 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 469 ----------VVNSRNSEIEELKAIIEHLQENQEQLQkakaEEIEQLHEVIEKLQSE 515
Cdd:COG2433 456 eerreirkdrEISRLDREIERLERELEEERERIEELK----RKLERLKELWKLEHSG 508
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
401-624 |
9.79e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 401 VELLQEKLREKLDGFNELVIKKDLAD---------QQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVn 471
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDlherlngleSELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 472 srNSEIEELKAIIEHLQENQEQLqkakAEEIEQLHEVIEKLQSELSLMGPTVhEMSDLPPGSLHTELSCLQAEgmgGQAL 551
Cdd:PRK02224 257 --EAEIEDLRETIAETEREREEL----AEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREELEDR---DEEL 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758604 552 HNELQAAQAAKGAFGQLLadHGHSQALEALQERLQDAEAAAARHLTELEHC---VALRQAEVEAMASRIQEFEATL 624
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEA--ESLREDADDLEERAEELREEAAELESELEEAreaVEDRREEIEELEEEIEELRERF 400
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-516 |
1.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 283 VESLTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHRGCAQLAEEVTTLKQQLATldkhlrsqrqfmdeqaaereh 362
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE--------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 363 ereeFQQEIKWLEGQLRQATRPRPPGPRDSQCAKLDEEVELLQEKLrekldgfnelvikkdladQQLLIQEEEIKHLEET 442
Cdd:COG4717 107 ----LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL------------------EELEERLEELRELEEE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758604 443 NENIQRQMAQLQEELEKQRR--STEELEVVNSRNSEIEELKAIIEHLQENQEQLQkakaEEIEQLHEVIEKLQSEL 516
Cdd:COG4717 165 LEELEAELAELQEELEELLEqlSLATEEELQDLAEELEELQQRLAELEEELEEAQ----EELEELEEELEQLENEL 236
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1373-1638 |
1.09e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1373 RHLQREGQSSRALEELKISLEKQlaqnnQLCVALKHERAAkdnlqkELQIEASRCEALLAQEKGQLSELRKSLEAERSRS 1452
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQ-----NEVVEEADEQQE------ENEARAEAAEEEVDELKSQLADYQQALDVQQTRA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1453 LELSEALQ----------------------------HERLLTEQLSRNAQEACARQDTQAQHA----LLRKLKAEKAR-- 1498
Cdd:PRK04863 414 IQYQQAVQalerakqlcglpdltadnaedwleefqaKEQEATEELLSLEQKLSVAQAAHSQFEqayqLVRKIAGEVSRse 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1499 ----ALELEAMLEKVQKQAAHTQQQLEAQAqerclELRREKEvsgNLRSAVDALQTHKQELGCCLEREREKAAwLQAELE 1574
Cdd:PRK04863 494 awdvARELLRRLREQRHLAEQLQQLRMRLS-----ELEQRLR---QQQRAERLLAEFCKRLGKNLDDEDELEQ-LQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1575 QLSARVKQQEARQDEKRMDRRSSREDLDKR---------KWQRVKEKLRELELQ-------RQRDEHKIEQLQRLVRELR 1638
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARiqrlaarapAWLAAQDALARLREQsgeefedSQDVTEYMQQLLERERELT 644
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
395-515 |
1.14e-04 |
|
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: 45.69 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 395 AKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQ---------LQEELEKQRRSTE 465
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRIS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758604 466 ELE--------VVNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSE 515
Cdd:COG1579 107 DLEdeilelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
204-515 |
1.14e-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: 47.27 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 204 EKADLQEALGKKEESEQQLIVELEDLRKQLQQasrELLTLKEENSVLWNQKEtftnEAKEREAGTPVSAGREDAALQKEV 283
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ---ELKLKEQAKKALEYYQL----KEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 284 ESLTRDQWESRKQSEKDRATLLSQM-------RVLESELEDQLVQHRGCAQLAEEVTTLKQQLATLD---KHLRSQRQFM 353
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEeklaqvlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErrkVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 354 DEQAAEREHEREEFQQEIKWLEGQLRQATRPRppgprdsqcAKLDEEVELLQEKLREKLDGFNELVIKKDLAdQQLLIQE 433
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKR---------EAEEEEEEELEKLQEKLEQLEEELLAKKKLE-SERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 434 EEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEvvnsRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQ 513
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEE----KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
..
gi 1958758604 514 SE 515
Cdd:pfam02463 466 EL 467
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
108-501 |
1.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 108 ENTQECEQPIRKVYQSLSTAVEglLDMALDSSKQLEDARQLHRCVEK--EFRHRDEEMAQAVQKQQELLERLREESAAKD 185
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 186 rlALELHTAEGLLEgfKVEKADLQEALGKKEESEQQlivELEDLRKQlQQASRELLTLKEENSVLWNQKETFTNEAKERE 265
Cdd:PTZ00121 1466 --AEEAKKADEAKK--KAEEAKKADEAKKKAEEAKK---KADEAKKA-AEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 266 AGTPVSAGREDAALQKEVEslTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHR--GCAQLAEEVTTLKQQLATLD 343
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieEVMKLYEEEKKMKAEEAKKA 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 344 KHLRSQRQFM---DEQAAEREHEREEFQQEIKWLEgQLRQA-----TRPRPPGPRDSQCAKLDEEVELLQEKLREKLDGF 415
Cdd:PTZ00121 1616 EEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAE-ELKKAeeenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 416 NELVIKKDLADQQLLIQEEEIKHLEE---TNENIQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQE 492
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
....*....
gi 1958758604 493 QLQKAKAEE 501
Cdd:PTZ00121 1775 KEKEAVIEE 1783
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1262-1637 |
1.29e-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: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1262 QKTLSKEQEAAsDVRKRLMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEVLRLRYGHvtwsysgtssasagravldg 1341
Cdd:TIGR02168 670 SSILERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-------------------- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1342 keNELKVVLEELECERgkgqvlqaqqeeqqLRHLQREGQSSRALEELKISLEKQLAQNNQLCVALKHERAAKDNLQKELQ 1421
Cdd:TIGR02168 729 --SALRKDLARLEAEV--------------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1422 ieasRCEALLAQEKGQLSELRKSLEAERSRSLELSEALQHerlLTEQLSRNAQEAcarQDTQAQHALLRKLKAEKARALE 1501
Cdd:TIGR02168 793 ----QLKEELKALREALDELRAELTLLNEEAANLRERLES---LERRIAATERRL---EDLEEQIEELSEDIESLAAEIE 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1502 -LEAMLEKVQKQAAHTQQQLEAQAQERcLELRREKEvsgNLRSAVDALQTHKQELGCCLEREREKAAWLQAELEQLSARV 1580
Cdd:TIGR02168 863 eLEELIEELESELEALLNERASLEEAL-ALLRSELE---ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 1581 KQQEARQDEKRMDrrssredldkrKWQRVKEKLRELELQRQRDEHKIEQLQRLVREL 1637
Cdd:TIGR02168 939 DNLQERLSEEYSL-----------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1162-1634 |
1.59e-04 |
|
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: 47.04 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1162 LGDYNSLVKKLEKVIQEQGDLQKVRehaclpdrssllaeiqalRAQLRMTHLQNQEKLQQLCA---ALTSTEARGSQREH 1238
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQ------------------KFYLRQSVIDLQTKLQEMQMerdAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1239 QLRRQVELLAYKVEQEKCIANDLQKTLSKEQEaasDVRKRLMVEQGAVQDLKS--------------------------- 1291
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIE---QLRKMMLSHEGVLQEIRSilvdfeeasgkkiyehdsmstmhfrsl 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1292 ---------------------------ELHACKQENTNLLE-SLDKVQQEVLRLRYGHVTWSYSGTSSASAGRAVLDGKE 1343
Cdd:pfam15921 219 gsaiskilreldteisylkgrifpvedQLEALKSESQNKIElLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1344 NELKVVLEELECERGKgQVLQAQQEEQQLRHLQREGQSSRALEELKI-SLEKQLAQNNQlcvALKHERAAKDNLQKELQI 1422
Cdd:pfam15921 299 SQLEIIQEQARNQNSM-YMRQLSDLESTVSQLRSELREAKRMYEDKIeELEKQLVLANS---ELTEARTERDQFSQESGN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1423 EASRCEALLAQEKGQLSELrkSLEAERSRSL---ELSEALQHERLLTEQLSRNaqeacarQDTQAQHALLRKLKAEKARA 1499
Cdd:pfam15921 375 LDDQLQKLLADLHKREKEL--SLEKEQNKRLwdrDTGNSITIDHLRRELDDRN-------MEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1500 LE-----LEAMLEKVQKQAAHTQQQLEAQAQERCL--ELRREKEVSGNLRSAVDALQTHKQelgcclEREREKAAwLQAE 1572
Cdd:pfam15921 446 MErqmaaIQGKNESLEKVSSLTAQLESTKEMLRKVveELTAKKMTLESSERTVSDLTASLQ------EKERAIEA-TNAE 518
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758604 1573 LEQLSARV--KQQEARQDEKRMDR-RSSREDLDKRKWQrVKEKLRELELQRQrdehKIEQLQRLV 1634
Cdd:pfam15921 519 ITKLRSRVdlKLQELQHLKNEGDHlRNVQTECEALKLQ-MAEKDKVIEILRQ----QIENMTQLV 578
|
|
| CorA |
pfam01544 |
CorA-like Mg2+ transporter protein; The CorA transport system is the primary Mg2+ influx ... |
368-517 |
1.65e-04 |
|
CorA-like Mg2+ transporter protein; The CorA transport system is the primary Mg2+ influx system of Salmonella typhimurium and Escherichia coli. CorA is virtually ubiquitous in the Bacteria and Archaea. There are also eukaryotic relatives of this protein. The family includes the MRS2 protein from yeast that is thought to be an RNA splicing protein. However its membership of this family suggests that its effect on splicing is due to altered magnesium levels in the cell.
Pssm-ID: 460246 [Multi-domain] Cd Length: 292 Bit Score: 45.77 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 368 QQEIKWLEgQLRQATRPRPPGPRDSQcakldeevELLQEKLREKLDGFNELVikkDLADQQLLIQEEEIkhLEETNENIQ 447
Cdd:pfam01544 85 HEPLPALD-EVRKRLTLLGGGPLDPG--------DLLYRLLDEIVDRFLELL---EKLEDELDELEDEL--EDETNNELL 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 448 RQMAQLQEELEK-------QRRSTEELEVVNSRNSEIEELKAIIEHLQENQEQLqkakAEEIEQLHEVIEKLQSELS 517
Cdd:pfam01544 151 RELAALRRSLVYlrrsllpQRDVLNRLLRREDDPLLDDEQKEYLRDLLDRLERL----LEDLDALRERLRSLQDEYS 223
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
395-515 |
2.01e-04 |
|
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: 45.78 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 395 AKLDEEVELLQE---KLREKLDGFN-ELVIKKDLA------DQQLL-IQEEEIKHLEETNENIQRQMAQLQEELEkqrrs 463
Cdd:smart00787 161 KLLMKELELLNSikpKLRDRKDALEeELRQLKQLEdeledcDPTELdRAKEKLKKLLQEIMIKVKKLEELEEELQ----- 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958758604 464 teELE-VVNSRNSEIEELKAIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSE 515
Cdd:smart00787 236 --ELEsKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
137-486 |
2.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 137 DSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGLLEGFKVEKADLQEALGKKE 216
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 217 ESEQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEREAgtpvSAGREDAALQKEVESLTRDQWESRKq 296
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE----EAKKAEEDEKKAAEALKKEAEEAKK- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 297 sekdratlLSQMRVLESELEDQLVQHRGcaqlAEEVTTLKQqlatldkhlrsqrqfmdEQAAEREHEREEFQQEIKWLEG 376
Cdd:PTZ00121 1704 --------AEELKKKEAEEKKKAEELKK----AEEENKIKA-----------------EEAKKEAEEDKKKAEEAKKDEE 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 377 QLRQATRPRPpgprdsqcakldEEVELLQEKLREKLDGFNELVIKKDlaDQQLLIQEEEIKHLEETNENIQR--QMAQLQ 454
Cdd:PTZ00121 1755 EKKKIAHLKK------------EEEKKAEEIRKEKEAVIEEELDEED--EKRRMEVDKKIKDIFDNFANIIEggKEGNLV 1820
|
330 340 350
....*....|....*....|....*....|..
gi 1958758604 455 EELEKQRRSTEELEVVNSRNSEIEELKAIIEH 486
Cdd:PTZ00121 1821 INDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-513 |
2.21e-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: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 125 STAVEGLLDMALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERlrEESAAKDRLALELHTAEGLLEGFKVE 204
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK--KEQREKEELKKLKLEAEELLADRVQE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 205 KADLQEALGKKEESEQQLIVELEDLRKQLQ-QASRELLTLKEENSVLWNQKETFTNEAKEREAGTPVSAG----REDAAL 279
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKeEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQeeelRALEEE 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 280 QKEVESLTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHRGCAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAE 359
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 360 REHEREEFQQEIKWLEGQlrqatrprppgpRDSQCAKLDEEVELLQEKLREKLDGFNELVIKkdladqqLLIQEEEIKHL 439
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQ------------KLNLLEEKENEIEERIKEEAEILLKYEEEPEE-------LLLEEADEKEK 950
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758604 440 EETNENIQRQMAQLQEELEkqrrstEELEVVNSRNSEIEELKAIIEHLQEnqEQLQKAKAEEIEQLHEVIEKLQ 513
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAK------EELGKVNLMAIEEFEEKEERYNKDE--LEKERLEEEKKKLIRAIIEETC 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1414-1638 |
2.61e-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: 46.20 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1414 DNLQKELQIEASRCEAL---LAQEKGQLSELRKSLEAERSRSLELSEALQHERLLTEQLsRNAQEACARQDTQAQHALLR 1490
Cdd:TIGR02168 680 EELEEKIEELEEKIAELekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARL-EAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1491 kLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEVSGNLRSAVDALQTHKQELGCCLEREREKAAWLQ 1570
Cdd:TIGR02168 759 -LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1571 AELEQLSARVKQQEARQDEKRMDRRSSREDLDK--RKWQRVKEKLRELELQRQRDEHKIEQLQRLVRELR 1638
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEEleSELEALLNERASLEEALALLRSELEELSEELRELE 907
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-637 |
3.16e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 141 QLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREES--------------AAKDRLALELHTAEGLLE------- 199
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaeemrarlaARKQELEEILHELESRLEeeeersq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 200 GFKVEK-------ADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLwnQKETFTNEAKEREAGTPVSA 272
Cdd:pfam01576 93 QLQNEKkkmqqhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL--SKERKLLEERISEFTSNLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 273 GREDA----ALQKEVESLTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHrgcAQLAEEVTTLKQQLATLDKHLRS 348
Cdd:pfam01576 171 EEEKAkslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI---AELQAQIAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 349 QRQFMDE---QAAEREHEREEFQQEIKWLEGQLRQATRPRppGPRDSQCAKLDEEVELLQEKLREKLDGFN---ELVIKK 422
Cdd:pfam01576 248 ALARLEEetaQKNNALKKIRELEAQISELQEDLESERAAR--NKAEKQRRDLGEELEALKTELEDTLDTTAaqqELRSKR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 423 --DLADQQLLIQEEEIKHLEETNENIQRQMAQ---LQEELEKQRRS------------------TEELEVVNSRNSEIEE 479
Cdd:pfam01576 326 eqEVTELKKALEEETRSHEAQLQEMRQKHTQAleeLTEQLEQAKRNkanlekakqalesenaelQAELRTLQQAKQDSEH 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 480 LKAIIE-HLQENQEQLQKAKAEEIEqLHEVIEKLQSELSLMGPTVHEmSDLPPGSLHTELSCLQAEGMGGQALhneLQAA 558
Cdd:pfam01576 406 KRKKLEgQLQELQARLSESERQRAE-LAEKLSKLQSELESVSSLLNE-AEGKNIKLSKDVSSLESQLQDTQEL---LQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 559 QAAKGAFGQLLADHGHSQAleALQERLQDAEAAAARhlteLEHCVALRQAEVEAMASRIQEFEATLKAKEAII--VQRDL 636
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERN--SLQEQLEEEEEAKRN----VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKkrLQREL 554
|
.
gi 1958758604 637 E 637
Cdd:pfam01576 555 E 555
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1487-1643 |
4.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1487 ALLRKLKAEKARALELEAMLEKVQKQAAHtqQQLEAQAQERCLELRREKEVSGNLRSAVDALQ-THKQELgccLEREREK 1565
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL--LEPIRELAERYAAARERLAELEYLRAALRLWFaQRRLEL---LEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1566 aawLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRV---KEKLRELELQRQRDEHKIEQLQRLVRELRWKEE 1642
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeqlEREIERLERELEERERRRARLEALLAALGLPLP 376
|
.
gi 1958758604 1643 A 1643
Cdd:COG4913 377 A 377
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-518 |
4.26e-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: 45.73 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 108 ENTQECEQPIRKVYQSLSTAVEGLLDM--ALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKD 185
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESaqSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 186 RLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNEAKEre 265
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR-- 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 266 agtpvsagredaaLQKEVESLTRDQWESRKQSEKDRATLLSQMRVLESELEDQLVQHRgcaqLAEEVTTLKQQLATLDK- 344
Cdd:TIGR00618 596 -------------LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE----LALKLTALHALQLTLTQe 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 345 ----HLRSQRQFMDEQAAERehereefQQEIKWLEGQLRQATRPRPPGPRDSQCAKLDEEVELLQEKLREKldgfnelvI 420
Cdd:TIGR00618 659 rvreHALSIRVLPKELLASR-------QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE--------I 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 421 KKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQEQLQKAKAE 500
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKT 803
|
410
....*....|....*...
gi 1958758604 501 EIEQLHEVIEKLQSELSL 518
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNL 821
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-517 |
4.38e-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: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 392 SQCAKLDEEVELLQEKLREKLDGFNELVikkdladQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELE-VV 470
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKT-------TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkQL 290
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958758604 471 NSRNSEIEELKaiiehlQENQEQLQKAKAEEIEQLHEVIEKLQSELS 517
Cdd:TIGR04523 291 NQLKSEISDLN------NQKEQDWNKELKSELKNQEKKLEEIQNQIS 331
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1122-1615 |
7.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1122 EKEALGTHLTWSEELLQAIQEVFAREQENAELQprpyssdLGDYNSLVKKLEKVIQEQgDLQKVREHACLPDRSSLLAEI 1201
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEA-------QAEEYELLAELARLEQDI-ARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1202 QALRAQLRMTH---LQNQEKLQQLCAALTSTEARGSQREHQLRRQVELLAYKVEQEKCIANDLQKTLSKEQEAASDVRKR 1278
Cdd:COG1196 326 AELEEELEELEeelEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1279 LMVEQGAVQDLKSELHACKQENTNLLESLDKVQQEVLRLRyghvtwsysgtsSASAGRAVLDGKENELKVVLEELEcerg 1358
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE------------EAAEEEAELEEEEEALLELLAELL---- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1359 kgqvLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNNQLcVALKHERAAKDNLQKELQIE--------------- 1423
Cdd:COG1196 470 ----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG-VKAALLLAGLRGLAGAVAVLigveaayeaaleaal 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1424 --------------ASRCEALLAQEK-GQLSELRKSLEAERSRSLELSEALQHE--RLLTEQLSRNAQEACARQDTQAQH 1486
Cdd:COG1196 545 aaalqnivveddevAAAAIEYLKAAKaGRATFLPLDKIRARAALAAALARGAIGaaVDLVASDLREADARYYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1487 ALLRKLKAEKA--RALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEVSGNLRSAVDALQTHKQELGCCLERERE 1564
Cdd:COG1196 625 RTLVAARLEAAlrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1565 KAAWLQAELEQLSARVKQQEARQDEKRMDRRSSR-------------------EDLDKRKWQRVKEKLRE 1615
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLeelleeeelleeealeelpEPPDLEELERELERLER 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1229-1642 |
9.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1229 TEARGSQREHQLRRQVELLAYKVEQEKCIANDLQKTLSKEQEAASDVRK--RLMVEQGAVQDLKSELHA-CKQENTNLLE 1305
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGlTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1306 SLDKVQQEVLRLRyghvtwsysgtSSASAGRAVLDGKENELKVVLEELECERGKGQVLQAQQEEQQLRHLQREgqssrAL 1385
Cdd:PRK03918 395 ELEKAKEEIEEEI-----------SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE-----YT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1386 EELKiSLEKQLAQnnqlcvALKHERAAKDNLqKELQIEASRCEALLAQEK--GQLSELRKSLEAERSRSLElSEALQHER 1463
Cdd:PRK03918 459 AELK-RIEKELKE------IEEKERKLRKEL-RELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELE-KKAEEYEK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1464 LLTEQLSRNAQEACARQDTQAQHALLRKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEVSGNLRS 1543
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1544 AVDALQTHKQELGCC---LEREREKAAWLQAELEQLSARVKQQEARQDEKRMDRRSSREDLDKRKWQRVKEKLRELELQR 1620
Cdd:PRK03918 610 AEKELEREEKELKKLeeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
410 420
....*....|....*....|..
gi 1958758604 1621 QRDEHKIEQLQRLVRELRWKEE 1642
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKK 711
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
142-641 |
1.02e-03 |
|
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: 44.34 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 142 LEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAK-DRLALELHTAEGLLEGFKVEKADLQEALGKK-EESE 219
Cdd:pfam15921 129 MADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiYEHD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 220 QQLIVELEDLRKQLQQASRELLT----LKEENSVLWNQKETFTNEAKER-EAGTPVSAGREDAALQK---EVESLTRDQW 291
Cdd:pfam15921 209 SMSTMHFRSLGSAISKILRELDTeisyLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRIEQLISEhevEITGLTEKAS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 292 ESRKQSEkdraTLLSQMRVLESELEDQLVQH-RGCAQLAEEVTTLKQQLATLDK-------HLRSQRQFMDEQAAEREHE 363
Cdd:pfam15921 289 SARSQAN----SIQSQLEIIQEQARNQNSMYmRQLSDLESTVSQLRSELREAKRmyedkieELEKQLVLANSELTEARTE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 364 REEFQQEIKWLEGQLRQATrprppgprdSQCAKLDEEVELLQEKLRE--KLDGFNELVI---KKDLADQQLLIQEEE--I 436
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLL---------ADLHKREKELSLEKEQNKRlwDRDTGNSITIdhlRRELDDRNMEVQRLEalL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 437 KHLE-ETNENIQRQMAQLQ---EELEKQRRSTEELEvvnsrnSEIEELKAIIEHLQ------ENQEQLQKAKAEEIEQLH 506
Cdd:pfam15921 436 KAMKsECQGQMERQMAAIQgknESLEKVSSLTAQLE------STKEMLRKVVEELTakkmtlESSERTVSDLTASLQEKE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 507 EVIEKLQSELSLMGPTVhemsDLPpgslHTELSCLQAEGmggqalhNELQAAQAAKGAFGQLLAdhGHSQALEALQERLQ 586
Cdd:pfam15921 510 RAIEATNAEITKLRSRV----DLK----LQELQHLKNEG-------DHLRNVQTECEALKLQMA--EKDKVIEILRQQIE 572
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758604 587 DAEAAAARH-LTELEHCVALRQAEVEAMASR--IQEFEATLKAKEAIIVQ-----RDLEIDAV 641
Cdd:pfam15921 573 NMTQLVGQHgRTAGAMQVEKAQLEKEINDRRleLQEFKILKDKKDAKIRElearvSDLELEKV 635
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
398-515 |
1.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 398 DEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEetneniqRQMAQLQEELEKqrrsteELEVVNSRNSEI 477
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLE-------KRLLQKEENLDR------KLELLEKREEEL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958758604 478 EELKAIIEHLQEN----QEQLQKAKAEEIEQLhEVIEKLQSE 515
Cdd:PRK12704 113 EKKEKELEQKQQElekkEEELEELIEEQLQEL-ERISGLTAE 153
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1196-1513 |
1.23e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1196 SLLAEIQALRAQLRmTHLQNQEKLQQLCAALTSTEARGSQREHQLRRQVELLAYKVEQEKCIANDLQKTLSKEQEAASDV 1275
Cdd:TIGR02169 678 RLRERLEGLKRELS-SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1276 RKRLMVEQGAVQDLKSELHACKQENTNLLESL-----DKVQQEVLRLRYGHVTWSYSGTSsasagravLDGKENELKVVL 1350
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLRE--------IEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1351 EELECERgKGQVLQAQQEEQQLRHLQREGQSSRA-LEELKISLEKQLAQNNQLCVALKHERAAKDNLQK----------E 1419
Cdd:TIGR02169 829 EYLEKEI-QELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEELEAALRDLESRLGDLKKERDELEAqlrelerkieE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1420 LQIEASRCEALLAQEKGQLSELR---KSLEAERSRSLELSEALQHERLLTEQLSRNAQE------------------ACA 1478
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEiralepvnmlaiqeyeevLKR 987
|
330 340 350
....*....|....*....|....*....|....*
gi 1958758604 1479 RQDTQAQHAllrKLKAEKARALELEAMLEKVQKQA 1513
Cdd:TIGR02169 988 LDELKEKRA---KLEEERKAILERIEEYEKKKREV 1019
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1375-1631 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1375 LQREGQSSRALEELKISleKQLAQNNQLCVALKHERAAKDN-------------------LQKELQIEASRCEAL--LAQ 1433
Cdd:pfam17380 308 KAREVERRRKLEEAEKA--RQAEMDRQAAIYAEQERMAMERerelerirqeerkreleriRQEEIAMEISRMRELerLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1434 EKGQLSE-LRKSLEAERSRSLelseaLQHERLLTEQLSRNAQEACARQDTQAQHALLRKLKAEKARALELEAMLEKVQKQ 1512
Cdd:pfam17380 386 ERQQKNErVRQELEAARKVKI-----LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1513 AAHTQQQLEAQAQERCLELRREKE---VSGNLRSAV--DALQTHKQELgccLEREReKAAWLQAELEQLSA-------RV 1580
Cdd:pfam17380 461 QVERLRQQEEERKRKKLELEKEKRdrkRAEEQRRKIleKELEERKQAM---IEEER-KRKLLEKEMEERQKaiyeeerRR 536
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758604 1581 KQQEARQDEKRMD-RRSSREDLDKRKWQRVK----EKLRELELQRQRDEHKIEQLQ 1631
Cdd:pfam17380 537 EAEEERRKQQEMEeRRRIQEQMRKATEERSRleamEREREMMRQIVESEKARAEYE 592
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
140-518 |
1.30e-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: 43.88 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 140 KQLEDARQLHRCVEKEFRHRDEEMaQAVQKQQELLERLREESAAKDRlalELHTAEGLLEGFKVEKADLQEALGKKEESE 219
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMEL-KYLKQYKEKACEIRDQITSKEA---QLESSREIVKSYENELDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 220 QQlIVELEDLRKQLQQASRELLTLKEENSVL----WNQKETFTNEAKEREAGTPVSAGREDAALQKEVESLTRDqwesrk 295
Cdd:TIGR00606 262 SK-IMKLDNEIKALKSRKKQMEKDNSELELKmekvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE------ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 296 qsekdrATLLSQMRvleSELEDQLvqhrGCAQLAEEV---TTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIK 372
Cdd:TIGR00606 335 ------RRLLNQEK---TELLVEQ----GRLQLQADRhqeHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 373 WLEGQLRQATRprppgprdsQCAKLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQ 452
Cdd:TIGR00606 402 RQEDEAKTAAQ---------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 453 LQEELEKQRRSTEELEVVNsRNSEIEELKAIIEHLQENQEQLQKAK---AEEIEQLHEVIEKLQSELSL 518
Cdd:TIGR00606 473 ILELDQELRKAERELSKAE-KNSLTETLKKEVKSLQNEKADLDRKLrklDQEMEQLNHHTTTRTQMEML 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-516 |
1.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 135 ALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAK---DRLALELHTAEGLLEGFKVEKAdlqEA 211
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeeKKKADELKKAEELKKAEEKKKA---EE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 212 LGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENsvlwnQKETFTNEAKEREAGTPVSAGREDAALQKEVESLTRDQW 291
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE-----KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 292 ESRKQSEKdratllsqmrvLESELEDQLVQHRGCAQLAEEVTTLKQQL--ATLDKHLRSQRQFMDEQAAEREHEREEFQQ 369
Cdd:PTZ00121 1644 EEKKKAEE-----------LKKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 370 EIKWLEGQLRQATRPRPPgpRDSQCAKLDEEVELLQEKLREKLDGFNELvikkdladqQLLIQEEEIKHLEETNENIQRQ 449
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEKKKI---------AHLKKEEEKKAEEIRKEKEAVI 1781
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 450 MAQLQEELEKQRRSTEELEVVNSRNSEIeelkaIIEHLQENQEQLQKAKAEEIEQLHEVIEKLQSEL 516
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFDNFAN-----IIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
202-467 |
1.51e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 202 KVEKADLQEAL---GKKEESEQqlivELEDLRKQLQQASRELLTLKEEnsvLWNQKETFTNEAKEREAGTPVsagredAA 278
Cdd:PRK11281 59 KLVQQDLEQTLallDKIDRQKE----ETEQLKQQLAQAPAKLRQAQAE---LEALKDDNDEETRETLSTLSL------RQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 279 LQKEVESLTRDQwesrKQSEKDRATLLSQMRVLESELEdqlvqhRGCAQLAEEVTTLkQQLATLDKHLRsqrqfmDEQAA 358
Cdd:PRK11281 126 LESRLAQTLDQL----QNAQNDLAEYNSQLVSLQTQPE------RAQAALYANSQRL-QQIRNLLKGGK------VGGKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 359 EREHEREEFQQEIKWLEGQLRQATrprppgprdsqcaKLDEEVELLQEKLREKLDgfnELVIKKDLADQQLLIQEEEI-- 436
Cdd:PRK11281 189 LRPSQRVLLQAEQALLNAQNDLQR-------------KSLEGNTQLQDLLQKQRD---YLTARIQRLEHQLQLLQEAIns 252
|
250 260 270
....*....|....*....|....*....|.
gi 1958758604 437 KHLEETneniQRQMAQLQEELEKQRRSTEEL 467
Cdd:PRK11281 253 KRLTLS----EKTVQEAQSQDEAARIQANPL 279
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1385-1589 |
1.87e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1385 LEELKISLEK------QLAQNNQLcVALKHERAAKDNLQKELQIEASRCEALLAQEKGQLSELRKSLEAERSRSLELSEA 1458
Cdd:COG3206 184 LPELRKELEEaeaaleEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1459 LQHERLLTEQLSRNAQEACARQDTQAQHALLRKLKAEKAralELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEvs 1538
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASLEAELEALQAREASLQAQLA-- 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958758604 1539 gNLRSAVDALQTHKQELgccLEREREKAAwLQAELEQLSARvkQQEARQDE 1589
Cdd:COG3206 338 -QLEARLAELPELEAEL---RRLEREVEV-ARELYESLLQR--LEEARLAE 381
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
171-505 |
1.93e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 171 QELLERLRE---ESAAKDRLALE--LHTAEGLLEGFKVEKAdlqealgKKEESE-QQLIVELEDLRKQLQQASRELLTLK 244
Cdd:PRK04778 63 EEKFEEWRQkwdEIVTNSLPDIEeqLFEAEELNDKFRFRKA-------KHEINEiESLLDLIEEDIEQILEELQELLESE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 245 EENSvlwnqketftneakereagtpvsagredaalqKEVESLTRDQWESRKQSEKDRATLLSQMRVLE---SELEDQLVQ 321
Cdd:PRK04778 136 EKNR--------------------------------EEVEQLKDLYRELRKSLLANRFSFGPALDELEkqlENLEEEFSQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 322 HrgcAQLAEE--VTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRPPGPRDsqcaKLDE 399
Cdd:PRK04778 184 F---VELTESgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHL----DIEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 400 EVELLQEKLREKLDgfnelvikkdladqqlLIQEEEIKHLEETNENIQRQMAQLQEELEKqrrsteELEVVNSRNSEIEE 479
Cdd:PRK04778 257 EIQDLKEQIDENLA----------------LLEELDLDEAEEKNEEIQERIDQLYDILER------EVKARKYVEKNSDT 314
|
330 340
....*....|....*....|....*.
gi 1958758604 480 LKAIIEHLQENQEQLQkakaEEIEQL 505
Cdd:PRK04778 315 LPDFLEHAKEQNKELK----EEIDRV 336
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1336-1636 |
2.19e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1336 RAVLDGKENELKVVLEELECERGKGQVLQAQQEEQQLRHLQREGQSSRALEELKISLEKQLAQNNQLcVALKHERAAKDN 1415
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1416 LQKELQIEASRCEALLAQEKGQLSELRKSLEAERSRSL------------ELSEALQH-ERLLTEQLSRNAQEACARQDT 1482
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqaelskleeevsRIEARLREiEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1483 QAQHALLRKLKAEKARALE-LEAMLEKVQKQAAHTQQQLEAQAQERcLELRREKEvsgNLRSAVDALQTHKQELGCCLER 1561
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIEnLNGKKEELEEELEELEAALRDLESRL-GDLKKERD---ELEAQLRELERKIEELEAQIEK 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1562 EREKAAWLQAELEQLSARVKQQEarqDEKRMDRRSSREDLDKRKWQRV-------------------------------- 1609
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIE---DPKGEDEEIPEEELSLEDVQAElqrveeeiralepvnmlaiqeyeevlkrldel 991
|
330 340
....*....|....*....|....*..
gi 1958758604 1610 KEKLRELELQRQRDEHKIEQLQRLVRE 1636
Cdd:TIGR02169 992 KEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| BspD6I-like |
cd22316 |
nicking endonuclease Nt.BspD6I and similar endonucleases; Heterodimeric type II restriction ... |
395-515 |
2.25e-03 |
|
nicking endonuclease Nt.BspD6I and similar endonucleases; Heterodimeric type II restriction endonuclease nicking endonuclease BspD6I recognizes a pseudosymmetric DNA sequence (5'-GAGTC) and cuts both strands outside the recognition motif 4 nucleotides downstream. It forms the large subunit in a heterodimeric arrangement. This catalytic domain/subunit belongs to a superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411720 Cd Length: 345 Bit Score: 42.67 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 395 AKLDEEVELLQEKLREKLDGFNELVIKKDLADqqlliqeeeIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNS-- 472
Cdd:cd22316 38 EKKVEVEEILSNVERKPIFFDSDDDYLEYLFN---------PALPPLDNDDKANLVLELLRIRLKERGILIKISSKPLlt 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958758604 473 ---RNSEIEELKAIIEHLQENQeqLQKAKAEEIEQLHEVIEKLQSE 515
Cdd:cd22316 109 padLNIIRKELENKLKKLREKK--YAKRQAEDWEEILEYFDLIENR 152
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
184-517 |
2.47e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 184 KDRLALELHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENSVLWNQKETFTNE--A 261
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 262 KEREAGTPVSAGREDAALQKEVESL--TRDQWESRKQSEKDRatlLSQMRVLESELEDQLVqhrgcaQLAEEVTTLKQQL 339
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQE---INEKTTEISNTQTQLN------QLKDEQNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 340 AtlDKHLRSQRQfmDEQAAEREHEREEFQQEIKWLEGQLRQATRPRppgpRDSQCAKLDEEVELLQEKLREKLDGFNELv 419
Cdd:TIGR04523 270 S--EKQKELEQN--NKKIKELEKQLNQLKSEISDLNNQKEQDWNKE----LKSELKNQEKKLEEIQNQISQNNKIISQL- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 420 ikkdlaDQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEE-LEVVNSRNSEIEELKAIIEHlQENQEQLQKAK 498
Cdd:TIGR04523 341 ------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKIQN-QEKLNQQKDEQ 413
|
330
....*....|....*....
gi 1958758604 499 AEEIEQLHEVIEKLQSELS 517
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLK 432
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
262-522 |
3.23e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 262 KEREAGTPvsagrEDAALQKEVESLTRDQWESRKQSEKDRATLLSQM-RVLESELEDQLVQHRGCAQLAEEVTTLKQQLA 340
Cdd:PLN03229 422 KKREAVKT-----PVRELEGEVEKLKEQILKAKESSSKPSELALNEMiEKLKKEIDLEYTEAVIAMGLQERLENLREEFS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 341 TLDkhlrSQRQFMDEQAAER-EHEREEFQQ---------EIKWLEGQLRQATRPRPPGPRDSQCAKLDEEVEllqEKLRE 410
Cdd:PLN03229 497 KAN----SQDQLMHPVLMEKiEKLKDEFNKrlsrapnylSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEIN---KKFKE 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 411 KLDGFNelvIKKDLADQQLLIQEEEIKHL----EETNENIQRQMAQLQEELEKQRRSTE-ELEVVNSRNSEIEElKAIIE 485
Cdd:PLN03229 570 VMDRPE---IKEKMEALKAEVASSGASSGdeldDDLKEKVEKMKKEIELELAGVLKSMGlEVIGVTKKNKDTAE-QTPPP 645
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958758604 486 HLQENQEQLQKAKAEEIEQLHEV------IEKLQSELSLMGPT 522
Cdd:PLN03229 646 NLQEKIESLNEEINKKIERVIRSsdlkskIELLKLEVAKASKT 688
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
396-643 |
3.33e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 396 KLDEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEEL--EVVNSR 473
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELaeAIKNLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 474 NSeIEELKAIIEHLQENQEQLqkaKAEEIEQLHEVIEKLQSELSLMgptvhemsdlppgSLHTELSCLQAEGMGGQALHN 553
Cdd:pfam06008 96 DN-IKEINEKVATLGENDFAL---PSSDLSRMLAEAQRMLGEIRSR-------------DFGTQLQNAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 554 ELQA--------AQAAKGAFGQLLADhgHSQALEALQERLQDAeAAAARHLTELEHCVALRQAEVEAMASRIQE----FE 621
Cdd:pfam06008 159 RIQTwfqspqeeNKALANALRDSLAE--YEAKLSDLRELLREA-AAKTRDANRLNLANQANLREFQRKKEEVSEqknqLE 235
|
250 260
....*....|....*....|..
gi 1958758604 622 ATLKAKEAIIVQRDLEIDAVNK 643
Cdd:pfam06008 236 ETLKTARDSLDAANLLLQEIDD 257
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1410-1628 |
3.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1410 RAAKDNLQKELqieasrceALLAQEKGQLSELRKSLEAERSRSLELSEALQHERLLTEqlsrnaqeacARQDTQAQHALL 1489
Cdd:COG4913 609 RAKLAALEAEL--------AELEEELAEAEERLEALEAELDALQERREALQRLAEYSW----------DEIDVASAEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1490 RKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLELRREKEVSGNLRSAVDALQTHKQELGcclEREREKAAWL 1569
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 1570 QAELEQLSARVKQQEARQDEKRmDRRSSREDLDKRkwqrvKEKLRElELQRQRDEHKIE 1628
Cdd:COG4913 748 RALLEERFAAALGDAVERELRE-NLEERIDALRAR-----LNRAEE-ELERAMRAFNRE 799
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
98-337 |
4.06e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 98 HVCESFFMSPENTQECEQPIRKVYQSLSTAVEGL---LDMALDSSKQLEDARQLHRCVEKEFrhrdeEMAQAVQKQQELL 174
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELeqkLSVADAARRQFEKAYELVCKIAGEV-----ERSQAWQTARELL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 175 ERLREESAAKDR---LALELHTAEGLLEG-FKVEK--ADLQEALGKKEESEQQLIVELEDLRKQLQQASRELLTLKEENS 248
Cdd:COG3096 502 RRYRSQQALAQRlqqLRAQLAELEQRLRQqQNAERllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 249 VLWNQKETFTNEAKEREAGTPVSAGREDAALQkeVESLTRDQWESRKQSEKDRATLLSQMRVLESElEDQLVQHRgcAQL 328
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALER--LREQSGEALADSQEVTAAMQQLLEREREATVE-RDELAARK--QAL 656
|
....*....
gi 1958758604 329 AEEVTTLKQ 337
Cdd:COG3096 657 ESQIERLSQ 665
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
419-516 |
4.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 419 VIKKDLADQQLLIQEEEIKH-LEETN---ENIQRQ-MAQLQEELEKQRRSTEEleVVNSRNSEIEELKAII----EHLQE 489
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRiLEEAKkeaEAIKKEaLLEAKEEIHKLRNEFEK--ELRERRNELQKLEKRLlqkeENLDR 100
|
90 100 110
....*....|....*....|....*....|...
gi 1958758604 490 NQEQLQK------AKAEEIEQLHEVIEKLQSEL 516
Cdd:PRK12704 101 KLELLEKreeeleKKEKELEQKQQELEKKEEEL 133
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
139-516 |
4.27e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 139 SKQLEDARQLHRCVEKEFRH-RD-----EEMAQAVQKQQE-LLERLREE----SAAKDRL-ALELH-----TAEGLLEGF 201
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDlKDmldvkERKINVLQKKIEnLQEQLRDKdkqlAGLKERVkSLQTDssntdTALTTLEEA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 202 KVEKADLQEALGK-KEESEQQLIVELEDLRKQLQQASRELLTLKEENSvlwnQKETFTNEAKEREAGTPVSAGREDAALq 280
Cdd:pfam10174 445 LSEKERIIERLKEqREREDRERLEELESLKKENKDLKEKVSALQPELT----EKESSLIDLKEHASSLASSGLKKDSKL- 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 281 kevesltrDQWESRKQSEKDRAtllsqmrvleSELEDQLVQhrgcAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAER 360
Cdd:pfam10174 520 --------KSLEIAVEQKKEEC----------SKLENQLKK----AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 361 ehereefQQEIKWLEGQLRQATRPRppGPRDSQCAKLdEEVELLQEKLREKLDGFNELVIKKDLADQQLLIQEEEIKHLE 440
Cdd:pfam10174 578 -------QAEVERLLGILREVENEK--NDKDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDN 647
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758604 441 ETNENIQRQMAQLQEELEKQRrstEELEVVNSRNSEIEelkaiiEHLQENQEQLQKAKAEEIEQLHEVIEKLQSEL 516
Cdd:pfam10174 648 LADNSQQLQLEELMGALEKTR---QELDATKARLSSTQ------QSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1373-1643 |
4.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1373 RHLQREGQSSRALEELKISLEKQLAQNNQLCVALKHERAAKDNLQK--ELQIEASRCEALLAQEKGQLSELRKSLEAERS 1450
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1451 RSLELSEALQHERLLTEQLSRNAQEACARQDTQAQHA------LLRKLKAEKARALELEAMLEKVQKQAAHTQQQLEAQA 1524
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleeLQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1525 QERCLelrREKEVSGNLRSAVDALQTHKQELGCCLEREREKAAWLQA--ELEQLSARVKQQEARQDEKRMDRRSSREDLD 1602
Cdd:COG4717 241 LEERL---KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958758604 1603 KRKWQRVKEKLR-ELELQRQRDEHKIEQLQRLVRELRWKEEA 1643
Cdd:COG4717 318 EEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEEL 359
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
427-626 |
5.66e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 427 QQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNSRNSEIEELKAIIEHLQENQEQLQKAKA--EEIEQ 504
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErlEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 505 LHEVIEKLQSELSlmgptvhemsdlppgSLHTELSCLQAegmggqalhnelQAAQAAKGAFGQLLADHGH-SQALEALQE 583
Cdd:COG4717 161 LEEELEELEAELA---------------ELQEELEELLE------------QLSLATEEELQDLAEELEElQQRLAELEE 213
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958758604 584 RLQDAEAAAARHLTELEHCVAlrQAEVEAMASRIQEFEATLKA 626
Cdd:COG4717 214 ELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLI 254
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
153-515 |
6.81e-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: 41.75 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 153 EKEFRHRDEEMAQAVQKQQELLERLREEsaakdrlaleLHTAEGLLEGFKVEKADLQEALGKKEESEQQLIVELEDLRKQ 232
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQ----------LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDK 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 233 LQQASRELLTLKEENsvlwnqketftneakereagtpvsagREDAALQKEVESLTRDQW--ESRKQSEKDRATLLSQMRV 310
Cdd:pfam12128 669 KNKALAERKDSANER--------------------------LNSLEAQLKQLDKKHQAWleEQKEQKREARTEKQAYWQV 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 311 LESELEDQLvqhrgcAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQAAEREHEREEFQQEIKWLEGQLRQATRPRPPGPR 390
Cdd:pfam12128 723 VEGALDAQL------ALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 391 ---------DSQCAKLDEEVELLQEKLREkldgfnelvIKKDLADQQlliqeeeikhlEETNENIQRQMAQLQEELEKQR 461
Cdd:pfam12128 797 yfdwyqetwLQRRPRLATQLSNIERAISE---------LQQQLARLI-----------ADTKLRRAKLEMERKASEKQQV 856
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958758604 462 RSTEELEVVNSRNSEIEELkaiieHLQENQEQLQKAKAEEIEQLHEVIEKLQSE 515
Cdd:pfam12128 857 RLSENLRGLRCEMSKLATL-----KEDANSEQAQGSIGERLAQLEDLKLKRDYL 905
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
402-519 |
7.09e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 402 ELLQEKLREKLDGFNElvIKKdlADQQLLIQEEEIKHLEETNENIQRQMAQLQEELEKQRRSTEELEVVNSRNSE--IEE 479
Cdd:cd16269 170 EVLQEFLQSKEAEAEA--ILQ--ADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRqlKEK 245
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958758604 480 LKAIIEHLQENQEQLQKAKAEEIEQL-----HEVIEKLQSELSLM 519
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALleegfKEQAELLQEEIRSL 290
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
324-512 |
8.49e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 324 GCAQLAEEVTTLKQQLATLDKHLRSQRQFMDEQaaerehereefQQEIKWLEGQLR--QATRPRPpgprdsqcaklDEEV 401
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAER-----------ARELDLLRFQLEelEAAALQP-----------GEEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 402 ELLQEklREKLDGFNElvIKKDLADQQLLIQEEEI--------------------KHLEETNENIQRQMAQLQE---ELE 458
Cdd:COG0497 210 ELEEE--RRRLSNAEK--LREALQEALEALSGGEGgaldllgqalralerlaeydPSLAELAERLESALIELEEaasELR 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758604 459 KQRRSTE----ELEVVNSRNSEIEELK---------------------AIIEHLQENQEQLQKAKAEEIEQLHEVIEKL 512
Cdd:COG0497 286 RYLDSLEfdpeRLEEVEERLALLRRLArkygvtveellayaeelraelAELENSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1173-1594 |
9.08e-03 |
|
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: 41.31 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1173 EKVIQEQGDLQKVREHACLPDRSslLAEIQALRAQLRMTHLQNQEKLQ---QLCAALTSTEARGSQREHQLRRQVELLAY 1249
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESE--LKELEKKHQQLCEEKNALQEQLQaetELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1250 KVEQEKCIANDLQKTLSKEQEAASDVRKRLMVEQGAVQDLKSELHACK------QENTNLLESLDKVQQEVLRLRYGHVT 1323
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEakikklEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1324 WSYSGTSSASAGRAVLDGKENELKVVLEELEcERGKGQVLQAQQEEQQLRHLQREGQSSRA--------LEELKISLEKQ 1395
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLE-ERLKKEEKGRQELEKAKRKLEGESTDLQEqiaelqaqIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1396 LAQNNQLCVALKHERAAKDNLQKELQieasrceallaQEKGQLSELRKSLEAERSRSlelSEALQHERLLTEQLSRNAQE 1475
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIR-----------ELEAQISELQEDLESERAAR---NKAEKQRRDLGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 1476 ACARQDTQAQHALLRKLK----AEKARALELEAMLEKVQKQAAHTQQQLEAQAQERCLElrREKEVSGNLRSAVDALQTH 1551
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKReqevTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLE--QAKRNKANLEKAKQALESE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958758604 1552 KQELGCCL----------EREREKaawLQAELEQLSARVKQQEaRQDEKRMDR 1594
Cdd:pfam01576 386 NAELQAELrtlqqakqdsEHKRKK---LEGQLQELQARLSESE-RQRAELAEK 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-355 |
9.45e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 135 ALDSSKQLEDARQLHRCVEKEFRHRDEEMAQAVQKQQELLERLREESAAKDRLALELHTAEGllegfkvEKADLQEALGK 214
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758604 215 KEESEQQLIVELEDLRKQLQQASRELLTLKEENSV-LWNQKETFTNEAKEREAGTPVSAGRED-----AALQKEVESLTR 288
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREqaeelRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758604 289 DQWESRKQSEKDRATLLSQMRVLESELEDQLVQHrgcAQLAEEVTTLKQQLATLDKHLRSQRQFMDE 355
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| |
