|
Name |
Accession |
Description |
Interval |
E-value |
| CENP-F_N |
pfam10481 |
Cenp-F N-terminal domain; Mitosin or centromere-associated protein-F (Cenp-F) is found bound ... |
1-270 |
1.92e-31 |
|
Cenp-F N-terminal domain; Mitosin or centromere-associated protein-F (Cenp-F) is found bound across the centromere as one of the proteins of the outer layer of the kinetochore. Most of the kinetochore/centromere functions appear to depend upon binding of the C-terminal par to f the molecule, whereas the N-terminal part, here, may be a cytoplasmic player in controlling the function of microtubules and dynein.
Pssm-ID: 463106 [Multi-domain] Cd Length: 304 Bit Score: 126.09 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 1 MSWAGDDWTVGLTGHVLQKVKQLLAQNEKLNKEKQQRQLQLDNSEVALHKQKQKHEEVRVELAAVQRELGGVREAAQAEV 80
Cdd:pfam10481 1 MSWAVEEWKEGLPTKALQKIQELESQLDKLKKERQQKQFQLESLEAALQKQKQKVENEKNEGSALKRENQSLMESCDNLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 81 RTRERLSHDLQVKTGQVHSLEGQLESAKKLTQSLTQEIKRLEAELEKLQKGNGSGESTL---------FSTPCWNTSSPW 151
Cdd:pfam10481 81 KSRQKISHDLQVKESQVNFLEGQLNSSKKQIEKLEQELKRYKSELERSQQALLAGDVSLqpcstpqksFATPLTPSQRHN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 152 DNNGGFRAESESKAQHARQLQFGDVPKPSAGGASSPFPQQPYKSPPLRRHvrqsepSTPSSVFPWERD------------ 219
Cdd:pfam10481 161 DSKYEELQEKYNKEVEERKRLEAELKVLQVKKTNQTLPQSTVSHRDIARH------QASSSVFPWQQEktpsrqssdaqe 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190900 220 -----------VLW---STPKGRPTSLVSSSEVMIKSSNCGMEDALRNEIDELRVRVSDLQREAQ 270
Cdd:pfam10481 235 tplkrgftashFLWeheETPSKRSQRSSSNSSLQSNSSSSQLMDQLKAQNQELRSRVSELELRLQ 299
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-785 |
1.21e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHL 328
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEELKCQRQNAEssrcNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQhdkvclqkQ 408
Cdd:COG1196 350 EEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--------E 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 409 SLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEAlKLIKELQ 488
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 489 AQLAASPPPVAAPNFSSAGDSFSPCVSLHHDRsspfnNSSQRKRAPNTGRTREEERMKYPSGREPGEGIDSEHIDKfese 568
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAV-----LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 569 eksQKRIGVQT-LPSGSLKLTEF-DLDTSVMEQDTGIEDVDTDSFTSDSTRgtmpKSESDISRSLKLDNTSGKTEKYDST 646
Cdd:COG1196 568 ---AAKAGRATfLPLDKIRARAAlAAALARGAIGAAVDLVASDLREADARY----YVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 647 TLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEK 726
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 727 KESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDL 785
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CENP-F_C_Rb_bdg |
pfam10490 |
Rb-binding domain of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1632-1677 |
8.81e-18 |
|
Rb-binding domain of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. This domain is at the very C-terminus of the C-terminal coiled-coil, and is one of the key Rb-binding domains.
Pssm-ID: 463111 Cd Length: 47 Bit Score: 78.26 E-value: 8.81e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1207190900 1632 SAAYDETEYEPYGLPEVVMKGFADIPSGPACPYVLRRGLLGTDAMP 1677
Cdd:pfam10490 2 RAEQDDEEFEPEGLPEVVQKGFADIPSGEVSPYILRRTTLQLRCSP 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-994 |
9.89e-18 |
|
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: 90.12 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 247 MEDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVK 326
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 327 HLQEELKCQRQNAESSRCNAEQRRKDMEREHQrELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCLQ 406
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEA-ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 407 KQSLERDLEDVKGKLKN-TEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIK 485
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 486 ELQAQLAASPPPVAAPNF----SSAGDSFSPCVS----------------LHHDRSSPF-NNSSQRKRA------PNTGR 538
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKAllknQSGLSGILGVLSelisvdegyeaaieaaLGGRLQAVVvENLNAAKKAiaflkqNELGR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 539 treeeRMKYPSGREPGEGIDSEHIDKFESEE------------KSQKRIGVQTLPSGSLKLTEFDLDTSV---MEQDTGI 603
Cdd:TIGR02168 573 -----VTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfDPKLRKALSYLLGGVLVVDDLDNALELakkLRPGYRI 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 604 EDVDTDSFTSD--STRGTMPKSESDISRSLKLDNTSGKTEKYDStTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRR 681
Cdd:TIGR02168 648 VTLDGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 682 AETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKKESSKLKETlhalqseaenrKVNDQEEDSQLKKAL 761
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-----------EAEIEELEAQIEQLK 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 762 AEMEQKETIMEEEmmgiKKELQDLQLKLAQEREEREQERLEERKLIRREEGL--KIAQLQEELdilrksTGLEEKISKDN 839
Cdd:TIGR02168 796 EELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDI------ESLAAEIEELE 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 840 LPLTYLHLEHHQNTDQKADLTENKDLIPSpgvQEFSVNLQNTMVRNEAKTIELIMDlEAQTKPKTSPSDMNRARA-LSTE 918
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELE-ELREKLAQLELRLEGLEVrIDNL 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 919 ASDLDNSTVLVLE-VERLRAARDRESEKAkvsQRKLEELQKQVttqtKQL-------TQAFESQSKHIDNLLSELEDKEC 990
Cdd:TIGR02168 942 QERLSEEYSLTLEeAEALENKIEDDEEEA---RRRLKRLENKI----KELgpvnlaaIEEYEELKERYDFLTAQKEDLTE 1014
|
....
gi 1207190900 991 ALQK 994
Cdd:TIGR02168 1015 AKET 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-491 |
1.41e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 250 ALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQ 329
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 330 EelkcQRQNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVcLQKQS 409
Cdd:COG1196 309 E----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-EELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 410 LERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQA 489
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
..
gi 1207190900 490 QL 491
Cdd:COG1196 464 LL 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-491 |
5.52e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 255 IDELRVRVSDLQREAQL--------ETERMKDVESRLAQ---ANREISSKEQSLTRTQEQLTRAQTRstQETDRAQTAEQ 323
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryrelkEELKELEAELLLLKlreLEAELEELEAELEELEAELEELEAE--LAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 324 KVKHLQEELKCQRQNAESSRCNAEQRRKDMEREHQRELVEQ-QRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDk 402
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 403 vclQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALK 482
Cdd:COG1196 352 ---ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
....*....
gi 1207190900 483 LIKELQAQL 491
Cdd:COG1196 429 ALAELEEEE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-1019 |
2.10e-13 |
|
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: 75.86 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 257 ELRVRVSDLQREaqLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELkcQR 336
Cdd:TIGR02168 217 ELKAELRELELA--LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL--YA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 337 QNAESSRCNAEQRRKDMEREH---QRELVEQQRERQALEKQHQQEN-NRLNQEIQQARTLHNTLQAQHDKVCLQKQSLER 412
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANlerQLEELEAQLEELESKLDELAEElAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 413 DLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMK----KQEKVLQE-EVKRLTEELAEALKLIKEL 487
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieELLKKLEEaELKELQAELEELEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 488 QAQLAASPPPVaapnfSSAGDSFSPCVSLHHDRSSPFNNSSQRKRAPNTGRTREEermKYPSG-------REPGEGIDSE 560
Cdd:TIGR02168 453 QEELERLEEAL-----EELREELEEAEQALDAAERELAQLQARLDSLERLQENLE---GFSEGvkallknQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 561 HIDKFESEEKSQKRIGVqTLPSgslkltefDLDTSVME-QDTGIEDVDTDSFTSDSTRGTMPKSESDISRSLKLDNTSGK 639
Cdd:TIGR02168 525 LSELISVDEGYEAAIEA-ALGG--------RLQAVVVEnLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 640 TEKYDSTTLKDLKKQNAELQDELRD------VKYDLQKRLEDLETQRRAETEARTKLKQLSRKHST--QTEQQRAKALEL 711
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVItgGSAKTNSSILER 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 712 KDSLVKLETQLEQEKKESSKLKETLHALQSEAENRkvndQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQ 791
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEEL----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 792 EREEREQERLEerkliRREEGLKIAQLQEELDilrkstGLEEKISKDNLPLTYLHLEHHQNTDQKADLTENKDLipspgV 871
Cdd:TIGR02168 752 LSKELTELEAE-----IEELEERLEEAEEELA------EAEAEIEELEAQIEQLKEELKALREALDELRAELTL-----L 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 872 QEFSVNLQNTMVRNEaktielimdleaqtkpktspsdmNRARALSTEASDLDNSTvlvlevERLRAardrESEKAKVSQR 951
Cdd:TIGR02168 816 NEEAANLRERLESLE-----------------------RRIAATERRLEDLEEQI------EELSE----DIESLAAEIE 862
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190900 952 KLEELQKQVTTQTKQLTQAFESQSKHIDNLLSELEDKECALQKQAEELQKCQEKicfLEEKQTRTNDL 1019
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELREKLAQL 927
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
250-1011 |
3.85e-13 |
|
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: 75.10 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 250 ALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSK-EQSLTRTQEQL-----TRAQTRSTQE--TDRAQTA 321
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIgeleaEIASLERSIAekERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 322 EQKVKHLQEELKCQRQNAESSRCNAEQRRKDMER------EHQRELVEQQRERQALEKQHQ---QENNRLNQEIQQARTL 392
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyaELKEELEDLRAELEEVDKEFAetrDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 393 HNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKR 472
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 473 LTEELAEALKLIKELQAQLAASPppvaapnfSSAGDSFSPCVSLHHDRSSPFNNSSQrkrapnTGRTREEermkYPSGRE 552
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASE--------ERVRGGRAVEEVLKASIQGVHGTVAQ------LGSVGER----YATAIE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 553 PGEG-------IDSEHIDKFESEEKSQKRIGVQT-LPSGSLKLTEFDLDTSVME------------------------QD 600
Cdd:TIGR02169 543 VAAGnrlnnvvVEDDAVAKEAIELLKRRKAGRATfLPLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfGD 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 601 TGI-EDVDTDSFTSDSTRgtMPKSESDISRSLKLDNTSGKTEKYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQ 679
Cdd:TIGR02169 623 TLVvEDIEAARRLMGKYR--MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 680 RRAETEARTKLKQLSRKHSTqteqqrakalelkdslvkLETQLEQEKKESSKLKETLHALQSEaenrkvndqeedsqlkk 759
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGE------------------IEKEIEQLEQEEEKLKERLEELEED----------------- 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 760 aLAEMEQKETIMEEEMMGIKKELQDLQLKLAqereereQERLEERKLIRREEGLKIAQLQEELDILRKS-TGLEEKISKD 838
Cdd:TIGR02169 746 -LSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSHSRIPEIQAELSKLEEEvSRIEARLREI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 839 NLPLTYLHLEHHQNTDQKADLtenkdlipspgvQEFSVNLQNTMVRNEAKTIELIMDLEAQtkpktspsdmnRARALSTE 918
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQEL------------QEQRIDLKEQIKSIEKEIENLNGKKEEL-----------EEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 919 ASDLDnstvLVLEVERLRAARDRESEKAKVSQRKLEELQKQVTTQTKQLT------QAFESQSKHIDNLLSELED---KE 989
Cdd:TIGR02169 875 AALRD----LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaklEALEEELSEIEDPKGEDEEipeEE 950
|
810 820
....*....|....*....|..
gi 1207190900 990 CALQKQAEELQKCQEKICFLEE 1011
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIRALEP 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
269-506 |
5.34e-10 |
|
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: 63.24 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 269 AQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQRQNAESSRCNAEQ 348
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 349 RRKDMErEHQRELVEQQRERQALEKQHQQE----NNRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERdLEDVKGKLKNT 424
Cdd:COG4942 95 LRAELE-AQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 425 EADLKESQKREAQTEAKLTEALRECESLtvsLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQLAASPPPVAAPNFS 504
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
..
gi 1207190900 505 SA 506
Cdd:COG4942 250 AL 251
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
660-1000 |
6.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 660 DELRDVKYDLQKRLEDLETQRRA-------ETEARTKLKQLS----RKHSTQTEQQRAKALELKDSLVKLETQLEQEKKE 728
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 729 SSKLKETLHALQSEAENRkvndQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQEREEREQERLEERKLIR 808
Cdd:COG1196 269 LEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 809 REEGLKIAQLQEELDILRKSTGLEEKISKdnlpltylhlehhQNTDQKADLTENKDLIpspgvqefsvNLQNTMVRNEAK 888
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAE-------------LAEAEEELEELAEELL----------EALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 889 TIELIMDLEAQTKpktspsdmNRARALSTEASDLDNstvlVLEVERLRAARDRESEKAKVSQRKLEELQKQVTTQTKQLT 968
Cdd:COG1196 402 LEELEEAEEALLE--------RLERLEEELEELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350
....*....|....*....|....*....|..
gi 1207190900 969 QAFESQSKHIDNLLSELEDKECALQKQAEELQ 1000
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-1001 |
7.03e-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: 64.31 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRneidELRVRVSDLQREAQLeTERMKDVESRLAQANREIS-----SKEQSLTRTQEQLTRAQTRSTQETDRAQTAE 322
Cdd:TIGR02168 192 EDILN----ELERQLKSLERQAEK-AERYKELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 323 QKVkhlqEELKCQRQNAEssrcnaeqrrkdmerehqrelvEQQRERQALEKQHQQENNRLNQEIQQartlhntLQAQHDK 402
Cdd:TIGR02168 267 EKL----EELRLEVSELE----------------------EEIEELQKELYALANEISRLEQQKQI-------LRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 403 VCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALK 482
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 483 LIKELQAQLAASPPPVAAPNfsSAGDSFSPCVSLHHDRSSPFNNSSQRKRAPNTGRTREEERMKYPSGREPGEGID---- 558
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLE--DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELReele 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 559 --SEHIDKFESEEKS-QKRI---------------GVQTL------PSGSL----KLTEFD--------------LDTSV 596
Cdd:TIGR02168 472 eaEQALDAAERELAQlQARLdslerlqenlegfseGVKALlknqsgLSGILgvlsELISVDegyeaaieaalggrLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 597 ME-QDTGIEDVDTDSFTSDSTRGTMPKSESDISRSLKLDNTSGKTEKYDSTTLKDLKKQNAELQDELRD------VKYDL 669
Cdd:TIGR02168 552 VEnLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 670 QKRLEDLETQRRAET------------------EARTKLKQLSRK-----HSTQTEQQRAKALELKDSLVKLETQLEQEK 726
Cdd:TIGR02168 632 DNALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRreieeLEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 727 KESSKLKETLHALqseaeNRKVNDQEEDsqlkkaLAEMEQKETIMEEEMMGIKKELQDLQlklAQEREEREQERLEERKL 806
Cdd:TIGR02168 712 EELEQLRKELEEL-----SRQISALRKD------LARLEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 807 IRREEglKIAQLQEELDILRKSTG-LEEKISKDNLPLTYLHLEHHQNTDQKADLTENKDLIpspgvQEFSVNLQNTMVRN 885
Cdd:TIGR02168 778 AEAEA--EIEELEAQIEQLKEELKaLREALDELRAELTLLNEEAANLRERLESLERRIAAT-----ERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 886 EAKTIELIMDLEAQTKPKTSPSD-----------MNRARALSTEASDLDNSTVLVLEVERLRAARDRESEKAKVSQ--RK 952
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESeleallnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQleLR 930
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1207190900 953 LEELQKQVTTQTKQLTQAFESQSKHIDNLLSELEDKECALQKQAEELQK 1001
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-486 |
8.37e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELrvrvSDLQREAqLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAqtrstqetdRAQTAEQKVKHL 328
Cdd:COG4913 228 DALVEHFDDL----ERAHEAL-EDAREQIELLEPIRELAERYAAARERLAELEYLRAAL---------RLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEELKCQRQNAESsrcnAEQRRkdmeREHQRELVEQQRERQALEKQHQQEN----NRLNQEIQQARTLHNTLQAQHDKvc 404
Cdd:COG4913 294 EAELEELRAELAR----LEAEL----ERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRAR-- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 405 lqkqsLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECE----SLTVSLGQMKKQEKVLQEEVKRLT------ 474
Cdd:COG4913 364 -----LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAEIASLErrksni 438
|
250 260
....*....|....*....|
gi 1207190900 475 --------EELAEALKLIKE 486
Cdd:COG4913 439 parllalrDALAEALGLDEA 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
272-491 |
1.92e-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: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 272 ETE-RMKDVESRLAQANREISSKEQSLTRTQEQLTRAQtrstqetdRAQTAEQKVKHLQEELKCQRQNAESSRCNAEQRR 350
Cdd:COG1196 176 EAErKLEATEENLERLEDILGELERQLEPLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 351 KDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKE 430
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190900 431 SQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
248-972 |
1.95e-09 |
|
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: 62.68 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLT---RTQEQLTRAQTRSTQETDRAQTAEQK 324
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKeleIKREAEEEEEEELEKLQEKLEQLEEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 325 VKHLQEELKCQRQNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLN--QEIQQARTLHNTLQAQHDK 402
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEeeEESIELKQGKLTEEKEELE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 403 V--------CLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESL-------------TVSLGQMKK 461
Cdd:pfam02463 455 KqelkllkdELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLlalikdgvggriiSAHGRLGDL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 462 QEKVLQEEVKRLTEELAEALKLIKELQAQLAASPPPVAAPNF--------SSAGDSFSPCVSLHHDRSSPFNNSSQRKRA 533
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGarklrlliPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 534 PNTGRTREEERMKYPSGREPGEGIDSEHIDKFESEEKSQKRIGVQTLPSGSLKLTEFDLDTSVMEQDTGIEDVDTDSFTS 613
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 614 DSTRGTMPKSESDISRSLKLDNTSgKTEKYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQL 693
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLE-AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 694 SRKHSTQTEQQRAKALELKDSLVKLETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEE 773
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 774 EMmgiKKELQDLQLKLAQEREEREQERLEERKLIRREEGLKIAQLQEELDILRKSTGLEEKISKDNLPLTYLHLEHHQNT 853
Cdd:pfam02463 854 EE---LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL 930
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 854 DQKADLTENKDLIPSPGVQEFSVNLQNTMVRNeaktielimDLEAQTKPKTSPSDMNRARAlsteasdldnstvlvlEVE 933
Cdd:pfam02463 931 LKYEEEPEELLLEEADEKEKEENNKEEEEERN---------KRLLLAKEELGKVNLMAIEE----------------FEE 985
|
730 740 750
....*....|....*....|....*....|....*....
gi 1207190900 934 RLRAARDRESEKAKVSQRKLEELQKQVTTQTKQLTQAFE 972
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
253-765 |
2.73e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 253 NEIDELRVRVSDLQRE---AQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQ 329
Cdd:PRK03918 207 REINEISSELPELREElekLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 330 E----------------ELKCQRQNAESSRCNAEQRRKDMEREHQrELVEQQRERQALEKQHQQENNRLNQEIQQARTLH 393
Cdd:PRK03918 287 ElkekaeeyiklsefyeEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 394 NTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKV-------L 466
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 467 QEE-----VKRLTEELAEALKLIKELQAQLAASPPpvaapnfssagdsfspcvslhhdrsspfnnssqRKRAPNTGRTRE 541
Cdd:PRK03918 446 TEEhrkelLEEYTAELKRIEKELKEIEEKERKLRK---------------------------------ELRELEKVLKKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 542 EERMKYPSGREPGEGIDSEhIDKFESEEKSQKRIGVQTLPSGSLKLTEfdlDTSVMEQD-TGIEDVDTDSFTSDSTRGTM 620
Cdd:PRK03918 493 SELIKLKELAEQLKELEEK-LKKYNLEELEKKAEEYEKLKEKLIKLKG---EIKSLKKElEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 621 PKSESDISRSLK---------LDNTSGKTEKY--DSTTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTK 689
Cdd:PRK03918 569 EEELAELLKELEelgfesveeLEERLKELEPFynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190900 690 LKQLSRKHSTQT-EQQRAKALELKDSLVKLETQLEQEKKESSKLKETLHALQSEAENRKvNDQEEDSQLKKALAEME 765
Cdd:PRK03918 649 LEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVE 724
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
628-790 |
3.53e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 61.57 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 628 SRSLKLDNTSGKTEKYDS--TTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHS------- 698
Cdd:PHA02562 207 QRKKNGENIARKQNKYDElvEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggv 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 699 ----TQT-EQQRAKALELKDSLVKLETQLEQEKKESSKLKE----------TLHALQSEAENRKVNDQEEDSQLKKALAE 763
Cdd:PHA02562 287 cptcTQQiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdefneqskKLLELKNKISTNKQSLITLVDKAKKVKAA 366
|
170 180 190
....*....|....*....|....*....|
gi 1207190900 764 MEQKE---TIMEEEMMGIKKELQDLQLKLA 790
Cdd:PHA02562 367 IEELQaefVDNAEELAKLQDELDKIVKTKS 396
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
648-833 |
4.40e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQ--NA----ELQDELRDVKYDLQ-KRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLET 720
Cdd:COG1196 202 LEPLERQaeKAeryrELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 721 QLEQEKKESSKLKETLHALQS----------EAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLA 790
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQdiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207190900 791 QEREEREQERLEERKLIRREEGLKIAQLQEELDILRKSTGLEE 833
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-891 |
5.11e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 261 RVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKV--KHLQEELKcqrQN 338
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEAK---KK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 339 AESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTlHNTLQAQHDKVCLQKQSLERDLEDVK 418
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 419 GKLKNTEADLKESQKREAQTEAKLTEALRECESLtvslgQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQLAASPPPV 498
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEA-----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 499 AAPNFSSAGDSFspcvslhhdrsspfNNSSQRKRAPNTGRTREEERMKYPSGREPGEGIDSEHIDKFESEEKS------- 571
Cdd:PTZ00121 1478 KAEEAKKADEAK--------------KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeakkae 1543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 572 QKRIGVQTLPSGSLKLTEfdlDTSVMEQDTGIEDVDTDSFTSDSTRGTMPKSESDISRSLKLDNTSGKTEKYDSTTLKDL 651
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAE---EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 652 KKQNAELQDELRDVKYDLQKRLED----LETQRRAETEARTKLKQLSRKhstqTEQQRAKALELKDSLVKLETQLEQEKK 727
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEekkkAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 728 ESSKLKETLHALQSEAENRK----VNDQEEDSQLKKALAEMEQKETIMEEEMM----GIKKELQDLQLKLAQEREEREQE 799
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeEEKKKIAHLKKEEEKKAEEIRKE 1776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 800 RLEERK--LIRREEGLKIAQLQEELDILRKSTGLEEKISKDNLPLtylhlehhqNTDQKADLTENKDLIPSpgvqefsvn 877
Cdd:PTZ00121 1777 KEAVIEeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI---------NDSKEMEDSAIKEVADS--------- 1838
|
650
....*....|....
gi 1207190900 878 lqNTMVRNEAKTIE 891
Cdd:PTZ00121 1839 --KNMQLEEADAFE 1850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-487 |
6.77e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQreaqletERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHL 328
Cdd:TIGR02168 806 DELRAELTLLNEEAANLR-------ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEELKCQRQNAESSRCNAEQRRKDMeREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHdkvclqkq 408
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEEL-RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-------- 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 409 slERDLEDVKGKLKNTEADLKESQKREAQTEAKLTE-------ALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEAL 481
Cdd:TIGR02168 950 --SLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
....*.
gi 1207190900 482 KLIKEL 487
Cdd:TIGR02168 1028 REARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
248-491 |
1.08e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKH 327
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 328 LQEELkcQRQNAESSRCNAEQRRKDMEREHQRELVEQQR----ERQALEKQHQQENNRLNQEIQQARTLHNTLQAQhdkv 403
Cdd:COG1196 405 LEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEealeEAAEEEAELEEEEEALLELLAELLEEAALLEAA---- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 404 cLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEE-----VKRLTEELA 478
Cdd:COG1196 479 -LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalQNIVVEDDE 557
|
250
....*....|...
gi 1207190900 479 EALKLIKELQAQL 491
Cdd:COG1196 558 VAAAAIEYLKAAK 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-822 |
2.42e-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: 59.30 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 19 KVKQLLAQNEK----LNKEKQQRQLQLDNSEVALHKQKQKHEEVRVELAAVQRElggvREAAQAEVRTRERlshDLQVKT 94
Cdd:TIGR02168 201 QLKSLERQAEKaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEE----LEELTAELQELEE---KLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 95 GQVHSLEGQLESAKKLTQSLTQEIKRLEAELEKLQKGNGSGESTLFSTpcwntsspwdnnGGFRAESESKAQHARQL--- 171
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL------------EAQLEELESKLDELAEElae 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 172 ---QFGDVpKPSAGGASSPFPQQPYKSPPLRRHVRqsepstpssvfpwERDVLWSTPKGRPTSLVSSsevmikssncgmE 248
Cdd:TIGR02168 342 leeKLEEL-KEELESLEAELEELEAELEELESRLE-------------ELEEQLETLRSKVAQLELQ------------I 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQRE-----AQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQ 323
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 324 KVKHLQEELkcqrqNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKV 403
Cdd:TIGR02168 476 ALDAAEREL-----AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 404 CL-----QKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEaLRECESLTVSLGQMKKQ-EKVLQEEVKRL--TE 475
Cdd:TIGR02168 551 VVenlnaAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN-IEGFLGVAKDLVKFDPKlRKALSYLLGGVlvVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 476 ELAEALKLIKELQAQlaaspppvaAPNFSSAGDSFSPCVSLhhdrsspfNNSSQRKRAPNTGRTREEERMkypsgrepge 555
Cdd:TIGR02168 630 DLDNALELAKKLRPG---------YRIVTLDGDLVRPGGVI--------TGGSAKTNSSILERRREIEEL---------- 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 556 gidSEHIDKFES--EEKSQKRIGVQTLPSgSLKLTEFDLDTSVMEQDTGIEDVDTDSFTSDStrgtmpKSESDISRSLKL 633
Cdd:TIGR02168 683 ---EEKIEELEEkiAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEA------EVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 634 DNTSGKTEKYDSTTLKDLKKQNAELQ---DELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEqqraKALE 710
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----RLES 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 711 LKDSLVKLETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIM---EEEMMGIKKELQDLQL 787
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallRSELEELSEELRELES 908
|
810 820 830
....*....|....*....|....*....|....*..
gi 1207190900 788 KLAQEREEREQERLEERKLIRREEGLK--IAQLQEEL 822
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEvrIDNLQERL 945
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-785 |
3.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 250 ALRNEIDELRVRVSD-LQREAQLEtERMKDVESRLAQANREISSKEQSLTRTQEQLtraqtrstqetdraqtaeQKVKHL 328
Cdd:PRK03918 169 EVIKEIKRRIERLEKfIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREEL------------------EKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEELKCQRQNAESSRCNAEQRRKDMER--EHQRELVEQQRERQALEKQHQQENNRLNqEIQQARTLHNTLQAQHDKVCLQ 406
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKleEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 407 KQSLERDLEDVKGKLKNTEADLKESQKREAQteakltealrecesltvsLGQMKKQEKVLQEEVKRLtEELAEALKLIKE 486
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEER------------------LEELKKKLKELEKRLEEL-EERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 487 LQAQLaaspppvaapnfssagdsfspcvslhhdrsspfnnssQRKRAPNTGRTREEERMKYPSGREPGEGIDSEhIDKFE 566
Cdd:PRK03918 370 KKEEL-------------------------------------ERLKKRLTGLTPEKLEKELEELEKAKEEIEEE-ISKIT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 567 SEEksqkrigvqtlpsGSLKLTEFDLDTSVMEQDtgiedvdtdsftsdSTRGTMPKSesdiSRSLKLDNTSGKTEKYdST 646
Cdd:PRK03918 412 ARI-------------GELKKEIKELKKAIEELK--------------KAKGKCPVC----GRELTEEHRKELLEEY-TA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 647 TLKDLKKQNAELQDELRDvkydLQKRLEDLETQRRAETEartklkqLSRKHSTQTEqqrAKALELKDSLVKLEtQLEQEK 726
Cdd:PRK03918 460 ELKRIEKELKEIEEKERK----LRKELRELEKVLKKESE-------LIKLKELAEQ---LKELEEKLKKYNLE-ELEKKA 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 727 KESSKLKETLHALQSEAENRKvNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDL 785
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-436 |
8.58e-08 |
|
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: 56.31 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTR----AQTRSTQETDRAQTAEQ 323
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllraLYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 324 KVKHLQEELKCQRQNAESSRCNAEQRRKDMER--EHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHD 401
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQAEELRADLAElaALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
170 180 190
....*....|....*....|....*....|....*
gi 1207190900 402 KVCLQKQSLERDLEDVKGKLKNTEADLKESQKREA 436
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-481 |
1.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 17 LQKVKQLLAQNEKLNKEKQQRQLQLDNSEVALHKQKQKHEEVRVELAAVQRELGGVREAAQAEVRTRERLSHDLQVKTGQ 96
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 97 VHSLEGQLESAKKLTQSLTQEIKRLEAELEKLQkgngsgestlfstpcwntsspwdnnggfrAESESKAQHARQLQfgdv 176
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELE-----------------------------EELEEAEEELEEAE---- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 177 pkpsaggasspfpqqpykspplrrhvrqsepstpssvfpwerdvlwstpkgrptslvsssevmikssncgmedALRNEID 256
Cdd:COG1196 358 -------------------------------------------------------------------------AELAEAE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 257 ELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQR 336
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 337 QNAEssrcnAEQRRKDMEREHQRELVEQQRERQALEKQHQQEnnrLNQEIQQARTLHNTLQAQHDkvclqkqSLERDLED 416
Cdd:COG1196 445 EEAA-----EEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEA-------DYEGFLEG 509
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190900 417 VKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEAL 481
Cdd:COG1196 510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
648-1108 |
1.64e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDVKYDLQKRLEDLETQ----RRAETEARTKLKQLSRKHSTQTEQQRakalELKDSLVKLETQLE 723
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlaNSELTEARTERDQFSQESGNLDDQLQ----KLLADLHKREKELS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 724 QEKKESSKLKE-------TLHALQSEAENRKVNDQEEDSQLKKALAEMEQKetiMEEEMMGIKKELQDLQlKLAQEREER 796
Cdd:pfam15921 395 LEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMAAIQGKNESLE-KVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 797 EQERLEERKLIRREEGLKIAQLQEELDILRKSTGLEEK---ISKDNLPLTYL------------HL----EHHQNTDQKA 857
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKeraIEATNAEITKLrsrvdlklqelqHLknegDHLRNVQTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 858 DLTENKDLIPSPGVQEFSVNLQNTM--VRNEAKTIELIMDLEAQTKPKTSPSDMN-------------RARALSTEASDL 922
Cdd:pfam15921 551 EALKLQMAEKDKVIEILRQQIENMTqlVGQHGRTAGAMQVEKAQLEKEINDRRLElqefkilkdkkdaKIRELEARVSDL 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 923 DNSTVLVLEV--ERLRAARDRE--------------------SEKAKVSQRKLEELQKQVTTQTKQLTQAFESQSKHID- 979
Cdd:pfam15921 631 ELEKVKLVNAgsERLRAVKDIKqerdqllnevktsrnelnslSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEq 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 980 --NLLSELEDKECALQKQAEELQK-----------CQEKICFLEEKQTRTN-DLSAPPELSTEISRELSCDSVFSNTSIS 1045
Cdd:pfam15921 711 trNTLKSMEGSDGHAMKVAMGMQKqitakrgqidaLQSKIQFLEEAMTNANkEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 1046 DHEMFSDDTPPvLKEKVSEHTVQL---PVEASVIQNIDQTNTSE-ISDKLQATEHFK--QQSVDTSNSS 1108
Cdd:pfam15921 791 ELEVLRSQERR-LKEKVANMEVALdkaSLQFAECQDIIQRQEQEsVRLKLQHTLDVKelQGPGYTSNSS 858
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-390 |
5.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQRE-AQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVK 326
Cdd:COG4913 311 LERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190900 327 HLQEELKCQRQNAESSRCNAEQRRKDMEREHQrelvEQQRERQALEKQHqqenNRLNQEIQQAR 390
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELR----ELEAEIASLERRK----SNIPARLLALR 446
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
248-811 |
8.96e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDE--LRVRVSDLQREAQ----LETERMKDVESRLAQANR-EISSKEQSLTRTQEQLTRAQTRSTQETDRAQT 320
Cdd:PTZ00121 1173 EDAKKAEAARkaEEVRKAEELRKAEdarkAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 321 AEQKVKHLQEELKCQRQNAessrCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQH 400
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAA----IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 401 DKVCLQKQSLE---RDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLtvslgQMKKQEKVLQEEVKRLTEEL 477
Cdd:PTZ00121 1329 KKADAAKKKAEeakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-----KKKAEEKKKADEAKKKAEED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 478 AEALKLIKELQAQLAASPPPVAAPNFSSAGDSFSPCVSLHHDRSSPFNNSSQRKRAPNTGRTREEERMKYPSGREPGEGI 557
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 558 DSEHIDKfESEEKSQKRIGVQTLPSGSLKLTEFDLDTSVMEQDTGIEdvDTDSFTSDSTRGTMPKSESDISRSL----KL 633
Cdd:PTZ00121 1484 KADEAKK-KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAeelkKA 1560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 634 DNTSGKTEKYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKD 713
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 714 SLVKLETQLEQEKK--ESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQ 791
Cdd:PTZ00121 1641 KEAEEKKKAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
570 580
....*....|....*....|
gi 1207190900 792 EREEREQERLEERKLIRREE 811
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAE 1740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-491 |
9.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 300 TQEQLTRaqtrstqeTDRAQTAEQKVKHLQEELKCQRQNAESSR----CNAEQRRKDMEREH---QRELVEQQRERQALE 372
Cdd:COG4913 566 SPEELRR--------HPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELaelEEELAEAEERLEALE 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 373 KQHQQennrlnqeIQQARTLHNTLQaQHDKVCLQKQSLER---DLEDVKGKLKNTEADLKESQKREAQTEAKLTEALREC 449
Cdd:COG4913 638 AELDA--------LQERREALQRLA-EYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207190900 450 ESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
254-448 |
1.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 254 EIDELRVRVSDLQREAQletermkDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELK 333
Cdd:COG3883 17 QIQAKQKELSELQAELE-------AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 334 CQ-RQNAESSRCNAE--------------QRRKDMER--EHQRELVEQQRERQALEKQHQQEnnrLNQEIQQARTLHNTL 396
Cdd:COG3883 90 ERaRALYRSGGSVSYldvllgsesfsdflDRLSALSKiaDADADLLEELKADKAELEAKKAE---LEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207190900 397 QAqhdkvclQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRE 448
Cdd:COG3883 167 EA-------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
266-490 |
1.05e-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: 53.59 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 266 QREAQLETERMKDVEsRLA---QANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQRQNAESS 342
Cdd:pfam17380 367 QEEIAMEISRMRELE-RLQmerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 343 RCNAEQRRKDMEREHQRELVEQQ---RERQALEKQHQQENNRLNQEiQQARTLHNTLQAQHDKVCLQKQS---LERDLED 416
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQeeeRKRKKLELEKEKRDRKRAEE-QRRKILEKELEERKQAMIEEERKrklLEKEMEE 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190900 417 vkgklkNTEADLKESQKREAQTEAKLTEALRECEsltvslgQMKKQEKVLQEEVKRL--TEELAEALKLIKELQAQ 490
Cdd:pfam17380 525 ------RQKAIYEEERRREAEEERRKQQEMEERR-------RIQEQMRKATEERSRLeaMEREREMMRQIVESEKA 587
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-448 |
1.11e-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: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANR--EISSKEQSLTRTQEQLTRAQtrstQETDRAQTAEQKVK 326
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELE----AELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 327 HLQEELKcqrqnaessrcNAEQRRKdmerEHQRELVEQQRERQALEKQHQQennrLNQEIQQARTLHNT---LQAQHDKV 403
Cdd:COG4913 689 ALEEQLE-----------ELEAELE----ELEEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAaedLARLELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207190900 404 CLQKQSLERDLEDVKGKL-KNTEADLKESQKREAQTEAKLTEALRE 448
Cdd:COG4913 750 LLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
256-491 |
1.20e-06 |
|
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: 53.69 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 256 DELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQtaeqkvkhlQEELKCQ 335
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ---------SEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 336 RQNAESSRcNAEQRRKDMEREHQRELVEQQrerQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVclqKQSLERDLE 415
Cdd:pfam12128 671 KALAERKD-SANERLNSLEAQLKQLDKKHQ---AWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL---KAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 416 DVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQE-KVLQEEV----------KRLTEELAEALKLI 484
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRqEVLRYFDwyqetwlqrrPRLATQLSNIERAI 823
|
....*..
gi 1207190900 485 KELQAQL 491
Cdd:pfam12128 824 SELQQQL 830
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
266-1015 |
1.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 266 QREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQ-TRSTQETDRAQTA----------EQKVKHLQEELKC 334
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdARKAEEARKAEDArkaeearkaeDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 335 QRQNAESSRCN----AEQRRKDMEREHQRELVEQQRERQA-----LEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCL 405
Cdd:PTZ00121 1163 ARKAEEARKAEdakkAEAARKAEEVRKAEELRKAEDARKAeaarkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 406 QKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIK 485
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 486 ELQAQLAASPPPVAAPNFSSAGDSfspcVSLHHDRSSPFNNSSQRKRAPNTGRTREEERMKYPSGREPGEGIDSEHIDKF 565
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAE----AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 566 ESEEKSQKRIGVQTLPSGSLKLTEfdldtsvmeqdtgiedvdtdsftsdstrgtMPKSESDISRSLKLDNTSGKTEKYDS 645
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE------------------------------AKKKAEEKKKADEAKKKAEEAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 646 TTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAEtEARTKLKQLSRK--HSTQTEQQRAKALELKDSlvkletqle 723
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKadEAKKAAEAKKKADEAKKA--------- 1518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 724 QEKKESSKLKETLHALQSEaENRKVNDQEEDSQLKKAlAEMEQKETIMEEEMMGIKKELQDLQLKLAQEREE-REQERLE 802
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKKA-EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 803 ERKLIRREEGLKIAQLQEELDILRKSTGL--EEKISKDNLPLTYLHLEHHQNTDQKADLTEnkdlipspgvqefsvnlQN 880
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-----------------EN 1659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 881 TMVRNEAKTIELIMDLEAQTKPKTSPSDMNRARALSTEASDLDnstvlvlEVERLRAARDRESEKA-------KVSQRKL 953
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAeelkkaeEENKIKA 1732
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 954 EELQKQVTTQTKQLTQAF--ESQSKHIDNLLSELEDKECALQKQA-----EELQKCQEKICFLEEKQTR 1015
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIRKEKeavieEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
252-445 |
1.56e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 252 RNEIDELRVRVSDLQREaQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRStqetDRAQTA-EQKVKHLQE 330
Cdd:PRK11281 100 QAELEALKDDNDEETRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQP----ERAQAAlYANSQRLQQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 331 ---ELKCQRQNAESSRcnAEQRrkdmerehqrelVEQQRERQALEKQHQQenNRlnQEIQQARTLHNTLQAQHDKVCLQK 407
Cdd:PRK11281 175 irnLLKGGKVGGKALR--PSQR------------VLLQAEQALLNAQNDL--QR--KSLEGNTQLQDLLQKQRDYLTARI 236
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207190900 408 QSLERDLEDVKGKLknteadlkeSQKREAQTEAKLTEA 445
Cdd:PRK11281 237 QRLEHQLQLLQEAI---------NSKRLTLSEKTVQEA 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
319-491 |
1.60e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 319 QTAEQKVKHLQEELKCQRQNAESsrcnAEQRRKDMEREhQRELVEQQRERQALE---------KQHQQENNRLNQEIQQA 389
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAE----AEERLEALEAE-LDALQERREALQRLAeyswdeidvASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 390 RTLHN---TLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVL 466
Cdd:COG4913 681 DASSDdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|....*
gi 1207190900 467 QEEVKRLTEELAEALKLIKELQAQL 491
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRA 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
319-767 |
2.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 319 QTAEQKVKHLQEELKcQRQNAESSRCNAEQRRKDMEREhqRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQA 398
Cdd:COG4717 81 KEAEEKEEEYAELQE-ELEELEEELEELEAELEELREE--LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 399 QHDkvclqkqsLERDLEDVKGKLKNTEADLKESQKR-EAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEEL 477
Cdd:COG4717 158 LRE--------LEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 478 aEALKLIKELQAQLAASPPPVAAPNFSSAGDSFSPCVSLHHDRSSPFNNSSQRKRAPNTGRTREEERMKYPSGREPGEGI 557
Cdd:COG4717 230 -EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 558 DSEHIDKFESEEKSQ--KRIGVQTLPSGSLKLTEFDLDTSVMEQDTGIEDVdtdsftsdstrgtmpksESDISRSLKLDN 635
Cdd:COG4717 309 ALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQELLREAEEL-----------------EEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 636 TSGKTEKYDSTTLKDLkKQNAELQDELRdvkyDLQKRLEDLETQRRAETEARtklkqLSRKHSTQTEQQRAKALELKDSL 715
Cdd:COG4717 372 IAALLAEAGVEDEEEL-RAALEQAEEYQ----ELKEELEELEEQLEELLGEL-----EELLEALDEEELEEELEELEEEL 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1207190900 716 VKLETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEdsQLKKALAEMEQK 767
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAELLQELE--ELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
250-487 |
2.07e-06 |
|
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: 52.76 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 250 ALRNEIDELRVRVSDLQREAQLETERMKDVESRLA-----QANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQK 324
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 325 VKHLQEELKcQRQNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQH---QQENNRLNQEIQQARTLHNTLQAQHD 401
Cdd:TIGR02169 835 IQELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlKKERDELEAQLRELERKIEELEAQIE 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 402 KVCLQKQSLERDLEDVKGKLKNTEADLKE--SQKREAQTEAKLTEALRECESLTVSLG-----------QMKKQEKVLQE 468
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiqeyeEVLKRLDELKE 993
|
250
....*....|....*....
gi 1207190900 469 EVKRLTEELAEALKLIKEL 487
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-491 |
2.32e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 267 REAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETD-RAQTAEQKVKHLQEELKcqrqnaessrcN 345
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELE-----------E 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 346 AEQRRKDMEREHqRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQhdkvclqKQSLERDLEDVKGKLKNTE 425
Cdd:TIGR02168 244 LQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190900 426 ADLKESQKREAQTEAKLTEALREcesltvsLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEE-------LAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
353-491 |
2.93e-06 |
|
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: 50.31 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 353 MEREHQRELVE-QQRERQALEKQHQQEN-----NRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEA 426
Cdd:COG1579 1 AMPEDLRALLDlQELDSELDRLEHRLKElpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190900 427 DLKESQK-REaqteakLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:COG1579 81 QLGNVRNnKE------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-448 |
4.61e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLtRAQTRSTQET------------ 315
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GERARALYRSggsvsyldvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 316 --------DRAQTAEQKVKHLQEELKCQrqnaessrcnaeQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQ 387
Cdd:COG3883 111 sesfsdflDRLSALSKIADADADLLEEL------------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190900 388 QARTLHNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRE 448
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
319-486 |
7.48e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 319 QTAEQKVKHLQEELKCQRQNAESsrcNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQartlhntlqa 398
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALL---EAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL---------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 399 qhdkvcLQKQslERDLEDVKGKLKNTEADLKesqKREAQTEAKLTEALRECESLTvslgQMKKQE--KVLQEEVKrltEE 476
Cdd:PRK12704 105 ------LEKR--EEELEKKEKELEQKQQELE---KKEEELEELIEEQLQELERIS----GLTAEEakEILLEKVE---EE 166
|
170
....*....|.
gi 1207190900 477 L-AEALKLIKE 486
Cdd:PRK12704 167 ArHEAAVLIKE 177
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
248-790 |
9.62e-06 |
|
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: 50.61 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQ---REAQLETERMKDVESRLAQANREisskeqSLTRTQEQLTRAQTRSTQETDRAQTAEQK 324
Cdd:pfam12128 296 DDQWKEKRDELNGELSAADaavAKDRSELEALEDQHGAFLDADIE------TAAADQEQLPSWQSELENLEERLKALTGK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 325 VKHLQEELKCQRQNAeSSRCNAEQRRKDMEREHQRELVEQQR--ERQALEKQHQQENNRLNQEIQQARTlhntlqaqhdk 402
Cdd:pfam12128 370 HQDVTAKYNRRRSKI-KEQNNRDIAGIKDKLAKIREARDRQLavAEDDLQALESELREQLEAGKLEFNE----------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 403 vclQKQSLERDLEDVKGKLKNTEA------DLKESQKREAQTEAKLTEALRECESLTVSLGQMK----KQEKVLQEEVKR 472
Cdd:pfam12128 438 ---EEYRLKSRLGELKLRLNQATAtpelllQLENFDERIERAREEQEAANAEVERLQSELRQARkrrdQASEALRQASRR 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 473 LtEELAEALkliKELQAQLaaspppvaapnfssagdsFSPCVSLHHdrsspFNNSSQRKRAPNTGRTreeermkypsgre 552
Cdd:pfam12128 515 L-EERQSAL---DELELQL------------------FPQAGTLLH-----FLRKEAPDWEQSIGKV------------- 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 553 pgegIDSE--HIDKFESEEKSQKRIGVQTLPSGSLKLTEFDLDTSVMEQDTGIEDVDTDSFTSDSTRGTMPKSESDISR- 629
Cdd:pfam12128 555 ----ISPEllHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQa 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 630 SLKLDNTSgKTEKYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEdlETQRRAETEART---KLKQLSRKHSTQTEQQRA 706
Cdd:pfam12128 631 NGELEKAS-REETFARTALKNARLDLRRLFDEKQSEKDKKNKALA--ERKDSANERLNSleaQLKQLDKKHQAWLEEQKE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 707 KALELkdSLVKLETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAemeqKETIMEEEMMGIKKELQDLQ 786
Cdd:pfam12128 708 QKREA--RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA----SLGVDPDVIAKLKREIRTLE 781
|
....
gi 1207190900 787 LKLA 790
Cdd:pfam12128 782 RKIE 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
648-1023 |
1.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKK 727
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 728 ESSKLKETLHALQSEAENrkVNDQEEDSQLKKALAEMEQ--------------KETIMEEEMMGIKKELQDLQLKLAQER 793
Cdd:COG4717 214 ELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 794 EEREQERLEERKLIRREEGLKIAQL-QEELDILRKSTGLEEKISKDNLPLTYLHLEHHQNTDQKADlTENKDLIPSPGVQ 872
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELeEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE-ELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 873 EFSVNLQNTMVRNEAKTIELIMDLEAQTKPKtspSDMNRARALSTEASDLDNSTVLVLEVERLRAARDRESEKAKVSQRK 952
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELK---EELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207190900 953 LEELQKQVTTQTKQLTQAFESQSkhIDNLLSELEDKECALQKQAEELQKCQEKICFLEEKQTRTNDLSAPP 1023
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPP 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
648-782 |
1.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDVKYDLQ----KRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLE 723
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 724 QEKKESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKEL 782
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
249-452 |
1.81e-05 |
|
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: 49.82 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEqKVKHL 328
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND-RIRLL 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEELkcQRQNAESSRCNAEQRR-----KDME-----REHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQA 398
Cdd:pfam10174 564 EQEV--ARYKEESGKAQAEVERllgilREVEnekndKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207190900 399 QHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESL 452
Cdd:pfam10174 642 RRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNL 695
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
323-491 |
2.37e-05 |
|
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: 49.12 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 323 QKVKHLQEELKCQRQNAESSRCNAEQRRKDME-------------REHQRELVEQQRERQALEKQHQQENNRLNQE---- 385
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELEsrvaelkeelrqsREKHEELEEKYKELSASSEELSEEKDALLAQraah 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 386 IQQARTLHNTLQAQHDKVCLQKQSLERDLEDVK---GKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQ 462
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKkagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQ 207
|
170 180
....*....|....*....|....*....
gi 1207190900 463 EKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:pfam07888 208 VLQLQDTITTLTQKLTTAHRKEAENEALL 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
269-490 |
2.80e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 269 AQLETERMKDVESRLAQANREISSKEQSLTRTQEQLT--RAQTRSTQETDRAQTAEQKVKHLQEELkcqrQNAESSRCNA 346
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQL----AEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 347 EQRRKDMEREHQRELVEQQRERQ-ALEKQHQQENNRLNQEIQQARTlhnTLQAQHDKVclqkQSLERDLEDVKGKLKNTE 425
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAELSA---RYTPNHPDV----IALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 426 ADLKESQKREAQT----EAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQ 490
Cdd:COG3206 312 QRILASLEAELEAlqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
648-879 |
3.13e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDVKYDLQkRLEDLETQRRAETEARTKLKQL-SRKHSTQTEQQRA-KAL-ELKDSLVKLETQLEQ 724
Cdd:PRK11281 82 TEQLKQQLAQAPAKLRQAQAELE-ALKDDNDEETRETLSTLSLRQLeSRLAQTLDQLQNAqNDLaEYNSQLVSLQTQPER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 725 EKKEsskLKETLHALQsEAENRKVNDQEEDSQLK---KALAEMEQKetimeeemmgikkeLQDLQLKLAQEREEREQERL 801
Cdd:PRK11281 161 AQAA---LYANSQRLQ-QIRNLLKGGKVGGKALRpsqRVLLQAEQA--------------LLNAQNDLQRKSLEGNTQLQ 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190900 802 EERKLIRREEGLKIAQLQEELDILRkstgleEKISKDNLPLTYLHLEHHQNTDQKADLTENkDLIpspgVQEFSVNLQ 879
Cdd:PRK11281 223 DLLQKQRDYLTARIQRLEHQLQLLQ------EAINSKRLTLSEKTVQEAQSQDEAARIQAN-PLV----AQELEINLQ 289
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
17-490 |
3.32e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 17 LQKVKQLLAQNEKLNKEKQQRQLQLDNSEVALHKQKQ-------KHEEVRVELAAVQRELGGVREAAQAEVRTRERLSHD 89
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 90 LQVK----TGQVHSLEGQLESAKKLTQSLTQEIKRLEAELEKLQkgngsgESTLFSTpcwntsspwDNNGgfRAESESKA 165
Cdd:pfam01576 94 LQNEkkkmQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLE------EDILLLE---------DQNS--KLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 166 QHARQLQFgdvpkpsaggaSSPFPQQPYKSPPLrrhvrqsepstpssvfpwerdvlwSTPKGRPTSLVSSSEVMIKSsnc 245
Cdd:pfam01576 157 LEERISEF-----------TSNLAEEEEKAKSL------------------------SKLKNKHEAMISDLEERLKK--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 246 gmEDALRNEIDELRVRvsdLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKV 325
Cdd:pfam01576 199 --EEKGRQELEKAKRK---LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 326 KHLQEELKCQRQnaesSRCNAEQRRKDMERE----------------HQREL-VEQQRERQALEKQHQQENNRLNQEIQQ 388
Cdd:pfam01576 274 SELQEDLESERA----ARNKAEKQRRDLGEElealkteledtldttaAQQELrSKREQEVTELKKALEEETRSHEAQLQE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 389 ARTLHNT----LQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEK 464
Cdd:pfam01576 350 MRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRA 429
|
490 500
....*....|....*....|....*.
gi 1207190900 465 VLQEEVKRLTEELAEALKLIKELQAQ 490
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGK 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-487 |
3.76e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 18 QKVKQLLAQNEKLNKEKQQRQLQLDNSEVALHKQKQKHEEVRVELAAVQRELGGV---REAAQAEV----RTRERLSHDL 90
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaeLAEAEEELeelaEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 91 QVKTGQVHSLEGQLESAKKLTQSLTQEIKRLEAEL-------------------------EKLQKGNGSGESTLFSTPCW 145
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALaeleeeeeeeeealeeaaeeeaeleEEEEALLELLAELLEEAALL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 146 NTSspWDNNGGFRAESESKAQHARQLQFGDVPKPSAGGASSPFPQQPYKSPPLRRH-----------------VRQSEPS 208
Cdd:COG1196 476 EAA--LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigveaayeaaleaalaaALQNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 209 TPSSVFPWERDVLWSTPKGR----PTSLVSSSEVMIKSSNCGMEDALRNEIDELRVRVSDLQREAQLETERMKDVESRLA 284
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 285 QANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEElkcqrqnaessrcnaEQRRKDMEREHQRELVEQ 364
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---------------LEELAERLAEEELELEEA 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 365 QRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTE 444
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1207190900 445 -------ALRECESLTVSLGQMKKQEKVLQEEVKRLteelaeaLKLIKEL 487
Cdd:COG1196 779 lgpvnllAIEEYEELEERYDFLSEQREDLEEARETL-------EEAIEEI 821
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
648-786 |
4.28e-05 |
|
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: 46.84 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDvkydLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSL--VK-------L 718
Cdd:COG1579 19 LDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRnnkeyeaL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190900 719 ETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQ 786
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
624-834 |
4.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 624 ESDISRSLKLDNTSGKTEKYDSTTLKDLKKQNAELQdELRDVKYDLQKRLEDLETQRRAETEARTKLKQLsrkhstqteQ 703
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELP-ELREELEKLEKEVKELEELKEEIEELEKELESL---------E 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 704 QRAKALELKdsLVKLETQLEQEKKESSKLKETLHALQS--EAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKE 781
Cdd:PRK03918 252 GSKRKLEEK--IRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190900 782 LQDLQLKLAQEREEREQERLEERKLIRREEGLK----IAQLQEELDILRKSTGLEEK 834
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHElyeeAKAKKEELERLKKRLTGLTP 386
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
249-390 |
4.91e-05 |
|
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: 46.84 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQetdrAQTAEQkVKHL 328
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN----VRNNKE-YEAL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190900 329 QEE---LKCQRQNAESSRCNAEQRRKDMER---EHQRELVEQQRERQALEKQHQQENNRLNQEIQQAR 390
Cdd:COG1579 95 QKEiesLKRRISDLEDEILELMERIEELEEelaELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-488 |
5.72e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 256 DELR----VRVSDLQREAQletERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKhlQEE 331
Cdd:PTZ00121 1537 DEAKkaeeKKKADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK--AEE 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 332 LKcqrqNAESSRCNAEQRRKDmerEHQRELVEQQRERQALEKQhQQENNRLNQEIQQARTLHNTLQAQHDKvclqkqsle 411
Cdd:PTZ00121 1612 AK----KAEEAKIKAEELKKA---EEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKAEEDK--------- 1674
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190900 412 RDLEDVKgKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQ 488
Cdd:PTZ00121 1675 KKAEEAK-KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
629-822 |
5.76e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 629 RSLKLDNTSGKTEKYDSTTLKDLKKQNAELQDELRDVKyDLQKRLEDLETQRRAETEARTKLKQLSRKHstqteQQRAKA 708
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKL-----EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 709 LELKDSLVKLETQLEQEKKESSKLKETLHALQsEAENRKVNDQEEDSQLKKALAE-MEQKETIMEEEMMGIKKELQDLQL 787
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEElLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*
gi 1207190900 788 KLAQEREEREQERLEERKLIRREEGLKIAQLQEEL 822
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
648-834 |
6.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRkhstQTEQQRAKALELKDSLVKLETQLEQEKK 727
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 728 EsskLKETLHALQSEAENRKVN---DQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQEREEREQERLEER 804
Cdd:COG4942 105 E---LAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190
....*....|....*....|....*....|..
gi 1207190900 805 KLIRREEGLK--IAQLQEELDILRKSTGLEEK 834
Cdd:COG4942 182 ELEEERAALEalKAERQKLLARLEKELAELAA 213
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
250-469 |
9.64e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.79 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 250 ALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQET-------------- 315
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEkaadesergrkvle 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 316 DRAQTAEQKVKHLQEELKCQRQNAEssrcnaEQRRKDMEREHQRELVEQQRERqALEKQHQQENN--RLNQEIQQARTLH 393
Cdd:pfam00261 85 NRALKDEEKMEILEAQLKEAKEIAE------EADRKYEEVARKLVVVEGDLER-AEERAELAESKivELEEELKVVGNNL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190900 394 NTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEakltealRECESLTVSLGQMKKQEKVLQEE 469
Cdd:pfam00261 158 KSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLE-------KEVDRLEDELEAEKEKYKAISEE 226
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
252-474 |
9.65e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 252 RNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQET------DRAQT----- 320
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqalERAKQlcglp 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 321 --AEQKVKHLQEELKCQRQNAESSRCNAEQRRKDMEREHQR-----ELV----------EQQRERQALEKQHQQENNrLN 383
Cdd:PRK04863 434 dlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayQLVrkiagevsrsEAWDVARELLRRLREQRH-LA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 384 QEIQQARTLHNTLQAQHDkvclQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQE 463
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
250
....*....|.
gi 1207190900 464 KVLQEEVKRLT 474
Cdd:PRK04863 589 EQLQARIQRLA 599
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
249-466 |
1.22e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQRE-AQLETErMKDVEsrlAQANREISSkeqsltrTQEQLTRAQTRSTQETDRAQTAEQKVKH 327
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQiQQLRTE-LQELE---AQQQEEAES-------SREQLQELEEQLATERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 328 LQEELKCQRQNAESSRCNAEQRRKDMEREHQReLVEQQRERQALEKQHQQENNRLNQ---EIQQARTLHNTLQAQHDKVC 404
Cdd:pfam09787 119 LQEELRYLEEELRRSKATLQSRIKDREAEIEK-LRNQLTSKSQSSSSQSELENRLHQlteTLIQKQTMLEALSTEKNSLV 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190900 405 LQKQSLERDLEDVKGKLKNTEADLKESQKREAQTE-AKLTEALRECESLTVS-LGQMKKQEKVL 466
Cdd:pfam09787 198 LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRlRNVPGLFSESDSDRAGmYGKVRKAASVI 261
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
642-1003 |
1.65e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 642 KYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQ-QRAKA------LELKDS 714
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElNKAKAahsfvvTEFEAT 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 715 LVKLETQLEQEKKESSKLKETLHALQSEAENR----------KVNDQEEDSQLKKALAEME-------QKETIMEE---- 773
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKsseleemtkfKNNKEVELEELKKILAEDEklldekkQFEKIAEElkgk 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 774 --EMMGI----KKELQDLQLKLAQEREERE--QERLEERKLIRREEGLKIAQLQEELDILRkstgLEEKISKDNLPLTYL 845
Cdd:pfam05483 438 eqELIFLlqarEKEIHDLEIQLTAIKTSEEhyLKEVEDLKTELEKEKLKNIELTAHCDKLL----LENKELTQEASDMTL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 846 HLEHHQNTDQKADLTENKDLIPSPGVQEFSVNLQNTMvrnEAKTIELIMDLEaQTKPKTSPSDMNRARALSTEASDLDNS 925
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL---ESVREEFIQKGD-EVKCKLDKSEENARSIEYEVLKKEKQM 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 926 TVLVLEVERLRAARDRESEKAKVSQRKLEELQKQVTTQTKQLT--------------QAFESQSKHIDNLLSELEDKECA 991
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvnklelelaSAKQKFEEIIDNYQKEIEDKKIS 669
|
410
....*....|..
gi 1207190900 992 LQKQAEELQKCQ 1003
Cdd:pfam05483 670 EEKLLEEVEKAK 681
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
18-448 |
1.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 18 QKVKQLLAQNEKLNKEKQQRQLQLDNSEVALhkqkQKHEEVRVELAAVQRELGGVREAAQAEVRTRERLSHDLQVKTGQV 97
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVL----EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 98 HSLEGQLESAKKLTQSLTQEIKRLEAELEKLQKGNGSGESTLF--STPCWNTSSPWDNNGGFRAESESKAQHAR------ 169
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecRVAAQAHNEEAESLREDADDLEERAEELReeaael 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 170 ----------------QLQFGDVPKPSAGGASSPFPQQPYKSPPLRRHVRQsepstpssvfpwERDVLWSTPKGRPTSLV 233
Cdd:PRK02224 369 eseleeareavedrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE------------ERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 234 SSSEVMI---------KSSNCG--MEDALRNE-IDELRVRVSDLQRE-AQLETERmKDVESR------LAQANREISSKE 294
Cdd:PRK02224 437 TARERVEeaealleagKCPECGqpVEGSPHVEtIEEDRERVEELEAElEDLEEEV-EEVEERleraedLVEAEDRIERLE 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 295 QSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQRQNAESSRCNAEQRR---KDMEREHQ------------- 358
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKLAelkerieslerir 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 359 -----RELVEQQRERQALEKQHQQENNRLNQE-IQQARTLHNTLQAQHDKVCLQ-----KQSLERDLEDVKGKLKNTEAD 427
Cdd:PRK02224 596 tllaaIADAEDEIERLREKREALAELNDERRErLAEKRERKRELEAEFDEARIEearedKERAEEYLEQVEEKLDELREE 675
|
490 500
....*....|....*....|...
gi 1207190900 428 LKESQKREAQTEAKLT--EALRE 448
Cdd:PRK02224 676 RDDLQAEIGAVENELEelEELRE 698
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
249-488 |
1.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHL 328
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEELKCQRQNAESSRCNAEQR--RKDMEREHQREL-VEQQRERQALEKQhQQENNRLNQEIQQARTLHNTLQAQHDKVCL 405
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLeeRAEELREEAAELeSELEEAREAVEDR-REEIEELEEEIEELRERFGDAPVDLGNAED 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 406 QKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKL-----------------TEALREC----ESLTVSLGQMKKQEK 464
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDrervEELEAELEDLEEEVE 492
|
250 260
....*....|....*....|....
gi 1207190900 465 VLQEEVKRLtEELAEALKLIKELQ 488
Cdd:PRK02224 493 EVEERLERA-EDLVEAEDRIERLE 515
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
249-503 |
1.90e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHL 328
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 329 QEE---LKCQRQNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCL 405
Cdd:COG4372 128 EQQrkqLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 406 QKQSLERDLEDVKGKLKNTEAdLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIK 485
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLE-AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250
....*....|....*...
gi 1207190900 486 ELQAQLAASPPPVAAPNF 503
Cdd:COG4372 287 ALEEAALELKLLALLLNL 304
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
301-486 |
2.12e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 301 QEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQrqnaesSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQEnn 380
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ------AAIYAEQERMAMERERELERIRQEERKRELERIRQEE-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 381 rLNQEIQQARTLHNTLQAQHDKVCLQKQSLErdlEDVKGKLknteadLKESQKREAQTEAKLTEALRecesltvslgqmK 460
Cdd:pfam17380 370 -IAMEISRMRELERLQMERQQKNERVRQELE---AARKVKI------LEEERQRKIQQQKVEMEQIR------------A 427
|
170 180
....*....|....*....|....*.
gi 1207190900 461 KQEKVLQEEVKRLTEELAEALKLIKE 486
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRL 453
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
267-388 |
2.19e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 43.79 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 267 REAQLETErMKDVESRLAQAnreisskEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKhlQEELKCQRQNAESSRCNA 346
Cdd:PRK07352 51 RREAILQA-LKEAEERLRQA-------AQALAEAQQKLAQAQQEAERIRADAKARAEAIR--AEIEKQAIEDMARLKQTA 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207190900 347 EQrrkDMEREHQRELVEQQRE--RQALEKQHQQENNRLNQEIQQ 388
Cdd:PRK07352 121 AA---DLSAEQERVIAQLRREaaELAIAKAESQLPGRLDEDAQQ 161
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
264-772 |
2.62e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 264 DLQREAQLETERMKDVESRLAqANREISSKEQSLTRTQEQLtrAQTRSTQETDRAQTAEQKVKHLQEELK---CQRQNAE 340
Cdd:PRK02224 157 DLLQLGKLEEYRERASDARLG-VERVLSDQRGSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIEryeEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 341 SSRCNAEQRRKDME--REHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVcLQKQSLER-DLEDV 417
Cdd:PRK02224 234 ETRDEADEVLEEHEerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL-LAEAGLDDaDAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 418 KGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQLAA--SP 495
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEleEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 496 PPVAAPNFSSAGDSFSPCVSLHHDRSSPFNNSSQRKRAPNTGRTREEERM----------KYPSGREPGEgiDSEHIDkf 565
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaealleagKCPECGQPVE--GSPHVE-- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 566 ESEEKSQKRIgvqtlpsgslkltefDLDTSVMEQDTGIEDVdtdsftsdstrgtmpksESDISRslkldntsgktekyds 645
Cdd:PRK02224 469 TIEEDRERVE---------------ELEAELEDLEEEVEEV-----------------EERLER---------------- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 646 ttLKDLKKQNAELqDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDS-------LVKL 718
Cdd:PRK02224 501 --AEDLVEAEDRI-ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEaeeareeVAEL 577
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190900 719 ETQLEQEKKESSKLkETLHALQSEAENrKVNDQEEDSQLKKALAEM--EQKETIME 772
Cdd:PRK02224 578 NSKLAELKERIESL-ERIRTLLAAIAD-AEDEIERLREKREALAELndERRERLAE 631
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
254-491 |
2.80e-04 |
|
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: 46.10 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 254 EIDELRVRVSDLQR---EAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKhLQE 330
Cdd:COG3096 390 EVDSLKSQLADYQQaldVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS-VAD 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 331 ELKCQRQNA---------ESSRCNAEQRRKDMEREHqRELVEQQRERQALEKQHQQENNRLNQEiQQARTLHNTLQAQHD 401
Cdd:COG3096 469 AARRQFEKAyelvckiagEVERSQAWQTARELLRRY-RSQQALAQRLQQLRAQLAELEQRLRQQ-QNAERLLEEFCQRIG 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 402 KVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLtealrecESLTVSLGQMKKQEKV---LQEEVKRLTEELA 478
Cdd:COG3096 547 QQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL-------EQLRARIKELAARAPAwlaAQDALERLREQSG 619
|
250
....*....|...
gi 1207190900 479 EALKLIKELQAQL 491
Cdd:COG3096 620 EALADSQEVTAAM 632
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-470 |
3.94e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 247 MEDALRNEIDELrvrVSDLQREAQLETERMKDVESRLaqanREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVK 326
Cdd:COG4717 47 LLERLEKEADEL---FKPQGRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 327 HLQEELKCQRQNAEssrcnaeqrrkdmEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCLQ 406
Cdd:COG4717 120 KLEKLLQLLPLYQE-------------LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190900 407 KQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEV 470
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-1010 |
4.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 669 LQKRLEDLETQRRAETEARTKLKQLsRKHSTQTEQQRAKALELKDSLVKLE----TQLEQEKKESSKLKETLHALQSEAE 744
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEK-RQQLERLRREREKAERYQALLKEKReyegYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 745 NRKVNDQEEDSQLKKalaEMEQKETIMEE-----------EMMGIKKELQDLQLKLAQEREEREQERLEERKLIRReegl 813
Cdd:TIGR02169 251 EELEKLTEEISELEK---RLEEIEQLLEElnkkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 814 kIAQLQEELD-ILRKSTGLEEKISKDNLPLTYLhlehhqnTDQKADLTENKDLIPSPgVQEFSVNLQNTMVRNEAKTIEL 892
Cdd:TIGR02169 324 -LAKLEAEIDkLLAEIEELEREIEEERKRRDKL-------TEEYAELKEELEDLRAE-LEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 893 imdleAQTKPKTSPSDMNRARAlsteasdLDNSTVLVLEVERLRAARDRESEKAKVSQRKLEELQKQVTTQTKQLTQAFE 972
Cdd:TIGR02169 395 -----EKLKREINELKRELDRL-------QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350
....*....|....*....|....*....|....*...
gi 1207190900 973 SQSKhidnLLSELEDKECALQKQAEELQKCQEKICFLE 1010
Cdd:TIGR02169 463 DLSK----YEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
318-1015 |
4.81e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 318 AQTAEQKVKHL--QEELKCQRQNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNT 395
Cdd:pfam02463 179 IEETENLAELIidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 396 LQAQHDKVcLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECES--LTVSLGQMKKQEKVLQEEVKRL 473
Cdd:pfam02463 259 EIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEekLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 474 TEELAE---------ALKLIKELQAQLAASPPPVAAPNFSSAGDSFSPCVS-------LHHDRSSPFNNSSQRKRAPNTG 537
Cdd:pfam02463 338 EELEKElkeleikreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeeELELKSEEEKEAQLLLELARQL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 538 RTREEERMKYPSGREPGEGIDSEHIDKFESEEKSQKRIGVQTLPS-------GSLKLTEFDLDTSVMEQDTGIEDVDTDS 610
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelelkkSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 611 FTSDST----RGTMPKSESDISRSLKLDNTSGKTEKY-----------------DSTTLKDLKKQNAELQDELRDVKYDL 669
Cdd:pfam02463 498 RSQKESkarsGLKVLLALIKDGVGGRIISAHGRLGDLgvavenykvaistavivEVSATADEVEERQKLVRALTELPLGA 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 670 QKRLEDLETQRRAETEARTK--------LKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKKESSKLKETlhALQS 741
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLeidpilnlAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG--VSLE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 742 EAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQEREEREQERLEERKLIRREEGLKIAQLQEE 821
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 822 LDILRKSTGLEEKISKDNLPLtylhlehHQNTDQKADLTENKDLIPSPGVQEFSVNLQNTMVRNEAKTIELIMDLEAQTK 901
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSR-------LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEE 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 902 PKTSPSDMNRARALSTEASDLDNSTVLVLEVERLRAARDRESEKAKVSQRKLEELQKQVTTQTKQLTQAFESQSKHidnl 981
Cdd:pfam02463 809 ELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL---- 884
|
730 740 750
....*....|....*....|....*....|....
gi 1207190900 982 LSELEDKECALQKQAEELQKCQEKICFLEEKQTR 1015
Cdd:pfam02463 885 KDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-840 |
5.03e-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: 43.76 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 667 YDLQK---RLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKKESSKLKETLHALQSea 743
Cdd:COG1579 10 LDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 744 eNRKVND-QEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAqereerEQERLEERKLIRREEglKIAQLQEEL 822
Cdd:COG1579 88 -NKEYEAlQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA------ELEAELEEKKAELDE--ELAELEAEL 158
|
170
....*....|....*....
gi 1207190900 823 DILR-KSTGLEEKISKDNL 840
Cdd:COG1579 159 EELEaEREELAAKIPPELL 177
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
641-743 |
6.73e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 641 EKYDSTtLKDLKKQNAELQDELRDVKYDLQKRLEDLET--QRRAETEAR-TKLKQLSRKHSTQTE---------QQRAKA 708
Cdd:COG0497 257 AEYDPS-LAELAERLESALIELEEAASELRRYLDSLEFdpERLEEVEERlALLRRLARKYGVTVEellayaeelRAELAE 335
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207190900 709 LE-LKDSLVKLETQLEQEKKESSKLKETLHALQSEA 743
Cdd:COG0497 336 LEnSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
647-1019 |
7.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 647 TLKDLKKQNAELqDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHST----QTEQQRAKALELKDSLVKLETQL 722
Cdd:TIGR02168 177 TERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYKELKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 723 EQEKKESSKLK---ETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAqereereqe 799
Cdd:TIGR02168 256 EELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE--------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 800 rLEERKLIRREEGLkiAQLQEELDILRKS-TGLEEKISKDNLPLTYLHLehhQNTDQKADLTENKDLIPSPGVQEFSvnL 878
Cdd:TIGR02168 327 -ELESKLDELAEEL--AELEEKLEELKEElESLEAELEELEAELEELES---RLEELEEQLETLRSKVAQLELQIAS--L 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 879 QNTMVRNEAKtielIMDLEAqtkpktspsdmnRARALSTEASDLDNSTVL--VLEVERLRAARDRESEKAKVSQRKLEEL 956
Cdd:TIGR02168 399 NNEIERLEAR----LERLED------------RRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207190900 957 QKQVTTQTKQLTQAFESQSKHIDNLLSELEdkecALQKQAEELQKCQEKICFLEEKQTRTNDL 1019
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLD----SLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
249-488 |
7.73e-04 |
|
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: 44.65 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLT------RTQEQLTRAQTRSTQETDRAQTAE 322
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdvtimeRFQMELKDVERKIAQQAAKLQGSD 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 323 ---------QKVKHLQEELKCQRQNAESSRCNAEQRRKDME---------REHQRELVEQQRERQALEKQHQQ---ENNR 381
Cdd:TIGR00606 820 ldrtvqqvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksktnelKSEKLQIGTNLQRRQQFEEQLVElstEVQS 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 382 LNQEIQQARTLHNTLQAQHDKVCLQKQSL-----------ERDLEDVKGKLKNTEA----------DLKESQKREAQTE- 439
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELissketsnkkaQDKVNDIKEKVKNIHGymkdienkiqDGKDDYLKQKETEl 979
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 440 AKLTEALRECE-----------SLTVSLGQMKKQEKVLQ---------EEVKRLTEELAEALKLIKELQ 488
Cdd:TIGR00606 980 NTVNAQLEECEkhqekinedmrLMRQDIDTQKIQERWLQdnltlrkreNELKEVEEELKQHLKEMGQMQ 1048
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
248-479 |
7.80e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKH 327
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 328 LQ---EELKCQRQNAESSRCNAEQRRKDME--REHQRELVEQQRERQALEK------------------QHQQENNRLNQ 384
Cdd:PRK02224 403 APvdlGNAEDFLEELREERDELREREAELEatLRTARERVEEAEALLEAGKcpecgqpvegsphvetieEDRERVEELEA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 385 EIQQARTLHNTLQAQHDKVcLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEK 464
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
250
....*....|....*
gi 1207190900 465 VLQEEVKRLTEELAE 479
Cdd:PRK02224 562 EAEEEAEEAREEVAE 576
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
699-790 |
8.17e-04 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 43.06 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 699 TQTE-QQRAKALELKDSLVKLETQLEQEKKESSKLKETLHALQSEAENRkvNDQEEDSQLKKALAEMEQKETIMEEemmg 777
Cdd:pfam03961 141 TKTEiEVGVDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQ--LPPEKREQLEKLLETKNKLSEELEE---- 214
|
90
....*....|...
gi 1207190900 778 IKKELQDLQLKLA 790
Cdd:pfam03961 215 LEEELKELKEELE 227
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
261-437 |
9.59e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.49 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 261 RVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRST--QETDRAQTAEQKVKHLQEELKCQRQN 338
Cdd:pfam15558 38 RRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVieKESRWREQAEDQENQRQEKLERARQE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 339 AESSRCNAEQRRKDMEREHQ--RELVEQQ---RERQALEKQHQ---------QENNRLNQEIQQARTLHNTLQAQHDKVC 404
Cdd:pfam15558 118 AEQRKQCQEQRLKEKEEELQalREQNSLQlqeRLEEACHKRQLkereeqkkvQENNLSELLNHQARKVLVDCQAKAEELL 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207190900 405 LQK---QSLERDLEDVKGKLKNTEADLKESQKREAQ 437
Cdd:pfam15558 198 RRLsleQSLQRSQENYEQLVEERHRELREKAQKEEE 233
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
251-470 |
9.98e-04 |
|
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: 44.17 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 251 LRNEIDELRVRVSDLQR---EAQL---ET--ERMKDVESRLAQAN---REISSKEQSLTRTQEQLTRAQTRSTQEtDRAQ 319
Cdd:COG3096 862 LRQQLDQLKEQLQLLNKllpQANLladETlaDRLEELREELDAAQeaqAFIQQHGKALAQLEPLVAVLQSDPEQF-EQLQ 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 320 TAEQKVKHLQEELKCQ-------RQN------AESSRCNAEQRRKDMEREHQRELVEQQRERQALE-KQHQQENNRLNQE 385
Cdd:COG3096 941 ADYLQAKEQQRRLKQQifalsevVQRrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQlRQAQAQYSQYNQV 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 386 IQQARTLHNTLQAQHdkvclqkQSLERDLEDV------------KGKLKNTEADLKESQKREAQTEAKLTEALRECESLT 453
Cdd:COG3096 1021 LASLKSSRDAKQQTL-------QELEQELEELgvqadaeaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
250
....*....|....*..
gi 1207190900 454 VSLGQMKKQEKVLQEEV 470
Cdd:COG3096 1094 KRLRKAERDYKQEREQV 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
653-827 |
1.04e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 653 KQNAEL-QDELRDVKYDLQKRLEDLETQRRaetEARTKLKQLSRKHSTQTEQQRAKALElkDSLVKLETQLEQEKKESSK 731
Cdd:COG3206 163 EQNLELrREEARKALEFLEEQLPELRKELE---EAEAALEEFRQKNGLVDLSEEAKLLL--QQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 732 LKETLHALQSEAENRK-----VNDQEEDSQLKKALAEMEQKETIMEE-------EMMGIKKELQDLQLKLAQEREEREQE 799
Cdd:COG3206 238 AEARLAALRAQLGSGPdalpeLLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180
....*....|....*....|....*...
gi 1207190900 800 RLEERKLIRREEglkiAQLQEELDILRK 827
Cdd:COG3206 318 LEAELEALQARE----ASLQAQLAQLEA 341
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
250-786 |
1.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 250 ALRNEIDELRVRVSDL--QREAQLET-ERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVK 326
Cdd:PRK02224 210 GLESELAELDEEIERYeeQREQARETrDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 327 HLQEELKCQRQNAESSRCNAE---QRRKDME--REHQRELVEQQRERQaleKQHQQENNRLNQEIQQARTlhntlqaqhd 401
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEaveARREELEdrDEELRDRLEECRVAA---QAHNEEAESLREDADDLEE---------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 402 kvclQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEAL 481
Cdd:PRK02224 357 ----RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 482 KLIKELQAQLAASPPPVAAPNFSSAGDSF--SPCVSLHHDRsspfnnssqRKRApntgRTREEERMKYPSGREPGEgids 559
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKCPECGQPVegSPHVETIEED---------RERV----EELEAELEDLEEEVEEVE---- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 560 EHIDKFESEEKSQKRIgvqtlpsGSLKLTEFDLDTSVMEQDTGIEDvDTDSFTSDSTRGTMPKSESDISRslklDNTSGK 639
Cdd:PRK02224 496 ERLERAEDLVEAEDRI-------ERLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAEAEEKR----EAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 640 TEKYDST--TLKDLKKQNAELQDELRDVKyDLQKRLEDLETQRRAETEARTKLKQLsrkhSTQTEQQRAKALELKDSLVK 717
Cdd:PRK02224 564 EEEAEEAreEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREAL----AELNDERRERLAEKRERKRE 638
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 718 LETQLEQEKKEssklketlhalqsEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQ 786
Cdd:PRK02224 639 LEAEFDEARIE-------------EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
284-511 |
1.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 284 AQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKcqrqnaessrcNAEQRRKDMERE--HQREL 361
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEiaEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 362 VEQQRERQALEKQHQQENNR--------LNQE-----IQQARTLhNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADL 428
Cdd:COG3883 81 IEERREELGERARALYRSGGsvsyldvlLGSEsfsdfLDRLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 429 KESQKREAQTEAKLTEALRECESLtvsLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQLAASPPPVAAPNFSSAGD 508
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEAL---LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
...
gi 1207190900 509 SFS 511
Cdd:COG3883 237 AAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
251-820 |
1.35e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 251 LRNEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQE 330
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 331 ------ELKCQRQNAESSRCNA---------EQRRKDMEREHQrELVEQQRERqALEKQHQQENNRLNQEIQQARTLHNT 395
Cdd:TIGR00618 272 lraqeaVLEETQERINRARKAAplaahikavTQIEQQAQRIHT-ELQSKMRSR-AKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 396 LQAQHDKvclqkqsLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTealrecesltvslgqMKKQEKVLQEEVKRLTE 475
Cdd:TIGR00618 350 LHSQEIH-------IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT---------------LTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 476 ELAEALKLIKE---LQAQLAASPPPVAapnfssagdsfspcvsLHHDRSSPFNNSSQRKRAPNTGRTREEERMKYPSGRE 552
Cdd:TIGR00618 408 EQATIDTRTSAfrdLQGQLAHAKKQQE----------------LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 553 PGEGIDSEHIDKFESEEKSQKRIGVQTLPSGSLKLTEFDLDTSVMEQDTGIEDVDTDSFTS-DSTRGTMPKSESDISRSL 631
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 632 KLDNTSGKTEKYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHS------------T 699
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlqdvR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 700 QTEQQRAKALELKD-SLVKLETQLEQEKKESSKLKETLHALQSEAENRKVND--QEEDSQLKKALAEMEQKETIMEEEMM 776
Cdd:TIGR00618 632 LHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQkmQSEKEQLTYWKEMLAQCQTLLRELET 711
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1207190900 777 GIK---KELQDLQLKLAQEREEREQERLEERKLIRREEGLKIAQLQE 820
Cdd:TIGR00618 712 HIEeydREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
248-784 |
1.52e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 248 EDALRNEIDELRVRVSDLQREAQLETERmkdvESRLAQANREISSKEQSLTRTQEQLTRAQTRstqetdrAQTAEQKVKH 327
Cdd:pfam05557 68 EEALREQAELNRLKKKYLEALNKKLNEK----ESQLADAREVISCLKNELSELRRQIQRAELE-------LQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 328 LQEELKCQRQNAEssrcNAEQRR-----------------KDMEREHQ-----RELVEQQRERQALEKQHQQENNRLNQE 385
Cdd:pfam05557 137 LQERLDLLKAKAS----EAEQLRqnlekqqsslaeaeqriKELEFEIQsqeqdSEIVKNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 386 IQQARTLHNTLQAQHDKVCLQKQSLERdLEDVKGKLKNTEADlKESQKREAQTEAKLTEA----LRECESLTVSLGQMKK 461
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLER-EEKYREEAATLELE-KEKLEQELQSWVKLAQDtglnLRSPEDLSRRIEQLQQ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 462 QEKVLQEEVKRLTEELAEALKLIKELQAQLAASPPPVAAPNFSsagdsfspcvslhHDRSSPFNNSSQRKRapntgRTRE 541
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKK-------------LKRHKALVRRLQRRV-----LLLT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 542 EERMKYpsgREPGEGIDSEHIDKFESEEKSQKRIGVQTLpsgslkLTEFDLDTSVMEQDTgieDVDTDSFTSDSTRGTMP 621
Cdd:pfam05557 353 KERDGY---RAILESYDKELTMSNYSPQLLERIEEAEDM------TQKMQAHNEEMEAQL---SVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 622 KSESDISRSLKLDNTSGKT-EKYDSttlkdLKKQNAELQ---DELRDVKYDLQKRLEDLETQRRAETeARTKLKQLSRKH 697
Cdd:pfam05557 421 ERELQALRQQESLADPSYSkEEVDS-----LRRKLETLElerQRLREQKNELEMELERRCLQGDYDP-KKTKVLHLSMNP 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 698 STQTEQQRAKALElkdslvKLETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMG 777
Cdd:pfam05557 495 AAEAYQQRKNQLE------KLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQA 568
|
....*..
gi 1207190900 778 IKKELQD 784
Cdd:pfam05557 569 KIQEFRD 575
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
253-446 |
1.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 253 NEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLtraqtrstqetdraQTAEQKVKHLQEEL 332
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------------EEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 333 KCQRQNaessrcnaeqrrKDMErEHQRELVEQQRERQALEKQHQQennrLNQEIQQARTLHNTLQAQHDKVclqKQSLER 412
Cdd:COG1579 83 GNVRNN------------KEYE-ALQKEIESLKRRISDLEDEILE----LMERIEELEEELAELEAELAEL---EAELEE 142
|
170 180 190
....*....|....*....|....*....|....
gi 1207190900 413 DLEDVKGKLKNTEADLKESQKREAQTEAKLTEAL 446
Cdd:COG1579 143 KKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
679-1012 |
1.86e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 679 QRRAETEartklKQLsrkHSTQTEQQRAKAL--ELKDSLVKLETQLEQEKK---ESSKLKETLHALQSeaeNRKVNDQEE 753
Cdd:TIGR02168 172 ERRKETE-----RKL---ERTRENLDRLEDIlnELERQLKSLERQAEKAERykeLKAELRELELALLV---LRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 754 DSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQEREEREQERLEERKLirreeGLKIAQLQEELDILRKStgleE 833
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-----ANEISRLEQQKQILRER----L 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 834 KISKDNLPLTYLHLEHHQNT--DQKADLTENKDLIpspgvQEFSVNLQNTMVRNEAKTIELIMDLEAQTKPKTSPSDMNR 911
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKldELAEELAELEEKL-----EELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 912 ARALSTEASDLDNSTVLVLEVERLRAARDREsekaKVSQRKLEELQKQVTTQTKQLTQAFESQSKHIDNLLSELEDKECA 991
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRE----RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
330 340
....*....|....*....|.
gi 1207190900 992 LQKQAEELQKCQEKICFLEEK 1012
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERE 483
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
245-491 |
1.87e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 245 CGMEDALRNEIDELRVRVSDLQRE---AQLETERMKDvesrLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQT- 320
Cdd:pfam00038 46 SRLYSLYEKEIEDLRRQLDTLTVErarLQLELDNLRL----AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVd 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 321 AEQKVKHLQEELKCQRQNaessrcnaeqrrkdmereHQRELVEqqrerqaLEKQHQQENnrLNQEIQQARTLH-----NT 395
Cdd:pfam00038 122 LEAKIESLKEELAFLKKN------------------HEEEVRE-------LQAQVSDTQ--VNVEMDAARKLDltsalAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 396 LQAQHDkvCLQKQSLERDLEDVKGKLKN--TEADLKESQKREAQTEakLTEALRECESLTVSLGQMKKQ----EKVLQEE 469
Cdd:pfam00038 175 IRAQYE--EIAAKNREEAEEWYQSKLEElqQAAARNGDALRSAKEE--ITELRRTIQSLEIELQSLKKQkaslERQLAET 250
|
250 260
....*....|....*....|..
gi 1207190900 470 VKRLTEELAEALKLIKELQAQL 491
Cdd:pfam00038 251 EERYELQLADYQELISELEAEL 272
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
50-424 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 50 KQKQKHEEVRVELAAVQRELggvrEAAQAEVRTRERLSHDLQVK----TGQVHSLEGQLESAKKLTQSLTQEIKRLEAEL 125
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQElsdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 126 EKLQKGNGSGESTLfstpcwntsspwDNNGGFRAESESKAqHARQLQFGDvpkPSAGGASSPFPQQPYKSPPLRRHVRQS 205
Cdd:TIGR02169 747 SSLEQEIENVKSEL------------KELEARIEELEEDL-HKLEEALND---LEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 206 EPSTPSSvfpwERDVLWSTPKGRPTSLVSSSEVMIKSSNCGMEDALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQ 285
Cdd:TIGR02169 811 EARLREI----EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 286 ANREISskeqsltRTQEQLTRAQtrstQETDRAQTAEQKVKHLQEELKCQRQNAESSRCNAEQRRKDMEREHQRELVEQ- 364
Cdd:TIGR02169 887 LKKERD-------ELEAQLRELE----RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEd 955
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190900 365 -QRERQALEKQHQQ---ENNRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERDLEDVKGKLKNT 424
Cdd:TIGR02169 956 vQAELQRVEEEIRAlepVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
254-491 |
2.25e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 254 EIDELRVRVSDLQREAQLETERMKDVESRLAQA---NREISSKEQSLTRTQEQ----LTRAQTRSTQETDRAQTAEQKVk 326
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTeeeLRSLSKEFQELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKE- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 327 hLQEELKCQRQNAESSRCNAEQRRKDMEREHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKvclQ 406
Cdd:pfam07888 230 -AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQ---E 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 407 KQSLERDLEDVKGKLKNTEADLKesqkreaQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKE 486
Cdd:pfam07888 306 RETLQQSAEADKDRIEKLSAELQ-------RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQK 378
|
....*
gi 1207190900 487 LQAQL 491
Cdd:pfam07888 379 EKEQL 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
355-491 |
2.43e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 355 REHQRELVEQQRERQALEKQH----------QQENNRLNQEIQQARTLHNTLQAQHDKVCLQK--QSLERDLEDVKGKLK 422
Cdd:COG1579 27 KELPAELAELEDELAALEARLeaakteledlEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 423 NTEADLKESQKREAQTEAKLTEALRECESLtvslgqmKKQEKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAEL-------EAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
369-491 |
2.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 369 QALEKQHQQENNRLNQEIQQARTLHNtlqaqhdkvclqkqslerDLEDVKGKLKNTEADLKESQKREAQteAKLTEALRE 448
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKE------------------ELEEKKEKLQEEEDKLLEEAEKEAQ--QAIKEAKKE 585
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207190900 449 CESLTVSLGQMKKQ------EKVLQEEVKRLT---EELAEALKLIKELQAQL 491
Cdd:PRK00409 586 ADEIIKELRQLQKGgyasvkAHELIEARKRLNkanEKKEKKKKKQKEKQEEL 637
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1060-1311 |
2.53e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 1060 EKVSEHTVQLPVEASVIQNIDQTNT--SEISDKLQATEHFKQQsvdtsnsstASDAPI-ISDVTEEKSSsvLQDEQLNVV 1136
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQQ---------LAQAPAkLRQAQAELEA--LKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 1137 NCQNDSIPehsihdIKELER----VTKELQAAQLELNVM------------KAQN--SELALQGDMIKDKLLNVQQENQE 1198
Cdd:PRK11281 115 RETLSTLS------LRQLESrlaqTLDQLQNAQNDLAEYnsqlvslqtqpeRAQAalYANSQRLQQIRNLLKGGKVGGKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 1199 LKSTLKHLCEdtgAKQDgALNLANSKNKSLLSSNEGLQSISPLGKEKLVVQHGNSEAEVQSLQEQIqklQDQILDLFEQn 1278
Cdd:PRK11281 189 LRPSQRVLLQ---AEQA-LLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAI---NSKRLTLSEK- 260
|
250 260 270
....*....|....*....|....*....|...
gi 1207190900 1279 rtQAEQLElwklsTVEETAGNNSPSIVLKEFEL 1311
Cdd:PRK11281 261 --TVQEAQ-----SQDEAARIQANPLVAQELEI 286
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
249-487 |
2.62e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 249 DALRNEIDELRVRVSDLQREAQLETERMKDVESRLAQ-------ANR---EISSKEQSLTRTQEQLTRAQTRSTQetdrA 318
Cdd:PRK10929 105 DALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQlpqqqteARRqlnEIERRLQTLGTPNTPLAQAQLTALQ----A 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 319 QTAEQKVKHLQEELK----CQRQnaESSRCNAE-----QRRKDMEREHQRELVEQQRER---QALEKQHQQENNR----- 381
Cdd:PRK10929 181 ESAALKALVDELELAqlsaNNRQ--ELARLRSElakkrSQQLDAYLQALRNQLNSQRQReaeRALESTELLAEQSgdlpk 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 382 -LNQEIQQARTLHNTL--QAQH-DKVCLQKQSLERDLEDVKGKLkNTeadLKEsQKREAQTEAKLTEALReceSLTVSLG 457
Cdd:PRK10929 259 sIVAQFKINRELSQALnqQAQRmDLIASQQRQAASQTLQVRQAL-NT---LRE-QSQWLGVSNALGEALR---AQVARLP 330
|
250 260 270
....*....|....*....|....*....|....*
gi 1207190900 458 QMKKQEKVLQE----EVKRLT-EELAEALKLIKEL 487
Cdd:PRK10929 331 EMPKPQQLDTEmaqlRVQRLRyEDLLNKQPQLRQI 365
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
355-491 |
3.08e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 355 REHQRELVEQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDK--------VCLQKQSLERDLEDVKGKLKNTEA 426
Cdd:pfam04012 32 RDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKgneelareALAEKKSLEKQAEALETQLAQQRS 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190900 427 DLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQAQL 491
Cdd:pfam04012 112 AVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIEER 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
365-790 |
3.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 365 QRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHD---KVCLQKQSLERDLEDVKGKLKNTEADLK--ESQKREAQTE 439
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEklEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 440 AKLTEALRECESLTVSLGQMKKQEKV---LQEEVKRLTEELAEALKLIKELQAQLAASPPPVAApnfssagdsfspcvsl 516
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQ---------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 517 hhDRSSPFNNSSQRKRAPNTGRTREEERMKypSGREPGEGIDSEHIDKFESEEKSQKRIGVQTLPSGSLKLTEFDLDTSV 596
Cdd:COG4717 196 --DLAEELEELQQRLAELEEELEEAQEELE--ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 597 MEQDTGIEDVDTDSFTSDSTRGTmpKSESDISRSLKLDNTSGKTEKYDSTTLKDLKKQNAELQDELRDVKYDLQKRLEDL 676
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLA--REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 677 ETQRRAETEARTKLKQLSRKHSTQTEQQRAKAlELKDSLVKLETQLEQEKKESSKLKETLHALQSEA-ENRKVNDQEEDS 755
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGV-EDEEELRAALEQAEEYQELKEELEELEEQLEELLgELEELLEALDEE 428
|
410 420 430
....*....|....*....|....*....|....*
gi 1207190900 756 QLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLA 790
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELE 463
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
259-390 |
3.29e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 259 RVRVSDLQREAQLET-ERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQtAEQKVKhLQEELKCQ-- 335
Cdd:COG2268 202 RIAEAEAERETEIAIaQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYE-IAEANAERev 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190900 336 RQNAESSRCNAEQRRKDMERE-HQRELVEQQRERQALEKQHQQENNRLNQEIQQAR 390
Cdd:COG2268 280 QRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAK 335
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
632-1018 |
3.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 632 KLDNTSGKTEKYDSTtlkdlKKQNAELQDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRK---HSTQTEQQRAKA 708
Cdd:PRK02224 214 ELAELDEEIERYEEQ-----REQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREreeLAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 709 LELKDSLVKLETQLEQEKKESsklkETLHALQSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLK 788
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADA----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 789 LAQEREEREQERLEERKliRREEglkIAQLQEELDILRKSTGleekiskdNLPLTYLHLEhhqntDQKADLTENKDLIPS 868
Cdd:PRK02224 365 AAELESELEEAREAVED--RREE---IEELEEEIEELRERFG--------DAPVDLGNAE-----DFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 869 PgVQEFSVNLQNT--------MVRNEAKTIELIMDLEAQTKPKTSPSDMNRARALSTEASDLDNSTVLVLE-VERLRAAR 939
Cdd:PRK02224 427 R-EAELEATLRTArerveeaeALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEErLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 940 DRESEKAKVSQRK--LEELQKQVTTQTKQLTQAFESQSKHIDNLLSELEDKECALQKQAEELQKCQEKICFLEEKQTRTN 1017
Cdd:PRK02224 506 EAEDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
.
gi 1207190900 1018 D 1018
Cdd:PRK02224 586 E 586
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
246-491 |
3.64e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 246 GMEDALRNEIDELRVRVS----DLQREAQLETERMKDVESRLAQANRE----ISSKEQSLTRTQEQLTRAQTRSTQETDR 317
Cdd:pfam07111 16 GHQDVLERRLDTQRPTVTmweqDVSGDGQGPGRRGRSLELEGSQALSQqaelISRQLQELRRLEEEVRLLRETSLQQKMR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 318 AQTAEQKVKHLQEELKCQRQNAESSR---CNAEQRRKDMEREHQRELVEqqrerqaLEKQHQQENNRLNQEIQQARtlhn 394
Cdd:pfam07111 96 LEAQAMELDALAVAEKAGQAEAEGLRaalAGAEMVRKNLEEGSQRELEE-------IQRLHQEQLSSLTQAHEEAL---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 395 tlqaqhDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESLTVSLGQMKKQ--EKVLQE---- 468
Cdd:pfam07111 165 ------SSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYvgEQVPPEvhsq 238
|
250 260
....*....|....*....|....*
gi 1207190900 469 --EVKRltEELAEALKLIKELQAQL 491
Cdd:pfam07111 239 twELER--QELLDTMQHLQEDRADL 261
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
657-827 |
3.73e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 657 ELQDELRDVKYDLQKRleDLETQRRAETEART-KLKQLSRKHSTQTEQQRAKALELKDSLVKLETQ-LEQEKKESSKLKE 734
Cdd:pfam17380 405 KILEEERQRKIQQQKV--EMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQeEERKRKKLELEKE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 735 TLHALQSEAENRKVNDQEEDSQlKKALAEMEQKETIMEEEMMGIKKELQDLQLKLAQEREEREQERLEERKLIRR----- 809
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEER-KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEqmrka 561
|
170
....*....|....*....
gi 1207190900 810 -EEGLKIAQLQEELDILRK 827
Cdd:pfam17380 562 tEERSRLEAMEREREMMRQ 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-377 |
3.96e-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: 41.98 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 19 KVKQLLAQNEKLNKEKQQRQLQLDNSEVALHKQKQKHEEVRVELAAVQRELggvrEAAQAEVrtrERLSHD--LQVKTgQ 96
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL----EELNKKI---KDLGEEeqLRVKE-K 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 97 VHSLEGQLESAKKLTQSLTQEIKRLEAELEKLQKGNGSGESTLfstpcwntsspwdnnGGFRAESESKAQHARQLQfgdv 176
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI---------------EELEREIEEERKRRDKLT---- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 177 pkpsaggasspfpqQPYKSPPLRRHVRQSEPSTPSSVFPWERDVLwstpkgrptslvsssevmikssncgmeDALRNEID 256
Cdd:TIGR02169 357 --------------EEYAELKEELEDLRAELEEVDKEFAETRDEL---------------------------KDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 257 ELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKcqr 336
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY--- 472
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1207190900 337 qnaessrcnaeqRRKDMEREHQRELVEQQRERQALEKQHQQ 377
Cdd:TIGR02169 473 ------------DLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
291-464 |
4.07e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.91 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 291 SSKEQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQRQNAESSRCNAEQRRKDMEREHQRE--LVEQQRER 368
Cdd:pfam05262 188 EDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAknLPKPADTS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 369 QALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKvclqkqslERDLEDVKgklknteadlKESQKREAQTEAKLTEALRE 448
Cdd:pfam05262 268 SPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK--------DHKAFDLK----------QESKASEKEAEDKELEAQKK 329
|
170
....*....|....*.
gi 1207190900 449 CESLTVSLGQMKKQEK 464
Cdd:pfam05262 330 REPVAEDLQKTKPQVE 345
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
294-480 |
4.17e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 294 EQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEelKCQRQNAESSRCN---AEQRRKDMEREHQRElvEQQRERQA 370
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNR--RIQLLEEELERTEerlAEALEKLEEAEKAAD--ESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 371 LEKQHQQENNRLNQeiqqartlhntLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTE------ 444
Cdd:pfam00261 83 LENRALKDEEKMEI-----------LEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVEleeelk 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207190900 445 -ALRECESLTVSLGQMKKQEKVLQEEVKRLTEELAEA 480
Cdd:pfam00261 152 vVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEA 188
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
682-790 |
4.65e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 682 AETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKKESSKLKETLHALQSEAENRKVNDQEEDsqLKKAL 761
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEIKD--LQKEL 188
|
90 100 110
....*....|....*....|....*....|
gi 1207190900 762 AEMEQKETI-MEEEMMGIKKELQDLQLKLA 790
Cdd:cd22656 189 EKLNEEYAAkLKAKIDELKALIADDEAKLA 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
14-490 |
4.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 14 GHVLQKVKQLLAQNEKLNKEKQQRQLQLDNSEVALHKQKQKHEEVRVELAAVQRElggvreaAQAEVRTRERLSHDLQVk 93
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE-------AAALLEALEEELEALEE- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 94 tgQVHSLEGQLESAKKLTQSLTQEIKRLEAeleklQKGNGSGESTLfstpcwntsspwdnnggFRAESESKAQHAR-QLQ 172
Cdd:COG4913 406 --ALAEAEAALRDLRRELRELEAEIASLER-----RKSNIPARLLA-----------------LRDALAEALGLDEaELP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 173 FG----DVP------KPSAGGASSPF------PQQPYK-------SPPLRRHVRqsepstpssvfpWERdVLWSTPKGRP 229
Cdd:COG4913 462 FVgeliEVRpeeerwRGAIERVLGGFaltllvPPEHYAaalrwvnRLHLRGRLV------------YER-VRTGLPDPER 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 230 TSLVSSS---EVMIKSSNCG--MEDALRNEIDELRVR-VSDLQREA----------QLETERMKDVESRLAQA------N 287
Cdd:COG4913 529 PRLDPDSlagKLDFKPHPFRawLEAELGRRFDYVCVDsPEELRRHPraitragqvkGNGTRHEKDDRRRIRSRyvlgfdN 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 288 RE-ISSKEQSLTRTQEQLTRAQtrstqetDRAQTAEQKVKHLQeelkcQRQNAESSRCNAEQRRKDMeREHQRELVEQQR 366
Cdd:COG4913 609 RAkLAALEAELAELEEELAEAE-------ERLEALEAELDALQ-----ERREALQRLAEYSWDEIDV-ASAEREIAELEA 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 367 ERQALEKQHqQENNRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEAL 446
Cdd:COG4913 676 ELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1207190900 447 RECESLTVSLGQMKKQekvLQEEVKRLTEELAEALKLIKELQAQ 490
Cdd:COG4913 755 FAAALGDAVERELREN---LEERIDALRARLNRAEEELERAMRA 795
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
648-834 |
5.40e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.89 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 648 LKDLKKQNAELQDELRDVKyDLQKRlEDLETQRRAETEArtKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKK 727
Cdd:pfam15619 20 LAELQSKLEELRKENRLLK-RLQKR-QEKALGKYEGTES--ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 728 ESSKLKETLHALQSEAENRKVNDQEEdsqLKKALAEMEQKetiMEEEmmgiKKELQDLQLKLAQEREEREQERLEERKLI 807
Cdd:pfam15619 96 ELLRLRDQLKRLEKLSEDKNLAEREE---LQKKLEQLEAK---LEDK----DEKIQDLERKLELENKSFRRQLAAEKKKH 165
|
170 180
....*....|....*....|....*..
gi 1207190900 808 rREEGLKIAQLQEELDILRKStgLEEK 834
Cdd:pfam15619 166 -KEAQEEVKILQEEIERLQQK--LKEK 189
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
316-452 |
5.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 316 DRAQTAEQKVKHLQEELKCQR--QNAESSRCNAEQRRKDMerehQRELVEQQRERQALEKQHQQENNRLNqeiqqartLH 393
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRelYTSRRQLAAEQYRLVEM----ARELAELNEAESDLEQDYQAASDHLN--------LV 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190900 394 NTLQAQHDKVclqkQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEALRECESL 452
Cdd:PRK04863 341 QTALRQQEKI----ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
253-789 |
5.94e-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: 41.54 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 253 NEIDELRVRVSDLQREAQLETERMKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQetdrAQTAEQKVKHLQ--- 329
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN----LKKKIQKNKSLEsqi 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 330 EELKCQRQNAESsrcNAEQRRKDMErEHQRELVEQQRERQALEKQHQQENNRLN---QEIQQARTLHNTLQAQHDKV--- 403
Cdd:TIGR04523 221 SELKKQNNQLKD---NIEKKQQEIN-EKTTEISNTQTQLNQLKDEQNKIKKQLSekqKELEQNNKKIKELEKQLNQLkse 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 404 --CLQKQSLERDLEDVKGKLKNTEADLKESQKREAQTEAKLTEalrecesLTVSLGQMKKQEKVLQEEVKRLTEELAEAL 481
Cdd:TIGR04523 297 isDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ-------LNEQISQLKKELTNSESENSEKQRELEEKQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 482 KLIKELQAQlaaspppvaapnfssagdsfspcvslhhdrsspfnNSSQRKRAPNTGRTREEERMKYPSGREPGEGIDSEh 561
Cdd:TIGR04523 370 NEIEKLKKE-----------------------------------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 562 IDKFESE----EKSQKRIGVQTLpsgSLKLTEFDLDTSVMEQDTGIEDVdtdsftsDSTRGTMPKSESDISRSLKLDNTS 637
Cdd:TIGR04523 414 IKKLQQEkellEKEIERLKETII---KNNSEIKDLTNQDSVKELIIKNL-------DNTRESLETQLKVLSRSINKIKQN 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 638 GKTEKydsttlKDLKKQNAELqDELRDVKYDLQKRLEDLETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVK 717
Cdd:TIGR04523 484 LEQKQ------KELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190900 718 --LETQLEQEKKESSKLKETLHAL---QSEAENRKVNDQEEDSQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKL 789
Cdd:TIGR04523 557 enLEKEIDEKNKEIEELKQTQKSLkkkQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
254-489 |
6.69e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 254 EIDELRVRVSDLQREAQLETERMKDVESRL--AQANREISSKEQSLTRtqeqltraqtRSTQETDRAQtAEQKVKHLQEE 331
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLsvAQAAHSQFEQAYQLVR----------KIAGEVSRSE-AWDVARELLRR 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 332 LKCQRQNAEssrcNAEQRR---KDMEREHQrelveQQRERQALEKQHQQENNRLNQEIQQARTLHNTLQAQHDKVCLQKQ 408
Cdd:PRK04863 505 LREQRHLAE----QLQQLRmrlSELEQRLR-----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 409 SLERDLEDVKGKLKNTEADLKESQKREA---QTEAKLtEALREC--------ESLTVSLGQMKKQEKVLQEEVKRLTEEL 477
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPawlAAQDAL-ARLREQsgeefedsQDVTEYMQQLLERERELTVERDELAARK 654
|
250
....*....|..
gi 1207190900 478 AEALKLIKELQA 489
Cdd:PRK04863 655 QALDEEIERLSQ 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-130 |
6.94e-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: 40.90 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 50 KQKQKHEEVRVELAAVQRELGGVREAAQAEVRTRERLSHDLQVKTGQVHSLEGQLESAKKLTQSLTQEIKRLEAELEKLQ 129
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
.
gi 1207190900 130 K 130
Cdd:COG4942 104 E 104
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
649-767 |
7.57e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 649 KDLKKQNAELQDELRDVKYDLQKRLEdlETQRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLETQLEQEKKE 728
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAE--AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207190900 729 SSKLKETLHALQSEAENRKVNDQEEDSQLKKALAEMEQK 767
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
241-488 |
7.92e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 241 KSSNCGMEDALRNEIDELRVRVSD--LQREAQLETER-----MKDVESRLAQANREISSKEQSLTRTQEQLTRAQTRSTQ 313
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDqiTSKEAQLESSReivksYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 314 -ETDRAQTAEQKVKHLQ---EELKcqrqnaessrcNAEQRRKDMEREHQRELVEQQRERQALEKQHQ---QENNRLNQEI 386
Cdd:TIGR00606 281 mEKDNSELELKMEKVFQgtdEQLN-----------DLYHNHQRTVREKERELVDCQRELEKLNKERRllnQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 387 QQARTLHNTLQAQHDKVCLQKQSLERDLE--------DVKGKLKNTEADLKESQKREAQTEAKLTEALRECESL-----T 453
Cdd:TIGR00606 350 GRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLkqeqaD 429
|
250 260 270
....*....|....*....|....*....|....*
gi 1207190900 454 VSLGQMKKQEKVLQEEVKRLTEELAEALKLIKELQ 488
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ 464
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
294-388 |
8.44e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 294 EQSLTRTQEQLTRAQTRSTQETDRAQTAEQKVKHLQEELKCQRQNAE----SSRCNAEQRRKDMEREHQRELVEQQR--- 366
Cdd:pfam02841 189 EEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEaqerSYQEHVKQLIEKMEAEREQLLAEQERmle 268
|
90 100
....*....|....*....|....*..
gi 1207190900 367 -----ERQALEKQHQQENNRLNQEIQQ 388
Cdd:pfam02841 269 hklqeQEELLKEGFKTEAESLQKEIQD 295
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-785 |
9.29e-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: 40.82 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 338 NAESSRCNAEQRRKDMEREHQRELVEQQRERQALekqhQQENNRLNQEIQQARTLHNTLQAQHDKVCLQKQSLERDLEDV 417
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 418 KGKLKNTEADLKESQKREAQTEAKLTEalrecesltvslgqmkkqekvLQEEVKRLTEELAEALKLIKELQAqlaasppp 497
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKE---------------------LEARIEELEEDLHKLEEALNDLEA-------- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 498 vaapnfssagdsfspcvslhHDRSSPFNNSSQRKRAPNTGRTREEERMKYPSGREPGEGIDSEHIDKfESEEKSQKRIgv 577
Cdd:TIGR02169 787 --------------------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK-EIQELQEQRI-- 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 578 qtlpsgSLKLTEFDLDTSVMEQDTGIEDVDTdsftsdstrgtmpksesdisrslKLDNTSGKTEKYDSTtLKDLKKQNAE 657
Cdd:TIGR02169 844 ------DLKEQIKSIEKEIENLNGKKEELEE-----------------------ELEELEAALRDLESR-LGDLKKERDE 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 658 LQDELRdvkyDLQKRLEDLETQRRaetEARTKLKQLSRKHSTQTEQQRA--KALELKDSLVKLETQLEQEKKESSKLKET 735
Cdd:TIGR02169 894 LEAQLR----ELERKIEELEAQIE---KKRKRLSELKAKLEALEEELSEieDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1207190900 736 LHALqsEAENRKVNDQEEDSQlkKALAEMEQKETIMEEEMMGIKKELQDL 785
Cdd:TIGR02169 967 IRAL--EPVNMLAIQEYEEVL--KRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
528-775 |
9.74e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 528 SQRKRAPNTGRTReeeRMKYPSGREPGEGIDSEHidKFESEEKSQKRIgvQTLPSGSLKLTEFDLDTSVMEQDTGIE-DV 606
Cdd:PLN02939 16 PIRSRAPFYLPSR---RRLAVSCRARRRGFSSQQ--KKKRGKNIAPKQ--RSSNSKLQSNTDENGQLENTSLRTVMElPQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 607 DTDSFTSDSTRGTMPKSESDISRSLKLDNTSGKTEKYDSTTLKDLKK--QNAE----LQDELR-----DV------KYDL 669
Cdd:PLN02939 89 KSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGmiQNAEknilLLNQARlqaleDLekilteKEAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 670 QKRLEDLETqRRAETEARTKLKQLSRKHSTQTEQQRAKALELKDSLVKLET--------QLEQEKKESSKLKETLHALQS 741
Cdd:PLN02939 169 QGKINILEM-RLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGlcvhslskELDVLKEENMLLKDDIQFLKA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1207190900 742 ------EAENRKVNDQEEDSQLKKALAEMEQKETIMEEEM 775
Cdd:PLN02939 248 elievaETEERVFKLEKERSLLDASLRELESKFIVAQEDV 287
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
319-1019 |
9.95e-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: 40.80 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 319 QTAEQKVKHLQEELKCQRQNAESSrcnAEQRRKDMEREHQRElvEQQRERQALEKQHQQENNRLnQEIQQART----LHN 394
Cdd:TIGR00606 196 QTQGQKVQEHQMELKYLKQYKEKA---CEIRDQITSKEAQLE--SSREIVKSYENELDPLKNRL-KEIEHNLSkimkLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 395 TLQAqHDKVCLQKQSLERDLEDVKGK-LKNTEADLKESQKREAQTEAKLTEALRECESltvSLGQMKKQEKVLQEEVKRL 473
Cdd:TIGR00606 270 EIKA-LKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQR---ELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 474 TEELAEALKLIKELQAQLAASPPPVAAPNFSSAGDSFS--PCVSLHHDRSSPFNNSSQRKRAPNTGRTREEERMKypsgr 551
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFErgPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK----- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 552 epgEGIDSEHIDKFESEEKSQKRIGVQTLPSGSLKLTEFDLDTSVMEQDTGIEDvdtDSFTSDStrgTMPKSESDISRSL 631
Cdd:TIGR00606 421 ---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD---RILELDQ---ELRKAERELSKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 632 KLDNTsgktekydsttlKDLKKQNAELQDELRDVKYDLQKRLEDLEtQRRAETEARTKLKQLSRKHSTQTEQQRAKALEL 711
Cdd:TIGR00606 492 KNSLT------------ETLKKEVKSLQNEKADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 712 KDSLVKLETQLEQEKkessKLKETLHALQSEaenrkVNDQEED-SQLKKALAEMEQKETIMEEEMMGIKKELQDLQLKLA 790
Cdd:TIGR00606 559 SDELTSLLGYFPNKK----QLEDWLHSKSKE-----INQTRDRlAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 791 QEREEreqerleerklirREEGLKIAQLQEELdilrkstgleEKISKDNLPLTYLHLEHHQNTDQKADLTE------NKD 864
Cdd:TIGR00606 630 DVCGS-------------QDEESDLERLKEEI----------EKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcQRV 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 865 LIPSPGVQEFSVNLQN-------------TMVRNEAKTIELIMDL------EAQTKPKTSPSDMNRARALSTEASDLDNS 925
Cdd:TIGR00606 687 FQTEAELQEFISDLQSklrlapdklksteSELKKKEKRRDEMLGLapgrqsIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 926 tvlVLEVERLRAARDRESEKAKVSQRK---LEELQKQVTTQTKQLTQ-AFESQSKHIDNLLSEL----EDKECALQK--- 994
Cdd:TIGR00606 767 ---IEEQETLLGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQqAAKLQGSDLDRTVQQVnqekQEKQHELDTvvs 843
|
730 740
....*....|....*....|....*.
gi 1207190900 995 QAEELQKC-QEKICFLEEKQTRTNDL 1019
Cdd:TIGR00606 844 KIELNRKLiQDQQEQIQHLKSKTNEL 869
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
413-491 |
9.97e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.44 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190900 413 DLEDVKGKLK--NTEADLKE-----SQKREAQTEaklTEALR-ECESLTVSLGQMKKQEK---VLQEEVKRLTEELAEAL 481
Cdd:PRK05431 10 NPEAVKEALAkrGFPLDVDElleldEERRELQTE---LEELQaERNALSKEIGQAKRKGEdaeALIAEVKELKEEIKALE 86
|
90
....*....|
gi 1207190900 482 KLIKELQAQL 491
Cdd:PRK05431 87 AELDELEAEL 96
|
|
|