|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-742 |
0e+00 |
|
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: 1230.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 1 MYMRQLSDLESTVSQLRSELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL 80
Cdd:pfam15921 314 MYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 81 SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST 160
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 161 KEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL 240
Cdd:pfam15921 474 KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 241 KLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELE 320
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 321 KVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRN 400
Cdd:pfam15921 634 KVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 401 TLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELE 480
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 481 VLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSVKPRLLQPASVTRSH 560
Cdd:pfam15921 794 VLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTH 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 561 SNIPSSQSTTSFLSHHSIKTNTPKEDPTRDLKQLLQELRTVINEEPAMALSKTEEDGRTPSLGALEDRVRDCITESSLRA 640
Cdd:pfam15921 874 SNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRS 953
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 641 ELCHRSNNSLResTEGSKSSETLSREPVPLHPGDLEDPSSCFTFTSTASPSGKMSASRSFSSSPKKSPVHSLLTSSAEES 720
Cdd:pfam15921 954 DICHSSSNSLQ--TEGSKSSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGS 1031
|
730 740
....*....|....*....|..
gi 568935751 721 VNSTPQYRSTKPIHSPTSAKVS 742
Cdd:pfam15921 1032 IGSSSQYRSAKTIHSPDSVKDS 1053
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-385 |
4.39e-16 |
|
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: 83.18 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 28 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE 107
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 108 LDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVS 186
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREaLDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 187 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMT 262
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 263 QLVGQHGRTAGAMQVEKAQLEKEINDR-KLELQEFKILKDKKDAKIRELEARVSDLELEKVKL--VNagserLRAVKDIR 339
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpVN-----LAAIEEYE 996
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568935751 340 herdqllnEVKTSRTELNHLSEDYEVLKRNFRNKSEEM-ESTTNRLK 385
Cdd:TIGR02168 997 --------ELKERYDFLTAQKEDLTEAKETLEEAIEEIdREARERFK 1035
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-536 |
2.48e-15 |
|
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: 80.49 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 3 MRQLSDLESTVSQLRSELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL---LADLHKREKE 79
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILrerLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 80 LS--LEKEQNKRLWDRDTGNSIT--IDHLRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLE---- 148
Cdd:TIGR02168 321 LEaqLEELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEELESrleELEEQLETLRSKVAQLELQIAslnn 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 149 KVSSLTAQLESTKEMLRKVVEELTAKKMNLESSE-----RTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 223
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 224 KNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEkAQLEKEI-------------NDRK 290
Cdd:TIGR02168 481 ERELAQLQA---RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD-EGYEAAIeaalggrlqavvvENLN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 291 LELQEFKILKDKKDAKIRELEARV------------------------SDLELEKVKLVNAGSERL---RAVKDIrherD 343
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTFLPLDSikgteiqgndreilkniegflgvaKDLVKFDPKLRKALSYLLggvLVVDDL----D 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 344 QLLNEVKTSRTELNHLSEDYEVLKRNF----------------RNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEG 407
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 408 SDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQER 487
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 568935751 488 RLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 536
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-525 |
7.06e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 2 YMRQLSDLESTVSQLRSELRESkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 81
Cdd:COG1196 230 LLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 82 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmERQMAAIQGKNESLEKVSSLTAQLESTK 161
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---EAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 162 EMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 241
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 242 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE---------KEINDRKLELQEFKILKDKKDAKIRELEA 312
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 313 RVSDLELEKV-KLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELN-----------------HLSEDYEVLKRNFRNKS 374
Cdd:COG1196 543 ALAAALQNIVvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALaaalargaigaavdlvaSDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 375 EEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFL 454
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935751 455 KEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 525
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-482 |
1.48e-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: 74.71 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 105 RRELDDRNMEVQRLEALLKamksecqgQMERQMAAIQGKNESLEKVSSLTAQLE------STKEMLRKVvEELTAKKMNL 178
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILN--------ELERQLKSLERQAEKAERYKELKAELRelelalLVLRLEELR-EELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 179 ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQI 258
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE---ISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 259 EnmtqlvgQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDI 338
Cdd:TIGR02168 326 E-------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 339 RHERDQLLNEVKTSRTELNHLSEDYEVLKRNF-RNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAmkvam 417
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA----- 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935751 418 gmQKQITAKRGQIDALQSKVQFLEEavtsankerhfLKEEKSKLSQELSTVATEKNKMAGELEVL 482
Cdd:TIGR02168 474 --EQALDAAERELAQLQARLDSLER-----------LQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-496 |
3.84e-12 |
|
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: 70.09 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 165 RKVVEELTAKkmnLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQM 244
Cdd:TIGR02168 676 RREIEELEEK---IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---LARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 245 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 324
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 325 VNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESttnrLKMQLKSAQSELEQTRNTLKT 404
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS----LEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 405 MEgsdghamkvamgmqKQITAKRGQIDALQSKVQFLEEAVTSA-NKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLR 483
Cdd:TIGR02168 906 LE--------------SKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
|
330
....*....|...
gi 568935751 484 SQERRLKEKVANM 496
Cdd:TIGR02168 972 RRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-369 |
9.86e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 19 ELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ-------ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW 91
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 92 DRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaIQGKNESLEK-VSSLTAQLESTKEMLRKVVEE 170
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE---IQAELSKLEEeVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 171 LTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKV 250
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR---LGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 251 IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKdAKIRELEARVSDLELEKVKLVNAGSE 330
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ-AELQRVEEEIRALEPVNMLAIQEYEE 983
|
330 340 350
....*....|....*....|....*....|....*....
gi 568935751 331 RLRAVKDIRHERDQLLNEvktsRTELNHLSEDYEVLKRN 369
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEE----RKAILERIEEYEKKKRE 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-497 |
1.19e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRMYedkiEELEKQlvlaNSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 83
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEV----KELEEL----KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 84 KEQNKRLwDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGqMERQMAAIQGKNESLEKVSSLTAQLESTKEM 163
Cdd:PRK03918 279 EEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 164 LRKVV---EELTAKKMNLES-----SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT 235
Cdd:PRK03918 357 LEERHelyEEAKAKKEELERlkkrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 236 ECEALKLQMAEKDK--VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrklelQEFKILKDKKDAK-IRELEA 312
Cdd:PRK03918 437 KCPVCGRELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK------KESELIKLKELAEqLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 313 RVSDLELEKVKLVNAGSERLRAV-----KDIRHERDQL--LNEVKTSRTELNH----LSEDYEVLKRNFRNKS----EEM 377
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKliklkGEIKSLKKELekLEELKKKLAELEKkldeLEEELAELLKELEELGfesvEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 378 ESTTNRLK------MQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKvqFLEEavtsankER 451
Cdd:PRK03918 591 EERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--YSEE-------EY 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568935751 452 HFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 497
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-406 |
1.58e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 43 SELTEARTERDQFSQESgnldDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitiDHLRRELDDRnmEVQRLEALL 122
Cdd:TIGR02169 170 RKKEKALEELEEVEENI----ERLDLIIDEKRQQLERLRREREKAERY-----------QALLKEKREY--EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 123 KAMKSECQgQMERQMAAIQgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNLESSE-----RTVSDLTASLQEKER 197
Cdd:TIGR02169 233 EALERQKE-AIERQLASLE---EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 198 AIEATN-------AEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgQHGR 270
Cdd:TIGR02169 309 SIAEKEreledaeERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELE-------EVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 271 TAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLelekvklvNAGSERLRA-VKDIRHERDQLLNEV 349
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL--------NAAIAGIEAkINELEEEKEDKALEI 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 568935751 350 KTSRTELNHLSEDYEVLKRNFRNKSEEMesttNRLKMQLKSAQSELEQTRNTLKTME 406
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEY----DRVEKELSKLQRELAEAEAQARASE 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
5-479 |
1.90e-11 |
|
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: 67.74 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 5 QLSDLESTVSQLRSELRESKrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 84
Cdd:TIGR04523 76 KIKILEQQIKDLNDKLKKNK----DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 85 EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML 164
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK-LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 165 RKVVE----ELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE--CE 238
Cdd:TIGR04523 231 KDNIEkkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 239 ALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLE 318
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQ-------LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 319 LEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKR-NFRNKSE--EMESTTNRLKMQLKSAQSEL 395
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKEtIIKNNSEikDLTNQDSVKELIIKNLDNTR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 396 EQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKE-------EKSKLSQELSTV 468
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEkieklesEKKEKESKISDL 543
|
490
....*....|.
gi 568935751 469 ATEKNKMAGEL 479
Cdd:TIGR04523 544 EDELNKDDFEL 554
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-374 |
3.74e-11 |
|
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: 67.00 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 28 EDKIEELEKQLvlansELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdtgnsiTIDHLRRE 107
Cdd:TIGR02168 192 EDILNELERQL-----KSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQE------------ELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 108 LDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLekvSSLTAQLESTKEMLRKvveeltakkmNLESSERTVSD 187
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYAL---ANEISRLEQQKQILRE----------RLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 188 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQtecEALKLQMAEKDKVIEILRQQIENMTQLVGQ 267
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL---EELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 268 HGRTAGAMQVEKAQLEKEINDRKLELQEfkILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLN 347
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*..
gi 568935751 348 EVKTSRTELNHLSEDYEVLKRNFRNKS 374
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-350 |
4.76e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 28 EDKIEELEKQL-VLANS--------ELTEARTERDQfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlwdrdtgns 98
Cdd:COG1196 192 EDILGELERQLePLERQaekaeryrELKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELEELEA--------- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 99 iTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNL 178
Cdd:COG1196 261 -ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 179 ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKDKVIEILRQQI 258
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL----------LEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 259 ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDI 338
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330
....*....|..
gi 568935751 339 RHERDQLLNEVK 350
Cdd:COG1196 490 AARLLLLLEAEA 501
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
22-528 |
6.39e-11 |
|
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: 65.90 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 22 ESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHkrEKELSLEKEQNKRLWDRDTGNSIti 101
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDH--EKIQHLEEEYKKEINDKEKQVSL-- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 102 dhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNLESS 181
Cdd:pfam05483 245 --LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 182 ERTVSDLT----ASLQEKERAIEATNAEITKLRSRV----DLKLQELQHLKNEGDHLR---------------------N 232
Cdd:pfam05483 323 TKTICQLTeekeAQMEELNKAKAAHSFVVTEFEATTcsleELLRTEQQRLEKNEDQLKiitmelqkksseleemtkfknN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 233 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEkaqlEKEINDRKLELQEFKILKDKKDAKIRELEA 312
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR----EKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 313 RVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSE-------EMESTTNRLK 385
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnlrdELESVREEFI 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 386 MQLKSAQSELEQTRNTLKTMEGSDGHAMKVAM-------GMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEK 458
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935751 459 SKLSQELSTVATEKNKMAG----ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQH 528
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
132-487 |
7.75e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 132 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVE-ELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLR 210
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 211 SRVDLKLQELQHLKNE-----GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEKE 285
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA--------------EERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 286 IndrklelqefkilkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEV 365
Cdd:TIGR02169 331 I--------------DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 366 LKRnfrnKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGsdghamKVAmGMQKQITAKRGQIDALQSKVQFLEEAVT 445
Cdd:TIGR02169 397 LKR----EINELKRELDRLQEELQRLSEELADLNAAIAGIEA------KIN-ELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568935751 446 SANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQER 487
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-531 |
1.14e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 5 QLSDLESTVSQLRSELRE-SKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL--- 80
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEElLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaql 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 81 SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLK-------AMKSECQGQMerQMAAIQGKNESLEKVSSL 153
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyeaAIEAALGGRL--QAVVVENLNAAKKAIAFL 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 154 tAQLESTKEML----RKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH 229
Cdd:TIGR02168 566 -KQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPG 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 230 LRNVQTECEALK-------------LQMAEKDKVIEILRQQIEnmtqlvgqhgrtagAMQVEKAQLEKEINDRKLELQEF 296
Cdd:TIGR02168 645 YRIVTLDGDLVRpggvitggsaktnSSILERRREIEELEEKIE--------------ELEEKIAELEKALAELRKELEEL 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 297 KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRnfrnKSEE 376
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA----EIEE 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 377 MESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKE 456
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568935751 457 EKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ--RQEQESVRLKLQHTLD 531
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlELRLEGLEVRIDNLQE 943
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-502 |
7.15e-10 |
|
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: 62.73 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 18 SELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD--DQLQKLLadlhkrEKELSLEKEQNKRLWDrdt 95
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkIQKNKSL------ESQISELKKQNNQLKD--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 96 gnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK---EMLRKVVEELT 172
Cdd:TIGR04523 233 ----NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQKEQDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 173 AK--KMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKV 250
Cdd:TIGR04523 309 NKelKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEKLKKENQSYKQE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 251 IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSE 330
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 331 R-------LRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKmQLKSAQSELEQTRNTLK 403
Cdd:TIGR04523 466 LetqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 404 TMEGSDGHAMKvAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLR 483
Cdd:TIGR04523 545 DELNKDDFELK-KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
490
....*....|....*....
gi 568935751 484 SQERRLKEKVANMEVALDK 502
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNK 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-396 |
2.63e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 101 IDHLRRELDDRNMEVQRLEALLKAMK---SECQGQMERQMAAIQGKNESLEKVSsltAQLESTKEMLRKVVEELTAKKMN 177
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSqelSDASRKIGEIEKEIEQLEQEEEKLK---ERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 178 LESSERTVSDLTASLQEKERAIEATNAEItkLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDKviEILRQQ 257
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEK--EYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 258 IENMTQLVGqhgrtagAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD 337
Cdd:TIGR02169 835 IQELQEQRI-------DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935751 338 IRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTN--RLKMQLKSAQSELE 396
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIR 968
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
6-294 |
1.33e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 57.77 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 6 LSDLESTVSQLRSELRESkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 85
Cdd:pfam19220 99 LREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 86 QNKRLWDRDTGNSITIDHLRRELDD----RNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE--------KVSSL 153
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAEletqLDATRARLRALEGQLAAE-QAERERAEAQLEEAVEAHRaeraslrmKLEAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 154 TAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdlkLQELQHLKNEGDHlrnv 233
Cdd:pfam19220 254 TARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ----FQEMQRARAELEE---- 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935751 234 qtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRKLELQ 294
Cdd:pfam19220 326 --RAEMLTKALAAKDAALERAEERIASLSDRIAELTK---RFEVERAALEQANRRLKEELQ 381
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-527 |
2.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 2 YMRQLSDLESTVSQLRSELRESKRmyedKIEELEKqlvlansELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 81
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLA----EIEELER-------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 82 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 161
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 162 EMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNV----QTEC 237
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVgeryATAI 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 238 EA-----LKLQMAEKDKV----IEILRQ-QIENMTQL----VGQHGRTAGAMQvEKAQLEKEIN----DRKLE------L 293
Cdd:TIGR02169 542 EVaagnrLNNVVVEDDAVakeaIELLKRrKAGRATFLplnkMRDERRDLSILS-EDGVIGFAVDlvefDPKYEpafkyvF 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 294 QEFKILKDKKDAKIRELEARVSDLE---LEKVKLVNAGSERLRavkdirherdqllnevktsRTELNHLSEDYEVLKrnF 370
Cdd:TIGR02169 621 GDTLVVEDIEAARRLMGKYRMVTLEgelFEKSGAMTGGSRAPR-------------------GGILFSRSEPAELQR--L 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 371 RNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKE 450
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 451 RHFLKEEKSKLSQELSTVATEKNKM------------AGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQE 518
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
....*....
gi 568935751 519 QESVRLKLQ 527
Cdd:TIGR02169 840 EQRIDLKEQ 848
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-497 |
2.96e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 112 NMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMNLESSERT 184
Cdd:PRK03918 175 KRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeiEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 185 VSDLTASLQEKERAIEATNAEITKLRSRVdlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 264
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKV----KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 265 VGQ---HGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDaKIRELEARVSDLELEKVK-----LVNAGSERLRAVK 336
Cdd:PRK03918 330 IKEleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLTPEKLEkeleeLEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 337 DIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEE-----MESTT---NRLKMQLKSAQSELEQTRNTLKTMEGs 408
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTaelKRIEKELKEIEEKERKLRKELRELEK- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 409 dghamkvAMGMQKQITAKRG---QIDALQSKVQ-FLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAG---ELEV 481
Cdd:PRK03918 488 -------VLKKESELIKLKElaeQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAE 560
|
410
....*....|....*.
gi 568935751 482 LRSQERRLKEKVANME 497
Cdd:PRK03918 561 LEKKLDELEEELAELL 576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-504 |
6.08e-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: 55.54 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 271 TAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLElekvklvNAGSERLRAVKDIRHERDQLLNEVK 350
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-------RRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 351 TSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQI 430
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935751 431 DALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 504
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-495 |
7.77e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 1 MYMRQLSDLESTVSQLRSELRESKRMYEDKIEELE-KQLVlanSELTEARTERDQFSQESGNLDDqlQKLLADLHKREKE 79
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLH---ERLNGLESELAELDEEIERYEE--QREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 80 LSLEKEQNKRLwdrdtgnsiTIDHLRRELDDrnmevqrlealLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES 159
Cdd:PRK02224 241 EVLEEHEERRE---------ELETLEAEIED-----------LRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 160 TKEMLRKVVEELTAKKMNLESSERTVSDltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLrnvQTECEA 239
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL---ESELEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 240 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKilkdkkdAKIRELEARVSDLE- 318
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE-------ATLRTARERVEEAEa 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 319 -LEKVKLVNAG-----SERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKrnfrnKSEEMESTTNRLKMQLKSAQ 392
Cdd:PRK02224 448 lLEAGKCPECGqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLE 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 393 SELEQTRNTLKTMEgsdghamkvamgmqKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEK 472
Cdd:PRK02224 523 ELIAERRETIEEKR--------------ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
490 500
....*....|....*....|....*....
gi 568935751 473 NKMA------GELEVLRSQERRLKEKVAN 495
Cdd:PRK02224 589 ESLErirtllAAIADAEDEIERLREKREA 617
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
29-231 |
8.28e-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: 55.16 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 29 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 108
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 109 DDRNmevQRLEALLKAM-------------KSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAKK 175
Cdd:COG4942 100 EAQK---EELAELLRALyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 176 MNLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 231
Cdd:COG4942 174 AELEALLAELEEERAALEalkaERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
51-520 |
9.47e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 51 ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKA-MKSEC 129
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 130 QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-----TAKKMNLESSERTVSDLTASLQEKERAIEATNA 204
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqeeleELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 205 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE----------------KDKVIEILRQQIENMTQLVGQH 268
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllslILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 269 GRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKLVNAGSERLRA---VKDIRHERD 343
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELldRIEELQELLREAEELEEelqLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 344 QLLNEVK-TSRTELNHLSEDYEvlkrNFRNKSEEMESTTNRLKMQLKSAQSELEQTrntlktmegsdghamkvamgmqkq 422
Cdd:COG4717 374 ALLAEAGvEDEEELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLEAL------------------------ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 423 itakrgQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEknkmaGELEVLRSQERRLKEKVAnmEVALDK 502
Cdd:COG4717 426 ------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELR--ELAEEW 492
|
490 500
....*....|....*....|
gi 568935751 503 ASLQFAEC--QDIIQRQEQE 520
Cdd:COG4717 493 AALKLALEllEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-525 |
1.19e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 8 DLESTVSQLRSELRESkrmyEDKIEELEKQLVLANSELTEAR---TERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 84
Cdd:PRK02224 203 DLHERLNGLESELAEL----DEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 85 EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEAL---LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 161
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARreeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 162 EMLRKVVEELTAKkmnLESSERTVSDltaslqeKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALK 241
Cdd:PRK02224 359 EELREEAAELESE---LEEAREAVED-------RREEIEELEEEIEELRERFGDAPVDLGNAE---DFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 242 LQMAEKDKVIEILRQQIENMTQLV--------GQ------HGRTAGAMQVEKAQLEKEINDRKLELQEfkiLKDKKDA-- 305
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLeagkcpecGQpvegspHVETIEEDRERVEELEAELEDLEEEVEE---VEERLERae 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 306 KIRELEARVSDLElEKVKLVnagsERLRAVKDIRHERDQLlnEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLK 385
Cdd:PRK02224 503 DLVEAEDRIERLE-ERREDL----EELIAERRETIEEKRE--RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 386 mQLKSAQSELEQTRNTLKTMEGSdghamkvamgmQKQITAKRGQIDALQSKVQFLEEavtsANKERHFLKEEKSKLSQEL 465
Cdd:PRK02224 576 -ELNSKLAELKERIESLERIRTL-----------LAAIADAEDEIERLREKREALAE----LNDERRERLAEKRERKREL 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 466 STVATEKNkmageLEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 525
Cdd:PRK02224 640 EAEFDEAR-----IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-206 |
1.31e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSE-----LRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD-----L 73
Cdd:COG3206 189 KELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 74 HKREKELSLEKEQnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE-KVSS 152
Cdd:COG3206 269 RAQLAELEAELAE-----------------LSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQaREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568935751 153 LTAQLESTKEMLRKVVE---ELTAKKMNLESSERTVSDLTASLQEK--ERAIEATNAEI 206
Cdd:COG3206 332 LQAQLAQLEARLAELPEleaELRRLEREVEVARELYESLLQRLEEArlAEALTVGNVRV 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-379 |
1.72e-07 |
|
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: 54.38 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 154 TAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNV 233
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 234 QtecEALKLQMAEKDKVIEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRE 309
Cdd:COG4942 99 L---EAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 310 LEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMES 379
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
231-531 |
2.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 231 RNVQTECEALKLQMAEKDkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIREL 310
Cdd:COG1196 216 RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 311 EARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMEsttnrlkmqlKS 390
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----------EA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 391 AQSELEQTRNTLKTMEGSDGHamkvamgmQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVAT 470
Cdd:COG1196 364 EEALLEAEAELAEAEEELEEL--------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935751 471 EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLD 531
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
29-501 |
3.36e-07 |
|
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: 54.03 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 29 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH---KREKELSLEKEQNKRLWDRDTGNsitidhLR 105
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEerlKKEEKGRQELEKAKRKLEGESTD------LQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 106 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKemlrkvvEELTAKKMNLESSERTV 185
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ-------EDLESERAARNKAEKQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 186 SDLTASLQ----EKERAIEATNAEiTKLRSRvdlKLQELQHLKNEGDHLRNVQtecEALKLQMAEKDKvieilrQQIENM 261
Cdd:pfam01576 295 RDLGEELEalktELEDTLDTTAAQ-QELRSK---REQEVTELKKALEEETRSH---EAQLQEMRQKHT------QALEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 262 TQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHE 341
Cdd:pfam01576 362 TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 342 RDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTnRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKvamGMQK 421
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET-RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR---NVER 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 422 QITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKmagelevLRSQERRLKEKVANMEVALD 501
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK-------LEKTKNRLQQELDDLLVDLD 590
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
44-506 |
3.88e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 53.54 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 44 ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT---IDHLRRELDDRNMEVQRLEA 120
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGgkkYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 121 LLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLtASLQEKERAIE 200
Cdd:pfam05622 81 ARDDYRIKCE-ELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDL-GDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 201 ATNAEITK--------------LRSRVDL---KLQELQHlKNEGDHLRNVQTECEALKLQ------MAEKDKVIE---IL 254
Cdd:pfam05622 159 ERNAEYMQrtlqleeelkkanaLRGQLETykrQVQELHG-KLSEESKKADKLEFEYKKLEeklealQKEKERLIIerdTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 255 RQQIENM--TQLVGQHGRTAGAMQVEKAQ---------LEKEINDRKLELQ-EFKILKDKKDAKIRELEARVSDLELEKV 322
Cdd:pfam05622 238 RETNEELrcAQLQQAELSQADALLSPSSDpgdnlaaeiMPAEIREKLIRLQhENKMLRLGQEGSYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 323 KLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFrnkSEEMEsttnrlkmQLKSAQSELEQTRNTL 402
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKL---EEHLE--------KLHEAQSELQKKKEQI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 403 KTMEgsdghamkvamgmQKQITAKRGQIDALQSKVQFLEEAVtSANKERHFLKEEKSKlsQELSTVATEKNKMAG-ELEV 481
Cdd:pfam05622 387 EELE-------------PKQDSNLAQKIDELQEALRKKDEDM-KAMEERYKKYVEKAK--SVIKTLDPKQNPASPpEIQA 450
|
490 500
....*....|....*....|....*
gi 568935751 482 LRSQERRLKEKVANMEVALDKASLQ 506
Cdd:pfam05622 451 LKNQLLEKDKKIEHLERDFEKSKLQ 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-525 |
6.67e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRM--YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 81
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 82 LEKEQNKRLwdrdtgNSITIDHlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE----KVSSLTAQL 157
Cdd:PRK03918 346 KLKELEKRL------EELEERH--ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEeeisKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 158 ESTKEMLRKVVEELTAKK---------MNLESSERTVSDLTASLQEKERAIEATNAEITKLRSR------VDLKLQELQH 222
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKElrelekVLKKESELIK 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 223 LKNEGDHLRNVQTECEALKLQMAEKDKvieilrqqiENMTQLVGQHGRTAGAMQVEKAQLEKeINDRKLELQEFKILKDK 302
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNLEELEKKA---------EEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 303 KDAKIRELEARVSDLELEKVKLVNAGSERLR-------AVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSE 375
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEpfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 376 EMEsttnrlkmQLKSAQSELEQTRNTLKTMEGSDGHAmkvamGMQKQITAKRGQIDALQSKVQFLEEAVtsanKERHFLK 455
Cdd:PRK03918 648 ELE--------ELEKKYSEEEYEELREEYLELSRELA-----GLRAELEELEKRREEIKKTLEKLKEEL----EEREKAK 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568935751 456 EEKSKLsqelstvatekNKMAGELEVLRSQERRLKEKVAnmEVALDK----ASLQFAECQD-----IIQRQEQESVRLK 525
Cdd:PRK03918 711 KELEKL-----------EKALERVEELREKVKKYKALLK--ERALSKvgeiASEIFEELTEgkysgVRVKAEENKVKLF 776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-219 |
7.83e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 28 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL--LADLHKREKEL-SLEKE---QNKRLWDRDTGNSiTI 101
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVaSAEREiaeLEAELERLDASSD-DL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 102 DHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMNLESS 181
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGE-IGRLEKELEQAE------EELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*...
gi 568935751 182 ERTVSDLTASLQEKeraIEATNAEITKLRSRVDLKLQE 219
Cdd:COG4913 761 DAVERELRENLEER---IDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-531 |
8.10e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 2 YMRQLSDLESTVSQLR------SELRESKRMYEDKIEELEK-QLVLANSELTEARTERDQFSQESGNLDDQLQKL---LA 71
Cdd:COG4913 233 HFDDLERAHEALEDAReqiellEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLeaeLE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 72 DLHKREKELSLEKEQNKRLWDRDTGNSIT-----IDHLRRELDDRNMEVQRLEALLKAMKsecqgqmerqMAAIQGKNES 146
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEqlereIERLERELEERERRRARLEALLAALG----------LPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 147 LEKVSSLTAQLESTKEMLRKVVEELTakkmnlessertvsDLTASLQEKERAIEATNAEITKLRSR---VDLKLQEL--- 220
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALA--------------EAEAALRDLRRELRELEAEIASLERRksnIPARLLALrda 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 221 --QHLKNEGDHLRNVqteCEAlkLQMAEKDkviEILRQQIEnmtQLVGQHGRTagaMQVEKAQLE---KEINDRKLE--L 293
Cdd:COG4913 449 laEALGLDEAELPFV---GEL--IEVRPEE---ERWRGAIE---RVLGGFALT---LLVPPEHYAaalRWVNRLHLRgrL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 294 QEFKILKDKKDAKIRELEARvsDLeLEKVKL-VNAGSERLRA-------------VKDIRHERDQLLNE--VKTSRT--E 355
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPD--SL-AGKLDFkPHPFRAWLEAelgrrfdyvcvdsPEELRRHPRAITRAgqVKGNGTrhE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 356 LN---HLSEDYeVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAM--GMQKQITAKRGQI 430
Cdd:COG4913 592 KDdrrRIRSRY-VLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEysWDEIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 431 DALQSKVQFLEEA---VTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 507
Cdd:COG4913 671 AELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
570 580
....*....|....*....|....*.
gi 568935751 508 AE--CQDIIQRQEQESVRLKLQHTLD 531
Cdd:COG4913 751 LEerFAAALGDAVERELRENLEERID 776
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
5-506 |
1.03e-06 |
|
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: 52.44 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 5 QLSDLESTVSQLRSELRESKRMYEDKIEELEKqlvlanseltEARTERDQFSQESgnldDQLQKLLADLHKREKELSLEK 84
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEK----------KASALKRQLDRES----DRNQELQKRIRLLEKREAEAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 85 EQNKRLWDRD---TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEkvssltaQLESTK 161
Cdd:pfam05557 69 EALREQAELNrlkKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-------ELQERL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 162 EMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIE--ATNAEITKLR----SRVDLKLQELQHLKNEGDHLRNVQT 235
Cdd:pfam05557 142 DLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqEQDSEIVKNSkselARIPELEKELERLREHNKHLNENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 236 ECEALKLQMAEKDKVIEilrqQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDA---KIRELEA 312
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLE----REEKYRE-------EAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlsrRIEQLQQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 313 RVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMesttNRLKMQLKSAQ 392
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKER----DGYRAILESYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 393 SELEQTRNTLKTMEGSDGhAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSklSQELSTVATEK 472
Cdd:pfam05557 367 KELTMSNYSPQLLERIEE-AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQES--LADPSYSKEEV 443
|
490 500 510
....*....|....*....|....*....|....
gi 568935751 473 NKMAGELEVLRSQERRLKEKVANMEVALDKASLQ 506
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKNELEMELERRCLQ 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
236-524 |
1.59e-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: 51.99 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 236 ECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEK--EINDRKLELQEFKILKDKK--DAKIRELE 311
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERL--------------RREREKAERyqALLKEKREYEGYELLKEKEalERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 312 ARVSDLELEKVKLvnagSERLRAVKDIRHERDQLLNEVKTsrtELNHLSEDYEvlkRNFRNKSEEMESTTNRLKMQLKSA 391
Cdd:TIGR02169 244 RQLASLEEELEKL----TEEISELEKRLEEIEQLLEELNK---KIKDLGEEEQ---LRVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 392 QSELEQtrntlktmegsdghamkvamgMQKQITAKRGQIDALQSKVQFLEEAVTSANKERhflkeekSKLSQELSTVATE 471
Cdd:TIGR02169 314 ERELED---------------------AEERLAKLEAEIDKLLAEIEELEREIEEERKRR-------DKLTEEYAELKEE 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568935751 472 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 524
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-366 |
1.68e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL 80
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 81 SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsecqgqmerqmaaiqgkneslEKVSSLTAQLEST 160
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE---------------------TQLKVLSRSINKI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 161 KEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcEAL 240
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-ENL 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 241 KLQMAEKDKVIEILRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELE 320
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKSLK-------KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568935751 321 KVKLVNAGSERLRAVKDIRHERDQL---LNEVKTSRTELNHLSEDYEVL 366
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIrnkWPEIIKKIKESKTKIDDIIEL 681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-507 |
1.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 243 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKV 322
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 323 KLVNAGSERLRAV-KDIRHERDQLLnevkTSRTELNHLSEDYEVLKRNFRNKSEEMEsttnrlkmQLKSAQSELEQTRNT 401
Cdd:COG4942 101 AQKEELAELLRALyRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAE--------ELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 402 LktmegsdghamkvamgmQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEV 481
Cdd:COG4942 169 L-----------------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|....*.
gi 568935751 482 LRSQERRLKEKVANMEVALDKASLQF 507
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
6-519 |
2.05e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 6 LSDLESTVSQLrSELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 85
Cdd:PRK01156 175 IDMLRAEISNI-DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 86 QNKRLWDRDTGNSITIDHLRR--ELDDRNMEVQRLEAL------------------LKAMKSECQGQMERQMAAIQgKNE 145
Cdd:PRK01156 254 YESEIKTAESDLSMELEKNNYykELEERHMKIINDPVYknrnyindyfkykndienKKQILSNIDAEINKYHAIIK-KLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 146 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 225
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 226 E-GDHLRNVQTECEALKlqmAEKDKVIEILRQQIENMTQLVGQH-----GRTAGAMQV---------EKAQLEKEINDRK 290
Cdd:PRK01156 413 EiNVKLQDISSKVSSLN---QRIRALRENLDELSRNMEMLNGQSvcpvcGTTLGEEKSnhiinhyneKKSRLEEKIREIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 291 LELQefkilkdKKDAKIRELEARVSDLELEKvklVNAGSERLRAVKDIRHERDQL---LNEVKTSRTELNHLSEDYEVLK 367
Cdd:PRK01156 490 IEVK-------DIDEKIVDLKKRKEYLESEE---INKSINEYNKIESARADLEDIkikINELKDKHDKYEEIKNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 368 -----------------------RNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQIT 424
Cdd:PRK01156 560 ledldskrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 425 AKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQelstVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 504
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIND----IEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
|
570
....*....|....*
gi 568935751 505 LQFAECQDIIQRQEQ 519
Cdd:PRK01156 716 DRINDINETLESMKK 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
4-357 |
2.48e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRM----------YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 73
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEieklkkenqsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 74 HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQMAAIQGKNESLEKVSSL 153
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN----LEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 154 TAQLESTKEMLRKVVEELTAKKMNLESserTVSDLTASLQEKERAIEATNAEITK--LRSRVDLKLQELQHLKNEGDHLR 231
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLES---EKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLK 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 232 NVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRKLELQEFKILKDKKDAKIRELE 311
Cdd:TIGR04523 582 KKQEE---KQELIDQKEKEKKDLIKEIEEKEKKI--------------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568935751 312 ARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELN 357
Cdd:TIGR04523 645 QEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
307-527 |
3.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 307 IRELEARVSDLELEKVKLvnagsERLRAVKDIRHERDQLLnevktSRTELNHLSEDYEVLkrnfRNKSEEMESTTNRLKM 386
Cdd:COG1196 195 LGELERQLEPLERQAEKA-----ERYRELKEELKELEAEL-----LLLKLRELEAELEEL----EAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 387 QLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELS 466
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935751 467 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 527
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
7-318 |
5.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 7 SDLESTVSQLRSELRESkrmyEDKIEELEKQLVLANSELTEARTERDqfsqESGNLDDQLQKLLADLHKREKELSLE--- 83
Cdd:PRK02224 366 AELESELEEAREAVEDR----REEIEELEEEIEELRERFGDAPVDLG----NAEDFLEELREERDELREREAELEATlrt 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 84 ----KEQNKRLWDR----DTGNSITIDHLRRELDDRNMEVQRLEALLKamksecqgQMERQMAAIQGKNESLEKVSSLTA 155
Cdd:PRK02224 438 arerVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELE--------DLEEEVEEVEERLERAEDLVEAED 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 156 QLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE-------LQHLKNEGD 228
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaelnskLAELKERIE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 229 HLRNVQTECEALklqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLE---------------- 292
Cdd:PRK02224 590 SLERIRTLLAAI----ADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEearedkeraeeyleqv 665
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568935751 293 ------------------------LQEFKILKDKKDAkireLEARVSDLE 318
Cdd:PRK02224 666 eekldelreerddlqaeigaveneLEELEELRERREA----LENRVEALE 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-221 |
7.90e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESkrmyEDKIEELEKQLVLANSELTEARTERDQfsqesgnLDDQLQKLLADLHKREKELSle 83
Cdd:COG4942 41 KELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE-------LEKEIAELRAELEAQKEELA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 84 kEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsecqgqmeRQMAAIQgknESLEKVSSLTAQLESTKEM 163
Cdd:COG4942 108 -ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR--------EQAEELR---ADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568935751 164 LRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 221
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
141-368 |
1.73e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 141 QGKNESLEKVSSLTAQLESTKEMLRKVVEEL-----TAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 215
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLnplreEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 216 KLQELQHLKNEGD---------HLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlVGQHGRTAGAMQVEKAQLEKEI 286
Cdd:PRK05771 119 LEQEIERLEPWGNfdldlslllGFKYVSVFVGTVPEDKLEELKLESDVENVEY-----ISTDKGYVYVVVVVLKELSDEV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 287 ND--RKLELQEFKILKDKK-DAKIRELEARVSDLElekvklvnagSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDY 363
Cdd:PRK05771 194 EEelKKLGFERLELEEEGTpSELIREIKEELEEIE----------KERESLLEELKELAKKYLEELLALYEYLEIELERA 263
|
....*
gi 568935751 364 EVLKR 368
Cdd:PRK05771 264 EALSK 268
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
14-178 |
2.18e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 14 SQLRSELRESKRMYEDKIEELEKQL-VLANSELTEARTE----RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEqnk 88
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAeAIKKEALLEAKEEihklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 89 rlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqgkNESLEKVSSLTAQlESTKEMLRKVV 168
Cdd:PRK12704 104 -----------LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ-------LQELERISGLTAE-EAKEILLEKVE 164
|
170
....*....|
gi 568935751 169 EELTAKKMNL 178
Cdd:PRK12704 165 EEARHEAAVL 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
5-206 |
3.47e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 5 QLSDLESTVSQLRSELRESkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELsleK 84
Cdd:COG3883 17 QIQAKQKELSELQAELEAA----QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 85 EQNKRLWDrdtgNSITIDHLRRELDDRNME--VQRLEALLKAMksecqgqmERQMAAIQGKNESLEKVSSLTAQLESTKE 162
Cdd:COG3883 90 ERARALYR----SGGSVSYLDVLLGSESFSdfLDRLSALSKIA--------DADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568935751 163 MLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEI 206
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-404 |
4.85e-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: 46.30 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 180 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILR 255
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 256 QQIENMTQLVGQHGRTAGAM-QVEKAQL---EKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSER 331
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568935751 332 LRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLkrnfRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKT 404
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
149-336 |
5.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 149 KVSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELqhlkneGD 228
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL------GE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 229 HLRNVQTECEALKL-----------QMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFK 297
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsesfsDFLDR---LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 568935751 298 ILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 336
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
7-473 |
5.89e-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: 46.74 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 7 SDLESTVSQLRSELRESKRMYEDKIEELEkqlvLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRekelSLEKEQ 86
Cdd:pfam10174 105 EDKFSTPELTEENFRRLQSEHERQAKELF----LLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSK----GLPKKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 87 NKRLWDRdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESlekvssltaqleSTKEMLRK 166
Cdd:pfam10174 177 GEEDWER-----------TRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDP------------AKTKALQT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 167 VVEELTAKKMNLESSERTVSDLTASL-----------QEKERAIEATNA-------EITKLRSRVDLKLQELQHLKNEGD 228
Cdd:pfam10174 234 VIEMKDTKISSLERNIRDLEDEVQMLktngllhtedrEEEIKQMEVYKShskfmknKIDQLKQELSKKESELLALQTKLE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 229 HLRN-------------------------VQTECEALKLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGAMQVEKAQLe 283
Cdd:pfam10174 314 TLTNqnsdckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTE---EKSTLAGEIRDLKDML- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 284 kEINDRKLELQEFKI------LKDkKDAKIRELEARVSDLELEK-------VKLVNAGSERLRAVKDIRHERD----QLL 346
Cdd:pfam10174 390 -DVKERKINVLQKKIenlqeqLRD-KDKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIERLKEQREredrERL 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 347 NEVKTSRTELNHLSEDYEVLKRNFRNKseemESTTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAK 426
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTEK----ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA 543
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568935751 427 RGQIDALQ------SKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKN 473
Cdd:pfam10174 544 HNAEEAVRtnpeinDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKN 596
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-495 |
8.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 130 QGQMErqmaAIQGKNESLEKVSSLTAQL---ESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEI 206
Cdd:PRK03918 134 QGEID----AILESDESREKVVRQILGLddyENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 207 TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEI 286
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 287 NDRKLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagsERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVL 366
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLE-----------EEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 367 KRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKTMEgsdgHAMKVAMGMQKQITAKRGQIDA----LQSKVQFLEE 442
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE----KAKEEIEEEISKITARIGELKKeikeLKKAIEELKK 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568935751 443 A-----VTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 495
Cdd:PRK03918 434 AkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-213 |
8.93e-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: 45.53 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRE---SKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL 80
Cdd:COG4942 27 AELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 81 SlekEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEK----------- 149
Cdd:COG4942 107 A---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAeraeleallae 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935751 150 VSSLTAQLESTKEMLRKVVEELTAKKmnlESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 213
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
4-485 |
1.01e-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: 46.19 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRMYEDKIEELEKQL-----------VLANSELTEARTERDQFSQESGNLDD------QL 66
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKkglgrtielkkEILEKKQEELKFVIKELQQLEGSSDRileldqEL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 67 QKLLADLHKREKELSLEKEQNKRLWDRDtgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNES 146
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQN--EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 147 LEKVSSLTAQLESTKEmLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 226
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 227 GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTqlvgQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKkdaK 306
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT----DENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD---K 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 307 IRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMEST------ 380
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltd 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 381 ---TNRLKMQLKSAQSELEQTRNTLKTMEGSdghamKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEE 457
Cdd:TIGR00606 791 vtiMERFQMELKDVERKIAQQAAKLQGSDLD-----RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
490 500 510
....*....|....*....|....*....|.
gi 568935751 458 KSKLSQE---LSTVATEKNKMAGELEVLRSQ 485
Cdd:TIGR00606 866 TNELKSEklqIGTNLQRRQQFEEQLVELSTE 896
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
100-366 |
1.08e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 100 TIDHLRRELDDRNMEVQRLEALLKAMKsecqgqmerqmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNLE 179
Cdd:pfam00038 55 EIEDLRRQLDTLTVERARLQLELDNLR-----------LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 180 SS---------------ERTVSDLTASLQEKERAIEATNAeitklrSRVDLklqelqhlkneGDHLRNVQTECEalklQM 244
Cdd:pfam00038 124 AKieslkeelaflkknhEEEVRELQAQVSDTQVNVEMDAA------RKLDL-----------TSALAEIRAQYE----EI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 245 AEKDK--VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSdlelekv 322
Cdd:pfam00038 183 AAKNReeAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYE------- 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568935751 323 klvnagserlRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVL 366
Cdd:pfam00038 256 ----------LQLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-231 |
1.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSElreskrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLaDLHKREKELSLE 83
Cdd:COG4913 668 REIAELEAELERLDAS--------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE-EELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 84 KEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEAL------LKAMKSECQGQMERQMAAIqgKNESLEKVSSLTAQL 157
Cdd:COG4913 739 AEDLARLELRA-----LLEERFAAALGDAVERELRENLeeridaLRARLNRAEEELERAMRAF--NREWPAETADLDADL 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 158 ESTKE---MLRKVVE----ELTAK--KMNLESSERTVSDLTASLQEKERAIeatnaeitklRSRVDLKLQELQHLK-NEG 227
Cdd:COG4913 812 ESLPEylaLLDRLEEdglpEYEERfkELLNENSIEFVADLLSKLRRAIREI----------KERIDPLNDSLKRIPfGPG 881
|
....
gi 568935751 228 DHLR 231
Cdd:COG4913 882 RYLR 885
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
243-500 |
1.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 243 QMAEKDKVIEILRQQIENMTQLVGQHGrtagAMQVEKAQLE--KEINDRKLELQEFKILKDKKDAKIRELEARVSDLELE 320
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLERAHE----ALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 321 KVKlvnagserlRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFR-NKSEEMEsttnRLKMQLKSAQSELEQTR 399
Cdd:COG4913 292 LLE---------AELEELRAELARLEAELERLEARLDALREELDELEAQIRgNGGDRLE----QLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 400 N-------TLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKvqfLEEAVTSANKERHFLKEEKSKLSQELSTVATEK 472
Cdd:COG4913 359 RrrarleaLLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
250 260
....*....|....*....|....*...
gi 568935751 473 NKMAGELEVLRsqeRRLKEKVANMEVAL 500
Cdd:COG4913 436 SNIPARLLALR---DALAEALGLDEAEL 460
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-399 |
1.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 19 ELRESKRMYEDKIEELEKQlVLANSELTEARTERDQFSQESGNLDDQLQKllADLHKREKELSLEKEQNKRLWDRDTGNS 98
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEAKKADEAKKAEEAKK--ADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 99 ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK--EMLRKVVEELTA--- 173
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKkea 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 174 ---------KKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQM 244
Cdd:PTZ00121 1644 eekkkaeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 245 AE---KDKVIEILRQQIEN---MTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIR-ELEARVSDL 317
Cdd:PTZ00121 1724 AEeenKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRmEVDKKIKDI 1803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 318 ELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEE---MESTTNRLKMQLKSAQSE 394
Cdd:PTZ00121 1804 FDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnKEADFNKEKDLKEDDEEE 1883
|
....*
gi 568935751 395 LEQTR 399
Cdd:PTZ00121 1884 IEEAD 1888
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-537 |
1.29e-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: 45.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 3 MRQLSDLESTVSQLRSELRESKrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL 82
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEE---EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 83 EKEQnkrlwdrdtgnsitidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEStkE 162
Cdd:pfam02463 333 EKEE--------------------------IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--E 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 163 MLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKL 242
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 243 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKV 322
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 323 KLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNT- 401
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKv 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 402 ----LKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAG 477
Cdd:pfam02463 625 vegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935751 478 ELEVLRSQERRLKEKV----ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQG 537
Cdd:pfam02463 705 EQREKEELKKLKLEAEellaDRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-530 |
1.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 160 TKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQ--------------------- 218
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllplyqelealeaelael 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 219 --ELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMT-QLVGQHGRTAGAMQVEKAQLEKEINDRKLELQ- 294
Cdd:COG4717 145 peRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEe 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 295 --------EFKILKDKKDAKIRELEA-----------RVSDLELEKVKLVNAG-------------SERLRAVKDIRHER 342
Cdd:COG4717 225 leeeleqlENELEAAALEERLKEARLllliaaallalLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 343 DQLLNEVKTSR---TELNHLSEDYEVLK-------RNFRNKSEEMESTTNRLKMQLKSAQ-SELEQTRNTLKTMEGSDGH 411
Cdd:COG4717 305 EELQALPALEEleeEELEELLAALGLPPdlspeelLELLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 412 AMKVAMGMQKQitakrgQIDALQSKVQFLEEAVTSANKERHFL--KEEKSKLSQELSTVATEKNKMAGELEVLRSQERRL 489
Cdd:COG4717 385 EELRAALEQAE------EYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568935751 490 KEKVANME--VALDKASLQFAECQDIIQRQEQESVRLKLQHTL 530
Cdd:COG4717 459 EAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-497 |
1.72e-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: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 191 SLQEKERAiEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQLVGQHGR 270
Cdd:TIGR02169 669 SRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 271 TAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKlvnagsERLRAVKDIRHERDQLLNEVK 350
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ------AELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 351 TsrtELNHLSEDYEVLkrnfRNKSEEMESTTNRLKMQLKSAQSELEQtrntlktmegsdghamkvamgMQKQITAKRGQI 430
Cdd:TIGR02169 819 Q---KLNRLTLEKEYL----EKEIQELQEQRIDLKEQIKSIEKEIEN---------------------LNGKKEELEEEL 870
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568935751 431 DALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 497
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-403 |
1.84e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 3 MRQLSDLESTVSQLRSELREskrmYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADL-HKREKELS 81
Cdd:COG4717 124 LLQLLPLYQELEALEAELAE----LPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLsLATEEELQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 82 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 161
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 162 EMLRKVVEELTAKKMNLESSERTVSD-LTASLQEKERAIEATNAEITKLRSRV----DLKLQELQHLKNEGDHLRNVQTE 236
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGkEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLRE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 237 CEALKLQMAekdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEfkilkdKKDAKIRELEARVSD 316
Cdd:COG4717 356 AEELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE------QLEELLGELEELLEA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 317 LELEKVKlvNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSED--YEVLKRNFRNKSEEMESTTNRlKMQLKSAQSE 394
Cdd:COG4717 425 LDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEE-WAALKLALEL 501
|
....*....
gi 568935751 395 LEQTRNTLK 403
Cdd:COG4717 502 LEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
28-221 |
1.85e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 28 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKrlwdrdtgNSITIDHLRR 106
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdKLQAEIAE--------AEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 107 ELDDRNMEVQR-------LEALLKA-MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNL 178
Cdd:COG3883 87 ELGERARALYRsggsvsyLDVLLGSeSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568935751 179 ESSErtvSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 221
Cdd:COG3883 167 EAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-261 |
1.94e-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: 45.05 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 5 QLSDLESTVSQLRSELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 84
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 85 EQNKRlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEML 164
Cdd:TIGR02168 838 RRLED--------------LEEQIEELSEDIESLAAEIEELEELI--------------EELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 165 RKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELqhLKNEGDHLRNVQTECEALKLQM 244
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL--SEEYSLTLEEAEALENKIEDDE 967
|
250
....*....|....*..
gi 568935751 245 AEKDKVIEILRQQIENM 261
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL 984
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-451 |
2.08e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 9 LESTVSQLRSELRESKRMYEDKIEELE----------KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL-HKRE 77
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEaleegkkrlqRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLdHQRQ 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 78 KELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVS-SLTAQ 156
Cdd:pfam01576 595 LVSNLEKKQKK--FDQMLAEEKAISARYAEERDR-AEAEAREKETRAL------SLARALEEALEAKEELERTNkQLRAE 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 157 LE---STKEMLRKVVEELTAKKMNLESSertVSDLTASLQEKERAIEATnaEITKLRSRVDLKL------QELQHLKNEG 227
Cdd:pfam01576 666 MEdlvSSKDDVGKNVHELERSKRALEQQ---VEEMKTQLEELEDELQAT--EDAKLRLEVNMQAlkaqfeRDLQARDEQG 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 228 D--------HLRNVQTECEALKLQMAE---KDKVIEILRQQIENMTQLVGQhGRTAGAMQVEKAQleKEINDRKLELQEF 296
Cdd:pfam01576 741 EekrrqlvkQVRELEAELEDERKQRAQavaAKKKLELDLKELEAQIDAANK-GREEAVKQLKKLQ--AQMKDLQRELEEA 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 297 KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEE 376
Cdd:pfam01576 818 RASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEE 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 377 MESTTN----------RLKMQLKSAQSELEQTRNTLKTMEGSDGHA------MKVAMG-MQKQITAK-RGQIDALQSKVQ 438
Cdd:pfam01576 898 LEEEQSntellndrlrKSTLQVEQLTTELAAERSTSQKSESARQQLerqnkeLKAKLQeMEGTVKSKfKSSIAALEAKIA 977
|
490
....*....|...
gi 568935751 439 FLEEAVTSANKER 451
Cdd:pfam01576 978 QLEEQLEQESRER 990
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
5-490 |
2.15e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 5 QLSDLESTVSQLRSELRESKrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 84
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESR----DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 85 EQNKRLWDRDTGNSITIDHLRRE----LDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQL 157
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEMTKFKNNK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 158 ESTKEMLRKVVEE----LTAKKMNLESSER---TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE--GD 228
Cdd:pfam05483 404 EVELEELKKILAEdeklLDEKKQFEKIAEElkgKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEleKE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 229 HLRNVQTECEALKLQMAEK-------DKVIEILRQQ--IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQ----E 295
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKeltqeasDMTLELKKHQedIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 296 FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSE 375
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 376 EMESTTNRLKMQLKSAQSELEQTR----NTLKTMEGSDG---HAMKVAMGMQKQITAKRGQIDALQSKVQ-----FLEEA 443
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAiadEAVKLQKEIDKRCQHKIAEMVALMEKHKhqydkIIEER 723
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 568935751 444 VTSANKERHFLKEEKS---KLSQELSTVATEKNKMAGELEVLRSQERRLK 490
Cdd:pfam05483 724 DSELGLYKNKEQEQSSakaALEIELSNIKAELLSLKKQLEIEKEEKEKLK 773
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-399 |
2.70e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 27 YEDKIEELEKQLVLANSELTEARTERDQFSQ--ESGNLDDQLQKLLADLHKREKELS-----LEKEQNK----RLWDRDT 95
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRaqeavLEETQERinraRKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 96 GNSITIDHLRRELDDRNMEVQRLEALLKamksecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKK 175
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRA--------KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 176 MNLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdLKLQELQHLKNEGDHLRNV-QTECEALKLQMAEKDKVIEIL 254
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL-----DILQREQATIDTRTSAFRDlQGQLAHAKKQQELQQRYAELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 255 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKI-------RELEARVSDLELEKVKLVNA 327
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNP 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 328 GSERLR-------------AVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSE 394
Cdd:TIGR00618 524 GPLTRRmqrgeqtyaqletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL 603
|
....*
gi 568935751 395 LEQTR 399
Cdd:TIGR00618 604 SEAED 608
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-536 |
2.91e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 165 RKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-DLKLQelqhLKNEGDHLRNVQTECEALKLQ 243
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIkDLNDK----LKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 244 MAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVK 323
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEK--------------QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 324 LVNAGSERLRAVKDIRHERDQLL----------NEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRL--------- 384
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqtqlnq 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 385 --------KMQLKSAQSELEQTRNTLKT---------MEGSDGHAMKVA---MGMQKQITAKRGQIDALQSKVQFLEEAV 444
Cdd:TIGR04523 258 lkdeqnkiKKQLSEKQKELEQNNKKIKElekqlnqlkSEISDLNNQKEQdwnKELKSELKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 445 TSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 524
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
410
....*....|..
gi 568935751 525 KLQHTLDVKELQ 536
Cdd:TIGR04523 418 QQEKELLEKEIE 429
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-334 |
3.60e-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: 42.99 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 149 KVSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdlklqeLQHLKNEgD 228
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-------LGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 229 HLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrtagAMQVEKAQLEKEINDRKLELQEfkiLKDKKDAKIR 308
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIE--------------ELEEELAELEAELAELEAELEE---KKAELDEELA 152
|
170 180
....*....|....*....|....*.
gi 568935751 309 ELEARVSDLELEKVKLVNAGSERLRA 334
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPELLA 178
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
4-430 |
4.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRMYeDKIEELEKQLVLA-----NSELTEARTERDQfSQESGNLDDQLQKLLADLHKREK 78
Cdd:PRK04863 851 RALADHESQEQQQRSQLEQAKEGL-SALNRLLPRLNLLadetlADRVEEIREQLDE-AEEAKRFVQQHGNALAQLEPIVS 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 79 ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmksecqgqmerQMAAIQGKNESLekVSSLTAQLE 158
Cdd:PRK04863 929 VLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE-----------DAAEMLAKNSDL--NEKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 159 STKEMLRKVVEELTakkmnlessertvsdltaslQEKERAIEAtNAEITKLRSRVDLKLQELQHLKNEGDHLrNVQTECE 238
Cdd:PRK04863 996 QAEQERTRAREQLR--------------------QAQAQLAQY-NQVLASLKSSYDAKRQMLQELKQELQDL-GVPADSG 1053
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 239 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEinDRKLELQEFKILKDKKD-AKIRELeARVSDL 317
Cdd:PRK04863 1054 AEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL--ERDYHEMREQVVNAKAGwCAVLRL-VKDNGV 1130
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 318 E--LEKVKLVNAGSERLR------------AVKDIRHERDQLLNEVKTSRTE--LNHLSEDYEVLKRNFRN---KSEEME 378
Cdd:PRK04863 1131 ErrLHRRELAYLSADELRsmsdkalgalrlAVADNEHLRDVLRLSEDPKRPErkVQFYIAVYQHLRERIRQdiiRTDDPV 1210
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568935751 379 STTNRLKMQLKSAQSELEQTRNTLKTMEGSdghamkVAMGMQKQITAKRGQI 430
Cdd:PRK04863 1211 EAIEQMEIELSRLTEELTSREQKLAISSES------VANIIRKTIQREQNRI 1256
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
165-492 |
5.22e-04 |
|
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: 43.35 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 165 RKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKL--------RSRVDLKLQELQHLKNEGDH---LRNV 233
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELeekykelsASSEELSEEKDALLAQRAAHearIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 234 QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEAR 313
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 314 VSDLelekvklvnagSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRL-KMQLKSAQ 392
Cdd:pfam07888 215 ITTL-----------TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhQARLQAAQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 393 SELEQTRNTLKTMEGSdGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEkskLSQELSTVATEK 472
Cdd:pfam07888 284 LTLQLADASLALREGR-ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE---LGREKDCNRVQL 359
|
330 340
....*....|....*....|.
gi 568935751 473 NKMAGELEVLRSQERRL-KEK 492
Cdd:pfam07888 360 SESRRELQELKASLRVAqKEK 380
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
291-480 |
5.56e-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: 42.22 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 291 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNhlsedyevlkrnf 370
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 371 RNKSEEMESTTNRlkmQLKSAQSELEQTRNTLKTMEgsdghamKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKE 450
Cdd:COG1579 77 KYEEQLGNVRNNK---EYEALQKEIESLKRRISDLE-------DEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
170 180 190
....*....|....*....|....*....|
gi 568935751 451 rhfLKEEKSKLSQELSTVATEKNKMAGELE 480
Cdd:COG1579 147 ---LDEELAELEAELEELEAEREELAAKIP 173
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
167-342 |
6.03e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 167 VVEEltAKKMNLESSERtVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH----LKNEGDHLRNVQTEC--EAL 240
Cdd:PRK00409 503 IIEE--AKKLIGEDKEK-LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEkkekLQEEEDKLLEEAEKEaqQAI 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 241 KLQMAEKDKVIEILRQQIENMT------QLVGQHGRTAGAMQ-VEKAQLEKEINDRKLEL-QEFKILK-----------D 301
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYasvkahELIEARKRLNKANEkKEKKKKKQKEKQEELKVgDEVKYLSlgqkgevlsipD 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568935751 302 KKDAKIRE----LEARVSDLEL------EKVKLVNAGSERLRAVK---DIRHER 342
Cdd:PRK00409 660 DKEAIVQAgimkMKVPLSDLEKiqkpkkKKKKKPKTVKPKPRTVSlelDLRGMR 713
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-393 |
8.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 186 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-------------GDHLRNVQTECEALKLQMAEKDKVIE 252
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeakllLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 253 ILRQQIENMTQLVGQHGRTAGAmqvekAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL 332
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935751 333 RA-VKDIRHERDQLLNEVKTSRTELNHLSE---DYEVLKRNFRNKSEEMESTTNRLKmQLKSAQS 393
Cdd:COG3206 319 EAeLEALQAREASLQAQLAQLEARLAELPEleaELRRLEREVEVARELYESLLQRLE-EARLAEA 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-520 |
8.35e-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: 43.12 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 282 LEKEINDRKLELQEFKILKDKKDAkIRELEARVSDLELEKVKlvnagsERLRAVKDirhERDQLLNEVKTSRTELNHLSE 361
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAE-LRELELALLVLRLEELR------EELEELQE---ELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 362 DYEVLKRNFRNKSEEMESttnrlkmqlksAQSELEQTRNTLKTMEgsdghamkvamgMQKQITAKRgqIDALQSKVQFLE 441
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEE-----------LQKELYALANEISRLE------------QQKQILRER--LANLERQLEELE 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568935751 442 EAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfaecQDIIQRQEQE 520
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR------SKVAQLELQI 395
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
18-406 |
8.61e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 18 SELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGN 97
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 98 SITIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNESleKVSSLTAQLESTKEMlrk 166
Cdd:pfam01576 298 GEELEALKTELEDtldttaaqqelRSKREQEVTELKKALEEETRSH-EAQLQEMRQKHTQ--ALEELTEQLEQAKRN--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 167 vveeltakKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcEALKLQMae 246
Cdd:pfam01576 372 --------KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAE-KLSKLQS-- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 247 kdkvieilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDL------ELE 320
Cdd:pfam01576 441 ----------ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLqeqleeEEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 321 KVKLVNAGSERLRA-VKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKS---EEMESTTNRLKMQLKSAQSELE 396
Cdd:pfam01576 511 AKRNVERQLSTLQAqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAaayDKLEKTKNRLQQELDDLLVDLD 590
|
410
....*....|
gi 568935751 397 QTRNTLKTME 406
Cdd:pfam01576 591 HQRQLVSNLE 600
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
295-667 |
1.00e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 295 EFKILKDKKDAKIRELE----ARVSDLELEKvklvnagSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYeVLKRNF 370
Cdd:PTZ00108 1025 ELVITNAKKKDLVKELKklgyVRFKDIIKKK-------SEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDY-LLSMPI 1096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 371 RNKSEEMestTNRLKMQLKSAQSELEQTRNT-LKTMEGSDghamkvamgmqkqitakrgqIDALQSKVQFLEE-AVTSAN 448
Cdd:PTZ00108 1097 WSLTKEK---VEKLNAELEKKEKELEKLKNTtPKDMWLED--------------------LDKFEEALEEQEEvEEKEIA 1153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 449 KERHFLKEEKSKLS----QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQrQEQESVRL 524
Cdd:PTZ00108 1154 KEQRLKSKTKGKASklrkPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSD-QEDDEEQK 1232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 525 KLQHTLDVKELQGPGYTSNSSVKPRLLQPASVTRSHSNIPSSQSTTSFLSHHSIKTNTP----------KEDPTRDLKQL 594
Cdd:PTZ00108 1233 TKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgesnggskPSSPTKKKVKK 1312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935751 595 LQELRTVINEEPAMALSKTEEDGRtpslgaLEDRVRDCITESSLR--AELCHRSNNSLRESTEGSKSSETLSREP 667
Cdd:PTZ00108 1313 RLEGSLAALKKKKKSEKKTARKKK------SKTRVKQASASQSSRllRRPRKKKSDSSSEDDDDSEVDDSEDEDD 1381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-451 |
1.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 248 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLElEKVK---- 323
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-EELGerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 324 --------------LVNAGS-----ERLRAVKDIRHERDQLLNEVKTSRTELnhlsedyEVLKRNFRNKSEEMESTTNRL 384
Cdd:COG3883 94 alyrsggsvsyldvLLGSESfsdflDRLSALSKIADADADLLEELKADKAEL-------EAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568935751 385 KMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKER 451
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
54-224 |
1.27e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 54 QF--SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLkamkSECQG 131
Cdd:PRK09039 41 QFflSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDS-------VANLRASLSAAEAERSRLQALL----AELAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 132 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTakkmnlesseRTVSDLTASLQEKERAIEATNAEITKLRS 211
Cdd:PRK09039 110 AGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALR----------RQLAALEAALDASEKRDRESQAKIADLGR 179
|
170
....*....|....
gi 568935751 212 RVDLKL-QELQHLK 224
Cdd:PRK09039 180 RLNVALaQRVQELN 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-401 |
1.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 180 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIE 259
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 260 NMTQLVGQHGRTAGAMQV-----------EKAQLEKEINDRKLE-LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNA 327
Cdd:COG3883 90 ERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935751 328 GSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNT 401
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
274-524 |
1.49e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 274 AMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSR 353
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 354 TELNHLSEDYEVLKRNFRNKSEEMESTTNRLK---MQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQI 430
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKERAKkagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 431 DALQSKVQFLEEAVTSANK----------------ERHFLKEEKSK-LSQELSTVATEKNKMAGELEVLRSQERRLKEKV 493
Cdd:pfam07888 209 LQLQDTITTLTQKLTTAHRkeaenealleelrslqERLNASERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL 288
|
250 260 270
....*....|....*....|....*....|..
gi 568935751 494 ANMEVALDKASLQFA-ECQDIIQRQEQESVRL 524
Cdd:pfam07888 289 ADASLALREGRARWAqERETLQQSAEADKDRI 320
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
39-226 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 39 VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRL 118
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-------IDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 119 EALLKAM-----KSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV---VEELTAKKMNLESSERTVSDLTA 190
Cdd:COG3883 85 REELGERaralyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 568935751 191 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 226
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-467 |
1.81e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELREskrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 83
Cdd:COG1196 260 AELAELEAELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 84 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEM 163
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 164 LRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 243
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 244 MAEKDKVIEILRQQIENMTQLVGQHG------------------------------------------------------ 269
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaalaaalqnivveddevaaaaieylkaakagrat 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 270 ---------RTAGAMQVEKAQLEKEINDRKLELQEFKIL-----------------KDKKDAKIRELEARVSDLELEKVK 323
Cdd:COG1196 576 flpldkiraRAALAAALARGAIGAAVDLVASDLREADARyyvlgdtllgrtlvaarLEAALRRAVTLAGRLREVTLEGEG 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 324 LVNAGSERLRAVKDI-------RHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELE 396
Cdd:COG1196 656 GSAGGSLTGGSRRELlaalleaEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568935751 397 QTRNTLKTMEGSDGHAMKVAMG-------MQKQITAKRGQIDALqSKVQFL-EEAVTSANKERHFLKEEKSKLSQELST 467
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPeppdleeLERELERLEREIEAL-GPVNLLaIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
148-497 |
2.03e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 148 EKVSSLTAQLESTKEMLRKVVEELTakkmNLESSERTVSDLTASLQEKERAI-----------EATNAEITKLRSRVDLK 216
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELD----ELLESEEKNREEVEELKDKYRELrktllanrfsyGPAIDELEKQLAEIEEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 217 LQELQHLKNEGDHLrnvqtecEALK-LQMAEKDkvIEILRQQIENMTQLVGQhgrtagAMQVEKAQLEkEIND--RKLEL 293
Cdd:pfam06160 162 FSQFEELTESGDYL-------EAREvLEKLEEE--TDALEELMEDIPPLYEE------LKTELPDQLE-ELKEgyREMEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 294 QEFKILKDKKDAKIRELEARVSDLE--LEKVKLVNAgSERLRAVKD-IRHERDQLLNEVKTSRTELNHLSEDYEVL---K 367
Cdd:pfam06160 226 EGYALEHLNVDKEIQQLEEQLEENLalLENLELDEA-EEALEEIEErIDQLYDLLEKEVDAKKYVEKNLPEIEDYLehaE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 368 RNFRNKSEEMEsttnRLKMQLKSAQSELEQTRNTLKtmegsdghamkvamgmqkqitakrgQIDALQSKVQFLEEAVTSA 447
Cdd:pfam06160 305 EQNKELKEELE----RVQQSYTLNENELERVRGLEK-------------------------QLEELEKRYDEIVERLEEK 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568935751 448 NKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 497
Cdd:pfam06160 356 EVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFK 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
31-536 |
2.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 31 IEELEKQLVLANSELTEARTERDQFSQESGNL------DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 104
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHvkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 105 RRELDDRNMEVQRLEALlKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR-------KVVEELTAKKMN 177
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSL-CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaitCTAQCEKLEKIH 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 178 LESSERTVSDLTASLQEKERaIEATNAEITKLRSRVDLKLQELQHLKNEgdhlrnvQTECEALKLQMAEKDKVIEILRQQ 257
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCG-------SCIHPNPARQDIDNPGPLTRRMQR 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 258 IENMTQLVGQHGRTA-GAMQVEKAQLEKEINDRKLELQEFKILKdkkdAKIRELEARVSDLELEKVKLVNAGSERLRavk 336
Cdd:TIGR00618 533 GEQTYAQLETSEEDVyHQLTSERKQRASLKEQMQEIQQSFSILT----QCDNRSKEDIPNLQNITVRLQDLTEKLSE--- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 337 dirhERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQ----TRNTLKTMEGSDGHA 412
Cdd:TIGR00618 606 ----AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLA 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 413 MKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRS---QERRL 489
Cdd:TIGR00618 682 LQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlKARTE 761
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 568935751 490 KEKVANMEVALDKASLQfaECQDIIQR-QEQESVRLKLQHTLDVKELQ 536
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGA--ELSHLAAEiQFFNRLREEDTHLLKTLEAE 807
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
134-404 |
2.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 134 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 213
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 214 DLKLQELQHLKNEGDHLR----NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR 289
Cdd:COG4372 111 EELQEELEELQKERQDLEqqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 290 KLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQllnEVKTSRTELNHLSEDYEVLKRN 369
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE---EDKEELLEEVILKEIEELELAI 267
|
250 260 270
....*....|....*....|....*....|....*
gi 568935751 370 FRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKT 404
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2-91 |
3.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 2 YMRQLSDLESTVSQLRSELREskrmYEDKIEELEKQLVLANSELTEARTERDQ---FSQESGNLD---DQLQKLLADLHK 75
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEE----LEAELEEKDERIERLERELSEARSEERReirKDREISRLDreiERLERELEEERE 486
|
90
....*....|....*.
gi 568935751 76 REKELSLEKEQNKRLW 91
Cdd:COG2433 487 RIEELKRKLERLKELW 502
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
275-508 |
3.10e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 275 MQVEKAQLEKEINDRkLELQEF----KILKDKkdakIRELEARVSDLEL------EKVKLVNAGSERLRAVKDIRHER-- 342
Cdd:PHA02562 145 MQLSAPARRKLVEDL-LDISVLsemdKLNKDK----IRELNQQIQTLDMkidhiqQQIKTYNKNIEEQRKKNGENIARkq 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 343 ---DQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTN---RLKMQLKSAQSELE--QTRNTLKT-MEGSDGHAM 413
Cdd:PHA02562 220 nkyDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTaaaKIKSKIEQFQKVIKmyEKGGVCPTcTQQISEGPD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 414 KVAMGMQK--QITAKrgqIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKM---------------- 475
Cdd:PHA02562 300 RITKIKDKlkELQHS---LEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAkkvkaaieelqaefvd 376
|
250 260 270
....*....|....*....|....*....|....
gi 568935751 476 -AGELEVLRSQERRLKEKVAnmEVALDKASLQFA 508
Cdd:PHA02562 377 nAEELAKLQDELDKIVKTKS--ELVKEKYHRGIV 408
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
31-128 |
3.17e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 31 IEELEKQLVLANSELTEARTERDQFSQESgnlddqlqklLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD 110
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFER----------LAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90
....*....|....*...
gi 568935751 111 RNMEVQRLEALLKAMKSE 128
Cdd:COG0542 483 RYGKIPELEKELAELEEE 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
161-536 |
3.50e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 161 KEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE----LQHLKNE-GDHLRNVQT 235
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEdhekIQHLEEEyKKEINDKEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 236 ECEALKLQMAEKDK-------VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEF----KILKDKKD 304
Cdd:pfam05483 241 QVSLLLIQITEKENkmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqKALEEDLQ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 305 AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTnRL 384
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-KF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 385 KMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQE 464
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568935751 465 LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfaecQDIIQRQEQESVRLKLQHTLDVKELQ 536
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------EDIINCKKQEERMLKQIENLEEKEMN 545
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
49-287 |
3.78e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 49 RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdtgNSITIDhlrrelDDRNMEVQRLEALlkamkse 128
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKN---------GLVDLS------EEAKLLLQQLSEL------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 129 cqgqmERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVE--ELTAKKMNLESSERTVSDLTASLQEKERAIEATNAE 205
Cdd:COG3206 225 -----ESQLAEARAELAEAEaRLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 206 ITKLRSRVDLKLQELqhlknegdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgrtagamQVEKAQLEKE 285
Cdd:COG3206 300 IAALRAQLQQEAQRI---------LASLEAELEALQAREASLQAQLAQLEARLAELPEL-----------EAELRRLERE 359
|
..
gi 568935751 286 IN 287
Cdd:COG3206 360 VE 361
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
96-406 |
4.50e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 96 GNSITIDHLRRELDDRNMEVQRLEALLKAMkSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK---VVEELT 172
Cdd:TIGR01612 1105 ENIKYADEINKIKDDIKNLDQKIDHHIKAL-EEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKienIVTKID 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 173 AKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLrnvqtecealklqmaekdkvIE 252
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHM--------------------IK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 253 ILRQQIENMTQLVGQHGRTAGAMQVEKaqlekeinDRKLELQEFKILKDK-KDAKI--RELEARVSDLELEKVKLVNAGS 329
Cdd:TIGR01612 1244 AMEAYIEDLDEIKEKSPEIENEMGIEM--------DIKAEMETFNISHDDdKDHHIisKKHDENISDIREKSLKIIEDFS 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 330 ERlRAVKDIRHERDQLLNEVKTSRTE----LNHLSEDYEVLKRN-FRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLKT 404
Cdd:TIGR01612 1316 EE-SDINDIKKELQKNLLDAQKHNSDinlyLNEIANIYNILKLNkIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKK 1394
|
..
gi 568935751 405 ME 406
Cdd:TIGR01612 1395 IK 1396
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
150-505 |
4.85e-03 |
|
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: 40.73 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 150 VSSLTAQLESTKEMLRKVVEELTAKKMNLESSERTVSDLTasLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH 229
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK--EQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 230 LR-----NVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgrtaGAMQVEKAQLEKEINDRKLELQEFKILKDKKD 304
Cdd:pfam02463 242 LQellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK--------KLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 305 AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRnKSEEMESTTNRL 384
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-LESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 385 KMQLKSAQSELEQTRNTLKTmegsdgHAMKVAMGMQKQITAKRGQIDALQSKVQFLEEAVTSANKERHFLKEEKSKLSQE 464
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLE------LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568935751 465 LSTVATEKNKmAGELEVLRSQERRLKEKVANMEVALDKASL 505
Cdd:pfam02463 467 LKKSEDLLKE-TQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
356-524 |
4.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 356 LNHLSEDYevLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNTLK---------TMEGSDGHAMKVAMGMQKQITAK 426
Cdd:COG3206 154 ANALAEAY--LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 427 RGQIDALQSKVQFLEEAV---------TSANKERHFLKEEKSKLSQ---ELSTVATEKN----KMAGELEVLRSQ-ERRL 489
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAelaELSARYTPNHpdviALRAQIAALRAQlQQEA 311
|
170 180 190
....*....|....*....|....*....|....*
gi 568935751 490 KEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 524
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
274-525 |
5.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 274 AMQVEKAQLEKEINDRKLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSR 353
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELK-------EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 354 TELNHLSEDYEVLKRNFRNKSEEMEStTNRLKMQLKSAQSELEQTRNTLKTMEGSDGHAMKVAM---GMQKQITAKRGQI 430
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAE-LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEkikELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 431 DaLQSKVQFLEEAVTSANKERHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEC 510
Cdd:COG1340 157 E-KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250
....*....|....*
gi 568935751 511 QDIIQRQEQESVRLK 525
Cdd:COG1340 236 QKELRELRKELKKLR 250
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
4-415 |
5.29e-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: 40.34 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 83
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF----SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 84 KEQNKRlwdrdtGNSITIDHLRRELDDRNM--EVQRLEALLKAMKSECQGQMERQMAAI--QGKNESLEKVSSLTAQLES 159
Cdd:TIGR00618 614 QHALLR------KLQPEQDLQDVRLHLQQCsqELALKLTALHALQLTLTQERVREHALSirVLPKELLASRQLALQKMQS 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 160 TKEMLRKVVEELTAKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhlrnvQTECEA 239
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART-------VLKART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 240 LKLQMAEKDKVIEILR-QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKirELEARVSDLE 318
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ--EEEQFLSRLE 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 319 lEKVKLVNAGSERLRAVKDIRHERDQLLNEVKTSRTELNHLsEDYEVLKRNFR-NKSEEMESTTNRLKMQLKSAQSELEQ 397
Cdd:TIGR00618 839 -EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL-NGINQIKIQFDgDALIKFLHEITLYANVRLANQSEGRF 916
|
410
....*....|....*...
gi 568935751 398 TRNTLKTMEGSDGHAMKV 415
Cdd:TIGR00618 917 HGRYADSHVNARKYQGLA 934
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
4-353 |
5.51e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKRMYE----------DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 73
Cdd:pfam10174 366 KQLQDLTEEKSTLAGEIRDLKDMLDvkerkinvlqKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 74 HKREKELSLEKEQNKRLwDRDTGNSitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSL 153
Cdd:pfam10174 446 SEKERIIERLKEQRERE-DRERLEE--LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 154 TAQLESTKEMLRKVVEELTaKKMNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlrnv 233
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLK-KAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKN----- 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 234 qtecealklqmaEKDKVIEILrqqiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRKLELQEFKILKDKKDAKIRELEAR 313
Cdd:pfam10174 597 ------------DKDKKIAEL----ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEEL 660
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568935751 314 VSDLELEKVKLvNAGSERLRAVKDIRHERDQLLNEVKTSR 353
Cdd:pfam10174 661 MGALEKTRQEL-DATKARLSSTQQSLAEKDGHLTNLRAER 699
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
192-357 |
5.71e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 192 LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrt 271
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEAR---LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 272 agamqvekAQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIRHERDQLLNEVKT 351
Cdd:COG1579 85 --------VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 568935751 352 SRTELN 357
Cdd:COG1579 157 ELEELE 162
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
333-465 |
6.00e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 40.03 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 333 RAVKDIRHERDQLLNEVKTSRTELNHLSEDYEVLKRNFRNKSEEMESTTNRLKMQLKSAQS--------------ELEQT 398
Cdd:pfam10168 561 KRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSqlpvlsdaeremkkELETI 640
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568935751 399 RNTLKTMegsdGHAMK-VAMGMQKQitakRGQIDALQSKVQflEEAVTSANKERHFLKEEKSKLSQEL 465
Cdd:pfam10168 641 NEQLKHL----ANAIKqAKKKMNYQ----RYQIAKSQSIRK--KSSLSLSEKQRKTIKEILKQLGSEI 698
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
324-451 |
6.53e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.83 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 324 LVNAGSERLR--AVKDIRHERDQLLNEVKTSRTELnhlsedyevlkRNFRNK---------SEEMESTTNRLKMQLKSAQ 392
Cdd:COG3524 166 LVNQLSERARedAVRFAEEEVERAEERLRDAREAL-----------LAFRNRngildpeatAEALLQLIATLEGQLAELE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568935751 393 SELEQTRNTLktmegSDGHAmkvamgmqkQITAKRGQIDALQSKVQFLEEAVTSANKER 451
Cdd:COG3524 235 AELAALRSYL-----SPNSP---------QVRQLRRRIAALEKQIAAERARLTGASGGD 279
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-175 |
9.46e-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: 39.67 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 2 YMRQLSDLESTVSQLRSELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 81
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 82 LEKEQNKRLWDRDTgnsiTIDHLRRELDDRNMEVQRLEAlLKAMKSECQGQMER----QMAAIQGKNESLEKVSSLTAQ- 156
Cdd:TIGR02169 921 ELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKr 995
|
170 180
....*....|....*....|.
gi 568935751 157 --LESTKEMLRKVVEELTAKK 175
Cdd:TIGR02169 996 akLEEERKAILERIEEYEKKK 1016
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
4-297 |
9.48e-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: 39.49 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 4 RQLSDLESTVSQLRSELRESKrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH-------KR 76
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSR----EKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 77 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGK----NESLEKVSS 152
Cdd:pfam07888 149 ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS-LAQRDTQVLQLQDTittlTQKLTTAHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 153 LTAQLESTKEMLRKVVEEltakkmnLESSERTVSDLTASLQEKERAIEATNAEITKLR---SRVDLKLQELQHLKNEGDh 229
Cdd:pfam07888 228 KEAENEALLEELRSLQER-------LNASERKVEGLGEELSSMAAQRDRTQAELHQARlqaAQLTLQLADASLALREGR- 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935751 230 lRNVQTECEALkLQMAEKDKV-IEILRQQIENMTQLVGQHGRTAGAMQVEKAQlEKEIN-----DRKLELQEFK 297
Cdd:pfam07888 300 -ARWAQERETL-QQSAEADKDrIEKLSAELQRLEERLQEERMEREKLEVELGR-EKDCNrvqlsESRRELQELK 370
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-401 |
9.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 196 ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK------LQMAEKDKVIEILRQQIENMtqlvgqhg 269
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeIDVASAEREIAELEAELERL-------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 270 rTAGAMQVEkaQLEKEINDRKLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagsERLRAVKDIRHERDQLLNEV 349
Cdd:COG4913 681 -DASSDDLA--ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE-----------EELDELQDRLEAAEDLARLE 746
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568935751 350 KTSRTElNHLSEdyEVLKRNFRNKSEEMESTTNRLKMQLKSAQSELEQTRNT 401
Cdd:COG4913 747 LRALLE-ERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
10-290 |
9.96e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 10 ESTVSQLRSELRESKRMYEDKIEELEKQLVLANSELTEARTERDQFS----QESGNLDDQLQKLLADLHKREKELSLEKE 85
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIKIKINELKD 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 86 QNKRLWDRDTG-NSITIDHLRrelddrnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES----- 159
Cdd:PRK01156 544 KHDKYEEIKNRyKSLKLEDLD----------SKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIgfpdd 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935751 160 ---TKEMLRKVVEELTakkmNLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 236
Cdd:PRK01156 614 ksyIDKSIREIENEAN----NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKA 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568935751 237 CEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRK 290
Cdd:PRK01156 690 LDDAKANRARLESTIEILRTRINELSDRINDINETLESMK----KIKKAIGDLK 739
|
|
| |
