|
Name |
Accession |
Description |
Interval |
E-value |
| CNH |
smart00036 |
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2; |
1233-1529 |
1.82e-78 |
|
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
Pssm-ID: 214481 Cd Length: 302 Bit Score: 261.90 E-value: 1.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1233 DMNCTLPFSDQ--VVLVGTEEGLYALNVLK--NSLTHIPGIGAVFQIYIIKDLEKLLMIAGE---ERALCLVDVKKVKQS 1305
Cdd:smart00036 2 TAKWNHPITCDgkWLLVGTEEGLYVLNISDqpGTLEKLIGRRSVTQIWVLEENNVLLMISGKkpqLYSHPLSALVEKKEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1306 LAQSHLPAQPDVSPNiFEAVKGCHLFAAGKIENSLCICAAMPSKVVIL-RYNDNLSKYCIR-----KEIETSEPCSCIHF 1379
Cdd:smart00036 82 LGSARLVIRKNVLTK-IPDVKGCHLCAVVNGKRSLFLCVALQSSVVLLqWYNPLKKFKLFKskflfPLISPVPVFVELVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1380 TNY---SILIGTNKfYEIDMKQYTLDeFLDKNDHSLAPAVFASSSNSFPVSIVQANsagqreEYLLCFHEFGVFVDSYG- 1455
Cdd:smart00036 161 SSFerpGICIGSDK-GGGDVVQFHES-LVSKEDLSLPFLSEETSLKPISVVQVPRD------EVLLCYDEFGVFVNLYGk 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 1456 RRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSLGSPARAylEIPNPRYLGPaiSSGAIYLASSY 1529
Cdd:smart00036 233 RRSRNPILHWEFMPESFAYHSPYLLAFHDNGIEIRSIKTGELLQELADR--ETRKIRLLGS--SDRKILLSSSP 302
|
|
| CNH |
pfam00780 |
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ... |
1241-1493 |
4.89e-68 |
|
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished observations.
Pssm-ID: 459938 Cd Length: 261 Bit Score: 230.21 E-value: 4.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1241 SDQVVLVGTEEGLYALNV-LKNSLTHIPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKkvkqSLAQSHLPAQPDVSP 1319
Cdd:pfam00780 1 GGQNLLLGTEEGLYVLNRsGPREPVRIIDKKRVTQLAVLEEFNLLLLLSGKDKRLYVYPLS----ALDSREENDRKDAAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1320 NIFEAVKGCHLFAAGKIENSLCICAAMPSKVVILRYNDNLS-KYCIRKEIETSEPCSCIHFTNYSILIGTNKFYE-IDMK 1397
Cdd:pfam00780 77 NKLPETKGCHFFKVGRHSNGRFLVVAVKRTIKLLEWYEPLLdKFRKFKEFYLPSPPVSIELLKSKLCVGCAKGFEiVSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1398 QYTLDEFLdkndhsLAPAVFASSSNSFPVSIVQANsagqREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREP 1477
Cdd:pfam00780 157 SKATESLL------TSLLFANRQENLKPLAVVRLD----RSEFLLCYNEFGVYVNLQGRRSRPWEIEWEGAPEAVAYLYP 226
|
250
....*....|....*.
gi 1907160229 1478 YLFVTHFNSLEVIEIQ 1493
Cdd:pfam00780 227 YLLAFHDNFIEIRDVE 242
|
|
| CRIK |
cd20814 |
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ... |
984-1039 |
4.53e-38 |
|
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410364 Cd Length: 56 Bit Score: 136.22 E-value: 4.53e-38
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 984 HNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLP 1039
Cdd:cd20814 1 HNIPHRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTCGLP 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-827 |
5.47e-25 |
|
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: 113.61 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 85 EDDKALQLLHDIREQSRKLQEIKEQ--------------EYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAA 150
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERYKELKAElrelelallvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 151 EEFKRKANECQHKLMKVVShpprgdsggtaldDLHKMQGHAGLTSAKDQGkpEVGEYSKLEKINAEQQLKIQELQEKLEK 230
Cdd:TIGR02168 277 SELEEEIEELQKELYALAN-------------EISRLEQQKQILRERLAN--LERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 231 AVKASTEATELLQNIRQAKERAERELEKLHNR----EDSSEGIKKKLVEAEERRHSLENKVKRLET----MERRENRLKD 302
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRleelEEQLETLRSKVAQLELQIASLNNEIERLEArlerLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 303 DIQTKSEQIQ--QMADKILELEEKHREAQVSAQHLEVH------LKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRH 374
Cdd:TIGR02168 422 EIEELLKKLEeaELKELQAELEELEEELEELQEELERLeealeeLREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 375 EEEAHEKGKILSEQKAM---INAMDSKIRSLEQRIVELSEAnkLAANSSLFTQRNMKAQEEMISELRQQK-----FYLET 446
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLsgiLGVLSELISVDEGYEAAIEAA--LGGRLQAVVVENLNAAKKAIAFLKQNElgrvtFLPLD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 447 QAGKLEAQNRKLEE------------QLEKISHQDHSDKSRLL-----------------ELETRLREVSLEHE------ 491
Cdd:TIGR02168 580 SIKGTEIQGNDREIlkniegflgvakDLVKFDPKLRKALSYLLggvlvvddldnalelakKLRPGYRIVTLDGDlvrpgg 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 492 ----------------EQKL-ELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHR 554
Cdd:TIGR02168 660 vitggsaktnssilerRREIeELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 555 DEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQnfyLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQK 634
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE---LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 635 QTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESR--- 711
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRsel 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 712 QVVELAVKEHKAEILALQQALKEqklkaesLSDKLNDLEKKHAMLEMNARSLQQKLeteRELKQRLLEEQAKLQQQMDLQ 791
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEE-------LREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDD 966
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 792 ----KNHIFRLTQGLQE-------ALD-------RADLLKTERSDLEYQLENIQ 827
Cdd:TIGR02168 967 eeeaRRRLKRLENKIKElgpvnlaAIEeyeelkeRYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-820 |
1.18e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 215 AEQQLKIQELQEKLEKAvkastEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLEtme 294
Cdd:COG1196 209 AEKAERYRELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 295 RRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEkikvLDNQIKKDLADKESLENMMQRH 374
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE----LEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 375 EEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKfylETQAGKLEAQ 454
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL---EELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 455 NRKLEEQLEKISHQDhSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKt 534
Cdd:COG1196 434 EEEEEEEEEALEEAA-EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 535 eLEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvitDLEEQLNQLTEDNAELNNQNFYLSKQLDEASG--ANDEIVQL 612
Cdd:COG1196 512 -AALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-----LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 613 RSEVDHLRREITEREMQLTSQKQTMEALKTTCTM--LEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFEcRVRELQ 690
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGdtLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA-GGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 691 RMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETE 770
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 771 RELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQE-------ALD-------RADLLKTERSDLE 820
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEeyeeleeRYDFLSEQREDLE 808
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-919 |
1.11e-21 |
|
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: 102.83 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 216 EQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEkLHNREDSSEG--IKKKLVEAEERRHSLENKVKRletM 293
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELalLVLRLEELREELEELQEELKE---A 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 294 ERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQ---VSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENM 370
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 371 MQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKlaansslftqrnmkAQEEMISELRQQKFYLETQAGK 450
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE--------------ELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 451 LEAQNRKLEEQLEKISHQDHSDKSRLLELETRLrevsleHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLR 530
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKL------EEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 531 QAKteleettaeaeeeiQALTAHRDEIQRkfdaLRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASgandEIV 610
Cdd:TIGR02168 472 EAE--------------QALDAAERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS----ELI 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 611 QLRSEV---------DHLRREITERemqLTSQKQTMEALK----TTCTMLEEQVL---DLEALNDELLEKERQWEAWRSV 674
Cdd:TIGR02168 530 SVDEGYeaaieaalgGRLQAVVVEN---LNAAKKAIAFLKqnelGRVTFLPLDSIkgtEIQGNDREILKNIEGFLGVAKD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 675 LGDEKSQFEcrvRELQRMLD-----------TEKQSRARADQRIT-------ESRQVVELAVKEHKAEILALQQALKEQK 736
Cdd:TIGR02168 607 LVKFDPKLR---KALSYLLGgvlvvddldnaLELAKKLRPGYRIVtldgdlvRPGGVITGGSAKTNSSILERRREIEELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 737 LKAESLSDKLNDLEKKHAMLemnaRSLQQKLETERELKQRLLEEqakLQQQMDLQKNHIFRLTQGLQEALDRADLLKTER 816
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAEL----RKELEELEEELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 817 SDLEYQLEniqvLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKAR 896
Cdd:TIGR02168 757 TELEAEIE----ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740
....*....|....*....|...
gi 1907160229 897 CAELEEALQKTRIELRSAREEAA 919
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIE 855
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
278-838 |
1.75e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 278 ERRHSLENKvkrLETMERRENRLKDDIQTKSEQIQQMAD--------KILELEEKHREAQVSAQHLEvHLKQKEQHYEEK 349
Cdd:COG1196 172 ERKEEAERK---LEATEENLERLEDILGELERQLEPLERqaekaeryRELKEELKELEAELLLLKLR-ELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 350 IKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAansslftQRNMKA 429
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 430 QEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVS----------LEHEEQKLELKR 499
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleelaeelLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 500 QLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLN 579
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 580 QLTEDNAELNNQNFYLSKQLDEASGAND----------------EIVQLRSEVDHLRREITEREMQLTSQ---------K 634
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEgvkaalllaglrglagAVAVLIGVEAAYEAALEAALAAALQNivveddevaA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 635 QTMEALKTT----CTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITES 710
Cdd:COG1196 561 AAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 711 RQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDL 790
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1907160229 791 QKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKME 838
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
242-827 |
4.53e-19 |
|
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: 93.93 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 242 LQNIRQAKERAERELEK--------LHNREDSSEGIKKKLVEAEERRHSLENKVKRLETmerRENRLKDDIQTKSEQIQQ 313
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKklktikneLKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQ---QIKDLNDKLKKNKDKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 314 M-AD-KILELEEKHREAQVSAQHLEV-HLKQKEQHYEEKIKVLDNQIKKDLAD--------------KESLENMMQRHEE 376
Cdd:TIGR04523 101 LnSDlSKINSEIKNDKEQKNKLEVELnKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkyndlkkqKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 377 EAHEKGKILSEQKAMINAMD---SKIRSLEQRIVEL-SEANKL-AANSSLFTQRNMKAQEemISELRQQKFYLETQAGKL 451
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLeSQISELkKQNNQLKDNIEKKQQE--INEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 452 EAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLE------------HEEQKLELK---RQLTELQLSLQERESQLT 516
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnnqkeqdwNKELKSELKnqeKKLEEIQNQISQNNKIIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 517 ALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQ--NFY 594
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikKLQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 595 LSKQLDEASGAN--DEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQV----LDLEALNDELLEKERQW 668
Cdd:TIGR04523 419 QEKELLEKEIERlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSKEKEL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 669 EAwrsvLGDEKSQFECRVRELqrmldTEKQSraradqritesrqvvELAVKEHKAEILALQqalKEQKLKaeSLSDKLN- 747
Cdd:TIGR04523 499 KK----LNEEKKELEEKVKDL-----TKKIS---------------SLKEKIEKLESEKKE---KESKIS--DLEDELNk 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 748 -DLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEAL-------DRADLLKTERSDL 819
Cdd:TIGR04523 550 dDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEkkissleKELEKAKKENEKL 629
|
....*...
gi 1907160229 820 EYQLENIQ 827
Cdd:TIGR04523 630 SSIIKNIK 637
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-769 |
5.89e-19 |
|
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: 93.97 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 10 KELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKA 89
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 90 LQLLHDIREQSRKLQEIKEQ--EYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKV 167
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEElaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 168 VSHPPRGDSGGTALDDLHKMQghagltsakDQGKPEVGEySKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQ 247
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERL---------QQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 248 AKERAERELEKLHNREDSSEGiKKKLVEAEERRHSLENKVKRLETMERreNRLKDDIQTKSEQIQ--------------- 312
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA-RLDSLERLQENLEGFSEGVKALLKNQ--SGLSGILGVLSELISvdegyeaaieaalgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 313 ----------QMADKILELEEKHREAQV--------SAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMM--- 371
Cdd:TIGR02168 546 rlqavvvenlNAAKKAIAFLKQNELGRVtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 372 -----------QRHEEEAHE-----KGKILSEQKAMINAMDSKIRSLEQRIVELSEANKlaansslftqrNMKAQEEMIS 435
Cdd:TIGR02168 626 lvvddldnaleLAKKLRPGYrivtlDGDLVRPGGVITGGSAKTNSSILERRREIEELEE-----------KIEELEEKIA 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 436 ELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKR---QLTELQLSLQERE 512
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAE 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 513 SQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSC-------TVITDLEEQLNQLTEDN 585
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaateRRLEDLEEQIEELSEDI 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 586 AELNNQNFYLSKQLDEasgandeivqLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKE 665
Cdd:TIGR02168 855 ESLAAEIEELEELIEE----------LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 666 RQWEAWRSVLGDEKSQFECRVRELQRML--------DTEKQSRARADQRITESRQ------VVELAVKEHKAEILALQQA 731
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTleeaealeNKIEDDEEEARRRLKRLENkikelgPVNLAAIEEYEELKERYDF 1004
|
810 820 830
....*....|....*....|....*....|....*...
gi 1907160229 732 LKEQKlkaESLSDKLNDLEKkhAMLEMNARSLQQKLET 769
Cdd:TIGR02168 1005 LTAQK---EDLTEAKETLEE--AIEEIDREARERFKDT 1037
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-786 |
3.50e-18 |
|
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: 91.57 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARME 81
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQLLHDI--REQSRKLQEIKEQEYQAQVEEMRlmmnQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANE 159
Cdd:pfam02463 323 KKKAEKELKKEKEEIeeLEKELKELEIKREAEEEEEEELE----KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 160 CQHKLMKVVShpprgdsggtALDDLHKMQGHAgLTSAKDQGKPEVGEyskLEKINAEQQLKIQELQEKLEKavKASTEAT 239
Cdd:pfam02463 399 LKSEEEKEAQ----------LLLELARQLEDL-LKEEKKEELEILEE---EEESIELKQGKLTEEKEELEK--QELKLLK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 240 ELLQNIRQAKERAERELEKLH-NREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLkDDIQTKSEQIQQMADKI 318
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQeQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI-ISAHGRLGDLGVAVENY 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 319 LELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKdLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSK 398
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRL-LIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 399 IRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLE 478
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 479 LETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQ 558
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 559 RKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTME 638
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 639 ALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSR-ARADQRITESRQVVELA 717
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERiKEEAEILLKYEEEPEEL 940
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 718 VKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQ 786
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-779 |
7.03e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.50 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 11 ELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKAL 90
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 91 QLLHDIREQSRKLQEIKEqeyqaQVEEMRLMMNQLEEDLVSARRRSDLYESELresrlaaEEFKRKANECQHKLMKVVSH 170
Cdd:TIGR02168 334 ELAEELAELEEKLEELKE-----ELESLEAELEELEAELEELESRLEELEEQL-------ETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 171 PPRGDSGGTALDDLHKMQghagltsakDQGKPEVGEySKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKE 250
Cdd:TIGR02168 402 IERLEARLERLEDRRERL---------QQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 251 RAERELEKLHNREDSSEGiKKKLVEAEERRHSLENKVKRLETMERreNRLKDDIQTKSEQIQ------------------ 312
Cdd:TIGR02168 472 EAEQALDAAERELAQLQA-RLDSLERLQENLEGFSEGVKALLKNQ--SGLSGILGVLSELISvdegyeaaieaalggrlq 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 313 -------QMADKILELEEKHREAQV--------SAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMM------ 371
Cdd:TIGR02168 549 avvvenlNAAKKAIAFLKQNELGRVtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvv 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 372 --------QRHEEEAHE-----KGKILSEQKAMINAMDSKIRSLEQRIVELSEANKlaansslftqrNMKAQEEMISELR 438
Cdd:TIGR02168 629 ddldnaleLAKKLRPGYrivtlDGDLVRPGGVITGGSAKTNSSILERRREIEELEE-----------KIEELEEKIAELE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 439 QQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKR---QLTELQLSLQERESQL 515
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAEEEL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 516 TALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNnqnfyl 595
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS------ 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 596 skqlDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTctmLEEQVLDLEALNDELLEKERQWEAwrsvL 675
Cdd:TIGR02168 852 ----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE---LEELSEELRELESKRSELRRELEE----L 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 676 GDEKSQFECRVRELQRMLDtEKQSRARADQRITEsrQVVELAVKEHKAEILALQQALK--EQKLKA------------ES 741
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRID-NLQERLSEEYSLTL--EEAEALENKIEDDEEEARRRLKrlENKIKElgpvnlaaieeyEE 997
|
810 820 830
....*....|....*....|....*....|....*....
gi 1907160229 742 LSDKLNDLEKKHAMLEMNARSLQQKL-ETERELKQRLLE 779
Cdd:TIGR02168 998 LKERYDFLTAQKEDLTEAKETLEEAIeEIDREARERFKD 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-751 |
9.99e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 208 SKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKV 287
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 288 KRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESL 367
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 368 ENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAAnsslftQRNMKAQEEMISELRQQKFYLETQ 447
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE------AALAELLEELAEAAARLLLLLEAE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 448 AGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEqkLELKRQLTELQLSLQERESQLTALQAARAA--- 524
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--AALQNIVVEDDEVAAAAIEYLKAAKAGRATflp 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 525 LESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASG 604
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 605 ANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEAlkttctMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFE- 683
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEEL------ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEa 732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 684 CRVRELQRMLDTEKQSRARADQRITE--SRQVVELAVKEHKAEI--------LALQQaLKEQKLKAESLSDKLNDLEK 751
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEppDLEELERELERLEREIealgpvnlLAIEE-YEELEERYDFLSEQREDLEE 809
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-623 |
3.06e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 70 SLKRSLEQARmevsqeddKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLA 149
Cdd:COG1196 204 PLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 150 AEEFKRKANECQHKLMKVVSHPPRgdsggTALDDLHKMQGHAGLTSAKDQGKPEvgeyskLEKINAEQQLKIQELQEKLE 229
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELAR-----LEQDIARLEERRRELEERLEELEEE------LAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 230 KAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETME----RRENRLKDDIQ 305
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeallERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 306 TKSEQIQQMADKILELEEKHREAQ----------VSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHE 375
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAeeeaeleeeeEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 376 EEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQK-----FYLETQAGK 450
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 451 LEAQNRKLEEQLEK-----------------------------ISHQDHSDKSRLLELETRLREVSLEHEEQkleLKRQL 501
Cdd:COG1196 585 RAALAAALARGAIGaavdlvasdlreadaryyvlgdtllgrtlVAARLEAALRRAVTLAGRLREVTLEGEGG---SAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 502 TELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQL 581
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907160229 582 TEDNAElnnqnfyLSKQLDEASGANDEIVQLRSEVDHLRREI 623
Cdd:COG1196 742 LEEEEL-------LEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-626 |
5.36e-17 |
|
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: 87.42 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARME 81
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQ 161
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 162 HKLMKVVS----HPPRGDSGGTALDDLHKMQGHAGLTSAKDQGKPEvgeYSK------------LEKINAEQQLKIQELQ 225
Cdd:TIGR02168 489 ARLDSLERlqenLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG---YEAaieaalggrlqaVVVENLNAAKKAIAFL 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 226 EKLEKA------------------------------------VKASTEATELLQN--------------IRQAKE----- 250
Cdd:TIGR02168 566 KQNELGrvtflpldsikgteiqgndreilkniegflgvakdlVKFDPKLRKALSYllggvlvvddldnaLELAKKlrpgy 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 251 -------------------RAERELEKLhNREDSSEGIKKKLVEAEERRHSLENKVKRLET----MERRENRLKDDIQTK 307
Cdd:TIGR02168 646 rivtldgdlvrpggvitggSAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKeleeLEEELEQLRKELEEL 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 308 SEQIQQMADKILELEEKHR--EAQVSAQHLEV-HLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKI 384
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEqlEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 385 LSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEK 464
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 465 ISHQDHSDKSRLLELETRLREVslehEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRqakteleettAEAE 544
Cdd:TIGR02168 885 LEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----------EEYS 950
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 545 EEIQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDN-------AELNNQNFYLSKQLDEASGAndeIVQLRSEVD 617
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRR---LKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKEDLTEA---KETLEEAIE 1024
|
....*....
gi 1907160229 618 HLRREITER 626
Cdd:TIGR02168 1025 EIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-871 |
2.01e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVElKASETQRSllEQDLATYITECSSLKRSLEQARME 81
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKA--EDAKRVEIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQLLHDIR--EQSRKLQEIKEQEYQAQVEEMRlmmnQLEEdlvsARRrsdlYESELR-ESRLAAEEFKRKAN 158
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRkaEELRKAEDARKAEAARKAEEER----KAEE----ARK----AEDAKKaEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 159 ECQHklmkvvSHPPRGDSGGTALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTE- 237
Cdd:PTZ00121 1241 EAKK------AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEa 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 238 --ATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQqma 315
Cdd:PTZ00121 1315 kkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK--- 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 316 dKILELEEKHREAQVSAQhlevHLKQKEqhyEEKIKVldNQIKKDLADKESLENMMQRHEE--EAHEKGKILSEQKamiN 393
Cdd:PTZ00121 1392 -KADEAKKKAEEDKKKAD----ELKKAA---AAKKKA--DEAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAK---K 1458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 394 AMDSKIRSLEQRIVElsEANKLAANSSLFTQRNMKAQE--EMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHS 471
Cdd:PTZ00121 1459 AEEAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEakKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 472 DKSRLLELETRLREVSLEHEEQKLELKRQLTElqlslQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALT 551
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEE-----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 552 AHRDEIQR-KFDALRNsctvitdlEEQLNQLTEDNAELNNQNFYLSKQLDEASGAND-EIVQLRSEVDHLRREITEREMQ 629
Cdd:PTZ00121 1612 AKKAEEAKiKAEELKK--------AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKA 1683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 630 LTSQKQTMEALKTTctmlEEQVLDLEALNDELLEKERQWEAWRSvlgdEKSQFECRVRELQRMLDTEKQSRARADQRITE 709
Cdd:PTZ00121 1684 EEDEKKAAEALKKE----AEEAKKAEELKKKEAEEKKKAEELKK----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 710 SRQVVELAVKEHKA--EILALQQALKEQKLKAESLSDKLnDLEKKHAMLEMNARSLQQ------------KLETERELKQ 775
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKaeEIRKEKEAVIEEELDEEDEKRRM-EVDKKIKDIFDNFANIIEggkegnlvindsKEMEDSAIKE 1834
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 776 RLLEEQAKLQQQMDLQKnHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVK---MEGTISQQT---KLID 849
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEK-HKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDkddIEREIPNNNmagKNND 1913
|
890 900
....*....|....*....|..
gi 1907160229 850 FLQAKMDQPAKKKKGLFSRRKE 871
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREE 1935
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
35-923 |
2.31e-16 |
|
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: 85.41 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 35 EVEAVLSQKEVElkasetqRSLLEQDLATYItecssLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQ 114
Cdd:pfam02463 143 KIEIIAMMKPER-------RLEIEEEAAGSR-----LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 115 VEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEfKRKANECQHKLMKvvshpprgdsggtalddlhkmqghAGLT 194
Cdd:pfam02463 211 EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD-EQEEIESSKQEIE------------------------KEEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 195 SAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLV 274
Cdd:pfam02463 266 KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 275 EAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLD 354
Cdd:pfam02463 346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 355 NQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMI 434
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKA 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 435 SELrqqkfyletqAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLehEEQKLELKRQLTELQLSLQERESQ 514
Cdd:pfam02463 506 RSG----------LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV--IVEVSATADEVEERQKLVRALTEL 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 515 LTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFY 594
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 595 LSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCT-MLEEQVLDLEALNDELLEKERQWEAWRS 673
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKeQREKEELKKLKLEAEELLADRVQEAQDK 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 674 VLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQaLKEQKLKAESLSDKLNDLEKKH 753
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE-EKEEKLKAQEEELRALEEELKE 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 754 AMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNhifrlTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHE 833
Cdd:pfam02463 813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLA-----EEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 834 KVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRS 913
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
890
....*....|
gi 1907160229 914 AREEAAHRKA 923
Cdd:pfam02463 968 AKEELGKVNL 977
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
206-669 |
3.11e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.73 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 206 EYSKLEKINAEqqlkIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLEN 285
Cdd:PRK03918 229 EVKELEELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 286 KVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVhLKQKEQHYEEKIKVLDN--QIKKDLAD 363
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKKEEleRLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 364 K--ESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEA-NKLAANSSLFTQRN----MKAQEEMISE 436
Cdd:PRK03918 384 LtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkGKCPVCGRELTEEHrkelLEEYTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 437 LRQQKFYLETQAGKLEAQNRKLEEQLEKISH--QDHSDKSRLLELETRLREVSLEHEEQKLE----LKRQLTEL---QLS 507
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLkgeIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 508 LQERESQLTALQAARAALESQLRQAKTELEETTAEAEEE-----------IQALtahrDEIQRKFDALRNSCTVITDLEE 576
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeleerLKEL----EPFYNEYLELKDAEKELEREEK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 577 QLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDH--LRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDL 654
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
490
....*....|....*
gi 1907160229 655 EALNDELLEKERQWE 669
Cdd:PRK03918 700 KEELEEREKAKKELE 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
246-838 |
9.71e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 246 RQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKH 325
Cdd:PRK03918 144 DESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 326 REAQVSAQHLEVHlkqkeqhyEEKIKVLDNQIKKDLADKESLENMMQRHEEeahekgkilseqkaMINAMDSKIRSLEQR 405
Cdd:PRK03918 224 EKLEKEVKELEEL--------KEEIEELEKELESLEGSKRKLEEKIRELEE--------------RIEELKKEIEELEEK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 406 IVELSEANKLAansslftqRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIShqdhSDKSRLLELETRLRE 485
Cdd:PRK03918 282 VKELKELKEKA--------EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 486 V-----SLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALEsqLRQAKTELEETTAEAEEEIQALTAHRDEIQRK 560
Cdd:PRK03918 350 LekrleELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 561 FDALRNS------CTVITDLEEQLNQLTEDNAELNNqnfyLSKQLDEASganDEIVQLRSEVDHLRREItEREMQLTSQK 634
Cdd:PRK03918 428 IEELKKAkgkcpvCGRELTEEHRKELLEEYTAELKR----IEKELKEIE---EKERKLRKELRELEKVL-KKESELIKLK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 635 QTMEALKTTCTMLEEQVL-DLEALNDE---LLEKERQWEAWRSVLGDE---KSQFECRVRELQRMLDTEKQSRARADQRI 707
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLeELEKKAEEyekLKEKLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 708 TE----SRQVVELAVKEHKA---EILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEE 780
Cdd:PRK03918 580 EElgfeSVEELEERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 781 Q-AKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIqvlyshEKVKME 838
Cdd:PRK03918 660 EyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER------EKAKKE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-827 |
1.68e-15 |
|
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: 82.81 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 29 LHRRVSEVEAVLSQKEVElkASETQRSLLEQDLAtyitecsSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKE 108
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKE--ALERQKEAIERQLA-------SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 109 QEY----------QAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHpprgdsgg 178
Cdd:TIGR02169 287 EEQlrvkekigelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 179 talddlhkmqghagLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKastEATELLQNIRQAKERAERELEK 258
Cdd:TIGR02169 359 --------------YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR---EINELKRELDRLQEELQRLSEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 259 LHNREDSSEGIKKKLVEAEERrhsLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVH 338
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEE---KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 339 LKQKEQ---HYEEKIKVLDNQIKK-------------------DLADKESLENMMQRHEEEAHEKGKILSEQKAM----- 391
Cdd:TIGR02169 499 ARASEErvrGGRAVEEVLKASIQGvhgtvaqlgsvgeryataiEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGratfl 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 392 -INAMDSKIRSLE--------QRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQ-KFYLETQAGKLeaqnrkleeq 461
Cdd:TIGR02169 579 pLNKMRDERRDLSilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgKYRMVTLEGEL---------- 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 462 LEKI-SHQDHSDKSRLLELETR-LREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEET 539
Cdd:TIGR02169 649 FEKSgAMTGGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 540 TAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLskqldEASGANDEIVQLRSEVDHL 619
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL-----EARLSHSRIPEIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 620 RREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQ---RMLDTE 696
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalRDLESR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 697 KQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEmnarSLQQKLETERELKQR 776
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----EIPEEELSLEDVQAE 959
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 777 LLEEQAKLQQQMDLQknhiFRLTQGLQEALDRADLLKTERSDLEYQLENIQ 827
Cdd:TIGR02169 960 LQRVEEEIRALEPVN----MLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
277-980 |
2.32e-15 |
|
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: 82.09 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 277 EERRHSLENKVKRL----ETMERRENRLKD---DIQTKSEQIQQMADKILELeeKHREAQvSAQHLEVHLkQKEQHYEEK 349
Cdd:pfam15921 81 EEYSHQVKDLQRRLnesnELHEKQKFYLRQsviDLQTKLQEMQMERDAMADI--RRRESQ-SQEDLRNQL-QNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 350 IKVLDNQIKKDLADK-ESLENMMQRHEEEAHE-----------KGKILSEQKAM---------------INAMDSKIRSL 402
Cdd:pfam15921 157 AKCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEirsilvdfeeaSGKKIYEHDSMstmhfrslgsaiskiLRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 403 EQRIVELSEA-NKLAANSS----LFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKS--- 474
Cdd:pfam15921 237 KGRIFPVEDQlEALKSESQnkieLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmym 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 475 -RLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAH 553
Cdd:pfam15921 317 rQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 554 RDEIQRKFDALRNSCTVITDLEEQLNQ-----------LTEDNAELNNQnfyLSKQLDEASGANDEI-------VQLRSE 615
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDrnmevqrlealLKAMKSECQGQ---MERQMAAIQGKNESLekvssltAQLEST 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 616 VDHLRREITEremqLTSQKQTMEALKTTctmleeqVLDLEAlndELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDT 695
Cdd:pfam15921 474 KEMLRKVVEE----LTAKKMTLESSERT-------VSDLTA---SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 696 EKQSR-------------ARADQRITESRQVVEL-------------AVKEHKA----EILALQQALKEQKLKAESLSDK 745
Cdd:pfam15921 540 GDHLRnvqtecealklqmAEKDKVIEILRQQIENmtqlvgqhgrtagAMQVEKAqlekEINDRRLELQEFKILKDKKDAK 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 746 LNDLEKKHAMLEMNARSL----QQKLETERELKQrlleEQAKLQQQMDLQKNHIFRLTQGLqEALDR-----ADLLKTER 816
Cdd:pfam15921 620 IRELEARVSDLELEKVKLvnagSERLRAVKDIKQ----ERDQLLNEVKTSRNELNSLSEDY-EVLKRnfrnkSEEMETTT 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 817 SDLEYQLENIQ--------VLYSHE---------KVKMEGTISQQTKLIDFLQAKMD------QPAKKKKGLFSRRK--- 870
Cdd:pfam15921 695 NKLKMQLKSAQseleqtrnTLKSMEgsdghamkvAMGMQKQITAKRGQIDALQSKIQfleeamTNANKEKHFLKEEKnkl 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 871 --EDPALPTQVPLQYNELKLALEKE---KARCAELEEALQKT------------RIELRSAREEAAHR---KATDHP-HP 929
Cdd:pfam15921 775 sqELSTVATEKNKMAGELEVLRSQErrlKEKVANMEVALDKAslqfaecqdiiqRQEQESVRLKLQHTldvKELQGPgYT 854
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 930 STPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSR-RKESSTPEEFSRRLKE 980
Cdd:pfam15921 855 SNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHsRKTNALKEDPTRDLKQ 906
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
215-905 |
4.89e-15 |
|
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: 81.27 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 215 AEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEgiKKKLVEAEERRHSLENKVKRLETME 294
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLK--EKREYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 295 RRENRLKDDIQTKSEQIQQMADKILELEEKHRE-------------AQVSAQHLEVH-----LKQKEQHYEEKIKVLDNQ 356
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlgeeeqLRVKEKIGELEaeiasLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 357 IKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLaansslfTQRNMKAQEEMISE 436
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE-------TRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 437 LRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELK----------RQLTELQL 506
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEqlaadlskyeQELYDLKE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 507 SLQERESQLTALQAARAALESQLRQAKTELEETTAEAE------------------------------------------ 544
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvved 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 545 -----EEIQALTAHR--------------------------------------DEIQRKFDALRNSCTVITDLEEQLNQL 581
Cdd:TIGR02169 557 davakEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdPKYEPAFKYVFGDTLVVEDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 582 TE--------------------DNAELNNQNFYLSkQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALK 641
Cdd:TIGR02169 637 GKyrmvtlegelfeksgamtggSRAPRGGILFSRS-EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 642 ttcTMLEEQVLDLEALNDElLEKERQweawrsvlgdEKSQFECRVRELQRMLDTEKQSRARADQRITEsrqvVELAVKEH 721
Cdd:TIGR02169 716 ---RKIGEIEKEIEQLEQE-EEKLKE----------RLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 722 KAEILALQQALKEQKLkaESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIfrltqg 801
Cdd:TIGR02169 778 EEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI------ 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 802 lQEALDRADLLKTERSDLEYQLENiqvlyshekvkmegtisqqtklidfLQAKMDQPAKKKKGLFSRRKEDPALPTQVPL 881
Cdd:TIGR02169 850 -KSIEKEIENLNGKKEELEEELEE-------------------------LEAALRDLESRLGDLKKERDELEAQLRELER 903
|
810 820
....*....|....*....|....
gi 1907160229 882 QYNELKLALEKEKARCAELEEALQ 905
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLE 927
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-622 |
7.54e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 4 KLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVS 83
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 84 QEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLM--MNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQ 161
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 162 HKlmkvvshpprgdsggtALDDLHKMQGHAGLTSAKDQgkpevgeysKLEKINAEQQLKIQELQEKLEKAVKASTEATEL 241
Cdd:COG1196 393 RA----------------AAELAAQLEELEEAEEALLE---------RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 242 LQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQ---MADKI 318
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 319 LELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSK 398
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 399 IRSLE---QRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDhsdkSR 475
Cdd:COG1196 608 LREADaryYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 476 LLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRD 555
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 556 EIQRKfdalrnsctvITDLEEQLNQL-------TEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRRE 622
Cdd:COG1196 764 ELERE----------LERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-820 |
1.46e-14 |
|
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: 79.63 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 206 EYSKLEKINAEQQlkIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEErrhsLEN 285
Cdd:TIGR00618 201 LRSQLLTLCTPCM--PDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE----LRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 286 KVKRLETMERRENRlkddiQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVldnqiKKDLADKE 365
Cdd:TIGR00618 275 QEAVLEETQERINR-----ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-----QSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 366 SLENMMQRHEEE---AHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKF 442
Cdd:TIGR00618 345 RLLQTLHSQEIHirdAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 443 YLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLRevSLEHEEQKLELKRQLTelqlslqERESQLTALQAAR 522
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ--SLKEREQQLQTKEQIH-------LQETRKKAVVLAR 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 523 AALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQ------NFYLS 596
Cdd:TIGR00618 496 LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeiqqSFSIL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 597 KQLDEASGANDEIVQ------------LRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLE- 663
Cdd:TIGR00618 576 TQCDNRSKEDIPNLQnitvrlqdltekLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTl 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 664 -KERQWEAWRSVLGDEKSQFECRVRELQRMldtekQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESL 742
Cdd:TIGR00618 656 tQERVREHALSIRVLPKELLASRQLALQKM-----QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 743 SDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALD-RADLLKTERSDLE 820
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREeDTHLLKTLEAEIG 809
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-774 |
5.78e-14 |
|
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: 77.80 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEavlsqKEVELKASETQRSLLEQdLATYITECSSLKRSLEQARME 81
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN-----KKIKDLGEEEQLRVKEK-IGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQLLHDIREQSRKLQEIKEQeyqaqVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQ 161
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELERE-----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 162 HKLMKVVSHpprgdsggtaLDDLHKMQGHAGLTSAKDQGKPEVGEySKLEKINAeqqlKIQELQEKLEKAVKASTEATEL 241
Cdd:TIGR02169 392 EKLEKLKRE----------INELKRELDRLQEELQRLSEELADLN-AAIAGIEA----KINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 242 LQNIRQAKERAERELEKLhnredssegiKKKLVEAEERRHSLENKVKRLETMER------RENR-----LKDDIQTKSEQ 310
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDL----------KEEYDRVEKELSKLQRELAEAEAQARaseervRGGRaveevLKASIQGVHGT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 311 IQQMadkiLELEEKHREAqvsaqhLEVHLKQKeqhyeekikvLDNQIKKDLADKESLENMMQRHE------------EEA 378
Cdd:TIGR02169 527 VAQL----GSVGERYATA------IEVAAGNR----------LNNVVVEDDAVAKEAIELLKRRKagratflplnkmRDE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 379 HEKGKILSEQKAMINAMD--------------------------------SKIR--SLEQRIVELSEANKLAANSSLFTQ 424
Cdd:TIGR02169 587 RRDLSILSEDGVIGFAVDlvefdpkyepafkyvfgdtlvvedieaarrlmGKYRmvTLEGELFEKSGAMTGGSRAPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 425 RNMKAQEEMISELRQQKfyletqaGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHE--EQKLE-LKRQL 501
Cdd:TIGR02169 667 LFSRSEPAELQRLRERL-------EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqlEQEEEkLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 502 TELQLSLQERESQLTALQAARAALESQLrQAKTELEETTAEAEEEIQALTAHR--DEIQRKFDALRnscTVITDLEEQLN 579
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEARLSHSriPEIQAELSKLE---EEVSRIEARLR 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 580 QLtedNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALND 659
Cdd:TIGR02169 816 EI---EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 660 ELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELA-----VKEHKAEILALQQALKE 734
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledVQAELQRVEEEIRALEP 972
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1907160229 735 QKLKA----ESLSDKLNDLEKKHAMLEMNARSLQQKLETERELK 774
Cdd:TIGR02169 973 VNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-527 |
7.86e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKElqDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQdLATYITECSSLKRSLEQarmE 81
Cdd:PRK03918 180 RLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELEKELESLEG---S 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQLLHDIREQSRKLQEIKE--------QEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELR--ESRLA-A 150
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEkvkelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgiEERIKeL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 151 EEFKRKANECQHKLMKVVSHPPRGDSGGTALDDLHKMQGHAGLTSAKDQGKPE---VGEYSKLEKINAEQQLKIQELQEK 227
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPeklEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 228 LEKAVKASTEATELLQNIRQAKERAE---RELEKLHNREDSSE------GIKKKLVEAEERRHSLENKVKRLETMERREN 298
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCPvcgRELTEEHRKELLEEytaelkRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 299 RLKddiqtkseQIQQMADKILELEEKHREaqVSAQHLEVHLKQKEQHYEEKIKVLDNQ--IKKDLADKESLENMMQRHEE 376
Cdd:PRK03918 494 ELI--------KLKELAEQLKELEEKLKK--YNLEELEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 377 EAHEKGKILSE-QKAMINAMDSKIRSLEQRIVELSEANK---LAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLE 452
Cdd:PRK03918 564 KLDELEEELAElLKELEELGFESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 453 AQNRKLEEQLEKISHQDHSDKS-RLLELETRLREVslehEEQKLELKRQLTELQLSLQERESQLTALQAARAALES 527
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELReEYLELSRELAGL----RAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-630 |
9.14e-14 |
|
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: 77.08 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 21 KMEQEMTRLHRRVSEVEAVL------SQKEVELKASETQRSLlEQDLATYITECSSLKRSLEQARmevSQEDDKALQLlH 94
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLealkseSQNKIELLLQQHQDRI-EQLISEHEVEITGLTEKASSAR---SQANSIQSQL-E 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 95 DIREQSRKlqeiKEQEYQAQVEEMRLMMNQLEEDLVSARRRSD-----------LYESELRESRLAAEEFKRKANECQHK 163
Cdd:pfam15921 303 IIQEQARN----QNSMYMRQLSDLESTVSQLRSELREAKRMYEdkieelekqlvLANSELTEARTERDQFSQESGNLDDQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 164 LMKVvshpprgdsggtaLDDLHKMQGHagLTSAKDQGK----PEVGEYSKLEKINAEQQLKIQELQ--EKLEKAVKASTE 237
Cdd:pfam15921 379 LQKL-------------LADLHKREKE--LSLEKEQNKrlwdRDTGNSITIDHLRRELDDRNMEVQrlEALLKAMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 238 A-TELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEaeerrhSLENKVKRLETMERRENRLKDDIQTKSEQIQQMAD 316
Cdd:pfam15921 444 GqMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVE------ELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 317 KILELEEKhreAQVSAQHLEvHLKQKEQHYEEkIKVLDNQIKKDLADK--------ESLENMMQ---------------- 372
Cdd:pfam15921 518 EITKLRSR---VDLKLQELQ-HLKNEGDHLRN-VQTECEALKLQMAEKdkvieilrQQIENMTQlvgqhgrtagamqvek 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 373 -RHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELS-EANKLAANSSlftqRNMKAqeemISELRQQKFYLETQAGK 450
Cdd:pfam15921 593 aQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGS----ERLRA----VKDIKQERDQLLNEVKT 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 451 LEAQNRKLEEQLEKishqdhsdksrlleLETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARA-ALESQL 529
Cdd:pfam15921 665 SRNELNSLSEDYEV--------------LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGhAMKVAM 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 530 RQAKTeleettaeaeeeiqaLTAHRDEIqrkfDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLD----EASGA 605
Cdd:pfam15921 731 GMQKQ---------------ITAKRGQI----DALQSK---IQFLEEAMTNANKEKHFLKEEKNKLSQELStvatEKNKM 788
|
650 660
....*....|....*....|....*
gi 1907160229 606 NDEIVQLRSEVDHLRREITEREMQL 630
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEVAL 813
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
197-705 |
1.37e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.96 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 197 KDQGKPEVGEYSKLEKinAEQQLK-IQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKkklvE 275
Cdd:COG4717 60 KPQGRKPELNLKELKE--LEEELKeAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ----E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 276 AEERRHSLENKVKRLETMERRENRLKD---DIQTKSEQIQQMADKILELEE-----KHREAQVSAQHLEvHLKQKEQHYE 347
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEqlslaTEEELQDLAEELE-ELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 348 EKIKVLDNQIKKDLADKESLENMMQRHEEEAH-EKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKL-AANSSLFTQR 425
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 426 NMKAQEEMISELRQqkfyLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREV-----SLEHEEQKLELKRQ 500
Cdd:COG4717 293 LAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELqellrEAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 501 LTELQLSLQ--------------ERESQLTALQAARAALESQLRQAKTELEEttaeaeeeiQALTAHRDEIQRKFDALRN 566
Cdd:COG4717 369 EQEIAALLAeagvedeeelraalEQAEEYQELKEELEELEEQLEELLGELEE---------LLEALDEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 567 SctvITDLEEQLNQLTEDNAELNNQNFYLSKQldeasganDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTM 646
Cdd:COG4717 440 E---LEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907160229 647 LEEQVLdlealnDELLEKERQW------EAWRSVLGDEKSQFECRvRELQRMLDTEKQSRARADQ 705
Cdd:COG4717 509 YREERL------PPVLERASEYfsrltdGRYRLIRIDEDLSLKVD-TEDGRTRPVEELSRGTREQ 566
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
208-663 |
7.47e-13 |
|
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: 73.52 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 208 SKLEKINAEQQLKIQELQEKLEKAVkasteatellQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKV 287
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQ----------TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 288 KRLETMERRE--NRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLD---NQIKKDLA 362
Cdd:TIGR04523 298 SDLNNQKEQDwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqNEIEKLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 363 DKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQrivelsEANKLAANSSLFTQRNMKAQEEmISELRQQKF 442
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ------EKELLEKEIERLKETIIKNNSE-IKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 443 YLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHE---EQKLELKRQLTELQLSLQERESQLTALQ 519
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKklnEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 520 AARAALESQLRQAKteleettaeaeeeiqaltahrDEIQRKFDALRNSC--TVITDLEEQLNQLTEDNAELNNQNFYLSK 597
Cdd:TIGR04523 531 SEKKEKESKISDLE---------------------DELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQE 589
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 598 QLDeasgandeivQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLE 663
Cdd:TIGR04523 590 LID----------QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
210-785 |
1.02e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 210 LEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAER---ELEKLhnREDSSEGIKKKLVEAEERRhslENK 286
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDL--RETIAETEREREELAEEVR---DLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 287 VKRLETMERRENRLKD------DIQTKSEQIQQMADKILELEEKHREAQVSAQHlevHLKQKEQhYEEKIKVLDNQIKKD 360
Cdd:PRK02224 286 ERLEELEEERDDLLAEaglddaDAEAVEARREELEDRDEELRDRLEECRVAAQA---HNEEAES-LREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 361 LADKESLENMMQRHEEEahekgkiLSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQ 440
Cdd:PRK02224 362 REEAAELESELEEAREA-------VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 441 kfyLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELEtrlrevslEHEEQKLELKRQLTELQLSLQERESQLTALQA 520
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE--------EDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 521 ARAAlESQLRQAKTELEETTaeaeeeiQALTAHRDEIQRKfdalrnsctvitdlEEQLNQLTEDNAELNnqnfylskqlD 600
Cdd:PRK02224 504 LVEA-EDRIERLEERREDLE-------ELIAERRETIEEK--------------RERAEELRERAAELE----------A 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 601 EASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEqVLDLEALNDELLEKERQWEAWRSVLGDEKS 680
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 681 QFECRVRELQRMLDTEKQSRARADQRITESRQvvelavkehkaeilalqqalkeqklkaESLSDKLNDLEKKHAMLEMNA 760
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEAREDKERAEEYL---------------------------EQVEEKLDELREERDDLQAEI 683
|
570 580
....*....|....*....|....*
gi 1907160229 761 RSLQQKLETERELKQRLLEEQAKLQ 785
Cdd:PRK02224 684 GAVENELEELEELRERREALENRVE 708
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
254-839 |
2.12e-12 |
|
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: 72.52 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 254 RELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLetMERReNRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQ 333
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQL--CEEK-NALQEQLQAETELCAEAEEMRARLAARKQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 334 HLEVHLKQKeqhyEEKIKVLDNQIKKDLADKESLENmmQRHEEEAhekgkilSEQKAMIN--AMDSKIRSLEQRIVELSE 411
Cdd:pfam01576 79 ELESRLEEE----EERSQQLQNEKKKMQQHIQDLEE--QLDEEEA-------ARQKLQLEkvTTEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 412 AN-KLaansslftQRNMKAQEEMISELRQQKFYLETQAGKL-------EAQNRKLEEQLEKishqdhSDKSRlLELETRL 483
Cdd:pfam01576 146 QNsKL--------SKERKLLEERISEFTSNLAEEEEKAKSLsklknkhEAMISDLEERLKK------EEKGR-QELEKAK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 484 REV---SLEHEEQKLELKRQLTELQLSLQERESQLTALQaARAALESQLRQAkteleettaeAEEEIQALTAHRDEIQRK 560
Cdd:pfam01576 211 RKLegeSTDLQEQIAELQAQIAELRAQLAKKEEELQAAL-ARLEEETAQKNN----------ALKKIRELEAQISELQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 561 FDALRNSCTVIT----DLEEQLNQLTEDnaelnnqnfyLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQT 636
Cdd:pfam01576 280 LESERAARNKAEkqrrDLGEELEALKTE----------LEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 637 MEALKTTCtmleeqvldLEALNDELLEKER---QWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQritesrQV 713
Cdd:pfam01576 350 MRQKHTQA---------LEELTEQLEQAKRnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG------QL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 714 VELAVKEHKAEILALQQALKEQKLKAE--SLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRllEEQAKLQ-----Q 786
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSEleSVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKLNlstrlR 492
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 787 QMDLQKNhifrltqGLQEALDRADllkTERSDLEYQLENIQVLYSHEKVKMEG 839
Cdd:pfam01576 493 QLEDERN-------SLQEQLEEEE---EAKRNVERQLSTLQAQLSDMKKKLEE 535
|
|
| C1_MgcRacGAP |
cd20821 |
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ... |
986-1040 |
2.71e-12 |
|
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410371 Cd Length: 55 Bit Score: 62.81 E-value: 2.71e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907160229 986 IPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPA 1040
Cdd:cd20821 1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPTS 55
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
43-642 |
2.90e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 71.86 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 43 KEV--ELKASETQRSLLEQDLATYITECSSLKRSLEQarmevsqeDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRL 120
Cdd:PRK01156 172 KDVidMLRAEISNIDYLEEKLKSSNLELENIKKQIAD--------DEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 121 MMNQLEEdlvsarrrSDLYESELR--ESRLAAEEFKR-KANECQHKLMKVVSHPprgdsggtALDDLHKMQGHAGLtsak 197
Cdd:PRK01156 244 LSSLEDM--------KNRYESEIKtaESDLSMELEKNnYYKELEERHMKIINDP--------VYKNRNYINDYFKY---- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 198 dqgKPEVGEYSK-LEKINAEqqlkIQELQEKLEKAvkasteatELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEA 276
Cdd:PRK01156 304 ---KNDIENKKQiLSNIDAE----INKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 277 EErrhSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKIL-ELEEKHREAQ------VSAQHLEVHLKQKEQHYEEK 349
Cdd:PRK01156 369 LK---SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKkELNEINVKLQdisskvSSLNQRIRALRENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 350 IKVLDNQIK-----KDLADKESlENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRI--VELSEANKLAANSSLF 422
Cdd:PRK01156 446 MEMLNGQSVcpvcgTTLGEEKS-NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKeyLESEEINKSINEYNKI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 423 TQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSR-LLELETrlrevsleHEEQKLELKRQL 501
Cdd:PRK01156 525 ESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIsLIDIET--------NRSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 502 TELQLSLQERESQLTALQAAraaLESQLRQAKTELEETTAEAEEeIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQL 581
Cdd:PRK01156 597 NDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNKYNE-IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEI 672
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 582 TEDNAELNNQNFYLSKQLDEasgANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKT 642
Cdd:PRK01156 673 TSRINDIEDNLKKSRKALDD---AKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
458-918 |
2.92e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 458 LEEQLEKISHQDHSDksRLLELETRLREVS--LEH-EEQKLELKRQLTELQLSLQERESQLTALQAARAALEsQLRQAKT 534
Cdd:PRK02224 192 LKAQIEEKEEKDLHE--RLNGLESELAELDeeIERyEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 535 ELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTV----ITDLEEQLNQLTEDNAE----LNNQNFYLSKQLDEASGAN 606
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadAEAVEARREELEDRDEElrdrLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 607 DEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRV 686
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 687 RELQRMLDTEKQSRARAD------------QRITESRQVVELAVKEHKAEILALQqaLKEQKLKAESLSDKLN------D 748
Cdd:PRK02224 429 AELEATLRTARERVEEAEalleagkcpecgQPVEGSPHVETIEEDRERVEELEAE--LEDLEEEVEEVEERLEraedlvE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 749 LEKKHAMLEMNARSLQQKLET-------ERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEY 821
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAErretieeKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 822 QLENIqvlyshekvkmeGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRkedpalptqvplqyNELKLALEKEKARCAELE 901
Cdd:PRK02224 587 RIESL------------ERIRTLLAAIADAEDEIERLREKREALAELN--------------DERRERLAEKRERKRELE 640
|
490
....*....|....*...
gi 1907160229 902 EALQKTRIE-LRSAREEA 918
Cdd:PRK02224 641 AEFDEARIEeAREDKERA 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
570-922 |
6.18e-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: 70.86 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 570 VITDLEEQLNQLtEDNAELNNQNFYLSKQLDEAsgandEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEE 649
Cdd:TIGR02168 194 ILNELERQLKSL-ERQAEKAERYKELKAELREL-----ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 650 QvldLEALNDELLEKERQWEAWRSVLGD---EKSQFECRVRELQRMLDTEKQSRARADQRITESRQVvelavKEHKAEIL 726
Cdd:TIGR02168 268 K---LEELRLEVSELEEEIEELQKELYAlanEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 727 A-LQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERElkqrlleEQAKLQQQMDLQKNHIFRLTQGLQEA 805
Cdd:TIGR02168 340 AeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-------KVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 806 LDRADLLKTERSDLEYQLENiqvlysHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEdpalptqVPLQYNE 885
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEE------AELKELQAELEELEEELEELQEELERLEEALEELREELEE-------AEQALDA 479
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907160229 886 LKLALEKEKARCAELEEALQKTRIELRSAREEAAHRK 922
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
249-923 |
1.19e-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: 70.10 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 249 KERAERELEKLHNREDSSEGIKKKLVE-----AEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEE 323
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQqlerlRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 324 KHREAQVSAQHLEVHLKQKEQHYEE---KIKVLD----NQIKKDLADKESLENMMQRHEEEAHEKGKILSEQ----KAMI 392
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEElnkKIKDLGeeeqLRVKEKIGELEAEIASLERSIAEKERELEDAEERlaklEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 393 NAMDSKIRSLEQRIVElsEANKLAANSSLFtqrnmKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHS- 471
Cdd:TIGR02169 332 DKLLAEIEELEREIEE--ERKRRDKLTEEY-----AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEl 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 472 --DKSRLLELETRLREVSLEH-------EEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAE 542
Cdd:TIGR02169 405 krELDRLQEELQRLSEELADLnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 543 AEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVD----- 617
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVakeai 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 618 -HLRREITEREMQLTSQK-QTMEALKTtcTMLEEQVLDLeALNdeLLEKERQWE-AWRSVLGDE--KSQFECRVRELQ-- 690
Cdd:TIGR02169 565 eLLKRRKAGRATFLPLNKmRDERRDLS--ILSEDGVIGF-AVD--LVEFDPKYEpAFKYVFGDTlvVEDIEAARRLMGky 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 691 RM--LDTE------------KQSRARADQRITESRQVVELA--VKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHA 754
Cdd:TIGR02169 640 RMvtLEGElfeksgamtggsRAPRGGILFSRSEPAELQRLRerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 755 MLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLT---QGLQEALD--RADLLKTERSDLEYQLENIQVL 829
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariEELEEDLHklEEALNDLEARLSHSRIPEIQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 830 YShekvKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRI 909
Cdd:TIGR02169 800 LS----KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730
....*....|....
gi 1907160229 910 ELRSAREEAAHRKA 923
Cdd:TIGR02169 876 ALRDLESRLGDLKK 889
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
211-878 |
1.49e-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: 69.37 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 211 EKINAEQQLKIQElQEKLEKAVKASTEATELLQNI--RQAKERAERELEKLHNRE---DSSEGIKKKLVEAEERRHSLEN 285
Cdd:pfam05483 130 EKVSLKLEEEIQE-NKDLIKENNATRHLCNLLKETcaRSAEKTKKYEYEREETRQvymDLNNNIEKMILAFEELRVQAEN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 286 -------KVKR-LETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVsaqhLEVHLKQKEQHYEEKIKVLDNQI 357
Cdd:pfam05483 209 arlemhfKLKEdHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDENL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 358 KKDLADKESLENMMqrhEEEAHEKGKILSEQKAMINAMDSKIRSL----EQRIVELSEANKLAANSSLFT---QRNMKAQ 430
Cdd:pfam05483 285 KELIEKKDHLTKEL---EDIKMSLQRSMSTQKALEEDLQIATKTIcqltEEKEAQMEELNKAKAAHSFVVtefEATTCSL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 431 EEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKL------ELKRQLTEL 504
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiaeELKGKEQEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 505 QLSLQERES-------QLTALQAARAALESQLRQAKTELEETTAEAEEeiqaLTAHRDEIQRKFDALRNSCtviTDLEEQ 577
Cdd:pfam05483 442 IFLLQAREKeihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE----LTAHCDKLLLENKELTQEA---SDMTLE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 578 LNQLTEDnaeLNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREIteremqltsqKQTMEALKTTCTMLEEQVLDLEAl 657
Cdd:pfam05483 515 LKKHQED---IINCKKQEERMLKQIENLEEKEMNLRDELESVREEF----------IQKGDEVKCKLDKSEENARSIEY- 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 658 ndELLEKERQWEAWRSVLGDEKSQFECRVRELQRMldtEKQSRARADQRITESRQvveLAVKEHKAEILALQQALKEQKL 737
Cdd:pfam05483 581 --EVLKKEKQMKILENKCNNLKKQIENKNKNIEEL---HQENKALKKKGSAENKQ---LNAYEIKVNKLELELASAKQKF 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 738 KaESLSDKLNDLEKKhamlemnaRSLQQKLETERELKQRLLEEQAKLQQQMDLQKNH-IFRLTQGLQEALDRADLLKTER 816
Cdd:pfam05483 653 E-EIIDNYQKEIEDK--------KISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHkIAEMVALMEKHKHQYDKIIEER 723
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 817 SDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQ 878
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-514 |
3.32e-11 |
|
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: 68.61 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1 MEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQ-RSLLEQDLATYITeCSSLKRSLEQAR 79
Cdd:pfam15921 347 LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnKRLWDRDTGNSIT-IDHLRRELDDRN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 80 MEV-----------SQEDDKALQLLHDIREQSRKLQEIkeQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRL 148
Cdd:pfam15921 426 MEVqrleallkamkSECQGQMERQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 149 AAEEFKRKANECQHKLMKVVSHPprgdsggtaldDLhKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKL 228
Cdd:pfam15921 504 SLQEKERAIEATNAEITKLRSRV-----------DL-KLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQI 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 229 EKAVK-----ASTEATELLQNIRQAKERAERELEK-----LHNREDSsegikkKLVEAEERRHSLE-NKVKRLETMERRE 297
Cdd:pfam15921 572 ENMTQlvgqhGRTAGAMQVEKAQLEKEINDRRLELqefkiLKDKKDA------KIRELEARVSDLElEKVKLVNAGSERL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 298 NRLKDDIQTKSEQIQQMADKILELEEKHREAQVsaqhLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEE 377
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV----LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 378 AHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRK 457
Cdd:pfam15921 722 DGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 458 LEEqlekishqdhsdksRLLELETRLREVSLEHEEQKLELKRQLTE-----LQLSLQERESQ 514
Cdd:pfam15921 802 LKE--------------KVANMEVALDKASLQFAECQDIIQRQEQEsvrlkLQHTLDVKELQ 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-615 |
4.89e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 72 KRSLEQARMEVSQEDDKAL--------QLLHDIREQSRKLQEIKEQEyQAQVEEMRLMMNQLEEdlvsARRRSDLYESEL 143
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLherlngleSELAELDEEIERYEEQREQA-RETRDEADEVLEEHEE----RREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 144 RESRLAAEEFKRKANECQHKLMKvvshppRGDSGGTALDDLHKMQGHAGLTSAKDQGKPEvgEYSKLEKINAEQQlkiQE 223
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRD------LRERLEELEEERDDLLAEAGLDDADAEAVEA--RREELEDRDEELR---DR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 224 LQEKLEKAVKASTEATELLQNIRQAKERAERELEKlhnREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRenrlkdd 303
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREE---AAELESELEEAREAVEDRREEIEELEEEIEELRER------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 304 IQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLD-------NQIKKDLADKESLENMMQRHEE 376
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecGQPVEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 377 EAHEkgkiLSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQR------NMKAQEEMISELRQQKFYLETQAGK 450
Cdd:PRK02224 480 LEAE----LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELiaerreTIEEKRERAEELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 451 LEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVS--------LEHEEQKLE-LKRQLTELQLSLQERESQLTALQAA 521
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllaaIADAEDEIErLREKREALAELNDERRERLAEKRER 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 522 RAALES--------QLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCtvitdleEQLNQLTEDNAELNNQNF 593
Cdd:PRK02224 636 KRELEAefdearieEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL-------EELEELRERREALENRVE 708
|
570 580
....*....|....*....|..
gi 1907160229 594 YLSKQLDEASGANDEIVQLRSE 615
Cdd:PRK02224 709 ALEALYDEAEELESMYGDLRAE 730
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
217-827 |
5.79e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 217 QQLKIQ-------ELQEKLEKAVKASTEATELLQNIRQAKERAERE-------------------------------LEK 258
Cdd:PRK04863 346 QQEKIEryqadleELEERLEEQNEVVEEADEQQEENEARAEAAEEEvdelksqladyqqaldvqqtraiqyqqavqaLER 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 259 -----------LHNREDSSEGIKKKLVEAEERRHSLENKVkrletmerrenRLKDDIQTKSEQIQQMADKIL-------- 319
Cdd:PRK04863 426 akqlcglpdltADNAEDWLEEFQAKEQEATEELLSLEQKL-----------SVAQAAHSQFEQAYQLVRKIAgevsrsea 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 320 -----ELEEKHREAQ---VSAQHLEVHLKQKEQHYEEKIKV--LDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQK 389
Cdd:PRK04863 495 wdvarELLRRLREQRhlaEQLQQLRMRLSELEQRLRQQQRAerLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 390 AMINAMDSKIR----SLEQRIVELS--EANKLAANSSLFTQRNMKAQE----EMISELRQQKFYLETQA----GKLEAQN 455
Cdd:PRK04863 575 SEARERRMALRqqleQLQARIQRLAarAPAWLAAQDALARLREQSGEEfedsQDVTEYMQQLLERERELtverDELAARK 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 456 RKLEEQLEKISHQDHSDKSRLLELETRLREVSLE--HEEQKLE-----------------------LKRQLTELQ----- 505
Cdd:PRK04863 655 QALDEEIERLSQPGGSEDPRLNALAERFGGVLLSeiYDDVSLEdapyfsalygparhaivvpdlsdAAEQLAGLEdcped 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 506 LSLQE------RESQLTALQAARAAL----ESQLRQAKTELEET--TAEAEEEIQALTAHRDEIQRKFDALRNSCTVITD 573
Cdd:PRK04863 735 LYLIEgdpdsfDDSVFSVEELEKAVVvkiaDRQWRYSRFPEVPLfgRAAREKRIEQLRAEREELAERYATLSFDVQKLQR 814
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 574 LEEQLNQLTednaelnNQNFYLSKQLDEasgaNDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEE---- 649
Cdd:PRK04863 815 LHQAFSRFI-------GSHLAVAFEADP----EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRllpr 883
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 650 -QVLDLEALNDELLEKERQWEAWR--------------------SVLGDEKSQFEcrvrELQRMLDTEKQSRARADQRI- 707
Cdd:PRK04863 884 lNLLADETLADRVEEIREQLDEAEeakrfvqqhgnalaqlepivSVLQSDPEQFE----QLKQDYQQAQQTQRDAKQQAf 959
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 708 --TESRQVVELAVKEHKAEILA----LQQALKEQKLKAESLSDKLNDLEKKHA--MLEMNAR------SLQQKLETEREL 773
Cdd:PRK04863 960 alTEVVQRRAHFSYEDAAEMLAknsdLNEKLRQRLEQAEQERTRAREQLRQAQaqLAQYNQVlaslksSYDAKRQMLQEL 1039
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 774 KQRL----------LEEQAKLQQQmdlqknhifRLTQGLQEALDRADLLKTERSDLEYQLENIQ 827
Cdd:PRK04863 1040 KQELqdlgvpadsgAEERARARRD---------ELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
|
| C1_ScPKC1-like_rpt2 |
cd20823 |
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ... |
984-1041 |
7.57e-11 |
|
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410373 Cd Length: 59 Bit Score: 58.86 E-value: 7.57e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 984 HNIPHRFNVGLNMRATKCAVCLDTVHFGR-QASKCLECQVMCHPKCSTCLPATCGLPAE 1041
Cdd:cd20823 1 HRIPHRFEPFTNLGANWCCHCGQMLPLGRkQIRKCTECGKTAHAQCAHLVPNFCGLSME 59
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
298-792 |
8.19e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 67.23 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 298 NRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYeekikvldNQIKKDLADKESLENMMQRHEEE 377
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY--------NNLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 378 AHEkgkiLSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQeemISELRQQKFYLETQAGKLEAQNRK 457
Cdd:PRK01156 258 IKT----AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKND---IENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 458 LEEqLEKISHQDHSDKSRLLELETRLREVSLEH-----------------EEQKLELKRQLTELQLSLQERESQLTALQA 520
Cdd:PRK01156 331 LSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEmdynsylksieslkkkiEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 521 ARAALESQLRQakteLEETTAEAEEEIQALTAHRDEIQRKFDAL--RNSCTVI-TDL-EEQLNQLTED-NAELNNQNFYL 595
Cdd:PRK01156 410 ELNEINVKLQD----ISSKVSSLNQRIRALRENLDELSRNMEMLngQSVCPVCgTTLgEEKSNHIINHyNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 596 SKQLDEASGANDEIVQLRSEVDHLR-----------REITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEK 664
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYLEseeinksineyNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 665 ER-QW------------EAWRSVLGDEKSQF---ECRVRELQ--------------RMLDTE------KQSRARADQRIT 708
Cdd:PRK01156 566 KRtSWlnalavislidiETNRSRSNEIKKQLndlESRLQEIEigfpddksyidksiREIENEannlnnKYNEIQENKILI 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 709 ESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETER----ELKQRLLEEQAKL 784
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRtrinELSDRINDINETL 725
|
....*...
gi 1907160229 785 QQQMDLQK 792
Cdd:PRK01156 726 ESMKKIKK 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-496 |
1.70e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQ---KEVELKASETQRSLLEQDLAtyitecsSLKRSLEqa 78
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLE-------ELEERHE-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 79 rmevsqEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKAN 158
Cdd:PRK03918 363 ------LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 159 ECQhklmkvvshpprgdSGGTALDDLHKMQGHAGLTSakdqgkpEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEA 238
Cdd:PRK03918 437 KCP--------------VCGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 239 TELLQNIRQAKERAER----ELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQM 314
Cdd:PRK03918 496 IKLKELAEQLKELEEKlkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 315 ADKILELEEKhreaqvSAQHLEVHLKQKEQHYEEKIKVLDnqIKKDLadkESLENMMQRHEEEAHEKGKILSEQKAMINA 394
Cdd:PRK03918 576 LKELEELGFE------SVEELEERLKELEPFYNEYLELKD--AEKEL---EREEKELKKLEEELDKAFEELAETEKRLEE 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 395 MDSKIRSLEQRIVElsEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSdKS 474
Cdd:PRK03918 645 LRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA-LE 721
|
490 500
....*....|....*....|..
gi 1907160229 475 RLLELETRLREVSLEHEEQKLE 496
Cdd:PRK03918 722 RVEELREKVKKYKALLKERALS 743
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
77-802 |
1.92e-10 |
|
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: 66.15 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 77 QARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEmrlmmNQLEEDLVSARRRSDLYESELresrlAAEEFKRK 156
Cdd:TIGR00618 215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-----LKKQQLLKQLRARIEELRAQE-----AVLEETQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 157 ANECQHKLMKVVSHPPRgdsggTALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEkLEKAVKAST 236
Cdd:TIGR00618 285 RINRARKAAPLAAHIKA-----VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT-LHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 237 EATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQiQQMAD 316
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ-QELQQ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 317 KILELEEKHREAQVSAQHLE-VHLKQKEQHYEEKIKVLDNqikkdladkesLENMMQRHEEEAHEKGKILSEQKaminam 395
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEkIHLQESAQSLKEREQQLQT-----------KEQIHLQETRKKAVVLARLLELQ------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 396 dSKIRSLEQRIVELSEANKLAANSSLFTQRnmkaqeemISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSR 475
Cdd:TIGR00618 501 -EEPCPLCGSCIHPNPARQDIDNPGPLTRR--------MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 476 LLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRD 555
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 556 EIQRKFDALRNSCTVITDLEEQLNQLTEdNAELNNQNFY--LSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQ 633
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQ-LALQKMQSEKeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 634 KQTMEALKTTCTML--EEQVLDLEALNDELLEKERQWEAWRSVL--GDEKSQFECRVRELQRMLDTEKQSRARADQRITE 709
Cdd:TIGR00618 731 GSDLAAREDALNQSlkELMHQARTVLKARTEAHFNNNEEVTAALqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 710 SRQVVELAVKehkAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMD 789
Cdd:TIGR00618 811 EIPSDEDILN---LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQ 887
|
730
....*....|...
gi 1907160229 790 LQKNHIFRLTQGL 802
Cdd:TIGR00618 888 FDGDALIKFLHEI 900
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
367-603 |
1.94e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.81 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 367 LENMMQRHEEEAHEKGKILSEQkamINAMDSKIRSLEQRIVELSEANKLAAnsslfTQRNMKAQEEMISELRQQKFYLET 446
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQ---LPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 447 QAGKLEAQNRKLEEQLEKISHQ--DHSDKSRLLELETRLREvsleheeqkleLKRQLTELQLSLQERESQLTALQAARAA 524
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDAlpELLQSPVIQQLRAQLAE-----------LEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 525 LESQLRQAkteLEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDnAELNNQNF-YLSKQLDEAS 603
Cdd:COG3206 303 LRAQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE-VEVARELYeSLLQRLEEAR 378
|
|
| C1 |
smart00109 |
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
988-1036 |
1.99e-10 |
|
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.
Pssm-ID: 197519 Cd Length: 50 Bit Score: 57.48 E-value: 1.99e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907160229 988 HRFNVGLNMRATKCAVCLDTVHFGR-QASKCLECQVMCHPKCSTCLPATC 1036
Cdd:smart00109 1 HKHVFRTFTKPTFCCVCRKSIWGSFkQGLRCSECKVKCHKKCADKVPKAC 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
239-801 |
2.36e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 239 TELLQNIRQA-KERAERELEKLHNREDssegikKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADK 317
Cdd:COG4717 37 STLLAFIRAMlLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 318 ILELEEKHREAQVSAQHLEVHLKQKEqhyeekikvldnqikkdlaDKESLENMMQRHEEeahekgkiLSEQKAMINAMDS 397
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEA-------------------LEAELAELPERLEE--------LEERLEELRELEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 398 KIRSLEQRIVELSEA-NKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIS--HQDHSDKS 474
Cdd:COG4717 164 ELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneLEAAALEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 475 RLLELETRLREVSLEHEeqklelkrqLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHR 554
Cdd:COG4717 244 RLKEARLLLLIAAALLA---------LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 555 DEIQRKfdalrnsctvitdLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQK 634
Cdd:COG4717 315 ELEEEE-------------LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 635 QTMEALKTTCTMLEEQV---LDLEALNDELLEKERQWEAWRSVLGDEksqfecrvrELQRMLDTEKQSRARADQRITESR 711
Cdd:COG4717 382 EDEEELRAALEQAEEYQelkEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELR 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 712 QvvELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAklqqqmdlq 791
Cdd:COG4717 453 E--ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERA--------- 521
|
570
....*....|.
gi 1907160229 792 kNHIF-RLTQG 801
Cdd:COG4717 522 -SEYFsRLTDG 531
|
|
| C1 |
cd00029 |
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
988-1036 |
2.38e-10 |
|
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.
Pssm-ID: 410341 Cd Length: 50 Bit Score: 57.14 E-value: 2.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907160229 988 HRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd00029 1 HRFVPTTFSSPTFCDVCGKLIwGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-827 |
2.45e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 376 EEAHEKGKILSEQKAM---INAMDSKIRSLEQRIVELSEAnkLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLE 452
Cdd:COG4913 238 ERAHEALEDAREQIELlepIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 453 AQNRKLEEQLEKISHQ-DHSDKSRLLELETRLREVSLEHEEQK---LELKRQLTELQLSLQERESQLTALQAARAALESQ 528
Cdd:COG4913 316 ARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 529 LRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVI--------TDLEEQLN-------------QLTEDNAE 587
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllalrDALAEALGldeaelpfvgeliEVRPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 588 --------LNNQNFYL---SKQLDEASGANDEIvqlrsevdHLRREI-TEREMQLTSQKQTMEALKTTctmleeqvldle 655
Cdd:COG4913 476 wrgaiervLGGFALTLlvpPEHYAAALRWVNRL--------HLRGRLvYERVRTGLPDPERPRLDPDS------------ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 656 aLNDELLEKERQWEAW-RSVLGDEKSqFEC--RVRELQR---------MLDTEKQSRARADQRITESRQV----VELAVK 719
Cdd:COG4913 536 -LAGKLDFKPHPFRAWlEAELGRRFD-YVCvdSPEELRRhpraitragQVKGNGTRHEKDDRRRIRSRYVlgfdNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 720 EHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEM---------NARSLQQKLETERELKQRLLEEQ---AKLQQQ 787
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSddlAALEEQ 693
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907160229 788 MDlqknhifRLTQGLQEALDRADLLKTERSDLEYQLENIQ 827
Cdd:COG4913 694 LE-------ELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-585 |
2.65e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 93 LHDIREQSRKLQEIKEQEyqAQVEEMRLMMNQLEEDLVSARRRSDLYESELR--ESRLAAEEFKRKANECQHKLmkvvsh 170
Cdd:COG4717 70 LKELKELEEELKEAEEKE--EEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAEL------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 171 pprgdsggtalddlhkmqghAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATEllQNIRQAKE 250
Cdd:COG4717 142 --------------------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE--EELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 251 RAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMER-RENRLKDDIQTKSEQIQQMADKILELEEKHRE-- 327
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 328 ---AQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKEsLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQ 404
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 405 RIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAgKLEAQNRKLEEQLEKISHQ-DHSDKSRLLELETRL 483
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELlEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 484 REVSLEHEEQKLELKRQLTELQLSLQERESQ--LTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKf 561
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPP- 516
|
490 500
....*....|....*....|....
gi 1907160229 562 dalrnsctVITDLEEQLNQLTEDN 585
Cdd:COG4717 517 --------VLERASEYFSRLTDGR 532
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
211-861 |
2.78e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 65.74 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 211 EKInAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERE--------------LEKLHNREDSSEGIKKKLVEA 276
Cdd:COG3096 347 EKI-ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslksqladyqqaLDVQQTRAIQYQQAVQALEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 277 EERRH----SLENKVKRLETMERREN-------------RLKDDIQTKSEQIQQMADKIL-------------ELEEKHR 326
Cdd:COG3096 426 RALCGlpdlTPENAEDYLAAFRAKEQqateevleleqklSVADAARRQFEKAYELVCKIAgeversqawqtarELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 327 EAQVSAQ---HLEVHLKQKEQHY------EEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDS 397
Cdd:COG3096 506 SQQALAQrlqQLRAQLAELEQRLrqqqnaERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 398 KIRSLEQRIVELS--EANKLAANSSLFTQRNMKAQE----EMISELRQQKFYLETQA----GKLEAQNRKLEEQLEKISH 467
Cdd:COG3096 586 QLEQLRARIKELAarAPAWLAAQDALERLREQSGEAladsQEVTAAMQQLLEREREAtverDELAARKQALESQIERLSQ 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 468 QDHSDKSRLLELETRLREV--SLEHEEQKLE-----------------------LKRQLTELQ-----LSLQER------ 511
Cdd:COG3096 666 PGGAEDPRLLALAERLGGVllSEIYDDVTLEdapyfsalygparhaivvpdlsaVKEQLAGLEdcpedLYLIEGdpdsfd 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 512 ESQLTALQAARAAL----ESQLRQAKTELEET--TAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLtedn 585
Cdd:COG3096 746 DSVFDAEELEDAVVvklsDRQWRYSRFPEVPLfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQF---- 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 586 aelnnqnfyLSKQLDEASGANDE--IVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTML---------------E 648
Cdd:COG3096 822 ---------VGGHLAVAFAPDPEaeLAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLnkllpqanlladetlA 892
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 649 EQVLDLEALNDELLEKER----------QWEAWRSVLGDEKSQFEcrvrELQRMLDTEKQSRARADQRI---TESRQVVE 715
Cdd:COG3096 893 DRLEELREELDAAQEAQAfiqqhgkalaQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLKQQIfalSEVVQRRP 968
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 716 LAVKEHKAEIL----ALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQ 791
Cdd:COG3096 969 HFSYEDAVGLLgensDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQ 1048
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 792 KNHifrltqglqEALDRAdllKTERSDLEYQLeniqvlyshekVKMEGTISQQTKLIDFLQAKMDQPAKK 861
Cdd:COG3096 1049 ADA---------EAEERA---RIRRDELHEEL-----------SQNRSRRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
458-918 |
3.02e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 458 LEEQLEKISHQDHSDKSRLLELE-TRLREVSLEHEEQKlELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTEL 536
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 537 EETTAEAEeeIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEAsgANDEIVQLRSEV 616
Cdd:COG4717 126 QLLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA--TEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 617 DHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNdELLEKERQWEAWRSVL-----GDEKSQFECRVRELQR 691
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLallglGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 692 MLdtekqSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLE--MNARSLQQKLET 769
Cdd:COG4717 281 LV-----LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEllDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 770 ERELKQRLLEEQAKLQQQMDLQKNHI-----FRltqGLQEALDRADLLKTERSDLEYQLENI-----QVLYSHEKVKMEG 839
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVedeeeLR---AALEQAEEYQELKEELEELEEQLEELlgeleELLEALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 840 TISQQTKLIDFLQAKMDQpAKKKKGLFSRRKEDpaLPTQVPLQynELKLALEKEKARCAELEE---ALQKTRIELRSARE 916
Cdd:COG4717 433 ELEELEEELEELEEELEE-LREELAELEAELEQ--LEEDGELA--ELLQELEELKAELRELAEewaALKLALELLEEARE 507
|
..
gi 1907160229 917 EA 918
Cdd:COG4717 508 EY 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-466 |
4.55e-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: 64.66 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 3 KKLLIKSKELQDSQDKCHK---MEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQAR 79
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 80 MEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAqveemrlMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANe 159
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD-------WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 160 cqhKLMKVVSHpprgdsggtalddlhkmqghagLTSAKDQGKPEVGE-YSKLEKINAEQQLKIQELQeKLEkavkasTEA 238
Cdd:TIGR04523 346 ---QLKKELTN----------------------SESENSEKQRELEEkQNEIEKLKKENQSYKQEIK-NLE------SQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 239 TELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQmadKI 318
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET---QL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 319 LELEEKHREAQVSAQHLEVHLKQKEQHYE---EKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAM 395
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKklnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 396 DS---------KIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIS 466
Cdd:TIGR04523 551 DFelkkenlekEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-790 |
7.52e-10 |
|
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: 64.04 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARME 81
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQLLHDIREQSRKLQEIKEQ--EYQAQVEEMRL-------MMNQLEED-LVSARRRSDLY-ESELRESRLAa 150
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQldEEEAARQKLQLekvtteaKIKKLEEDiLLLEDQNSKLSkERKLLEERIS- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 151 eEFKRKANECQHKLMKVVSHPPRGDSGGTALDDLHKMQGHAGLTSAKDQGKPEvGEYSKLEKINAEQQLKIQELQEKL-- 228
Cdd:pfam01576 163 -EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE-GESTDLQEQIAELQAQIAELRAQLak 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 229 -EKAVKASTEATELLQNIRQAKERAERELE-KLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETmerrenRLKDDIQT 306
Cdd:pfam01576 241 kEEELQAALARLEEETAQKNNALKKIRELEaQISELQEDLESERAARNKAEKQRRDLGEELEALKT------ELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 307 KSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILS 386
Cdd:pfam01576 315 TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 387 EQKAMINAMDSKIRSLEQRIVEL-SEANKLAANSSLFTQRNMKAQEE------MISELRQQKFYLETQAGKLEAQNRKLE 459
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELqARLSESERQRAELAEKLSKLQSElesvssLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 460 EQLEKISHQDHSDKSRLLELE---TRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTEL 536
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEderNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 537 EETTAEAEEEIQA---------------------------LTAHRDEIQRKFD-ALRNSCTVITDLEEQLNQLTEDNAEL 588
Cdd:pfam01576 555 EALTQQLEEKAAAydklektknrlqqelddllvdldhqrqLVSNLEKKQKKFDqMLAEEKAISARYAEERDRAEAEAREK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 589 NNQNFYLSKQLDEASGANDEI----VQLRSEVDHL-------RREITEREMQLTSQKQTMEALKTTCTMLEEQvldLEAL 657
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELertnKQLRAEMEDLvsskddvGKNVHELERSKRALEQQVEEMKTQLEELEDE---LQAT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 658 NDELLEKERQWEAW----------RSVLGDEK-SQFECRVRELQRMLDTEKQSRARAdqriTESRQVVELAVKEHKAEIL 726
Cdd:pfam01576 712 EDAKLRLEVNMQALkaqferdlqaRDEQGEEKrRQLVKQVRELEAELEDERKQRAQA----VAAKKKLELDLKELEAQID 787
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 727 ALQQ----ALKEQKLKAESLSDKLNDLEKKHAMLEmnaRSLQQKLETERELKQRlleEQAKLQQQMDL 790
Cdd:pfam01576 788 AANKgreeAVKQLKKLQAQMKDLQRELEEARASRD---EILAQSKESEKKLKNL---EAELLQLQEDL 849
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
194-925 |
1.03e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 194 TSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKAstEATELLQNIRQAKE--RAE--RELEKLHNREDSSEGI 269
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA--EEARKAEDARKAEEarKAEdaKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 270 KKKLVE----AEERRHSLEnkVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQhlEVHLKQKEQH 345
Cdd:PTZ00121 1168 EARKAEdakkAEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE--EAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 346 YEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKiRSLEQRIVElsEANKLAANSSLFTQR 425
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK-KAEEKKKAD--EAKKKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 426 NMKAQEemiSELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQ 505
Cdd:PTZ00121 1321 KKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 506 LSLQERESQLTALQAARAAlESQLRQAKTELEETTAEAEEEIQALTAHR-DEIQRKFDALRNSctvitdleEQLNQLTED 584
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKA--------EEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 585 naelnnqnfylSKQLDEASGANDEivqlRSEVDHLRREITEREMQLTSQKQTMEALKTTctmleeqvldlealnDELLEK 664
Cdd:PTZ00121 1469 -----------AKKADEAKKKAEE----AKKADEAKKKAEEAKKKADEAKKAAEAKKKA---------------DEAKKA 1518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 665 ERQWEAWRSVLGDEKSQFEcrvrELQRMLDTEKQSRARADQRITESRQV--VELAVKEHKAEILALQQAlkeqklkaesl 742
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKAD----EAKKAEEKKKADELKKAEELKKAEEKkkAEEAKKAEEDKNMALRKA----------- 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 743 sDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQ 822
Cdd:PTZ00121 1584 -EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 823 LENIQVLYSHEKVKMEgtisqqtklidflQAKMDQPAKKKKGLFSRRKEDPALPTQvplqynELKLALEKEKARCAEL-- 900
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAE-------------EAKKAEEDEKKAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELkk 1723
|
730 740
....*....|....*....|....*
gi 1907160229 901 EEALQKTRIELRSAREEAAHRKATD 925
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-724 |
1.28e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 91 QLLHDIREQSRKLQEIKE--QEYQAQVEEMRLMmNQLEEDLVS--ARRRSDLYESELRESRLAAEEFKRKANECQHKLmk 166
Cdd:COG4913 242 EALEDAREQIELLEPIRElaERYAAARERLAEL-EYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLEARL-- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 167 vvshpprgDSGGTALDDLHK-MQGHAGltSAKDQGKPEVGEyskLEKINAEQQLKIQELQEKLEKA-VKASTEATELLQN 244
Cdd:COG4913 319 --------DALREELDELEAqIRGNGG--DRLEQLEREIER---LERELEERERRRARLEALLAALgLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 245 IRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLE----TMERRENRLKDDIqtkSEQIQQMADKI-- 318
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksNIPARLLALRDAL---AEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 319 ----LELEEKHREAQ---------------VSAQHL--------EVHLKQK-------------------EQHYEEKIKV 352
Cdd:COG4913 463 vgelIEVRPEEERWRgaiervlggfaltllVPPEHYaaalrwvnRLHLRGRlvyervrtglpdperprldPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 353 LDNQ----IKKDLADK------ESLENM-----------MQRHEEEAHEKG---KILSEQ------KAMINAMDSKIRSL 402
Cdd:COG4913 543 KPHPfrawLEAELGRRfdyvcvDSPEELrrhpraitragQVKGNGTRHEKDdrrRIRSRYvlgfdnRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 403 EQRIVELSEANKLAANSslftQRNMKAQEEMISELRQQKFYlETQAGKLEAQNRKLEEQLEKIShqdhSDKSRLLELETR 482
Cdd:COG4913 623 EEELAEAEERLEALEAE----LDALQERREALQRLAEYSWD-EIDVASAEREIAELEAELERLD----ASSDDLAALEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 483 LREVSLEH---EEQKLELKRQLTELQLSLQERESQLTALQAA------------RAALESQLRQAKTELEETTAEAEEEi 547
Cdd:COG4913 694 LEELEAELeelEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlelRALLEERFAAALGDAVERELRENLE- 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 548 QALTAHRDEIQRKFDALRN------------SCTVITDLE------EQLNQLTEDNAELNNQNFylSKQLDEASgaNDEI 609
Cdd:COG4913 773 ERIDALRARLNRAEEELERamrafnrewpaeTADLDADLEslpeylALLDRLEEDGLPEYEERF--KELLNENS--IEFV 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 610 VQLRSEVDHLRREITER-----------------EMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKerqweawr 672
Cdd:COG4913 849 ADLLSKLRRAIREIKERidplndslkripfgpgrYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEA-------- 920
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 673 svlgdeksQFEcRVREL-QRMLDTEKQSRARADQRITESRQVVELAVKEHKAE 724
Cdd:COG4913 921 --------RFA-ALKRLiERLRSEEEESDRRWRARVLDVRNHLEFDAEEIDRE 964
|
|
| ROM1 |
COG5422 |
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ... |
1241-1492 |
2.31e-09 |
|
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];
Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 62.60 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1241 SDQVVLVGTEEGLYALNVLKNS--------LTHIPGIGavfQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLp 1312
Cdd:COG5422 868 SGRKLLTGTNKGLYISNRKDNVnrfnkpidLLQEPNIS---QIIVIEEYKLMLLLSDKKLYSCPLDVIDASTEENVKKS- 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1313 aqpDVSPNIFEAVK-----GCHLFAAGKiENSLCICAAMPSKVVILRYNDN------LSKYCIRKEIETSEPCScIHFTN 1381
Cdd:COG5422 944 ---RIVNGHVSFFKqgfcnGKRLVCAVK-SSSLSATLAVIEAPLALKKNKSgnlkkaLTIELSTELYVPSEPLS-VHFLK 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1382 YSILIGTNKFYEI-DMKQYTLDEFLDKNDHSlaPAVFASSSNSFPVSIVQANSagqreEYLLCFHEFGVFVDSYGRRSRT 1460
Cdd:COG5422 1019 NKLCIGCKKGFEIvSLENLRTESLLNPADTS--PLFFEKKENTKPIAIFRVSG-----EFLLCYSEFAFFVNDQGWRKRT 1091
|
250 260 270
....*....|....*....|....*....|...
gi 1907160229 1461 DDL-KWSRLPLAFAYREPYlfVTHFNSlEVIEI 1492
Cdd:COG5422 1092 SWIfHWEGEPQEFALSYPY--ILAFEP-NFIEI 1121
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
451-818 |
4.04e-09 |
|
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: 60.85 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 451 LEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEeqklELKRQLTELQLSLQERESQLTALQAARAALESQLR 530
Cdd:pfam19220 25 LKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYG----KLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 531 QAKTELEETTAeaeeeiqaltahrdeiqrkfdALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASgandeiv 610
Cdd:pfam19220 101 EAEAAKEELRI---------------------ELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 611 QLRSEVDHLRREITEREMQLTSQKQTMEALkttctmLEEQVLDLEALNDELLEKERQWEAWRSvlgdeksqfecRVRELQ 690
Cdd:pfam19220 153 KALQRAEGELATARERLALLEQENRRLQAL------SEEQAAELAELTRRLAELETQLDATRA-----------RLRALE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 691 RMLDTEKQSRARADQRItesrqvvELAVKEHKAEILALqqalkeqKLKAESLSDKLNDLEKkhaMLEMNARSLQQKLETE 770
Cdd:pfam19220 216 GQLAAEQAERERAEAQL-------EEAVEAHRAERASL-------RMKLEALTARAAATEQ---LLAEARNQLRDRDEAI 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 771 RELKQRLLE---EQAKLQQQMDLQKNHIFRLTQGLQEaLDRADLLKTERSD 818
Cdd:pfam19220 279 RAAERRLKEasiERDTLERRLAGLEADLERRTQQFQE-MQRARAELEERAE 328
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
242-828 |
4.76e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.39 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 242 LQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSlenkvkRLETMERRENRLKDDIQTKSEQIQQMADKiLEL 321
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIAS------RQEERQETSAELNQLLRTLDDQWKEKRDE-LNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 322 EEKHREAQVSA--QHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKI 399
Cdd:pfam12128 309 ELSAADAAVAKdrSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 400 RSLEQRIVELSEANKLAANSSLFTQRNMKAQEEmiSELRQQkfyletqagkLEAQNRKLEEQLEKIshqdhsdKSRLLEL 479
Cdd:pfam12128 389 NRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SELREQ----------LEAGKLEFNEEEYRL-------KSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 480 ETRLREVSLEHeeqklELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEettaeaeeeiQALTAHRDEIQR 559
Cdd:pfam12128 450 KLRLNQATATP-----ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD----------QASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 560 kfdalrnsctvitdLEEQLNQLTEDNAELNNQNFYLSKQL-DEASGANDEIVQLRSEvDHLRREITEREMQLTSQKQTME 638
Cdd:pfam12128 515 --------------LEERQSALDELELQLFPQAGTLLHFLrKEAPDWEQSIGKVISP-ELLHRTDLDPEVWDGSVGGELN 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 639 ALKTTCTMLEEQVLDLEALNDELLEKERQWEawrSVLGDEKS---QFECRVRELQRMLDTEKQSRARADQRITESRQVVE 715
Cdd:pfam12128 580 LYGVKLDLKRIDVPEWAASEEELRERLDKAE---EALQSAREkqaAAEEQLVQANGELEKASREETFARTALKNARLDLR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 716 LAVKEHKAEILALQQALKEQKLKAE----SLSDKLNDLEKKH-AMLEMNARSLQ----QKLETERELKQRLLEEQAKLQQ 786
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANerlnSLEAQLKQLDKKHqAWLEEQKEQKReartEKQAYWQVVEGALDAQLALLKA 736
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 787 QMDLQKNHIFRLTQGLQEALDRaDL------------LKTERSDLEYQLENIQV 828
Cdd:pfam12128 737 AIAARRSGAKAELKALETWYKR-DLaslgvdpdviakLKREIRTLERKIERIAV 789
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
8-822 |
5.04e-09 |
|
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: 61.60 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 8 KSKELQDSQDKCHKMEQEMTRLHRRVSEVEavLSQKEVELKASETQrslleqdlatyiteCSSLKRSLEQARMEVSQEDD 87
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRLLNQEKTELL--VEQGRLQLQADRHQ--------------EHIRARDSLIQSLATRLELD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 88 kALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKV 167
Cdd:TIGR00606 381 -GFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 168 VShppRGDSGGTALDDLHKMQghAGLTSAKdqgkpevGEYSKLEKINAEQQLKIQELQEKLEKAvkasteatELLQNIRQ 247
Cdd:TIGR00606 460 IK---ELQQLEGSSDRILELD--QELRKAE-------RELSKAEKNSLTETLKKEVKSLQNEKA--------DLDRKLRK 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 248 AKERAErELEKLHNREDSSEGIKKKLVEAEER------RHSLEnkVKRLETMERRENRLKDDIQTKSEQIQQMADKILEL 321
Cdd:TIGR00606 520 LDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQirkiksRHSDE--LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 322 EEKHREAQVSAQHLEVHLKQKEQH---YEEKIKvldnqikkDLADKESLENMMQRHEEEAHEKGKilseQKAMINAmdsK 398
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQlssYEDKLF--------DVCGSQDEESDLERLKEEIEKSSK----QRAMLAG---A 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 399 IRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKI--------SHQDH 470
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrqSIIDL 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 471 SDKsRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERES------QLTALQAARAALESQLRQ-AKTELEETTAEA 543
Cdd:TIGR00606 742 KEK-EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvcltDVTIMERFQMELKDVERKiAQQAAKLQGSDL 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 544 EEEIQALTAHRDEIQRKFDALRNSC----TVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHL 619
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIelnrKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 620 RREITEREMQLTSQKQTMEalkttctmleeqvlDLEALNDELLEKERQweawrsvlgdEKSQFECRVRELQRMLDTEKQS 699
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLE--------------KDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGY 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 700 RARADQRITESRqvvELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKL----------ET 769
Cdd:TIGR00606 957 MKDIENKIQDGK---DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlrkrenelkEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 770 ERELKQRLLE-----------EQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQ 822
Cdd:TIGR00606 1034 EEELKQHLKEmgqmqvlqmkqEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
246-938 |
7.89e-09 |
|
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: 60.75 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 246 RQAKERAE--RELEKLHNREDSSEGIKKKLVEAEERRHSLEnkvKRLETMERRENRLKDDIQTKSEqiqqmadkILELEE 323
Cdd:TIGR00618 160 AKSKEKKEllMNLFPLDQYTQLALMEFAKKKSLHGKAELLT---LRSQLLTLCTPCMPDTYHERKQ--------VLEKEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 324 KH-REAQVSAQHLEVHLKQKEQHYEEKIKvLDNQIKKDLADKESLENMMQRHE------EEAHEKGKILSEQKAMINaMD 396
Cdd:TIGR00618 229 KHlREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEetqeriNRARKAAPLAAHIKAVTQ-IE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 397 SKIRSLEQRIVElseanKLAANSSLFTQRNMKAQEEmiSELRQQKFYLETqagkLEAQNRKLEEQLEK-ISHQDHSDKSR 475
Cdd:TIGR00618 307 QQAQRIHTELQS-----KMRSRAKLLMKRAAHVKQQ--SSIEEQRRLLQT----LHSQEIHIRDAHEVaTSIREISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 476 LLELETRLREVSLEHEEQKLELKRQLTElqlSLQERESQLTALQAARAALESQLRQAKTEleettaeaeeeiQALTAHRD 555
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELD---ILQREQATIDTRTSAFRDLQGQLAHAKKQ------------QELQQRYA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 556 EIQRKFdalrnsctvitdLEEQLNQLTEDNAELNNqnfylskqldeasgandeivqlrsevdhLRREITEREMQLTSQKQ 635
Cdd:TIGR00618 441 ELCAAA------------ITCTAQCEKLEKIHLQE----------------------------SAQSLKEREQQLQTKEQ 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 636 TMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRsVLGDEKSQFECRVRELQRMLDTEKQSRARAD---QRITESRQ 712
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqlTSERKQRA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 713 VVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKkhaMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQK 792
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD---LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 793 nhifrLTQGLQEALDRadlLKTERSDLEYQLENIQVLYSHEKVKMEGTISQqtKLIDFLQAKMDQPAKKKKGLFSR---- 868
Cdd:TIGR00618 637 -----CSQELALKLTA---LHALQLTLTQERVREHALSIRVLPKELLASRQ--LALQKMQSEKEQLTYWKEMLAQCqtll 706
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 869 RKEDPALPTQVPlQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQ 938
Cdd:TIGR00618 707 RELETHIEEYDR-EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-917 |
1.23e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 346 YEEKIKVLDNQIKKDLADKESLENMMQRhEEEAHEKgkiLSEQKAMINAMDSKIRSLEQRIVELSEanKLAANSSLFtqR 425
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEEL---IKEKEKELEEVLREINEISSELPELRE--ELEKLEKEV--K 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 426 NMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIshqdhsdKSRLLELETRLREV-SLEHEEQK-LELKRQLTE 503
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL-------KKEIEELEEKVKELkELKEKAEEyIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 504 LQLSLQERESQLTALQAARAALESQLRQAKTELEEttaeaeeeIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTE 583
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEER--------LEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 584 DNAELNNQNF-YLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTC-------------TMLEE 649
Cdd:PRK03918 377 LKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteehrkELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 650 QVLDLEALNDELLEkerqweawrsvLGDEKSQFECRVRELQRMLdtEKQSRARADQRITESRQVVELAVKEHKAEilalq 729
Cdd:PRK03918 457 YTAELKRIEKELKE-----------IEEKERKLRKELRELEKVL--KKESELIKLKELAEQLKELEEKLKKYNLE----- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 730 qALKEQKLKAESLSDKLNDLEKKhamlemnARSLQQKLETERELKQRLLEEQAKLQQqmdlqknhifrltqglqealdra 809
Cdd:PRK03918 519 -ELEKKAEEYEKLKEKLIKLKGE-------IKSLKKELEKLEELKKKLAELEKKLDE----------------------- 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 810 dlLKTERSDLEYQLENIQVLYSHEkvkMEGTISQQTKLID-FLQAKmdqPAKKKKglfsRRKEDpalptqvplqynelkl 888
Cdd:PRK03918 568 --LEEELAELLKELEELGFESVEE---LEERLKELEPFYNeYLELK---DAEKEL----EREEK---------------- 619
|
570 580
....*....|....*....|....*....
gi 1907160229 889 ALEKEKARCAELEEALQKTRIELRSAREE 917
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
94-941 |
1.67e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 94 HDIREQSRKLQEIK------EQEYQAQVEEMRLMMNQL---------EEDLVSARRRsdLYES-----ELRESRLAAEEF 153
Cdd:PRK04863 307 YRLVEMARELAELNeaesdlEQDYQAASDHLNLVQTALrqqekieryQADLEELEER--LEEQnevveEADEQQEENEAR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 154 KRKANECQHKLMKVVSHPPRgdsggtALDDLHKM-----QGHAGLTSAKDQ-GKPEVgEYSKLEKINAEQQLKIQELQEK 227
Cdd:PRK04863 385 AEAAEEEVDELKSQLADYQQ------ALDVQQTRaiqyqQAVQALERAKQLcGLPDL-TADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 228 L----------EKAVKASTEATELLQNI----------RQAKErAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKV 287
Cdd:PRK04863 458 LlsleqklsvaQAAHSQFEQAYQLVRKIagevsrseawDVARE-LLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 288 KRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEE-------------KIKVLD 354
Cdd:PRK04863 537 RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaarapawlaaqdALARLR 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 355 NQIKKDLADKESLENMMQRHEEEAHEkgkiLSEQKAMINAmdsKIRSLEQRIVELSEANklaaNSSLFTQRNMKAQ--EE 432
Cdd:PRK04863 617 EQSGEEFEDSQDVTEYMQQLLERERE----LTVERDELAA---RKQALDEEIERLSQPG----GSEDPRLNALAERfgGV 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 433 MISELR-----QQKFYLETQAGK---------LEAQNRKLEEQlekishQDHSDKSRLLELE-TRLREVSLEHEEQKLEL 497
Cdd:PRK04863 686 LLSEIYddvslEDAPYFSALYGParhaivvpdLSDAAEQLAGL------EDCPEDLYLIEGDpDSFDDSVFSVEELEKAV 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 498 KRQLTELQLslqeRESQLTALQA-ARAALESQLRQakteleettaeaeeeiqaLTAHRDEIQRKFDALRNSCTVITDLEE 576
Cdd:PRK04863 760 VVKIADRQW----RYSRFPEVPLfGRAAREKRIEQ------------------LRAEREELAERYATLSFDVQKLQRLHQ 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 577 QLNQLTednaelnNQNFYLSKQLDEasgaNDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEE-----QV 651
Cdd:PRK04863 818 AFSRFI-------GSHLAVAFEADP----EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRllprlNL 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 652 LDLEALNDELLEKERQW----EAWRSVlgdekSQFECRVRELQRMLDTEKQSRARADQritesrqvVELAVKEHKAEILA 727
Cdd:PRK04863 887 LADETLADRVEEIREQLdeaeEAKRFV-----QQHGNALAQLEPIVSVLQSDPEQFEQ--------LKQDYQQAQQTQRD 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 728 LQQ---ALKE--QKLKAESLSDKLNDLEKKHAMLEmnarSLQQKLETERELKQRLLEEQAKLQQQMDlQKNHIFrltQGL 802
Cdd:PRK04863 954 AKQqafALTEvvQRRAHFSYEDAAEMLAKNSDLNE----KLRQRLEQAEQERTRAREQLRQAQAQLA-QYNQVL---ASL 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 803 QEALDRAdllKTERSDLEYQLENIQVLYshekvkmegtisqqtklidflqakmDQPAKKKkglfSRRKEDpalptqvplq 882
Cdd:PRK04863 1026 KSSYDAK---RQMLQELKQELQDLGVPA-------------------------DSGAEER----ARARRD---------- 1063
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 883 ynELKLALEKEKARCAELEEALQKTRIELRSA--REEAAHRKATDHPHPSTPATARQQIAM 941
Cdd:PRK04863 1064 --ELHARLSANRSRRNQLEKQLTFCEAEMDNLtkKLRKLERDYHEMREQVVNAKAGWCAVL 1122
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
23-531 |
2.12e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 23 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLatyiTECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRK 102
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR----DEADEVLEEHEERREELETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 103 LQEIKE--QEYQAQVEEMR---------LMMNQLEEDLVSARR-----RSDLYESELRESRLAAEEFKrkaNECQHKLMK 166
Cdd:PRK02224 274 REELAEevRDLRERLEELEeerddllaeAGLDDADAEAVEARReeledRDEELRDRLEECRVAAQAHN---EEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 167 VVSHPPRGDSGGTALDDLHkmqghAGLTSAKDQGKPEVGEYSKLEK---------INAEQQL-----KIQELQEKLEKAV 232
Cdd:PRK02224 351 ADDLEERAEELREEAAELE-----SELEEAREAVEDRREEIEELEEeieelrerfGDAPVDLgnaedFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 233 KASTEATELLQNIRQAKERAERELEK------------------LHNREDSSEGIKKKLVEAEERRHSLENKVKRLETM- 293
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 294 --ERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQK-----EQHYE-----EKIKVLDNQIKKDL 361
Cdd:PRK02224 506 eaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaEAEEEaeearEEVAELNSKLAELK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 362 ADKESLENmmqrheeeahekgkiLSEQKAMINAMDSKIRSLEQRIVELSEAN-----KLAANSSLFTQRNMKAQEEMISE 436
Cdd:PRK02224 586 ERIESLER---------------IRTLLAAIADAEDEIERLREKREALAELNderreRLAEKRERKRELEAEFDEARIEE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 437 LRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELEtRLREvslEHEEqklelkrqltelqlsLQERESQLT 516
Cdd:PRK02224 651 AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE-ELRE---RREA---------------LENRVEALE 711
|
570 580
....*....|....*....|..
gi 1907160229 517 A-------LQAARAALESQLRQ 531
Cdd:PRK02224 712 AlydeaeeLESMYGDLRAELRQ 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
425-820 |
2.25e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 425 RNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISH--QDHSDKSRLLELETRLREVSlEHEEQKLELKRQLT 502
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELE-ALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 503 ELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLT 582
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE---LEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 583 EDNAELNNQ--NFYLSKQLDEA-------------SGAND----------EIVQLRSEVDHLRREITEREMQLTSQKQTM 637
Cdd:COG4717 227 EELEQLENEleAAALEERLKEArlllliaaallalLGLGGsllsliltiaGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 638 EALKTTCTMLEEQV---------LDLEALNDELLEKERQWEAWRSVL-----GDEKSQFECRVRELQRMLDTEK-QSRAR 702
Cdd:COG4717 307 LQALPALEELEEEEleellaalgLPPDLSPEELLELLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAGvEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 703 ADQRITESRQVVELavkehKAEILALQQALKEQKLKAESLSDKLNDlekkhAMLEMNARSLQQKLETERELKQRLLEEQA 782
Cdd:COG4717 387 LRAALEQAEEYQEL-----KEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907160229 783 KLQQQMDLQKNhifrlTQGLQEALDRADLLKTERSDLE 820
Cdd:COG4717 457 ELEAELEQLEE-----DGELAELLQELEELKAELRELA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-465 |
2.63e-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: 57.85 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 217 QQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLhnrEDSSEGIKKKLVEAEERRHSLENKVKRLetmERR 296
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAEL---EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 297 ENRLKDDIQTKSEQIQQMAdkileleekhREAQVSAQHlevhlkqkeqhyeEKIKVLDNQikKDLADKESLENMMQRHEE 376
Cdd:COG4942 92 IAELRAELEAQKEELAELL----------RALYRLGRQ-------------PPLALLLSP--EDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 377 EAHEKGKILSEQKAMINAmdsKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNR 456
Cdd:COG4942 147 ARREQAEELRADLAELAA---LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
....*....
gi 1907160229 457 KLEEQLEKI 465
Cdd:COG4942 224 ELEALIARL 232
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
214-913 |
2.77e-08 |
|
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: 58.68 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 214 NAEQQLKIQELQEKLekavKASTEATELLQNIRQAKERAEREleKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETM 293
Cdd:pfam10174 69 NQHLQLTIQALQDEL----RAQRDLNQLLQQDFTTSPVDGED--KFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 294 ERRENRLKDDIQTKSEQIQQMAD--------KILELEEKHR-----EAQVSAQHLEVHLKQKEqhyeekikvldnqiKKD 360
Cdd:pfam10174 143 ELRIETQKQTLGARDESIKKLLEmlqskglpKKSGEEDWERtrriaEAEMQLGHLEVLLDQKE--------------KEN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 361 LADKESLENMMQRHEEEAHEKGkilseQKAMINAMDSKIRSLEQRIVELS-EANKLAANSSLFTqrnmkaqEEMISELRQ 439
Cdd:pfam10174 209 IHLREELHRRNQLQPDPAKTKA-----LQTVIEMKDTKISSLERNIRDLEdEVQMLKTNGLLHT-------EDREEEIKQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 440 QKFYletqagkleaqnrkleeqlekishQDHSDKsrlleletrlrevsleheeqkleLKRQLTELQLSLQERESQLTALQ 519
Cdd:pfam10174 277 MEVY------------------------KSHSKF-----------------------MKNKIDQLKQELSKKESELLALQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 520 AARAALESQLRQAKTELEETTaeaeeeiQALTAHRDE---IQRKFDALRNSC----TVITDLEEQLNQLTEDNAELNNQN 592
Cdd:pfam10174 310 TKLETLTNQNSDCKQHIEVLK-------ESLTAKEQRaaiLQTEVDALRLRLeekeSFLNKKTKQLQDLTEEKSTLAGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 593 FYLSKQLDEAsgaNDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEalnDELLEKERQWEAWR 672
Cdd:pfam10174 383 RDLKDMLDVK---ERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE---EALSEKERIIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 673 svlgdEKSQFECRVR--ELQRMLDTEKQSRARAD--QRITESRQVVELAVKEHkAEILALQQALKEQKLKA--------- 739
Cdd:pfam10174 457 -----EQREREDRERleELESLKKENKDLKEKVSalQPELTEKESSLIDLKEH-ASSLASSGLKKDSKLKSleiaveqkk 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 740 ESLSDKLNDLEKKHAMlEMNARSLQQKLETERELKQ---RLLEEQAKLQQQMDlqknhifRLTQGLQEAldradllKTER 816
Cdd:pfam10174 531 EECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQevaRYKEESGKAQAEVE-------RLLGILREV-------ENEK 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 817 SDLEYQLENIQVLYSHEkvkmegtISQQTKLIDflQAKMDQPAKKKKGLfsrRKEDPALPTQVPLQYNELKLALEkekar 896
Cdd:pfam10174 596 NDKDKKIAELESLTLRQ-------MKEQNKKVA--NIKHGQQEMKKKGA---QLLEEARRREDNLADNSQQLQLE----- 658
|
730
....*....|....*..
gi 1907160229 897 caELEEALQKTRIELRS 913
Cdd:pfam10174 659 --ELMGALEKTRQELDA 673
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
458-905 |
2.88e-08 |
|
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: 58.98 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 458 LEEQLEKISHQdhsdksrLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAAR-------AALESQLR 530
Cdd:pfam15921 76 IERVLEEYSHQ-------VKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRrresqsqEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 531 QAKTELEETTAEAEEEIQALTAHRDEIQRKF----DALRNSCTVITDLEEQ--------------------------LNQ 580
Cdd:pfam15921 149 NTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlsheGVLQEIRSILVDFEEAsgkkiyehdsmstmhfrslgsaiskiLRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 581 LTEDNAELNNQNFYLSKQLD--EASGANDEIVQLRSEVDHLRREITEREMQLT-------SQKQTMEALKTTCTMLEEQV 651
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEalKSESQNKIELLLQQHQDRIEQLISEHEVEITgltekasSARSQANSIQSQLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 652 LDLEALN-DELLEKERQWEAWRSVLGDEKSQFECRVRELQRML---DTE-KQSRARADQRITES----RQVVELAVKEHK 722
Cdd:pfam15921 309 RNQNSMYmRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlaNSElTEARTERDQFSQESgnldDQLQKLLADLHK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 723 AEilaLQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQ-QKLETerELKQRLLEEQAKLQQQMdlqknhifRLTQG 801
Cdd:pfam15921 389 RE---KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEvQRLEA--LLKAMKSECQGQMERQM--------AAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 802 LQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQakmdqpaKKKKGLFSRRKEDPALPTQVPL 881
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ-------EKERAIEATNAEITKLRSRVDL 528
|
490 500
....*....|....*....|....*.
gi 1907160229 882 QYNELK-LALEKEKARCAELE-EALQ 905
Cdd:pfam15921 529 KLQELQhLKNEGDHLRNVQTEcEALK 554
|
|
| C1_KSR |
cd20812 |
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ... |
986-1037 |
3.11e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410362 Cd Length: 48 Bit Score: 51.17 E-value: 3.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 986 IPHRFNVGLNMRATkCAVCLDTVHFGRqasKCLECQVMCHPKCSTCLPATCG 1037
Cdd:cd20812 1 IKHRFSKKLFMRQT-CDYCHKQMFFGL---KCKDCKYKCHKKCAKKAPPSCG 48
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
4-858 |
3.64e-08 |
|
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: 58.52 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 4 KLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLS---QKEVELKASETQRSLLEQDlatyitecsslKRSLEQARM 80
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSkimKLDNEIKALKSRKKQMEKD-----------NSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 81 EVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEM---RLMMNQLEEDLVSARRRSDLyESELRESRLAAEEFKRKA 157
Cdd:TIGR00606 294 KVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLnkeRRLLNQEKTELLVEQGRLQL-QADRHQEHIRARDSLIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 158 NECQHKLMKVvshpPRGDSGGTALDDLHKMqghagltsakdQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTE 237
Cdd:TIGR00606 373 LATRLELDGF----ERGPFSERQIKNFHTL-----------VIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 238 ATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQI---QQM 314
Cdd:TIGR00606 438 LGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKAdldRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 315 ADKILELEEKHREAQVSAQHLEVHLKQ----------KEQHYEEKIKVL-DNQIKKDLADK-ESLENMMQRHEEEAHEKG 382
Cdd:TIGR00606 518 RKLDQEMEQLNHHTTTRTQMEMLTKDKmdkdeqirkiKSRHSDELTSLLgYFPNKKQLEDWlHSKSKEINQTRDRLAKLN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 383 KILSEQKAMINAMDSKIRSLEQRIVELSEaNKLAANSSLFTQRNMKAQEEMISELRQQKFYLetqAGKLEAQNRKLEEQL 462
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYED-KLFDVCGSQDEESDLERLKEEIEKSSKQRAML---AGATAVYSQFITQLT 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 463 EK------ISHQDHSDKSRLLE----LETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALEsQLRQA 532
Cdd:TIGR00606 674 DEnqsccpVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNK 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 533 KTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITdLEEQLNQLTEDN--------AELNNQNFYLSKQL--DEA 602
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVerkiaqqaAKLQGSDLDRTVQQvnQEK 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 603 SGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQ- 681
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQd 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 682 ------FECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAES----LSDKLNDLEK 751
Cdd:TIGR00606 912 spletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntVNAQLEECEK 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 752 KHAMLEMNARSLQQKLETEReLKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQE-ALDRADLLKTERSDLEYQLENIQvly 830
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQK-IQERWLQDNLTLRKRENELKEVEEELKQHLKEmGQMQVLQMKQEHQKLEENIDLIK--- 1067
|
890 900
....*....|....*....|....*...
gi 1907160229 831 sHEKVKMEGTISQQTKLIDFLQAKMDQP 858
Cdd:TIGR00606 1068 -RNHVLALGRQKGYEKEIKHFKKELREP 1094
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
415-667 |
3.73e-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: 57.47 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 415 LAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIShqdhsdkSRLLELETRLREVslehEEQK 494
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-------RRIAALARRIRAL----EQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 495 LELKRQLTELQLSLQERESQLTALqaaRAALESQLRQAKTELEETTAeaeeeiqALTAHRDEIQRKFDALRNSCTVITDL 574
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQ---KEELAELLRALYRLGRQPPL-------ALLLSPEDFLDAVRRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 575 EEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEvdhLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDL 654
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|...
gi 1907160229 655 EALNDELLEKERQ 667
Cdd:COG4942 226 EALIARLEAEAAA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
8-343 |
3.87e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.21 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 8 KSKELQDSQDKCHKMEQEMTRlhrrvseveavlSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDD 87
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLR------------QEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 88 kalqlLHDIREQSRK--LQEIKEQEYQAQVEEMR-LMMNQLEEDLVSARRRSDLYESelRESRLAAEEFKRKANECQHKL 164
Cdd:pfam17380 350 -----LERIRQEERKreLERIRQEEIAMEISRMReLERLQMERQQKNERVRQELEAA--RKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 165 MKVvshppRGDSGGTALDDLHKMQGHAG--LTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELL 242
Cdd:pfam17380 423 EQI-----RAEQEEARQREVRRLEEERAreMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 243 QniRQAKERAERELEKLHNR---EDSSEGIKKKLVEAEERRHSLENKVKRLETMERREnrlkddIQtksEQIQQMADKIL 319
Cdd:pfam17380 498 E--KELEERKQAMIEEERKRkllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRR------IQ---EQMRKATEERS 566
|
330 340
....*....|....*....|....
gi 1907160229 320 ELEEKHREAQVSAQHLEVHLKQKE 343
Cdd:pfam17380 567 RLEAMEREREMMRQIVESEKARAE 590
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1-529 |
4.07e-08 |
|
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: 58.19 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1 MEKKLLIKSKELQDSQDKCHKMEQEM----TRLHRRVSEVEAV--------------LSQKEV---ELKASETQRSLLEQ 59
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELedikMSLQRSMSTQKALeedlqiatkticqlTEEKEAqmeELNKAKAAHSFVVT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 60 DLATYITECSSLKRSlEQARMEVSQEDDKALQLlhDIREQSRKLQEIKEQEYQAQVEemrlmmnqLEE-DLVSARRRSDL 138
Cdd:pfam05483 353 EFEATTCSLEELLRT-EQQRLEKNEDQLKIITM--ELQKKSSELEEMTKFKNNKEVE--------LEElKKILAEDEKLL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 139 YESELRESrlAAEEFKRKANECQHKLMkvvshpprgdsggTALDDLHKMQGHAGLTSAKDQgkpevgEYSKlekinaeqq 218
Cdd:pfam05483 422 DEKKQFEK--IAEELKGKEQELIFLLQ-------------AREKEIHDLEIQLTAIKTSEE------HYLK--------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 219 lKIQELQEKLEKAVKASTEATE-----LLQNIRQAKERAERELEKLHNREDSSEGIKKKlveaeerrhslENKVKRLETM 293
Cdd:pfam05483 472 -EVEDLKTELEKEKLKNIELTAhcdklLLENKELTQEASDMTLELKKHQEDIINCKKQE-----------ERMLKQIENL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 294 ERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIkvldNQIKKDLADKEslENMMQR 373
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKN--KNIEEL 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 374 HEEEAHEKGKILSEQKAMiNAMDSKIRSLEQrivelseanKLAANSSLFTQRNMKAQEEM-ISELRQQKFYLETQAGKLE 452
Cdd:pfam05483 614 HQENKALKKKGSAENKQL-NAYEIKVNKLEL---------ELASAKQKFEEIIDNYQKEIeDKKISEEKLLEEVEKAKAI 683
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 453 AQNR-KLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQ-ERESQLTALQAARAALESQL 529
Cdd:pfam05483 684 ADEAvKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKaALEIELSNIKAELLSLKKQL 762
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
557-789 |
5.42e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 557 IQRKFDALRNSctvITDLEEQLNQLTE--DNAELNNQNFYLSKQL----DEASGANDEIVQLRSEVDHLRREITEREMQL 630
Cdd:COG3206 166 LELRREEARKA---LEFLEEQLPELRKelEEAEAALEEFRQKNGLvdlsEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 631 TSQKQTMEALKTTCTMLEEQVLdLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTEKQSRARADQRITES 710
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPD----VIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 711 RQVvelAVKEHKAEILALQQALKEQKLKAESLSDKLNDLekkhamlemnaRSLQQKLETERELKQRLLE--EQAKLQQQM 788
Cdd:COG3206 318 LEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL-----------RRLEREVEVARELYESLLQrlEEARLAEAL 383
|
.
gi 1907160229 789 D 789
Cdd:COG3206 384 T 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
555-834 |
5.93e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 555 DEIQRKFDALRNSCTVITDLEEQLNQLTEdnaelnnqnfyLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLtsQK 634
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 635 QTMEALKTTCTMLEEQVLDLEALNDELLEKERQWE-AWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRItesrQV 713
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL----AA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 714 VELAVKEHKAEILALQQALKEQKLKAESLSDKlndlekkhamlemnarsLQQKLETERELKQRLLEEQAKLQQQMDLQKN 793
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEA-----------------LEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907160229 794 HIFRLTQGLQEALDR-ADLLKTERSDLEYQLENIQVLYSHEK 834
Cdd:COG4913 434 RKSNIPARLLALRDAlAEALGLDEAELPFVGELIEVRPEEER 475
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
482-808 |
6.30e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 482 RLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAkteleettAEAEEEIQALTAHRDEIQRKF 561
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA--------SDHLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 562 DALrnsctviTDLEEQLNQLTEDNAELNNQnfyLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALK 641
Cdd:COG3096 354 EDL-------EELTERLEEQEEVVEEAAEQ---LAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 642 TTCTMLEEQVLDLEALNDELLE-KERQWEAWRSVLGDE---------KSQFECRVRELQRMLDTEKQSRA--RADQRITE 709
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAfRAKEQQATEEVLELEqklsvadaaRRQFEKAYELVCKIAGEVERSQAwqTARELLRR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 710 SRQVVELAVKEH--KAEILALQQALKEQKlKAESLsdkLNDLEKKHA-------MLEMNARSLQQKLETERELKQRLLEE 780
Cdd:COG3096 504 YRSQQALAQRLQqlRAQLAELEQRLRQQQ-NAERL---LEEFCQRIGqqldaaeELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350
....*....|....*....|....*....|....
gi 1907160229 781 QAKLQQQMDLQKNHIFRLTQ------GLQEALDR 808
Cdd:COG3096 580 RSELRQQLEQLRARIKELAArapawlAAQDALER 613
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-406 |
7.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 3 KKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLAtyitecsslKRSLEQARMEV 82
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE---------LEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 83 SQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLM----------MNQLEEDLVSARRRSDLYESELRESRLAAEE 152
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 153 FKRKANECQHKLMK-------------------VVSHPPRGDSGGTALDDLHKMQ---------GHAGLTSAKDQGKPEV 204
Cdd:COG4717 225 LEEELEQLENELEAaaleerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLflvlgllalLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 205 GEYSKLEKINAEQQLKIQELQEKLEKAVKAS-TEATELLQNIRQAK------ERAERELEKLHNREDSSEGIKKKLVEAE 277
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQellreaEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 278 ErrhSLENKVKRLEtmerRENRLKDDIQTKSEQIQQMADKILELEEKHREAQvsaqhlevhLKQKEQHYEEKIKVLDNQI 357
Cdd:COG4717 385 E---ELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLEALDEEE---------LEEELEELEEELEELEEEL 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907160229 358 KKDLADKESLENMMQRHEEEahekgKILSEQKAMINAMDSKIRSLEQRI 406
Cdd:COG4717 449 EELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEW 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-533 |
7.53e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 339 LKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELS---EANKL 415
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaelEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 416 AANSSLFTQRNMKAQEEMISELRQQKFY-LETQAGKLEAQNRKLEEQLEKIshqdHSDKSRLLELETRLREVSLEHEEQK 494
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLdAVRRLQYLKYLAPARREQAEEL----RADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907160229 495 LELKRQLTELQLSLQERESQLTALQAARAALESQLRQAK 533
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
1069-1188 |
8.63e-08 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 51.79 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1069 LHLEGWMKVPRNNKRGqqGWDRKYIVLEGSKVLIYDNEAREAGQRPVeefelclpdGDVSIHGAVgASELANTAKADVPY 1148
Cdd:pfam00169 1 VVKEGWLLKKGGGKKK--SWKKRYFVLFDGSLLYYKDDKSGKSKEPK---------GSISLSGCE-VVEVVASDSPKRKF 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907160229 1149 ILKMESHPHTtcwPGRTLYLLAPSFPDKQRWVTALESVVA 1188
Cdd:pfam00169 69 CFELRTGERT---GKRTYLLQAESEEERKDWIKAIQSAIR 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
708-919 |
8.89e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 708 TESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQ 787
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 788 MDLQKNHIFRLTQGLQ------------------EALDRADLLKTERSDLEYQLENIQvlysHEKVKMEGTISQQTKLID 849
Cdd:COG4942 99 LEAQKEELAELLRALYrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 850 FLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAA 919
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
208-788 |
9.16e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 208 SKLEKINAEQQLKIQELQEKL---EKAVKASTEATELLQNirQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLE 284
Cdd:pfam12128 290 QLLRTLDDQWKEKRDELNGELsaaDAAVAKDRSELEALED--QHGAFLDADIETAAADQEQLPSWQSELENLEERLKALT 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 285 NKVKRLE-TMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSA-QHLEVHLKQKEQHYEEKIKVLDNQIKKDLA 362
Cdd:pfam12128 368 GKHQDVTaKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 363 DKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKF 442
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 443 YLETQAGKLEAQNRKlEEQLEKISHQDHSDKSRLL--ELETRLREVSLEHEEQ----KLELKR----QLTELQLSLQERE 512
Cdd:pfam12128 528 QLFPQAGTLLHFLRK-EAPDWEQSIGKVISPELLHrtDLDPEVWDGSVGGELNlygvKLDLKRidvpEWAASEEELRERL 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 513 SQL-TALQAAR---AALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITD--------LEEQLNQ 580
Cdd:pfam12128 607 DKAeEALQSARekqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKalaerkdsANERLNS 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 581 L-TEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVdhlrreITEREMQLTSQKQTMEALKTTctmLEEQVLDLEALND 659
Cdd:pfam12128 687 LeAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV------EGALDAQLALLKAAIAARRSG---AKAELKALETWYK 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 660 ELLEKerqweawRSVLGDEKSQFECRVRELQRMLDTEKQSRaradQRITESRQVVELAVKEHKaeilalqQALKEQKLKA 739
Cdd:pfam12128 758 RDLAS-------LGVDPDVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQETWLQRR-------PRLATQLSNI 819
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 740 ESlsdKLNDLEKKHAMLEMNARSLQQKLETER----ELKQRLLEEQAKLQQQM 788
Cdd:pfam12128 820 ER---AISELQQQLARLIADTKLRRAKLEMERkaseKQQVRLSENLRGLRCEM 869
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
207-914 |
1.06e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 207 YSKLEKINAEQQL---------KIQELQEKLEKAVKASTEATELLQNIRQAKERAER------EL-EKLHNREDSSEGIK 270
Cdd:COG3096 295 FGARRQLAEEQYRlvemareleELSARESDLEQDYQAASDHLNLVQTALRQQEKIERyqedleELtERLEEQEEVVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 271 KKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQM------ADKILELEEKHREAqvSAQHLEVHLKQKEQ 344
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAvqalekARALCGLPDLTPEN--AEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 345 HYEEkikVLDNQIKKDLAD--KESLENMMQRHE--------EEAHEKGKIL----SEQKAMI---NAMDSKIRSLEQRIV 407
Cdd:COG3096 453 ATEE---VLELEQKLSVADaaRRQFEKAYELVCkiageverSQAWQTARELlrryRSQQALAqrlQQLRAQLAELEQRLR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 408 ELSEANKLAANSSLFTQRNMKAQ---EEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSR---LLELET 481
Cdd:COG3096 530 QQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapaWLAAQD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 482 RLREVSlEHEEQKLELKRQLTELQLSLQERESQLTA----LQAARAALESQLRQAKTELEETTAEAEEEIQALTAH---- 553
Cdd:COG3096 610 ALERLR-EQSGEALADSQEVTAAMQQLLEREREATVerdeLAARKQALESQIERLSQPGGAEDPRLLALAERLGGVllse 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 554 -RDEIQRK----FDAL----RNScTVITDLE---EQLNQLT---------EDNAELNNQNFYLSKQLDEASGANDEIVQL 612
Cdd:COG3096 689 iYDDVTLEdapyFSALygpaRHA-IVVPDLSavkEQLAGLEdcpedlyliEGDPDSFDDSVFDAEELEDAVVVKLSDRQW 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 613 R----------------SEVDHLRRE---ITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDEllekerqwEAWRS 673
Cdd:COG3096 768 RysrfpevplfgraareKRLEELRAErdeLAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDP--------EAELA 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 674 VLGDEKSQFEcrvRELQRMLDTEKQSRARADQ---RITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLE 750
Cdd:COG3096 840 ALRQRRSELE---RELAQHRAQEQQLRQQLDQlkeQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQHG 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 751 KKHAMLEMNARSLQQKLETERELKQRLLEeqakLQQQMDLQKNHIFRLTQGLQ--EAL---DRADLLkTERSD----LEY 821
Cdd:COG3096 917 KALAQLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrPHFsyeDAVGLL-GENSDlnekLRA 991
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 822 QLENIQVLYSHEKVKMEGtisQQTKLIDFLQAKMDQPAK---KKKGLFSRRKEDPALPTQVP--------LQYNELKLAL 890
Cdd:COG3096 992 RLEQAEEARREAREQLRQ---AQAQYSQYNQVLASLKSSrdaKQQTLQELEQELEELGVQADaeaeerarIRRDELHEEL 1068
|
810 820
....*....|....*....|....
gi 1907160229 891 EKEKARCAELEEALQKTRIELRSA 914
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-614 |
1.16e-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: 57.11 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKelQDSQDKCHKMEQEMTRLHRRVSEVEAV-------LSQKEVELKASETQRSLLEQDLATYITECSSLKRS 74
Cdd:pfam01576 392 ELRTLQQAK--QDSEHKRKKLEGQLQELQARLSESERQraelaekLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 75 LEQARMEVSQEDDKALQLLHDIR---EQSRKLQEIKEQEYQA--------------------QVEEMRLMMNQLEEDLVS 131
Cdd:pfam01576 470 LQDTQELLQEETRQKLNLSTRLRqleDERNSLQEQLEEEEEAkrnverqlstlqaqlsdmkkKLEEDAGTLEALEEGKKR 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 132 ARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHPPRGDSGGTALDDLHK----MQGHAGLTSAKDQGKPEVGEY 207
Cdd:pfam01576 550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEKAISARYAEERDRAEA 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 208 SKLEKINAEQQL-----KIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNR-EDSSEGIKKKLVEAEERRH 281
Cdd:pfam01576 630 EAREKETRALSLaraleEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRAlEQQVEEMKTQLEELEDELQ 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 282 SLENKVKRLE-TMERRENRLKDDIQTKSEQ--------IQQMADKILELEE--KHREAQVSA-QHLEVHLKQKEQHYEEK 349
Cdd:pfam01576 710 ATEDAKLRLEvNMQALKAQFERDLQARDEQgeekrrqlVKQVRELEAELEDerKQRAQAVAAkKKLELDLKELEAQIDAA 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 350 IKVLDNQIKKdLADKESLENMMQRHEEEAHekgkiLSEQKAMINAMDS--KIRSLEQRIVELSEanKLAANSSLFTQRNM 427
Cdd:pfam01576 790 NKGREEAVKQ-LKKLQAQMKDLQRELEEAR-----ASRDEILAQSKESekKLKNLEAELLQLQE--DLAASERARRQAQQ 861
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 428 ---KAQEEMI------SELRQQKFYLETQAGKLEAQNRklEEQLEKISHQDHSDKSRLL--ELETRL---REVSLEHEEQ 493
Cdd:pfam01576 862 erdELADEIAsgasgkSALQDEKRRLEARIAQLEEELE--EEQSNTELLNDRLRKSTLQveQLTTELaaeRSTSQKSESA 939
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 494 KLELKRQLTELQLSLQERESQ--------LTALQAARAALESQLRQ--------AKTELEETTAEAEEEIQALTAHRDEI 557
Cdd:pfam01576 940 RQQLERQNKELKAKLQEMEGTvkskfkssIAALEAKIAQLEEQLEQesrerqaaNKLVRRTEKKLKEVLLQVEDERRHAD 1019
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 558 QRKfDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAND----EIVQLRS 614
Cdd:pfam01576 1020 QYK-DQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNEsmnrEVSTLKS 1079
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
549-918 |
1.30e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 549 ALTAHRDEIQRKFDAlrNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREM 628
Cdd:PRK02224 188 SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 629 QLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQS--------- 699
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAaqahneeae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 700 --RARADQRITESRQVVELAvKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRL 777
Cdd:PRK02224 346 slREDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 778 LEEQAKLQQQMDLQKNHIfRLTQGLQEA---------------LDRADLLKTERSDLEYQLENIQVlyshEKVKMEGTIS 842
Cdd:PRK02224 425 REREAELEATLRTARERV-EEAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEE----EVEEVEERLE 499
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 843 QQTKLIDfLQAKMDQPAKKKKGLFSRRKEDPAlptqvplQYNELKLALEKEKARCAELEEALQKTRIELRSAREEA 918
Cdd:PRK02224 500 RAEDLVE-AEDRIERLEERREDLEELIAERRE-------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
302-532 |
1.66e-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: 55.54 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 302 DDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQhyeeKIKVLDNQIKKDLADKESLENMMQRHEEEAHEK 381
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 382 GKILSEQKAMinamdskirsLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQ 461
Cdd:COG4942 96 RAELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 462 LEKISHQdhsdKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQA 532
Cdd:COG4942 166 RAELEAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
356-825 |
2.00e-07 |
|
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: 55.90 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 356 QIKKDLADKEsLENMMQRHEEE--AHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKlaansslftqrnmkaqeEM 433
Cdd:pfam05557 13 QLQNEKKQME-LEHKRARIELEkkASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR-----------------EQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 434 ISELRQQKFYLETQAGKLEAQnrklEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLE---LKRQLTELQLSLQE 510
Cdd:pfam05557 75 AELNRLKKKYLEALNKKLNEK----ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSEleeLQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 511 RE---SQLTALQAARAALESQLR--QAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRnsctvitDLEEQLNQLTEDN 585
Cdd:pfam05557 151 AEqlrQNLEKQQSSLAEAEQRIKelEFEIQSQEQDSEIVKNSKSELARIPELEKELERLR-------EHNKHLNENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 586 AELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTM---EALKTTCTMLEEQVLDLEALNDELL 662
Cdd:pfam05557 224 LLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 663 EKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRI---TESRQVVELAVKEHKAEiLALQQALKEQKLKA 739
Cdd:pfam05557 304 SSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVlllTKERDGYRAILESYDKE-LTMSNYSPQLLERI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 740 ESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQ-----KNHIFRLTQGLQEALDRADLLKT 814
Cdd:pfam05557 383 EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAdpsysKEEVDSLRRKLETLELERQRLRE 462
|
490
....*....|.
gi 1907160229 815 ERSDLEYQLEN 825
Cdd:pfam05557 463 QKNELEMELER 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
602-864 |
2.21e-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: 55.16 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 602 ASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTtctmleeqvlDLEALNDELLEKERQweawrsvlgdeksq 681
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----------QLAALERRIAALARR-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 682 fecrVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNAR 761
Cdd:COG4942 71 ----IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 762 SLQQKLETERELKQRLLEEQAKLQQQMDLQKnhifRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTI 841
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|...
gi 1907160229 842 SQQTKLIDFLQAKMDQPAKKKKG 864
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPA 245
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
1069-1188 |
3.25e-07 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 50.24 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1069 LHLEGWMKVPRNNKRGqqGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELClpdgDVSIhgavgaSELANTAKADVPY 1148
Cdd:smart00233 1 VIKEGWLYKKSGGGKK--SWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLS----GCTV------REAPDPDSSKKPH 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907160229 1149 ILKMeshphtTCWPGRTLYLLAPSFPDKQRWVTALESVVA 1188
Cdd:smart00233 69 CFEI------KTSDRKTLLLQAESEEEREKWVEALRKAIA 102
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
246-627 |
3.79e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 246 RQAKERAERELEKLHNREDSSeGIKKKLVEAEERrhsLENKVKRLETMERRENRLKDDIQTKS-------------EQIQ 312
Cdd:PRK04863 276 RHANERRVHLEEALELRRELY-TSRRQLAAEQYR---LVEMARELAELNEAESDLEQDYQAASdhlnlvqtalrqqEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 313 QMADKILELEEK-------HREAQVSAQHLEVHLKQKEQHYEEkikvldnqIKKDLADKESLENMMQRHEEEAHEKGKIL 385
Cdd:PRK04863 352 RYQADLEELEERleeqnevVEEADEQQEENEARAEAAEEEVDE--------LKSQLADYQQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 386 SEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQN-----RKLEE 460
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEawdvaRELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 461 QLEKISHQDhsdkSRLLELETRLREVSLEHEEQKlELKRQLTELQLSLQ---ERESQLTALQAARAALESQLRQAKTELE 537
Cdd:PRK04863 504 RLREQRHLA----EQLQQLRMRLSELEQRLRQQQ-RAERLLAEFCKRLGknlDDEDELEQLQEELEARLESLSESVSEAR 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 538 ETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVD 617
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
410
....*....|
gi 1907160229 618 HLRREITERE 627
Cdd:PRK04863 659 EEIERLSQPG 668
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-515 |
3.93e-07 |
|
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: 55.36 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 7 IKSKELQDSQdKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQ---RSLLEQDLATYITECSSLKRSLEQARMEVS 83
Cdd:TIGR00618 370 ISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsaFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 84 QEDDKALQLLHDIREQSRKLQEIKEQEYQAQ-----------VEEMRLMMNQLEEDLVSAR------RRSDLYESELRES 146
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQLQTKEqihlqetrkkaVVLARLLELQEEPCPLCGScihpnpARQDIDNPGPLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 147 RLAAEEFKRKANE-----CQHKLMKVVSHPPRGDSGGTALDD--LHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQL 219
Cdd:TIGR00618 529 RMQRGEQTYAQLEtseedVYHQLTSERKQRASLKEQMQEIQQsfSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 220 KIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHnredsseGIKKKLVEAEERRHSLENKVKRLETMERRENR 299
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH-------ALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 300 LkDDIQTKSEQIQQMADKILELEEKHREaqvsaqhLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAH 379
Cdd:TIGR00618 682 L-QKMQSEKEQLTYWKEMLAQCQTLLRE-------LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 380 EKGKILSEQKAMINamdSKIRSLEQRIVELSEAnklaansslftQRNMKAQEEMISELRQQKFYLETQAG-KLEAQNRKL 458
Cdd:TIGR00618 754 TVLKARTEAHFNNN---EEVTAALQTGAELSHL-----------AAEIQFFNRLREEDTHLLKTLEAEIGqEIPSDEDIL 819
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 459 EEQLEKISHQDHSDKSRLLELETRLREVS--LEHEEQKLELKRQLTELQLSLQERESQL 515
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEIThqLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
219-368 |
6.44e-07 |
|
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: 52.23 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 219 LKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNRedsSEGIKKKLVEAEERRHSLENKVKRLET--MERR 296
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE---LEDLEKEIKRLELEIEEVEARIKKYEEqlGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 297 ENR----LKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLE 368
Cdd:COG1579 87 NNKeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
206-368 |
6.81e-07 |
|
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: 52.23 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 206 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEgikKKLVEAeerrhsleN 285
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLGNV--------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 286 KVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKE 365
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
...
gi 1907160229 366 SLE 368
Cdd:COG1579 167 ELA 169
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-827 |
6.85e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 298 NRLKDDiqtKSEQIQQMADKILELEEKHREAQVSAqhlevhLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEE 377
Cdd:PRK02224 179 ERVLSD---QRGSLDQLKAQIEEKEEKDLHERLNG------LESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 378 AHEkgkilseqkaminamdskIRSLEQRIVELSEanKLAAnsslfTQRNMKAQEEMISELRQQKFYLETQagkleaqnrk 457
Cdd:PRK02224 250 REE------------------LETLEAEIEDLRE--TIAE-----TEREREELAEEVRDLRERLEELEEE---------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 458 LEEQLEKISHQDHSDKSRLLELEtrlrevslEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELE 537
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARRE--------ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 538 ETTaeaeeeiqaltahrDEIQRKFDALRNSCTVITDLEEQLNQLTE--DNAELnnqnfylskQLDEASGANDEivqLRSE 615
Cdd:PRK02224 367 ELE--------------SELEEAREAVEDRREEIEELEEEIEELRErfGDAPV---------DLGNAEDFLEE---LREE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 616 VDHLRreitEREMQLTSQKQTMEalkttcTMLEEqvldlealNDELLEKERQWEAWRSVLG----DEKSQFECRVRELQR 691
Cdd:PRK02224 421 RDELR----EREAELEATLRTAR------ERVEE--------AEALLEAGKCPECGQPVEGsphvETIEEDRERVEELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 692 MLDTEKQSRARADQRITESRQVVELAVK----EHKAEilALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKL 767
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLVEAEDRierlEERRE--DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 768 ETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQgLQEALDRADLLKTERSDLEYQLENIQ 827
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALA 619
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-587 |
7.66e-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: 53.23 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 362 ADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLaansslfTQRNMKAQEEMISELRQQK 441
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 442 FYLETQAGKLEAQNRKLEEQLEKISHQDH-------SDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQ 514
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 515 LTALQAARAALESQlrqaKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAE 587
Cdd:COG4942 173 RAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
373-801 |
8.39e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 373 RHEEEAHEK-GKILSEQKAMINAMDsKIRSLEQRIVELS-EANKLAANSSLFTQRNMKAQEE---MISELRQQKfYLETQ 447
Cdd:COG3096 275 RHANERRELsERALELRRELFGARR-QLAEEQYRLVEMArELEELSARESDLEQDYQAASDHlnlVQTALRQQE-KIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 448 AGKLEAQNRKLEEQLEKISHQDhsdkSRLLELETRLREVSLEHEEqkleLKRQLTELQLSLQERESQLTALQAARAALEs 527
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAA----EQLAEAEARLEAAEEEVDS----LKSQLADYQQALDVQQTRAIQYQQAVQALE- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 528 qlrQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRnsctvitDLEEQLNqLTEDNAELNNQNFYLSKQLD---EASG 604
Cdd:COG3096 424 ---KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVL-------ELEQKLS-VADAARRQFEKAYELVCKIAgevERSQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 605 ANDEIVQLRSE----------VDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEkerqWEAWRSV 674
Cdd:COG3096 493 AWQTARELLRRyrsqqalaqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE----LEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 675 LGDEKSQFECRVRELQRmldTEKQSRARADqritesrqvvELAVKEhkAEILALQQALkeqklkaESLSDKLND-LEKKH 753
Cdd:COG3096 569 LEEQAAEAVEQRSELRQ---QLEQLRARIK----------ELAARA--PAWLAAQDAL-------ERLREQSGEaLADSQ 626
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 754 AMleMNARslQQKLETERELKQ---RLLEEQAKLQQQmdlqknhIFRLTQG 801
Cdd:COG3096 627 EV--TAAM--QQLLEREREATVerdELAARKQALESQ-------IERLSQP 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
571-793 |
8.80e-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: 53.23 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 571 ITDLEEQLNQLTEDNAELNNQnfyLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQ 650
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKE---LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 651 vldLEALNDELleKERQWEAWRS---------VLGDEKSQFECRVRELQRMLdtekQSRARADQRITESRQVVELAVKEH 721
Cdd:COG4942 99 ---LEAQKEEL--AELLRALYRLgrqpplallLSPEDFLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 722 KAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKN 793
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
548-768 |
8.88e-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: 53.23 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 548 QALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLDEA----SGANDEIVQLRSEVDHLRREI 623
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQE---IAELEKELAALKKEEKALLKQLAALERRIAALarriRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 624 TEREMQLTSQKQTM-EALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTEKQSRar 702
Cdd:COG4942 93 AELRAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLAELAALR-- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 703 adQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLE 768
Cdd:COG4942 167 --AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
492-754 |
1.33e-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: 52.46 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 492 EQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeeeiQALTAHRDEIQrkfdalrnsctvi 571
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE--------------RRIAALARRIR------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 572 tDLEEQLNQLTEDNAELNNQnfylskqldeasgandeIVQLRSEVDHLRREITE--REMQLTSQKQTMEALKTTCTMLE- 648
Cdd:COG4942 73 -ALEQELAALEAELAELEKE-----------------IAELRAELEAQKEELAEllRALYRLGRQPPLALLLSPEDFLDa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 649 -EQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVvelaVKEHKAEILA 727
Cdd:COG4942 135 vRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL----LARLEKELAE 210
|
250 260
....*....|....*....|....*..
gi 1907160229 728 LQQALKEQKLKAESLSDKLNDLEKKHA 754
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-639 |
1.83e-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: 52.07 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 424 QRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTE 503
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 504 LQLSLQERE-----SQLTALQAARAA--LESQLRQAKTELEETTaeaeEEIQALTAHRDEIQRKFDALRnscTVITDLEE 576
Cdd:COG4942 113 LYRLGRQPPlalllSPEDFLDAVRRLqyLKYLAPARREQAEELR----ADLAELAALRAELEAERAELE---ALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 577 QLNQLTEDNAELNNQNFYLSKQLDEASganDEIVQLRSEVDHLRREITEREMQLTSQKQTMEA 639
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
699-976 |
1.90e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 699 SRARADQRITESRQvvelAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLET-ERELKQR- 776
Cdd:COG3883 10 TPAFADPQIQAKQK----ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 777 -LLEEQAKLQQQMDLQKNHIFRLT--QGLQEALDRADLLKTErsdleyqleniqvlyshekvkmegtISQQTKLIDFLQA 853
Cdd:COG3883 86 eELGERARALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKI-------------------------ADADADLLEELKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 854 KMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPA 933
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907160229 934 TARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSR 976
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
|
| C1_1 |
pfam00130 |
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
983-1038 |
1.97e-06 |
|
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.
Pssm-ID: 395079 Cd Length: 53 Bit Score: 46.28 E-value: 1.97e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907160229 983 HHNIPHRFNvglnmRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCGL 1038
Cdd:pfam00130 1 HHFVHRNFK-----QPTFCDHCGEFLwGLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
30-439 |
2.56e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 30 HRRVSEVEAVLSQKEVELKASETQRSLLEqDLATYITECSSLKRSLEQARMEVsQEDDKALQLLHDIREQSRKLQEIKEQ 109
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRYDDLNNQIL-ELEGYEMDYNSYLKSIESLKKKI-EEYSKNIERMSAFISEILKIQEIDPD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 110 EYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESR------------------LAAEEFKRKANECQHKLMKVVSHP 171
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSrnmemlngqsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 172 PRGDSGGTALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAE---QQLKIQELQEKLEKAVKASTEATEL-LQNIRQ 247
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADledIKIKINELKDKHDKYEEIKNRYKSLkLEDLDS 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 248 AKER-----AERELEKLHNREDSSEGIKKKLVEAEERRHSLE-----------NKVKRLETMERRENRLKDDIQTKSEQI 311
Cdd:PRK01156 566 KRTSwlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEigfpddksyidKSIREIENEANNLNNKYNEIQENKILI 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 312 QQMADKILELEE---KHREAQVSAQHLEVHLKQKEQHYEEKIKVLDnQIKKDLADKESLENMMQRHEEEahekgkiLSEQ 388
Cdd:PRK01156 646 EKLRGKIDNYKKqiaEIDSIIPDLKEITSRINDIEDNLKKSRKALD-DAKANRARLESTIEILRTRINE-------LSDR 717
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 389 KAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQ 439
Cdd:PRK01156 718 INDINETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRK 768
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
88-812 |
3.16e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 88 KALQLLHDIRE-QSRKLQEIKE-----QEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELresrlaaEEFKRKANECQ 161
Cdd:TIGR00606 186 KALETLRQVRQtQGQKVQEHQMelkylKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL-------DPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 162 HKLMKVVShpprgdsggtaLDDlhkmqghagltsakdqgkpevgEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATEL 241
Cdd:TIGR00606 259 HNLSKIMK-----------LDN----------------------EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 242 LQNIRQAKERA--------ERELEKLhNREDSSEGIKKKLVEAEERRHSLenKVKRLETMERRENRLKDDIQTKSE---- 309
Cdd:TIGR00606 306 LYHNHQRTVREkerelvdcQRELEKL-NKERRLLNQEKTELLVEQGRLQL--QADRHQEHIRARDSLIQSLATRLEldgf 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 310 ----------------QIQQMADK-------ILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLD---NQIKKDLAD 363
Cdd:TIGR00606 383 ergpfserqiknfhtlVIERQEDEaktaaqlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEkkqEELKFVIKE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 364 KESLENMMQRHEEEAHEKGKILSE-QKAMINA------------------MDSKIRSLEQRIVELSEANKLAANSSLFTQ 424
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERElSKAEKNSltetlkkevkslqnekadLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 425 RNMKAQEEMISELRQQKFYLETQAGKLeAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRqLTEL 504
Cdd:TIGR00606 543 DKMDKDEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELES-KEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 505 QLSLQERESQLTALQAARAALES---QLRQAKTELEETTAEAEEEIQALTAHRDE-------IQRKFDALRNSCTVITDL 574
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESDLERlkeEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 575 EEQLNQLTEDNAELNNQNFYLSKQLDEASGandeIVQLR-SEVDHLRREITEREMQLTSQKQTMEALKTTctmLEEQVLD 653
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLG----LAPGRqSIIDLKEKEIPELRNKLQKVNRDIQRLKND---IEEQETL 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 654 LEALNDELLEKErqwEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVElaVKEHK-----AEILAL 728
Cdd:TIGR00606 774 LGTIMPEEESAK---VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ--EKQHEldtvvSKIELN 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 729 QQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERElkqrLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDR 808
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
....
gi 1907160229 809 ADLL 812
Cdd:TIGR00606 925 KEEL 928
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
615-921 |
3.21e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 615 EVDHLRREITEREmQLTSQKQTMEALKTTctMLEEQVLDLEALNDELLEKERQwEAWRSVLGDEKSQFECRVRELQRMLD 694
Cdd:pfam12128 229 DIQAIAGIMKIRP-EFTKLQQEFNTLESA--ELRLSHLHFGYKSDETLIASRQ-EERQETSAELNQLLRTLDDQWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 695 TEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETEREL- 773
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKi 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 774 KQRLLEEQAKLQQQMDLQKNHIFRltqglQEALDRADLLKTErSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQA 853
Cdd:pfam12128 385 KEQNNRDIAGIKDKLAKIREARDR-----QLAVAEDDLQALE-SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 854 kmdqpakkkkglfsrrkeDPALPTQVPLQYNELKLALEKEKARCAELEeALQKTRIELRSAREEAAHR 921
Cdd:pfam12128 459 ------------------TPELLLQLENFDERIERAREEQEAANAEVE-RLQSELRQARKRRDQASEA 507
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
382-809 |
5.16e-06 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 51.15 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 382 GKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQ 461
Cdd:COG5281 3 ALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 462 LEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQlslQERESQLTALQAARAALESQLRQAKTELEETTA 541
Cdd:COG5281 83 ALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAA---AAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 542 EAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRR 621
Cdd:COG5281 160 AAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 622 EITE--REMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfecRVRELQRMLDTEKQS 699
Cdd:COG5281 240 ASAAaqALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQA---LAAAAAAAAAQLAAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 700 RARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDlekkhAMLEMNARSLQQKLETERELKQRLLE 779
Cdd:COG5281 317 AAAAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALE-----AAAAAAAAELAAAGDWAAGAKAALAE 391
|
410 420 430
....*....|....*....|....*....|
gi 1907160229 780 EQAKLQQQMDLQKNHIFRLTQGLQEALDRA 809
Cdd:COG5281 392 YADSATNVAAQVAQAATSAFSGLTDALAGA 421
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
300-790 |
5.68e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 300 LKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKikvldNQikkDLADKESLEnmmqrheeEAH 379
Cdd:PRK10246 424 LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEK-----TQ---QLADVKTIC--------EQE 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 380 EKGKILSEQKAMINAMDS--KIRSLEQRIVELSEANKLAANsslftQRNMKAQEEMISELRQQKFYLEtqaGKLEAqnrk 457
Cdd:PRK10246 488 ARIKDLEAQRAQLQAGQPcpLCGSTSHPAVEAYQALEPGVN-----QSRLDALEKEVKKLGEEGAALR---GQLDA---- 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 458 LEEQLekisHQDHSDKSRLLELETRLRE----------VSL-------------EHEEQKLELKRQLTELQLSLQERESQ 514
Cdd:PRK10246 556 LTKQL----QRDESEAQSLRQEEQALTQqwqavcaslnITLqpqddiqpwldaqEEHERQLRLLSQRHELQGQIAAHNQQ 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 515 LTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRkfdaLRNSCTVITDLEEQLNQLTEDNAELnnqnfy 594
Cdd:PRK10246 632 IIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQS----WQQRQNELTALQNRIQQLTPLLETL------ 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 595 lsKQLDEASgANDEIVQLrsevDHLrREITEREMQLTSQKQTMEALkttctmleeqvldlealndELLEKERQWEA---W 671
Cdd:PRK10246 702 --PQSDDLP-HSEETVAL----DNW-RQVHEQCLSLHSQLQTLQQQ-------------------DVLEAQRLQKAqaqF 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 672 RSVLgdEKSQFECRVRELQRMLDTEkqsrarADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEK 751
Cdd:PRK10246 755 DTAL--QASVFDDQQAFLAALLDEE------TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQ 826
|
490 500 510
....*....|....*....|....*....|....*....
gi 1907160229 752 KHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDL 790
Cdd:PRK10246 827 IQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQAL 865
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
207-822 |
6.33e-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: 50.89 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 207 YSKLEKINAEQQLKIQELQEKLEKAvkasteatELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSlenK 286
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHKRARI--------ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE---Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 287 VKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLkqKEQHYEekikvldnqikkdladkes 366
Cdd:pfam05557 75 AELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL--QSTNSE------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 367 LENMMQRHEEEaHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTqRNMKAQEEMISElrqqkfyLET 446
Cdd:pfam05557 134 LEELQERLDLL-KAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIV-KNSKSELARIPE-------LEK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 447 QAGKLEAQNRKLEEQLEKIS---HQDHSDKSRLLELE-TRLREVSLEHEEQKLELKrqLTELQLSLQERESQLTALQAAR 522
Cdd:pfam05557 205 ELERLREHNKHLNENIENKLllkEEVEDLKRKLEREEkYREEAATLELEKEKLEQE--LQSWVKLAQDTGLNLRSPEDLS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 523 AALEsQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLDea 602
Cdd:pfam05557 283 RRIE-QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK---IEDLNKKLKRHKALVRRLQRRVLLLTKERD-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 603 sgandeivqlrsevdhLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELlekerqweawrsvlgdeksqf 682
Cdd:pfam05557 357 ----------------GYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM--------------------- 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 683 ECRVRELQRMLDTEKQSRARADQRITESRQVVELA-VKEHKAEILALQQALKEQKLKAESLSDKLNDLEkkhamLEMNAR 761
Cdd:pfam05557 400 EAQLSVAEEELGGYKQQAQTLERELQALRQQESLAdPSYSKEEVDSLRRKLETLELERQRLREQKNELE-----MELERR 474
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 762 SLQQKLETER------------ELKQRLLEEQAKLQQQMDLQKnhifRLTQGLQEALDRADLLKTERSDLEYQ 822
Cdd:pfam05557 475 CLQGDYDPKKtkvlhlsmnpaaEAYQQRKNQLEKLQAEIERLK----RLLKKLEDDLEQVLRLPETTSTMNFK 543
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
239-584 |
7.33e-06 |
|
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: 50.45 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 239 TELLQNIRQAKERAErELEKLHNRE-DSSEGIKKKLVEAEERRHSLENKVKRLET-MERRENRLKDDIQTKSEQIQQMAD 316
Cdd:pfam19220 37 EAILRELPQAKSRLL-ELEALLAQErAAYGKLRRELAGLTRRLSAAEGELEELVArLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 317 KILELEEKHREAQVSAQHLEvHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMD 396
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNR-ALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 397 SKIRSLEQRI------VELSEANKLAANSSlfTQRNMKAQEEMISELRQQKfylETQAGKLEAQNRKLE--EQLekishq 468
Cdd:pfam19220 195 RRLAELETQLdatrarLRALEGQLAAEQAE--RERAEAQLEEAVEAHRAER---ASLRMKLEALTARAAatEQL------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 469 dhsdksrLLELETRLRevslEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQ 548
Cdd:pfam19220 264 -------LAEARNQLR----DRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTK 332
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907160229 549 ALTAHRdeiqrkfDALRNSCTVITDLEEQLNQLTED 584
Cdd:pfam19220 333 ALAAKD-------AALERAEERIASLSDRIAELTKR 361
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
221-831 |
9.80e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 221 IQELQEKLEKavkasteatELLQNIRQAKERAERELEkLHNREDSSEGIKKKlVEAEERRHSLENKVKRLETMERRENRL 300
Cdd:COG5022 819 IIKLQKTIKR---------EKKLRETEEVEFSLKAEV-LIQKFGRSLKAKKR-FSLLKKETIYLQSAQRVELAERQLQEL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 301 KDDIqtksEQIQQMADKILELEEKHREAQVSAQHLEV-HLKQKEQHYEEKIKVLDN-QIKKDLA-DKESLENMMQRHEEE 377
Cdd:COG5022 888 KIDV----KSISSLKLVNLELESEIIELKKSLSSDLIeNLEFKTELIARLKKLLNNiDLEEGPSiEYVKLPELNKLHEVE 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 378 A--HEKGKILSeqkAMINAMDSKIRSLEQRIVELSEANKLAAnsslftqrnmkaqeemisELRQQKFYLETQAGKLEAQN 455
Cdd:COG5022 964 SklKETSEEYE---DLLKKSTILVREGNKANSELKNFKKELA------------------ELSKQYGALQESTKQLKELP 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 456 RKLEE--QLEKISHQDHSDKSRLLELEtrlrEVSLEHEEQKLELKRQLTELQLslqERESQLTalqaaraaLESQLRQAK 533
Cdd:COG5022 1023 VEVAElqSASKIISSESTELSILKPLQ----KLKGLLLLENNQLQARYKALKL---RRENSLL--------DDKQLYQLE 1087
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 534 TELEETTAEAEEEIQALTahrdeiqRKFDALRNSCTVITDLEEQLNqLTEDNAELNNQNFYLSKQLDEASGANDEIVQLR 613
Cdd:COG5022 1088 STENLLKTINVKDLEVTN-------RNLVKPANVLQFIVAQMIKLN-LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGL 1159
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 614 SEVDHLRREITEREMQLTSQKQTME--ALKTTCTMLEEQVLDLEalnDELLEKERQ-WEAWRSVLGDEKSQFECRVRELQ 690
Cdd:COG5022 1160 FWEANLEALPSPPPFAALSEKRLYQsaLYDEKSKLSSSEVNDLK---NELIALFSKiFSGWPRGDKLKKLISEGWVPTEY 1236
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 691 RMLDTEKQSRAR--ADQRITESRQVVELAVKehkaeilaLQQALKEQKLKAESLSDKLNDLEKKHAM-----LEMNARSL 763
Cdd:COG5022 1237 STSLKGFNNLNKkfDTPASMSNEKLLSLLNS--------IDNLLSSYKLEEEVLPATINSLLQYINVglfnaLRTKASSL 1308
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 764 QQKLETERELKQRLLEEQAKLQQQMDLQKNhifrltqgLQEALDRADLLKTERSDLEYQLENIQVLYS 831
Cdd:COG5022 1309 RWKSATEVNYNSEELDDWCREFEISDVDEE--------LEELIQAVKVLQLLKDDLNKLDELLDACYS 1368
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
70-783 |
9.92e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 70 SLKRSLEQARMEVSQEDDKALQLLHDIREQSRkLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESE--LRESR 147
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTerLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 148 LAAEEFKRKANECQHKLMKVVSHPPRGDSG----GTALDDLHK-----MQGHAGLTSAKDQ-GKPE-----VGEYskLEK 212
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyQQALDVQQTraiqyQQAVQALEKARALcGLPDltpenAEDY--LAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 213 INAEQQL---KIQELQEKLEKAVKASTE---ATELLQNIRQAKERAE---------RELEKLHNREDSSEGIKKKLVEAE 277
Cdd:COG3096 446 FRAKEQQateEVLELEQKLSVADAARRQfekAYELVCKIAGEVERSQawqtarellRRYRSQQALAQRLQQLRAQLAELE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 278 ERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEE--------- 348
Cdd:COG3096 526 QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawl 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 349 ----KIKVLDNQIKKDLADKESLENMMQ---RHEEEAHEKGKILSEQKAminAMDSKIRSLEQ-------RIVELSE--- 411
Cdd:COG3096 606 aaqdALERLREQSGEALADSQEVTAAMQqllEREREATVERDELAARKQ---ALESQIERLSQpggaedpRLLALAErlg 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 412 --------------------------------------ANKLAA-------------NSSLFTQRNMKAQEE-----MIS 435
Cdd:COG3096 683 gvllseiyddvtledapyfsalygparhaivvpdlsavKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKL 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 436 ELRQQKFYL------------ETQAGKLEAQNRKLEEQLEKIS------HQDHSDKSRLLEL----------ETRLREVS 487
Cdd:COG3096 763 SDRQWRYSRfpevplfgraarEKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGhlavafapdpEAELAALR 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 488 leheEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAkteLEETTAEAEEEIQALTAHRDEIQRKFDALRNS 567
Cdd:COG3096 843 ----QRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQA---NLLADETLADRLEELREELDAAQEAQAFIQQH 915
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 568 CTVITDLEEQLNQLTED---NAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITERemqltsqkqtmealkttc 644
Cdd:COG3096 916 GKALAQLEPLVAVLQSDpeqFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVG------------------ 977
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 645 tMLEEQvldlEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQvvELAVKEHKAE 724
Cdd:COG3096 978 -LLGEN----SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQ--ELEELGVQAD 1050
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 725 ILALQQALKE-QKLKAE--SLSDKLNDLEKKHAMLEMNARSLQQKL-ETERELKQ-RLLEEQAK 783
Cdd:COG3096 1051 AEAEERARIRrDELHEElsQNRSRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQeREQVVQAK 1114
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1545-1636 |
1.34e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1545 ESGTEQHRVPSTSRSSPNKRGPP--TYNEHITKR--------------VASSPAPPEGPSHPREPSTPHRYRDREGRTEL 1608
Cdd:PTZ00449 527 KEGEEGEHEDSKESDEPKEGGKPgeTKEGEVGKKpgpakehkpskiptLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRP 606
|
90 100 110
....*....|....*....|....*....|
gi 1907160229 1609 RRDKSPGRP--LEREKSPGRMLSTRRERSP 1636
Cdd:PTZ00449 607 TRPKSPKLPelLDIPKSPKRPESPKSPKRP 636
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-690 |
1.39e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 246 RQAKERAERELEKLHNREDSSeGIKKKLVEAEERrhsLENKVKRLETMERRENRLKDDIQTKS-------------EQIQ 312
Cdd:COG3096 275 RHANERRELSERALELRRELF-GARRQLAEEQYR---LVEMARELEELSARESDLEQDYQAASdhlnlvqtalrqqEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 313 QMADKILELEEKHREAQ-VSAQHLEVHLKQKEQ--HYEEKIKVLDNQikkdLADKESLENMMQRheeeahekgKILSEQK 389
Cdd:COG3096 351 RYQEDLEELTERLEEQEeVVEEAAEQLAEAEARleAAEEEVDSLKSQ----LADYQQALDVQQT---------RAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 390 AminamdskIRSLEqRIVELSEANKLAANSSLFTQRNMKAQEEMISElrqqkfyletqagkleaqnrkleeqlekishqd 469
Cdd:COG3096 418 A--------VQALE-KARALCGLPDLTPENAEDYLAAFRAKEQQATE--------------------------------- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 470 hsdksRLLELETRLReVSLEHEEQKlelkRQLTELQLSLQERESQLTALQAARAALEsQLRQAKTELEETtaeaeeeiQA 549
Cdd:COG3096 456 -----EVLELEQKLS-VADAARRQF----EKAYELVCKIAGEVERSQAWQTARELLR-RYRSQQALAQRL--------QQ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 550 LTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQ 629
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 630 LTSQK----QTMEALKTTCTMLEEQVLDLEALND---ELLEKERQWEAWRSVLGDEKSQFECRVRELQ 690
Cdd:COG3096 597 LAARApawlAAQDALERLREQSGEALADSQEVTAamqQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
208-563 |
1.56e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 208 SKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNredssegikkklvEAEERRHSLENKV 287
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------------ELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 288 KRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEqhyeEKIKVLDNQIKKDLADKESL 367
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE----EELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 368 ENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQ 447
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 448 AGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALES 527
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907160229 528 QLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDA 563
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
9-280 |
1.62e-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: 48.99 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 9 SKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDK 88
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 89 ALQLLHDIREQSRKLQEIKEQEYqaqveeMRLMMNQleEDLVSARRRSDLYESELRESRLAAEEFKRKANEcqhklmkvv 168
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP------LALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 169 shpprgdsggtalddlhkmqghagLTSAKDQgkpevgeyskLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQA 248
Cdd:COG4942 162 ------------------------LAALRAE----------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
250 260 270
....*....|....*....|....*....|..
gi 1907160229 249 KERAERELEKLHNREDSSEGIKKKLVEAEERR 280
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
214-877 |
1.69e-05 |
|
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: 50.05 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 214 NAEQQLKIQELQEKLEKAVKAsteatelLQNIrqakeraERELEKLH--NREDSSEGIKKKLVEAEERRHSLENKV--KR 289
Cdd:TIGR01612 691 NTEDKAKLDDLKSKIDKEYDK-------IQNM-------ETATVELHlsNIENKKNELLDIIVEIKKHIHGEINKDlnKI 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 290 LETMERRENRLKDDIQTKS---EQIQQMADKILELEEKHREaQVSAQHL-EVHLKQ---KEQHYEEKIKVLDNQIKKDLA 362
Cdd:TIGR01612 757 LEDFKNKEKELSNKINDYAkekDELNKYKSKISEIKNHYND-QINIDNIkDEDAKQnydKSKEYIKTISIKEDEIFKIIN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 363 D----KESLENMMQRHEE-EAHEKGKILSEQKA---MINAMDSKIRSLEQRIVElseaNKLAANSSLFTQRNMKAQEEM- 433
Cdd:TIGR01612 836 EmkfmKDDFLNKVDKFINfENNCKEKIDSEHEQfaeLTNKIKAEISDDKLNDYE----KKFNDSKSLINEINKSIEEEYq 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 434 -ISELRQQKFYLETQAGKLEA----------QNRKLEEQLEKISHQDHSDKSRLLELETRLrevslehEEQKLELKRQLT 502
Cdd:TIGR01612 912 nINTLKKVDEYIKICENTKESiekfhnkqniLKEILNKNIDTIKESNLIEKSYKDKFDNTL-------IDKINELDKAFK 984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 503 ELqlSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEiqaltAHRDEIQRKFDALRNSC-------TVITDLE 575
Cdd:TIGR01612 985 DA--SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEK-----ATNDIEQKIEDANKNIPnieiaihTSIYNII 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 576 EQLNQLTEDNAELNNQNFYLS-----------------------------KQLDEASGANDEIVQLRSEVDHLRREITER 626
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKEILEEaeinitnfneikeklkhynfddfgkeeniKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 627 EMQltsQKQTMEALKTTCTMLEEqVLDLEALNDELLEKERQWEAWRSVLGDEKSQFEcrvrELQRMLDteKQSRARADQR 706
Cdd:TIGR01612 1138 KKK---SENYIDEIKAQINDLED-VADKAISNDDPEEIEKKIENIVTKIDKKKNIYD----EIKKLLN--EIAEIEKDKT 1207
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 707 ITESRQVVELAVKEHKAEiLALQQaLKEQKLKAE----SLSDKLNDLE--KKHAMLEMNARSLQQKLETEREL------- 773
Cdd:TIGR01612 1208 SLEEVKGINLSYGKNLGK-LFLEK-IDEEKKKSEhmikAMEAYIEDLDeiKEKSPEIENEMGIEMDIKAEMETfnishdd 1285
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 774 -KQRLLEEQAKLQQQMDLqKNHIFRLTQGLQEALDRADLLKT----------ERSDLEYQLENIQVLYSHEKV----KME 838
Cdd:TIGR01612 1286 dKDHHIISKKHDENISDI-REKSLKIIEDFSEESDINDIKKElqknlldaqkHNSDINLYLNEIANIYNILKLnkikKII 1364
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907160229 839 GTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPT 877
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEE 1403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
388-591 |
1.71e-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: 48.99 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 388 QKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISH 467
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 468 QDHSDKSRLLEL-------ETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETT 540
Cdd:COG4942 98 ELEAQKEELAELlralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 541 AEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQ 591
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
409-636 |
1.93e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 409 LSEANKLaaNSSLftqrnMKAQEEMISELRQQKFYLETQagkLEAQNRKLEEQlEKISHQDHSDKSrllELETRLREVSL 488
Cdd:PHA02562 165 LSEMDKL--NKDK-----IRELNQQIQTLDMKIDHIQQQ---IKTYNKNIEEQ-RKKNGENIARKQ---NKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 489 EHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELE------------ETTAEAEEEIQALTAHRDE 556
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 557 IQRKFDALRNSctvITDLEEQLNQ-------LTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQ 629
Cdd:PHA02562 311 LQHSLEKLDTA---IDELEEIMDEfneqskkLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
....*..
gi 1907160229 630 LTSQKQT 636
Cdd:PHA02562 388 LDKIVKT 394
|
|
| C1_SpBZZ1-like |
cd20824 |
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ... |
987-1037 |
2.04e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410374 Cd Length: 53 Bit Score: 43.46 E-value: 2.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 987 PHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCG 1037
Cdd:cd20824 1 PHNFKPHSFSIPTKCDYCGEKIwGLSKKGLSCKDCGFNCHIKCELKVPPECP 52
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
64-871 |
2.25e-05 |
|
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: 49.66 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 64 YITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSrklqeIKEQEYQAQVEEMRL-MMNQLEEDLVSARRRSdlYESE 142
Cdd:TIGR01612 922 YIKICENTKESIEKFHNKQNILKEILNKNIDTIKESN-----LIEKSYKDKFDNTLIdKINELDKAFKDASLND--YEAK 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 143 LRE-----SRLAAEEFKRKANECQHKLmkvvshpprgDSGGTALDDLHKMQGHAGltsaKDQGKPEVGEYSKLEKINAEQ 217
Cdd:TIGR01612 995 NNElikyfNDLKANLGKNKENMLYHQF----------DEKEKATNDIEQKIEDAN----KNIPNIEIAIHTSIYNIIDEI 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 218 QLKIQELQEKLEKAV--KASTEATellqNIRQAKERAereleKLHNREDSSEgikkklveaeerrhslENKVKRLETMer 295
Cdd:TIGR01612 1061 EKEIGKNIELLNKEIleEAEINIT----NFNEIKEKL-----KHYNFDDFGK----------------EENIKYADEI-- 1113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 296 reNRLKDDIQTKSEQIQQmadKILELEEkhreaqvsaqhlevhLKQKEQHYEEKIKVLDNQIkKDLADK-------ESLE 368
Cdd:TIGR01612 1114 --NKIKDDIKNLDQKIDH---HIKALEE---------------IKKKSENYIDEIKAQINDL-EDVADKaisnddpEEIE 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 369 NMMQRHEEEAHEKGKILSEQKAMINAMdSKIR----SLEQ-RIVELSEANKLAA----------NSSLFTQRNMKAQEEM 433
Cdd:TIGR01612 1173 KKIENIVTKIDKKKNIYDEIKKLLNEI-AEIEkdktSLEEvKGINLSYGKNLGKlflekideekKKSEHMIKAMEAYIED 1251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 434 ISELRQQKFYLETQAGKLEAQNRKLEeqLEKISHQDHSDKsrlleletrlREVSLEHEEQKLELKrqltELQLSLQERES 513
Cdd:TIGR01612 1252 LDEIKEKSPEIENEMGIEMDIKAEME--TFNISHDDDKDH----------HIISKKHDENISDIR----EKSLKIIEDFS 1315
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 514 QLTALQAARAALESQLRQAKTELEEttaeaeeeiqaLTAHRDEIQRKFDALR--NSCTVITDLEEQLNQLTEDNAELNNQ 591
Cdd:TIGR01612 1316 EESDINDIKKELQKNLLDAQKHNSD-----------INLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDE 1384
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 592 ---NFYLSKQLDEASGANDEIVQLRS-----EVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLdLEALNDELLE 663
Cdd:TIGR01612 1385 ldkSEKLIKKIKDDINLEECKSKIEStlddkDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVL-LLFKNIEMAD 1463
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 664 KERQWeawrsVLGDEK----SQFECRVRELQRMLDTEKQSRARADQRITESRQVVELaVKEHKAEILALQQALKEQKLK- 738
Cdd:TIGR01612 1464 NKSQH-----ILKIKKdnatNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKEL-FEQYKKDVTELLNKYSALAIKn 1537
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 739 --AESLSDK---LNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQ----MDLQKNhifrlTQGLQEALDRA 809
Cdd:TIGR01612 1538 kfAKTKKDSeiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSnkaaIDIQLS-----LENFENKFLKI 1612
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 810 DLLKTERSDLEYQLENIQVLYSHEKVKMEGT-ISQQTKLIDFLQAKMDQPAKKKKGLFSRRKE 871
Cdd:TIGR01612 1613 SDIKKKINDCLKETESIEKKISSFSIDSQDTeLKENGDNLNSLQEFLESLKDQKKNIEDKKKE 1675
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
339-532 |
2.37e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 339 LKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMIN----AMDSKIRSLEQRIVELSEANK 414
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerreELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 415 LAANSSL--FTQRN------MKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEkishqdhsdksrllELETRLREV 486
Cdd:COG3883 108 LLGSESFsdFLDRLsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA--------------ELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907160229 487 slehEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQA 532
Cdd:COG3883 174 ----EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
531-800 |
2.57e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.27 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 531 QAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAND--- 607
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEE---LEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNEllk 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 608 -----------------EIVQLRSEVDHLRREITER----EMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDElleker 666
Cdd:pfam15905 143 akfsedgtqkkmsslsmELMKLRNKLEAKMKEVMAKqegmEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE------ 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 667 qweawrsvlgdEKSQFECRVRELQRMldteKQSRARADQRITESRQVVELAvKEHKAEILALQQALKEqklKAESLSDKL 746
Cdd:pfam15905 217 -----------EKSETEKLLEYITEL----SCVSEQVEKYKLDIAQLEELL-KEKNDEIESLKQSLEE---KEQELSKQI 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 747 NDLEKKHAMLEmnaRSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQ 800
Cdd:pfam15905 278 KDLNEKCKLLE---SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
328-552 |
2.74e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 328 AQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIV 407
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 408 ELSEA-NKLAA----NSSLFTQRNMKAQEEMISELRQQKFYLETQAgklEAQNRKLEEQLEkishqdhsDKSRLLELETR 482
Cdd:COG3883 83 ERREElGERARalyrSGGSVSYLDVLLGSESFSDFLDRLSALSKIA---DADADLLEELKA--------DKAELEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 483 LREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTA 552
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
224-440 |
2.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 224 LQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSS-------------EGIKKKLVEAEERRHSLENKVKRL 290
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVdlseeaklllqqlSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 291 ETMERRENRLKDDIQTkSEQIQQMADKILELEEkhREAQVSAQHLEVHlkqkeqhyeEKIKVLDNQIkkdladkESLENM 370
Cdd:COG3206 246 RAQLGSGPDALPELLQ-SPVIQQLRAQLAELEA--ELAELSARYTPNH---------PDVIALRAQI-------AALRAQ 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 371 MQRheeeahEKGKILSEQKAMINAMDSKIRSLEQRIVEL-SEANKLAANSSLFT--QRNMKAQEEMISELRQQ 440
Cdd:COG3206 307 LQQ------EAQRILASLEAELEALQAREASLQAQLAQLeARLAELPELEAELRrlEREVEVARELYESLLQR 373
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
600-789 |
3.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 600 DEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQvldLEALNDELLEKERQWEAWRSVLGDek 679
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 680 sqfecRVRELQR------MLDTEKQSRARAD--QRITESRQVVElavkeHKAEILALQQALKEQ-KLKAESLSDKLNDLE 750
Cdd:COG3883 91 -----RARALYRsggsvsYLDVLLGSESFSDflDRLSALSKIAD-----ADADLLEELKADKAElEAKKAELEAKLAELE 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907160229 751 KKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMD 789
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
430-770 |
3.74e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 430 QEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELEtRLREVSLEHEEQKLELKRQLTELQlsLQ 509
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERIR--QE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 510 ERESQLTALQAARAALE-SQLRQAKTELEETTAEAEEEIQALTAHR------DEIQRKfdalrnsctvitdLEEQLNQLT 582
Cdd:pfam17380 357 ERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARkvkileEERQRK-------------IQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 583 EDNAELNNQNFYLSKQLDEasgandeivQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLD---LEALND 659
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEE---------ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkrAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 660 ELLEKErqWEAWRSVLGDEKSQfecrvrelQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEilaLQQALKEQKLKA 739
Cdd:pfam17380 495 KILEKE--LEERKQAMIEEERK--------RKLLEKEMEERQKAIYEEERRREAEEERRKQQEME---ERRRIQEQMRKA 561
|
330 340 350
....*....|....*....|....*....|.
gi 1907160229 740 ESLSDKLNDLEKKHAMLEMNARSLQQKLETE 770
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
283-464 |
4.38e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 283 LENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIK---- 358
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 359 -----------------KDLADKESLENMMQRHEeeahekGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSL 421
Cdd:COG3883 98 sggsvsyldvllgsesfSDFLDRLSALSKIADAD------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907160229 422 FTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEK 464
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
483-800 |
4.62e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 483 LREVSLEHEEQKLeLKRQLTELQLSLQERESQ---LTALQAARAALESQLRQAKTEleettaeaeeeIQALTAHRDEIQR 559
Cdd:PRK11281 48 LNKQKLLEAEDKL-VQQDLEQTLALLDKIDRQkeeTEQLKQQLAQAPAKLRQAQAE-----------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 560 KfdalRNSCTVITDLEEQLNQLTEDNAELNNqnfylskqldEASGANDEIVQLRSEVDHLRREITE---REMQLTSQKQT 636
Cdd:PRK11281 116 E----TLSTLSLRQLESRLAQTLDQLQNAQN----------DLAEYNSQLVSLQTQPERAQAALYAnsqRLQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 637 MEALKTTCTMLEEQVLDLE-ALNDELLEKERQWEAWRSVLGDeksqfecrVRELQRMLDTEKQsrARADQRITESRQVV- 714
Cdd:PRK11281 182 GKVGGKALRPSQRVLLQAEqALLNAQNDLQRKSLEGNTQLQD--------LLQKQRDYLTARI--QRLEHQLQLLQEAIn 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 715 --ELAVKEHKAEilALQQALKEQKLKAESLsdklndlekkhamlemnarsLQQKLETERELKQRLLEEQAKLQQ--QMDL 790
Cdd:PRK11281 252 skRLTLSEKTVQ--EAQSQDEAARIQANPL--------------------VAQELEINLQLSQRLLKATEKLNTltQQNL 309
|
330
....*....|.
gi 1907160229 791 Q-KNHIFRLTQ 800
Cdd:PRK11281 310 RvKNWLDRLTQ 320
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
211-927 |
4.82e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 211 EKINAEQQLKIQELQEKLEKAVKASTEATEL-LQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKR 289
Cdd:TIGR00606 177 EIFSATRYIKALETLRQVRQTQGQKVQEHQMeLKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 290 LEtmerrENRLKddiqtkseqIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLEN 369
Cdd:TIGR00606 257 IE-----HNLSK---------IMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 370 MMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAAnSSLFTQRNMKAQEEMISELRQQKFYLETQAG 449
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI-QSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 450 KLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQEREsQLTALQAARAALESQL 529
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-QLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 530 RQA--------KTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYL-SKQLD 600
Cdd:TIGR00606 481 RKAerelskaeKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIkSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 601 EASGA----------NDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEalnDELLEKERQwEA 670
Cdd:TIGR00606 561 ELTSLlgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE---DKLFDVCGS-QD 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 671 WRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAE------ILALQQALKEQKLKAESLSD 744
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEaelqefISDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 745 KLNDLEKKH----AMLEMNARSLQQKLETERELKQRLleeqAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSD-- 818
Cdd:TIGR00606 717 ELKKKEKRRdemlGLAPGRQSIIDLKEKEIPELRNKL----QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvt 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 819 ----LEYQLENIQVLYSHEKVKMEG-----TISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNEL--- 886
Cdd:TIGR00606 793 imerFQMELKDVERKIAQQAAKLQGsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkse 872
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1907160229 887 KLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHP 927
Cdd:TIGR00606 873 KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
388-677 |
5.58e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 388 QKAMINAMDSKIRSLEQRIVELSEANKLaansslftQRNMKAQEEMISELRQQKFYLETQAGKLEAQ--NRKLEEQLEKI 465
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAKQY--------QQVIDNFPKLSAELRQQLNNERDEPRSVPPNmsTDALEQEILQV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 466 SHQdHSDKSRLLELET-RLREVS---LEHEEQKLELKRQLTELQLSLQERESQLTAL-QAARAAL--ESQLRQAKTELEE 538
Cdd:PRK10929 115 SSQ-LLEKSRQAQQEQdRAREISdslSQLPQQQTEARRQLNEIERRLQTLGTPNTPLaQAQLTALqaESAALKALVDELE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 539 TTAEAEEEIQALTAHRDEI-QRKFDALRNSctvITDLEEQLNQLTEDNAElnnQNFYLSKQLDEASG--ANDEIVQLRse 615
Cdd:PRK10929 194 LAQLSANNRQELARLRSELaKKRSQQLDAY---LQALRNQLNSQRQREAE---RALESTELLAEQSGdlPKSIVAQFK-- 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 616 vdhLRREITereMQLTSQKQTMEALKTTCTMLEEQVLDL-EALNDelLEKERQWEAWRSVLGD 677
Cdd:PRK10929 266 ---INRELS---QALNQQAQRMDLIASQQRQAASQTLQVrQALNT--LREQSQWLGVSNALGE 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
394-563 |
5.58e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 394 AMDSKIRSLEQRIVELSEAnklaansslftqrnmkaqeemISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDK 473
Cdd:COG1579 14 ELDSELDRLEHRLKELPAE---------------------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 474 SRLLELETRLREVS-------LEHEEQKLELKRQLTELQLS-----LQERESQLTALQAARAALESQLRQAKTELEETTA 541
Cdd:COG1579 73 ARIKKYEEQLGNVRnnkeyeaLQKEIESLKRRISDLEDEILelmerIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|..
gi 1907160229 542 EAEEEIQALTAHRDEIQRKFDA 563
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
195-397 |
6.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 195 SAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLV 274
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 275 EAEERR-------------HSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQ 341
Cdd:COG3883 93 RALYRSggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 342 KEQHYEEK---IKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDS 397
Cdd:COG3883 173 LEAQQAEQealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
492-783 |
6.22e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 492 EQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDeiqrKFDALRNSctvI 571
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRE----KRDELNEK---V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 572 TDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEqV 651
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEK-A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 652 LDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQrITESRqvvelavKEHKAEILALQQA 731
Cdd:COG1340 153 KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE-LRKEA-------DELHKEIVEAQEK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 732 LKEQKLKAESLSDKLNDLEKKHAMLEmnarslQQKLETERELKQRLLEEQAK 783
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLR------KKQRALKREKEKEELEEKAE 270
|
|
| C1_CeDKF1-like_rpt2 |
cd20798 |
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ... |
987-1038 |
6.74e-05 |
|
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410348 Cd Length: 54 Bit Score: 42.10 E-value: 6.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 987 PHRFNVGLNMRATKCAVClDTVHFG--RQASKCLECQVMCHPKCSTCLPATCGL 1038
Cdd:cd20798 1 PHTLAEHNYKKPTVCKVC-DKLLVGlvRQGLKCRDCGVNVHKKCASLLPSNCRL 53
|
|
| PH_ROCK |
cd01242 |
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ... |
1070-1115 |
7.15e-05 |
|
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269948 Cd Length: 110 Bit Score: 43.50 E-value: 7.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907160229 1070 HLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPV 1115
Cdd:cd01242 2 RLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPI 47
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10-408 |
7.41e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 10 KELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARmevsqeddka 89
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR---------- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 90 lqllHDIREQSRKL---------QEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELREsrlaAEEFKRKANEC 160
Cdd:PRK02224 440 ----ERVEEAEALLeagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER----AEDLVEAEDRI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 161 QHKLMKVvshpprgdsggtalDDLHKM--QGHAGLTSAKDQgkpevgeyskLEKINAEQQlkiqELQEKLEKAVKASTEA 238
Cdd:PRK02224 512 ERLEERR--------------EDLEELiaERRETIEEKRER----------AEELRERAA----ELEAEAEEKREAAAEA 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 239 TELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKI 318
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 319 LE--LEEKHREAQVSAQHLEvHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHE--EEAHEKGKILSEQKAMINA 394
Cdd:PRK02224 644 DEarIEEAREDKERAEEYLE-QVEEKLDELREERDDLQAEIGAVENELEELEELRERREalENRVEALEALYDEAEELES 722
|
410
....*....|....*
gi 1907160229 395 MDSKIRS-LEQRIVE 408
Cdd:PRK02224 723 MYGDLRAeLRQRNVE 737
|
|
| C1_Munc13-1 |
cd20858 |
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ... |
986-1036 |
8.54e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410408 Cd Length: 60 Bit Score: 42.00 E-value: 8.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 986 IPHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20858 6 TPHNFEVWTATTPTYCYECEGLLwGIARQGMRCTECGVKCHEKCQDLLNADC 57
|
|
| C1_aPKC |
cd20794 |
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ... |
989-1037 |
8.89e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410344 Cd Length: 55 Bit Score: 41.87 E-value: 8.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907160229 989 RFNvglnmRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCG 1037
Cdd:cd20794 9 RFN-----RRAVCAYCSDRIwGLGRQGYKCINCKLLVHKKCHKLVKVACG 53
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2-377 |
8.96e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 47.32 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 2 EKKLLIKSKELQDSQDKchKMEQEMTRLHRRVSEVEAVLSQKEvelKASETQRsllEQDLATYITEC-SSLKRSLEQARM 80
Cdd:NF033838 112 EAELTSKTKKELDAAFE--QFKKDTLEPGKKVAEATKKVEEAE---KKAKDQK---EEDRRNYPTNTyKTLELEIAESDV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 81 EVSQEDdkaLQLLHDIREQSRKLQEIKEQEyqAQVEEMRLMMNQLEEdLVSARRRSDLYESELRESRLAAEEFKRKANEC 160
Cdd:NF033838 184 EVKKAE---LELVKEEAKEPRDEEKIKQAK--AKVESKKAEATRLEK-IKTDREKAEEEAKRRADAKLKEAVEKNVATSE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 161 QHKLMKVVShppRGDSGGTALDDlhKMQGHAgltsakDQGKPEVGEYS------KLEKINAEQQLKIQELQEKLEK---- 230
Cdd:NF033838 258 QDKPKRRAK---RGVLGEPATPD--KKENDA------KSSDSSVGEETlpspslKPEKKVAEAEKKVEEAKKKAKDqkee 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 231 ------AVKASTEATELLQNIRQAKErAERELEKLHNREDSSEgikKKLVEAEERRHSLENKVKRLEtmerrenRLKDDI 304
Cdd:NF033838 327 drrnypTNTYKTLELEIAESDVKVKE-AELELVKEEAKEPRNE---EKIKQAKAKVESKKAEATRLE-------KIKTDR 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 305 QTKSEQIQQMADKILELEEKHREAQVSAQHLEVhlkQKEQHYEEKIKVLDNQIKKDlaDKESLENMMQRHEEE 377
Cdd:NF033838 396 KKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQP---EKPAPKPEKPAEQPKAEKPA--DQQAEEDYARRSEEE 463
|
|
| PH_MRCK |
cd01243 |
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ... |
1072-1187 |
9.02e-05 |
|
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269949 Cd Length: 135 Bit Score: 44.21 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1072 EGWMKVPrnnKRG--QQGWDRKYIVLEGSKVLIYD-NEAREAGQRPVEEFELCLPDGDVSIhGAVGASELANTAKADVPY 1148
Cdd:cd01243 15 EGYVRVP---KPGgvKKGWQRQFAVVCDFKLFLFDiSEDKASQPSQVASQVLDMRDEEFSV-SSVLASDVIHANKKDIPC 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907160229 1149 ILKME-SHPHTTCWPGRTLyLLAPSFPDKQRWVTALESVV 1187
Cdd:cd01243 91 IFRVSaSQLAPPSLKFSLL-MLADSENEKQKWVDALNELH 129
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
398-694 |
9.23e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 398 KIRSLEQRIVEL-SEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIshqdhsdKSRL 476
Cdd:pfam00038 19 KVRFLEQQNKLLeTKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF-------RQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 477 lELETRLREvslEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALE-------SQLRQAKTELEETTAEAEEEIQA 549
Cdd:pfam00038 92 -EDELNLRT---SAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheeevRELQAQVSDTQVNVEMDAARKLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 550 LTAHRDEIQRKFDALRNSCTviTDLEEQLNQLTEdnaELNnqnfylskqlDEASGANDEIVQLRSEVDHLRREITEREMQ 629
Cdd:pfam00038 168 LTSALAEIRAQYEEIAAKNR--EEAEEWYQSKLE---ELQ----------QAAARNGDALRSAKEEITELRRTIQSLEIE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 630 LTSQKQTMEALKTTCTMLEEQ-VLDLEALNDELLEKERQweawrsvLGDEKSQFECRVRELQRMLD 694
Cdd:pfam00038 233 LQSLKKQKASLERQLAETEERyELQLADYQELISELEAE-------LQETRQEMARQLREYQELLN 291
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
686-940 |
1.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 686 VRELqrMLDtEKQSRARAD------QRITESRQVVELAVKEHKA--EILALQQALKEQKLKAESLSDKLNDLEKKHAMLE 757
Cdd:COG4913 213 VREY--MLE-EPDTFEAADalvehfDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 758 MNArsLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEA-LDRADLLKTERSDLEYQLENIqvlyshekvk 836
Cdd:COG4913 290 LEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEER---------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 837 mEGTISQQTKLIDFLQAKMDQPAKkkkGLFSRRKEDPALPTQVPLQYNELKLALekekarcAELEEALQKTRIELRSARE 916
Cdd:COG4913 358 -ERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|....
gi 1907160229 917 EAAHRKATDHPHPSTPATARQQIA 940
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALA 450
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
240-578 |
1.11e-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: 46.81 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 240 ELLQNIRQAKERAERELEKLHnrEDSSEGIKKKLVEAEERRHSLENKVKRLETmerrenrlkdDIQTKSEQIQQMADKIL 319
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQ--EAANRQREKEKERYKRDREQWERQRRELES----------RVAELKEELRQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 320 ELEEKHREAQVS----AQHLEVHLKQKEQH------YEEKIKVLD---------------------NQIKKDLADKESLE 368
Cdd:pfam07888 98 ELEEKYKELSASseelSEEKDALLAQRAAHearireLEEDIKTLTqrvleretelermkerakkagAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 369 NMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSeaNKLAAnsslfTQRNMKAQEEMISELRQQKFYLETQA 448
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTT-----AHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 449 GKLEAQNRKLEEQlekISHQDHS----DKSRL--LELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAAR 522
Cdd:pfam07888 251 RKVEGLGEELSSM---AAQRDRTqaelHQARLqaAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 523 AALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQL 578
Cdd:pfam07888 328 QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQL 383
|
|
| C1_nPKC_theta-like_rpt2 |
cd20837 |
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
988-1036 |
1.22e-04 |
|
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410387 Cd Length: 50 Bit Score: 41.27 E-value: 1.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 988 HRFNVGLNMRATKCAVClDTVHFG--RQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20837 1 HRFKVYNYMSPTFCDHC-GSLLWGlfRQGLKCEECGMNVHHKCQKKVANLC 50
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
223-721 |
1.26e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 223 ELQEKLEKAVKASTEATELlQNIRQAKERAERELEKLHNREDSSEGIKKK--LVEAEERRHSLE---------NKV---- 287
Cdd:PTZ00440 2171 EIIENIKKEIIEINENTEM-NTLENTADKLKELYENLKKKKNIINNIYKKinFIKLQEIENSSEkyndisklfNNVvetq 2249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 288 -KRLETMERRENRLKDDIQTKsEQIQQMADKILELEEKhREAQVSAQHLEVHLKQKEQHYEEKIKVLDN------QIKKD 360
Cdd:PTZ00440 2250 kKKLLDNKNKINNIKDKINDK-EKELINVDSSFTLESI-KTFNEIYDDIKSNIGDLYKLEDTNNDELKKvklyieNITHL 2327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 361 LADKESLENMMQRHEEEahekGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLaansslfTQRNMKAQEEMISELRQQ 440
Cdd:PTZ00440 2328 LNRINTLINDLDNYQDE----NYGKDKNIELNNENNSYIIKTKEKINNLKEEFSK-------LLKNIKRNNTLCNNNNIK 2396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 441 KFYLETqAGKLEAQNRKLEEQLEkishqdhsdksrlleletrLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQA 520
Cdd:PTZ00440 2397 DFISNI-GKSVETIKQRFSSNLP-------------------EKEKLHQIEENLNEIKNIMNETKRISNVDAFTNKILQD 2456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 521 ARAALEsqlrqaKTELEETTAEAEEEIQALTAHRDEIQRKF----DALRNSCTVITDLEEQLNQLTEDNAELNNQ-NFYL 595
Cdd:PTZ00440 2457 IDNEKN------KENNNMNAEKIDDLIENVTSHNEKIKSELliinDALRRVKEKKDEMNKLFNSLTENNNNNNNSaKNIV 2530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 596 SKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSqkqtmealkttctMLEEQVLDLEALNDELLEKERQweawrsvl 675
Cdd:PTZ00440 2531 DNSTYIINELESHVSKLNELLSYIDNEIKELENEKLK-------------LLEKAKIEESRKERERIESETQ-------- 2589
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1907160229 676 GDEKSQFECRVRELQRMLDTEKQsRARADQRITESRQVVELAVKEH 721
Cdd:PTZ00440 2590 EDNTDEEQINRQQQERLQKEEEQ-KAYSQERLNREVSGTDDTNKNH 2634
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
504-823 |
1.28e-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: 46.43 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 504 LQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRkfdALRNSCTVITDLEEQLNQLTE 583
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE---ELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 584 DNAELNNQNFYLSKQLDEASGandEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLE 663
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEA---RIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 664 KERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVvelavkehKAEILALQQALKEQKLKAESLS 743
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL--------LEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 744 DKLNDL--EKKHAMLEMNARSLQ------QKLETE---RELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLL 812
Cdd:pfam07888 258 EELSSMaaQRDRTQAELHQARLQaaqltlQLADASlalREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330
....*....|.
gi 1907160229 813 KTERSDLEYQL 823
Cdd:pfam07888 338 RMEREKLEVEL 348
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
704-861 |
1.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 704 DQRITESRQvvelAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLEterELKQRLLE---- 779
Cdd:COG1579 16 DSELDRLEH----RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNvrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 780 -EQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQP 858
Cdd:COG1579 89 kEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
...
gi 1907160229 859 AKK 861
Cdd:COG1579 169 AAK 171
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
225-519 |
1.46e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 225 QEKLEKAVKasteatellQNIRQAKERAERELEKlhnredssegiKKKLVEAEERRHSlenKVKRLETMERRENRLKDDI 304
Cdd:pfam17380 290 QEKFEKMEQ---------ERLRQEKEEKAREVER-----------RRKLEEAEKARQA---EMDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 305 QTKSEQIQQmadkilelEEKHREAQvsaqhlevHLKQKEQHYE-EKIKVLDNqikkdLADKESLENMMQRHEEEAHEKGK 383
Cdd:pfam17380 347 ERELERIRQ--------EERKRELE--------RIRQEEIAMEiSRMRELER-----LQMERQQKNERVRQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 384 ILSEQKAminamdskiRSLEQRIVELSEANKLAANSSlftQRNMKAQEEMISElrqqkfylETQAGKLEAQNRklEEQLE 463
Cdd:pfam17380 406 ILEEERQ---------RKIQQQKVEMEQIRAEQEEAR---QREVRRLEEERAR--------EMERVRLEEQER--QQQVE 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 464 KISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQ 519
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
491-705 |
1.53e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 491 EEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRN---- 566
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 567 ---SCTVITDLEEQLNQltEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTT 643
Cdd:COG3883 95 lyrSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 644 ctmLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQ 705
Cdd:COG3883 173 ---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
482-809 |
1.56e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 482 RLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEEttaeaeeeIQALTAHRDEIQRKF 561
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNL--------VQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 562 DALrnsctviTDLEEQLNQLTEDNAELNNQNFYLSKQLDEAsgaNDEIVQLRSEV-DHLRR--EITEREMQLTSQKQTME 638
Cdd:PRK04863 355 ADL-------EELEERLEEQNEVVEEADEQQEENEARAEAA---EEEVDELKSQLaDYQQAldVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 639 ALKTTC-----------TMLEEQVLDLEALNDELLEKERQWeawrSVLGDEKSQFECRVRELQRMLDTEKQSRAR--ADQ 705
Cdd:PRK04863 425 RAKQLCglpdltadnaeDWLEEFQAKEQEATEELLSLEQKL----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 706 RITESRQVVELAVKEH--KAEILALQQALKEQKlKAESLsdkLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAK 783
Cdd:PRK04863 501 LLRRLREQRHLAEQLQqlRMRLSELEQRLRQQQ-RAERL---LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSE 576
|
330 340
....*....|....*....|....*.
gi 1907160229 784 LQQQMDLQKNHIFRLTQGLQEALDRA 809
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARA 602
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
215-519 |
1.61e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 215 AEQQLKIQELQEKLEKAVKASTEATELLQNIR-QAKERAERElEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETM 293
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESKDQKELEKEIRaLVQERGEQD-KRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 294 ERRENRLKDDIQTK-SEQIQQMADKILELEekhreaqVSAQHLEVHLKQKEqhyeekikVLDNQIKKDLADKESLENMMQ 372
Cdd:pfam15905 131 LLELTRVNELLKAKfSEDGTQKKMSSLSME-------LMKLRNKLEAKMKE--------VMAKQEGMEGKLQVTQKNLEH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 373 RHEEEAHEKGKILSEQKAMINAmDSKIRSLEQRIVELSEANKLAANSSLftqrnmkaqeemisELRQQKFYLETQAGKLE 452
Cdd:pfam15905 196 SKGKVAQLEEKLVSTEKEKIEE-KSETEKLLEYITELSCVSEQVEKYKL--------------DIAQLEELLKEKNDEIE 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907160229 453 AQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQ 519
Cdd:pfam15905 261 SLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| C1_aPKC_iota |
cd21094 |
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ... |
988-1039 |
1.63e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota type; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain C1 domain found in aPKC isoform iota. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410447 Cd Length: 55 Bit Score: 41.14 E-value: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 988 HRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCGLP 1039
Cdd:cd21094 3 HTFQAKRFNRRAHCAICTDRIwGLGRQGYKCINCKLLVHKKCHKLVTIECGRH 55
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
569-788 |
1.79e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 569 TVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASG----ANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEAL---- 640
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEeyneLQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 641 ---KTTCTMLEeQVLDLEALNDELlekeRQWEAWRSVLGDEKSQFEcRVRELQRMLDTEKQSRARADQRITESRQVVELA 717
Cdd:COG3883 96 yrsGGSVSYLD-VLLGSESFSDFL----DRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 718 VKEhkaeilaLQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQM 788
Cdd:COG3883 170 KAE-------LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
435-912 |
1.79e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 435 SELRQQKFYLETQAGKLEAQNRKLEE---QLEKISH------QDHSDKSR-----------LLELETRLREVSLEHEEQK 494
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAIQElqfENEKVSLkleeeiQENKDLIKennatrhlcnlLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 495 LELKRQLTELQLSLqerESQLTALQAARAalesQLRQAKTELEETTAEAEEEIQALtahRDEIQRKFDALRNSCTVItdl 574
Cdd:pfam05483 179 EETRQVYMDLNNNI---EKMILAFEELRV----QAENARLEMHFKLKEDHEKIQHL---EEEYKKEINDKEKQVSLL--- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 575 eeqLNQLTEDNAELNNQNFYLSK------QLDEASGANDE-IVQLRSEVDHLRREITEREMQLTSQKQTMEAL------- 640
Cdd:pfam05483 246 ---LIQITEKENKMKDLTFLLEEsrdkanQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALeedlqia 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 641 -KTTCTMLEEQVLDLEALNDE-------LLEKERQWEAWRSVLGDEKSQFECRVRELqRMLDTEKQSRARADQRITESRQ 712
Cdd:pfam05483 323 tKTICQLTEEKEAQMEELNKAkaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 713 VVELAVKEHKaEILALQQALKEQKLKAESLSDKLNDLEKKHAML----EMNARSLQQKLETERELKQRLLEEQAKLQQQM 788
Cdd:pfam05483 402 NKEVELEELK-KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 789 DLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQqtklIDFLQAKMDQpakkkkglfsR 868
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ----IENLEEKEMN----------L 546
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907160229 869 RKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELR 912
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
269-665 |
1.91e-04 |
|
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: 46.00 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 269 IKKKLVEAEE--RRHSLeNKVKRleTMERRENRLkDDIQTKSEQIQQMADKILELEEKHREAqvsAQHLEVH-------L 339
Cdd:pfam06160 65 IEELLFEAEElnDKYRF-KKAKK--ALDEIEELL-DDIEEDIKQILEELDELLESEEKNREE---VEELKDKyrelrktL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 340 KQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHE-EEAHEkgkILSEQKAMINAMDSKIRSLEQRIVELseanklaan 418
Cdd:pfam06160 138 LANRFSYGPAIDELEKQLAEIEEEFSQFEELTESGDyLEARE---VLEKLEEETDALEELMEDIPPLYEEL--------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 419 sslftQRNMKAQ----EEMISELRQQKFYLETQagkleaqnrKLEEQLEKISHQDHSDKSRLLELEtrlrevsLEHEEQK 494
Cdd:pfam06160 206 -----KTELPDQleelKEGYREMEEEGYALEHL---------NVDKEIQQLEEQLEENLALLENLE-------LDEAEEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 495 LE-LKRQLTELQLSLqEREsqltalqaaraalesqlrqakteleettaeaeeeIQAltahRDEIQRKFDALRNSctvITD 573
Cdd:pfam06160 265 LEeIEERIDQLYDLL-EKE----------------------------------VDA----KKYVEKNLPEIEDY---LEH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 574 LEEQLNQLTEDNAELnNQNFYLS-KQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVL 652
Cdd:pfam06160 303 AEEQNKELKEELERV-QQSYTLNeNELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQE 381
|
410
....*....|....
gi 1907160229 653 DL-EALNDelLEKE 665
Cdd:pfam06160 382 EFkESLQS--LRKD 393
|
|
| C1_MTMR-like |
cd20828 |
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ... |
984-1037 |
1.99e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410378 Cd Length: 57 Bit Score: 40.89 E-value: 1.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907160229 984 HNIPHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCG 1037
Cdd:cd20828 2 FTQPHNFEPHSFVTPTNCDYCLQILwGIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
503-862 |
2.18e-04 |
|
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: 45.84 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 503 ELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeeeiqaltahrdEIQRKFDALRNSCTVIT----DLEEQL 578
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQ----------------------ERLDQLESGDDSGTPGGkkylLLQKQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 579 NQLTEDN--------------AELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRrEITER----EMQLTSQKQTMEA- 639
Cdd:pfam05622 69 EQLQEENfrletarddyrikcEELEKEVLELQHRNEELTSLAEEAQALKDEMDILR-ESSDKvkklEATVETYKKKLEDl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 640 --LKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTE-----------KQSRA----- 701
Cdd:pfam05622 148 gdLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQ----VQELHGKLSEEskkadklefeyKKLEEkleal 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 702 -RADQRITESRQVVELAVKE-----------HKAEILALQQALKEQKLKAESLS----DKLNDLEKKHAMLEMNAR---- 761
Cdd:pfam05622 224 qKEKERLIIERDTLRETNEElrcaqlqqaelSQADALLSPSSDPGDNLAAEIMPaeirEKLIRLQHENKMLRLGQEgsyr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 762 ----SLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLEniQVLYSHEKvkm 837
Cdd:pfam05622 304 erltELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLE--KLHEAQSE--- 378
|
410 420
....*....|....*....|....*
gi 1907160229 838 egtISQQTKLIDFLQAKMDQPAKKK 862
Cdd:pfam05622 379 ---LQKKKEQIEELEPKQDSNLAQK 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-272 |
2.21e-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: 46.21 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 10 KELQDSQDKCHKMEQEMTRL-----HRRVSEVEAVLSQKEVELKASETQRSLLEQDLatyitECSSLKRSLEQARMEVSQ 84
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQELQ 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 85 EDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKL 164
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 165 MKvvshppRGDSGGTALDDLhkmqghAGLTSAKDQGKPEVGEYSKLEKINAEQQlKIQELQEKLE----KAVKASTEATE 240
Cdd:TIGR02169 920 SE------LKAKLEALEEEL------SEIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEEIRALEpvnmLAIQEYEEVLK 986
|
250 260 270
....*....|....*....|....*....|..
gi 1907160229 241 LLQNIRQAKERAERELEKLHNREDSSEGIKKK 272
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
206-383 |
2.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 206 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERR----- 280
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 281 --------------HSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHY 346
Cdd:COG4942 115 rlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907160229 347 EEKIKVLD----------NQIKKDLADKESLENMMQRHEEEAHEKGK 383
Cdd:COG4942 195 AERQKLLArlekelaelaAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
245-398 |
2.54e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 245 IRQAKERAERELEKLhnrEDSSEGIKKKLVEAEERRHSLENKVKRLEtmerrenRLKDDIQTKSEQIQQMADKIL-ELEE 323
Cdd:PRK00409 504 IEEAKKLIGEDKEKL---NELIASLEELERELEQKAEEAEALLKEAE-------KLKEELEEKKEKLQEEEDKLLeEAEK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 324 KHREA-------------QVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKdlADKESLENMMQRHEEEAHEKGKILS-EQK 389
Cdd:PRK00409 574 EAQQAikeakkeadeiikELRQLQKGGYASVKAHELIEARKRLNKANEK--KEKKKKKQKEKQEELKVGDEVKYLSlGQK 651
|
....*....
gi 1907160229 390 AMINAMDSK 398
Cdd:PRK00409 652 GEVLSIPDD 660
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
291-531 |
2.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 291 ETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQvsAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENM 370
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR--QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 371 MQRHEEEAHEKGKILSEQKAminamDSKIRSLEQRIVELSEanKLAANSSLFTQRN--MKAQEEMISELRQQkfyletqa 448
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEA--ELAELSARYTPNHpdVIALRAQIAALRAQ-------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 449 gkLEAQNRKLEEQLEkishqdhsdkSRLLELETRLREVSLEHEEQKLELKRqltelqlsLQERESQLTALQAARAALESQ 528
Cdd:COG3206 307 --LQQEAQRILASLE----------AELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVAREL 366
|
...
gi 1907160229 529 LRQ 531
Cdd:COG3206 367 YES 369
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
206-533 |
2.62e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 206 EYSKLEKINAEqqLKIQELQEKLEKAVKASTEATELLQNIRQAKERAeRELEKLHNREDSSEGIKKKLVEAEERRHsLEN 285
Cdd:COG5185 254 KLEKLVEQNTD--LRLEKLGENAESSKRLNENANNLIKQFENTKEKI-AEYTKSIDIKKATESLEEQLAAAEAEQE-LEE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 286 KVKRLETMerrenrlkddIQTKSEQIQQMADKILELEEKHREaQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKE 365
Cdd:COG5185 330 SKRETETG----------IQNLTAEIEQGQESLTENLEAIKE-EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 366 SLENMMQRHEEEAHEKGKILSEQkamINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLE 445
Cdd:COG5185 399 NQRGYAQEILATLEDTLKAADRQ---IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 446 tqagkLEAQNRKLEEQLEKIshqdhsdKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQEREsqlTALQAARAAL 525
Cdd:COG5185 476 -----VRSKKEDLNEELTQI-------ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFM---RARGYAHILA 540
|
....*...
gi 1907160229 526 ESQLRQAK 533
Cdd:COG5185 541 LENLIPAS 548
|
|
| C1_PKD2_rpt2 |
cd20843 |
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ... |
986-1036 |
2.89e-04 |
|
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410393 Cd Length: 79 Bit Score: 41.11 E-value: 2.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 986 IPHRFNVGLNMRATKCAVCLDTVH-FGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20843 10 VPHTFVIHSYTRPTVCQFCKKLLKgLFRQGLQCKDCKFNCHKRCATRVPNDC 61
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
65-414 |
3.77e-04 |
|
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: 45.43 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 65 ITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSrKLQEIKEQEYQA----QVEEMRLMMNQLEEDLVSARRRSDLYE 140
Cdd:TIGR01612 1364 IDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI-NLEECKSKIESTlddkDIDECIKKIKELKNHILSEESNIDTYF 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 141 SELRESR----LAAEEFKRKANECQHkLMKVvshppRGDSGGTALD-DLHKMQGHagltsaKDQGKPEVGEYSKlekiNA 215
Cdd:TIGR01612 1443 KNADENNenvlLLFKNIEMADNKSQH-ILKI-----KKDNATNDHDfNINELKEH------IDKSKGCKDEADK----NA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 216 EQQLKIQELQEKLEKAVKA---STEATELLQNIRQAKERAE---RELEKLHNRED-SSEGIKKKLVEAEERRHSLENKVK 288
Cdd:TIGR01612 1507 KAIEKNKELFEQYKKDVTEllnKYSALAIKNKFAKTKKDSEiiiKEIKDAHKKFIlEAEKSEQKIKEIKKEKFRIEDDAA 1586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 289 RletmERRENRLKDDIQTKSEQIQQMADKILELEEKHREAqvsaqhlevhLKQKEQhYEEKIKVLD-NQIKKDLADKESL 367
Cdd:TIGR01612 1587 K----NDKSNKAAIDIQLSLENFENKFLKISDIKKKINDC----------LKETES-IEKKISSFSiDSQDTELKENGDN 1651
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 368 ENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLE---------------QRIVELSEANK 414
Cdd:TIGR01612 1652 LNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEidvdqhkknyeigiiEKIKEIAIANK 1713
|
|
| C1_Munc13-2-like |
cd20859 |
protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar ... |
982-1036 |
4.24e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar proteins; Munc13-2, also called protein unc-13 homolog B (Unc13B), plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410409 Cd Length: 82 Bit Score: 40.82 E-value: 4.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 982 MHHNIPHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20859 14 ISCTTPHNFEVWTATTPTYCYECEGLLwGIARQGMRCSECGVKCHEKCQDLLNADC 69
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
220-378 |
4.36e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.86 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 220 KIQELQEKLEKAVKASTEATELLQNIRQAKERAERE----------------------------LEKLHNREDSSEGIKK 271
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEvaalnrriqlleeelerteerlaealekLEEAEKAADESERGRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 272 KL----VEAEERRHSLENKVK-----------RLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLE 336
Cdd:pfam00261 82 VLenraLKDEEKMEILEAQLKeakeiaeeadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907160229 337 VHLK---QKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEA 378
Cdd:pfam00261 162 ASEEkasEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEV 206
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
198-351 |
4.43e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 198 DQGKPEVGEYSKLEKINAEQqlKIQELQEKLEKAVKAST-EATELLQNIRQAKERAERELEKLHNREDssegikkklvEA 276
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKE--EIHKLRNEFEKELRERRnELQKLEKRLLQKEENLDRKLELLEKREE----------EL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 277 EERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQM----ADKILeLEEKHREAQVSAQHLevhLKQKEQHYEEKIK 351
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaeeAKEIL-LEKVEEEARHEAAVL---IKEIEEEAKEEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
500-717 |
4.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 500 QLTELQLSLQERESQLTALQAARAALESQLRQAKTEleettaeaeeeIQALTAHRDEIQRKFDALRNSctvITDLEEQLN 579
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEE-----------YNELQAELEALQAEIDKLQAE---IAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 580 QLTEDNAELNNQNF---YLSKQLDEASGANDeIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEA 656
Cdd:COG3883 83 ERREELGERARALYrsgGSVSYLDVLLGSES-FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 657 LNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELA 717
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
556-856 |
5.01e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 556 EIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFY----LSKQLDEasgandEIVQLRSEVDHLRREITERE---- 627
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGenaeSSKRLNE------NANNLIKQFENTKEKIAEYTksid 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 628 -----MQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQF--ECRVRELQRMLDTEKQSR 700
Cdd:COG5185 307 ikkatESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 701 ARADQRITESRQVVELAVKEHKAeilALQQALKEQKLKAESLSDKLNDLEKKhamlemNARSLQQKLETERELKQRLLEE 780
Cdd:COG5185 387 ESTKESLDEIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSS------NEEVSKLLNELISELNKVMREA 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 781 QAKLQQQMDLQKNHIFRltqGLQEALDRADLlktERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMD 856
Cdd:COG5185 458 DEESQSRLEEAYDEINR---SVRSKKEDLNE---ELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLK 527
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
594-829 |
5.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 594 YLSKQLDEASGANDEIVQ-LRSEVDHLRREITEREMQLTS--QKQTMEALKTTCTMLEEQVLDLE----ALNDELLEKER 666
Cdd:COG3206 161 YLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELEsqlaEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 667 QWEAWRSVLGDEKSQF-----ECRVRELQRMLDTEKQSRARADQRITE-SRQVVELavkehKAEILALQQALKEQKLKAe 740
Cdd:COG3206 241 RLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELSARYTPnHPDVIAL-----RAQIAALRAQLQQEAQRI- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 741 slsdkLNDLEKKHAMLEMNARSLQQKLEterELKQRLLEEQAKLQQQMDLQKNhIFRLTQGLQEALDRADLLKTERSdle 820
Cdd:COG3206 315 -----LASLEAELEALQAREASLQAQLA---QLEARLAELPELEAELRRLERE-VEVARELYESLLQRLEEARLAEA--- 382
|
....*....
gi 1907160229 821 YQLENIQVL 829
Cdd:COG3206 383 LTVGNVRVI 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
614-747 |
5.79e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 614 SEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELlekerqwEAWRSVLGDEKSQFECRVRELQRML 693
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRL-------QALLAELAGAGAAAEGRAGELAQEL 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 694 DTEKQSRARADQRITE-SRQVVELavkehKAEILALQQAL-------KEQKLKAESLSDKLN 747
Cdd:PRK09039 126 DSEKQVSARALAQVELlNQQIAAL-----RRQLAALEAALdasekrdRESQAKIADLGRRLN 182
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
372-869 |
6.33e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 372 QRHEEEAHEKGKILSEQKAMINAMDS------KIRSLEQRIVELSEANKLAANSSLFTQRNMKAQ-EEMISELRQQKFYL 444
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESAELRlshlhfGYKSDETLIASRQEERQETSAELNQLLRTLDDQwKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 445 ETQAGKLEAQNRKLEEQLEKISHQD----HSDKSRLLELETRLREVSLEHE---------EQKLELKRQLTELQL----- 506
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKaltgkhqdvTAKYNRRRSKIKEQNnrdia 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 507 --------SLQERESQLTALQAARAALESQLRQAKTeleettaeaeeeiQALTAHRDEIQRKFDALRNSCTVITDL---E 575
Cdd:pfam12128 394 gikdklakIREARDRQLAVAEDDLQALESELREQLE-------------AGKLEFNEEEYRLKSRLGELKLRLNQAtatP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 576 EQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALK--------TTCTML 647
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpqagTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 648 EEQVLDLE-----ALNDELLEK-ERQWEAWRSVLGDEKSQFECRVReLQRM-----LDTEKQSRARADQritesrqvvel 716
Cdd:pfam12128 541 RKEAPDWEqsigkVISPELLHRtDLDPEVWDGSVGGELNLYGVKLD-LKRIdvpewAASEEELRERLDK----------- 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 717 aVKEhkaeilALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQmdlqknhif 796
Cdd:pfam12128 609 -AEE------ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKA--------- 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 797 rLTQGLQEALDRADLLKTERSDLEYQLEniQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRR 869
Cdd:pfam12128 673 -LAERKDSANERLNSLEAQLKQLDKKHQ--AWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARR 742
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1-152 |
7.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 1 MEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELK--ASETQRS---------LLE-QDLATYITEC 68
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerARALYRSggsvsyldvLLGsESFSDFLDRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 69 SSLKR----------SLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEqEYQAQVEEMRLMMNQLEEDLVSARRRSDL 138
Cdd:COG3883 122 SALSKiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKA-ELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
170
....*....|....
gi 1907160229 139 YESELRESRLAAEE 152
Cdd:COG3883 201 LEAELAAAEAAAAA 214
|
|
| C1_dGM13116p-like |
cd20831 |
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ... |
999-1036 |
7.63e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410381 Cd Length: 58 Bit Score: 39.25 E-value: 7.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907160229 999 TKCAVCLDTV--HFGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20831 17 PSCAVCNKLIpgRFGKQGYQCRDCGLICHKRCHVKVETHC 56
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
694-853 |
8.49e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 694 DTEKQSRARADQRITESRQVVELAVKE---HKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQ------ 764
Cdd:PHA02562 202 KNIEEQRKKNGENIARKQNKYDELVEEaktIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmy 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 765 ----------QKLETERELKQRLLEEQAKLQQQMDLQKNHIfrltQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEk 834
Cdd:PHA02562 282 ekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAI----DELEEIMDEFNEQSKKLLELKNKISTNKQSLITL- 356
|
170
....*....|....*....
gi 1907160229 835 vkmEGTISQQTKLIDFLQA 853
Cdd:PHA02562 357 ---VDKAKKVKAAIEELQA 372
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
205-299 |
9.09e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 205 GEYSKLEKINAEQQLKIQELQEKLEKAVKAsteatellqniRQAKERAERELEKLHNREDSsegIKKKLVEAEERRHSLE 284
Cdd:COG2433 427 AEVEELEAELEEKDERIERLERELSEARSE-----------ERREIRKDREISRLDREIER---LERELEEERERIEELK 492
|
90
....*....|....*
gi 1907160229 285 NKVKRLETMERRENR 299
Cdd:COG2433 493 RKLERLKELWKLEHS 507
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
300-468 |
1.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 300 LKDDIQTKSEQIQQMADKIleLEEKHREAqvsaqhlEVHLKQKEQHYEEKIKVLDNQIKKDLADKeslENMMQRHEEEAH 379
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRI--LEEAKKEA-------EAIKKEALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 380 EKGKILSEQKAMINAMDSKIRSLEQRIVELseanklaansslftQRNMKAQEEMISELR-QQKFYLETQAG--KLEAQNR 456
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQK--------------QQELEKKEEELEELIeEQLQELERISGltAEEAKEI 158
|
170
....*....|..
gi 1907160229 457 KLEEQLEKISHQ 468
Cdd:PRK12704 159 LLEKVEEEARHE 170
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
473-836 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 473 KSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTA 552
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 553 HRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEasgANDEIVQLRSEVDHLRREITEREMQLTS 632
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ---LEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 633 QKQTMEALKTTCTMLEEQVLDlEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQ 712
Cdd:COG4372 162 LQEELAALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 713 VVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEmNARSLQQKLETERELKQRLLEEQAKLQQQMDLQK 792
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL-EALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907160229 793 NHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVK 836
Cdd:COG4372 320 ALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-259 |
1.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 11 ELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSL--LEQDLATYIT---ECSSLKRSLEQARMEVSQE 85
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIaeLEAELERLDAssdDLAALEEQLEELEAELEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 86 DDKALQLLHDIREQSRKLQEIKEQ--EYQAQVEEMRLMMNQLEEDLVSARRRS---DLYESELRE---SRLAAEefKRKA 157
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEEldELQDRLEAAEDLARLELRALLEERFAAalgDAVERELREnleERIDAL--RARL 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 158 NECQHKLMKVVSH-----PPRGDSGGTALDDLHKMQGHagltsakdqgkpevgeYSKLEKINAEqqlkiqELQEKLEKAV 232
Cdd:COG4913 783 NRAEEELERAMRAfnrewPAETADLDADLESLPEYLAL----------------LDRLEEDGLP------EYEERFKELL 840
|
250 260
....*....|....*....|....*....
gi 1907160229 233 KASTEA--TELLQNIRQAKERAERELEKL 259
Cdd:COG4913 841 NENSIEfvADLLSKLRRAIREIKERIDPL 869
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
71-359 |
1.15e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 71 LKRSLEQARMEVSQEDDKalqlLHDIREQSRKLQEiKEQEYQAQVEEMRLMMNQLEEdlvsarRRSDLYEsELRESRLAA 150
Cdd:COG1340 13 LEEKIEELREEIEELKEK----RDELNEELKELAE-KRDELNAQVKELREEAQELRE------KRDELNE-KVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 151 EEFKRKANECQHKLMKVVSHPPRGDSGGTALDDLHKmqghagltsakdqgkpevgEYSKLEK--------INAEQQL--K 220
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRK-------------------EIERLEWrqqtevlsPEEEKELveK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 221 IQELQEKLE---KAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLenkVKRLETMERRE 297
Cdd:COG1340 142 IKELEKELEkakKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADEL---RKEADELHKEI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 298 NRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEqhYEEKIKVLDNQIKK 359
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE--LEEKAEEIFEKLKK 278
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
571-751 |
1.18e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 571 ITDLEEQLNQLTEDNAELNnqnfylskqlDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQ 650
Cdd:pfam05667 337 LEELQEQLEDLESSIQELE----------KEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 651 VLDLEALNDELLEKERQWEAWRSVLGDEksqfecrVRELqrmldtekqsRARADQRITESRQVVElAVKEHKAEIlalQQ 730
Cdd:pfam05667 407 QALVDASAQRLVELAGQWEKHRVPLIEE-------YRAL----------KEAKSNKEDESQRKLE-EIKELREKI---KE 465
|
170 180
....*....|....*....|.
gi 1907160229 731 ALKEQKLKAESLSDKLNDLEK 751
Cdd:pfam05667 466 VAEEAKQKEELYKQLVAEYER 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-255 |
1.26e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 4 KLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLE---QDLATYITECSSLKRSLEQArm 80
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEkeiQELQEQRIDLKEQIKSIEKE-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 81 evsQEDDKAlqllhDIREQSRKLQEIKEQEYQ--AQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKAN 158
Cdd:TIGR02169 856 ---IENLNG-----KKEELEEELEELEAALRDleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 159 ECQHKLMKVVSHPPRGDSGGTALDDLHKMQghagltsAKDQGKPEvgEYSKLEKIN-------AEQQLKIQELQEKLEKA 231
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSLEDVQ-------AELQRVEE--EIRALEPVNmlaiqeyEEVLKRLDELKEKRAKL 998
|
250 260
....*....|....*....|....
gi 1907160229 232 VKASTEATELLQNIRQAKERAERE 255
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREVFME 1022
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
211-411 |
1.32e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 211 EKINAEQQLKIQELQEKLEKAV---KASTEATELLQNIRQAKEraERELEKLHNREDSS-EGIKKKLVEAEERRHSLENK 286
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALdklRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEElEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 287 VKRLETMERRENRLKD-DIqtkseqiqqmaDKILELEEKH---REAQVSAQHLEVHLKQKEQHYEEKIKVLDN------- 355
Cdd:PRK05771 116 IKELEQEIERLEPWGNfDL-----------DLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYISTDKGyvyvvvv 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907160229 356 QIKKDLADKESLenmMQRHE---EEAHEKGK---ILSEQKAMINAMDSKIRSLEQRIVELSE 411
Cdd:PRK05771 185 VLKELSDEVEEE---LKKLGferLELEEEGTpseLIREIKEELEEIEKERESLLEELKELAK 243
|
|
| C1_MRCKalpha |
cd20864 |
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ... |
988-1041 |
1.42e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410414 Cd Length: 60 Bit Score: 38.46 E-value: 1.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907160229 988 HRFNVGLNMRATKCAVCLD-TVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAE 1041
Cdd:cd20864 3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKAPSVCPIPPE 57
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
261-348 |
1.43e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 40.41 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 261 NREDSSEGIKKKLVEAEERRHSLE-NKVKRLETMERRENRLKDDIQTKSEQIQQMADKIL----ELEEKHREAQVSAqhL 335
Cdd:pfam00836 39 KKDSSLEEIQKKLEAAEERRKSLEaQKLKQLAEKREKEEEALQKADEENNNFSKMAEEKLkqkmEAYKENREAQIAA--L 116
|
90
....*....|...
gi 1907160229 336 EVHLKQKEQHYEE 348
Cdd:pfam00836 117 KEKLKEKEKHVEE 129
|
|
| C1_MRCK |
cd20809 |
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ... |
988-1039 |
1.47e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410359 Cd Length: 53 Bit Score: 38.02 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 988 HRFNVGLNMRATKCAVClDTVHFG--RQASKCLECQVMCHPKCSTCLPATCGLP 1039
Cdd:cd20809 1 HKFIVRTFSTPTKCNHC-TSLMVGlvRQGLVCEVCGYACHVSCADKAPQVCPVP 53
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
499-921 |
1.65e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 499 RQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITD----- 573
Cdd:PRK10929 2 RLIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNfpkls 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 574 --LEEQLNQLTED---------NAELNNQNFYLSKQLDEASGandeivQLRSEVDHLrREITEREMQLTsQKQTmEALKt 642
Cdd:PRK10929 82 aeLRQQLNNERDEprsvppnmsTDALEQEILQVSSQLLEKSR------QAQQEQDRA-REISDSLSQLP-QQQT-EARR- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 643 tctMLEEQVLDLEALNDELLEKErqwEAWRSVLGDEKSQFECRVRELQrmldtekQSRARADQRITESRQVVELAVKEHk 722
Cdd:PRK10929 152 ---QLNEIERRLQTLGTPNTPLA---QAQLTALQAESAALKALVDELE-------LAQLSANNRQELARLRSELAKKRS- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 723 AEILALQQALKEQklkaeslsdkLNDLEKKHA--------MLEMNA----RSLQQKLETERELKQrLLEEQAklqQQMDL 790
Cdd:PRK10929 218 QQLDAYLQALRNQ----------LNSQRQREAeralesteLLAEQSgdlpKSIVAQFKINRELSQ-ALNQQA---QRMDL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 791 ----QK---NHIFRLTQGLQ----------------EALdRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKL 847
Cdd:PRK10929 284 iasqQRqaaSQTLQVRQALNtlreqsqwlgvsnalgEAL-RAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 848 IDFLQAKMDQPAKKKKGLFsrrkeDPALPTQVPL------QYNELKLALEKEKARCAELEEALQKTRielrsareEAAHR 921
Cdd:PRK10929 363 RQIRQADGQPLTAEQNRIL-----DAQLRTQRELlnsllsGGDTLILELTKLKVANSQLEDALKEVN--------EATHR 429
|
|
| C1_TNS1_v |
cd20888 |
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ... |
988-1035 |
1.76e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410438 Cd Length: 57 Bit Score: 38.31 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 988 HRFNVGLNMRATKCAVCLDTVhfGRQASKCLECQVMCHPKC-----STCLPAT 1035
Cdd:cd20888 6 HTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCeakvaTPCVPAV 56
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-588 |
1.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 289 RLETMERREnRLKD--DIQTKSEqiqqMaDKILEleEKHREAQVSAQHLEV---HLKQKEQHYEEKIKVLDNQIKKDLAD 363
Cdd:PHA02562 146 QLSAPARRK-LVEDllDISVLSE----M-DKLNK--DKIRELNQQIQTLDMkidHIQQQIKTYNKNIEEQRKKNGENIAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 364 KEsleNMMQRHEEEAhekgkilseqkamiNAMDSKIRSLEQRIVELS-EANKLAANSSLFTQRNMKAQEEMISELRQQKF 442
Cdd:PHA02562 218 KQ---NKYDELVEEA--------------KTIKAEIEELTDELLNLVmDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 443 YLETQAGKLEAQNrkLEEQLEKIShqdhSDKSRLLELETRLREVSlEHEEQKLELKRQLTELQLSLQERESQLTALQAAR 522
Cdd:PHA02562 281 YEKGGVCPTCTQQ--ISEGPDRIT----KIKDKLKELQHSLEKLD-TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 523 AALESQLRQAKteleettaeaeeeiqaltahrDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAEL 588
Cdd:PHA02562 354 ITLVDKAKKVK---------------------AAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
206-804 |
1.83e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 206 EYSKLEKINAEQQLKIQELQEKLEKAVKASTE--------ATELLQNIRQAKERAERELEKLHNREDSSegikkkLVEAE 277
Cdd:pfam07111 87 ETSLQQKMRLEAQAMELDALAVAEKAGQAEAEglraalagAEMVRKNLEEGSQRELEEIQRLHQEQLSS------LTQAH 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 278 ERrhSLENKVKRLETMERRENRLKddiQTKSEQIQQMAdkileleekhrEAQVSAQHLEVHLKQKEQHYEEKIKVLDNqI 357
Cdd:pfam07111 161 EE--ALSSLTSKAEGLEKSLNSLE---TKRAGEAKQLA-----------EAQKEAELLRKQLSKTQEELEAQVTLVES-L 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 358 KKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLaansslftqrnmkaQEEMISEL 437
Cdd:pfam07111 224 RKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAL--------------QEEELTRK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 438 RQQKFYLETQAGKleaqnrkleeqleKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTE-------------- 503
Cdd:pfam07111 290 IQPSDSLEPEFPK-------------KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAElqeqvtsqsqeqai 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 504 LQLSLQERESQLTALQAARAALESQLRQAKTELEETTaeaeeeiQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTE 583
Cdd:pfam07111 357 LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQ-------QQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 584 DNAELNNQNFYLSKQLDEASG---ANDEIVQLRSEVDHLRREITEREMQLTSQkqtMEALKTTCTMLEEQV-LDLEALND 659
Cdd:pfam07111 430 RIPSLSNRLSYAVRKVHTIKGlmaRKVALAQLRQESCPPPPPAPPVDADLSLE---LEQLREERNRLDAELqLSAHLIQQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 660 ELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKA 739
Cdd:pfam07111 507 EVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEV 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 740 ES-----LSD---KLNDLEKKHAMLEMNARSLQQKLETERELKQ---RLLEEQAKLQQQmdlqknhifRLTQGLQE 804
Cdd:pfam07111 587 ETrlreqLSDtkrRLNEARREQAKAVVSLRQIQHRATQEKERNQelrRLQDEARKEEGQ---------RLARRVQE 653
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
109-344 |
1.89e-03 |
|
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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 109 QEYQAQVEEMRlmMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANecqhklmkVVSHPPRGDSGGTALDDLHKmq 188
Cdd:COG3206 159 EAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--------LVDLSEEAKLLLQQLSELES-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 189 ghagltsakdqgkpevgEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATE--LLQNIRQAKERAERELEKLHNR--ED 264
Cdd:COG3206 227 -----------------QLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARytPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 265 SSE--GIKKKLVEAEERRHSLENKVK-----RLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEV 337
Cdd:COG3206 290 HPDviALRAQIAALRAQLQQEAQRILasleaELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
....*..
gi 1907160229 338 HLKQKEQ 344
Cdd:COG3206 370 LLQRLEE 376
|
|
| C1_ScPKC1-like_rpt1 |
cd20822 |
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ... |
983-1036 |
1.95e-03 |
|
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410372 Cd Length: 52 Bit Score: 37.65 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907160229 983 HHNIPHRF-NVglnmraTKCAVCLDtvHFGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20822 3 HKFVQKQFyQI------MRCAVCGE--FLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
373-786 |
1.95e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 373 RHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELS-EANKLAANSSLFTQRNMKAQEE---MISELRQQKfYLETQA 448
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMArELAELNEAESDLEQDYQAASDHlnlVQTALRQQE-KIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 449 GKLEAQNRKLEEQLEKISHQDhsdkSRLLELETRLREVslehEEQKLELKRQLTELQLSLQERESQLTALQAARAALESq 528
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEAD----EQQEENEARAEAA----EEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALER- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 529 LRQAKTELEETTAEAEEEIQALTAHRDEIQrkfDALRnsctvitDLEEQLNqLTEDNAELNNQNFYLSKQL-------DE 601
Cdd:PRK04863 426 AKQLCGLPDLTADNAEDWLEEFQAKEQEAT---EELL-------SLEQKLS-VAQAAHSQFEQAYQLVRKIagevsrsEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 602 ASGANDEIVQLRSEVDH------LRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAwrsvL 675
Cdd:PRK04863 495 WDVARELLRRLREQRHLaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES----L 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 676 GDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVElavkehkaeilALQQaLKEQKLKAESLSDKLNDLEKKHAM 755
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD-----------ALAR-LREQSGEEFEDSQDVTEYMQQLLE 638
|
410 420 430
....*....|....*....|....*....|.
gi 1907160229 756 LEmnaRSLQQKLETERELKQRLLEEQAKLQQ 786
Cdd:PRK04863 639 RE---RELTVERDELAARKQALDEEIERLSQ 666
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
552-752 |
2.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 552 AHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNnqnfylsKQLDEASGA----NDEIVQLRSEVDHLRREITERE 627
Cdd:PHA02562 213 ENIARKQNKYDELVEE---AKTIKAEIEELTDELLNLV-------MDIEDPSAAlnklNTAAAKIKSKIEQFQKVIKMYE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 628 ---------MQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSvlgdeksqfecRVRELQRMLDTEKQ 698
Cdd:PHA02562 283 kggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK-----------KLLELKNKISTNKQ 351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907160229 699 SRARADQRITESRQVVELAVKE---HKAEILALQQALKEqklkaesLSDKLNDLEKK 752
Cdd:PHA02562 352 SLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDK-------IVKTKSELVKE 401
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
17-664 |
2.22e-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: 43.12 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 17 DKCHKMEQEMTRLHRRVSEVEavlsQKEVELKASETQRSLLEQDLATYITEcsslkrsleqarmEVSQEDDKALQLLHDI 96
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIE----KDKTSLEEVKGINLSYGKNLGKLFLE-------------KIDEEKKKSEHMIKAM 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 97 REQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVsarrrsDLYESELRESRLAAEEFKRKANECQHKLMKVVshppRGDS 176
Cdd:TIGR01612 1246 EAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETF------NISHDDDKDHHIISKKHDENISDIREKSLKII----EDFS 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 177 GGTALDDLHKMQGHAGLTSAKDQGkpEVGEYskLEKI-NAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERE 255
Cdd:TIGR01612 1316 EESDINDIKKELQKNLLDAQKHNS--DINLY--LNEIaNIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKL 1391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 256 LEKLhnREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHL 335
Cdd:TIGR01612 1392 IKKI--KDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHI 1469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 336 evhLKQKEQHYEEKIKVLDNQIKKDLaDKEslenmmQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKL 415
Cdd:TIGR01612 1470 ---LKIKKDNATNDHDFNINELKEHI-DKS------KGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKF 1539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 416 AansslftqRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEqlEKISHQD---HSDKSrlleletrlrevslehee 492
Cdd:TIGR01612 1540 A--------KTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKK--EKFRIEDdaaKNDKS------------------ 1591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 493 qklelKRQLTELQLSLQERESQLTALQAARAALESQLRQAkteleettaeaeeeiqaltahrDEIQRKFDALR--NSCTV 570
Cdd:TIGR01612 1592 -----NKAAIDIQLSLENFENKFLKISDIKKKINDCLKET----------------------ESIEKKISSFSidSQDTE 1644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 571 ITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRRE----ITEREMQLT-SQKQTMEALKTTCT 645
Cdd:TIGR01612 1645 LKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigIIEKIKEIAiANKEEIESIKELIE 1724
|
650 660
....*....|....*....|....*.
gi 1907160229 646 MLEEQVL------DLEALN-DELLEK 664
Cdd:TIGR01612 1725 PTIENLIssfntnDLEGIDpNEKLEE 1750
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
703-839 |
2.63e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 703 ADQRITESRQVVELAVKEHKAEILALQQALKEqklKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQA 782
Cdd:PRK12704 62 AKEEIHKLRNEFEKELRERRNELQKLEKRLLQ---KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 783 KLQQQMDlqknHIFRLTQglQEAldRADLLKTERSDLEYQlenIQVLY--SHEKVKMEG 839
Cdd:PRK12704 139 EQLQELE----RISGLTA--EEA--KEILLEKVEEEARHE---AAVLIkeIEEEAKEEA 186
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
601-921 |
3.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 601 EASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEqvlDLEALNDEL---LEKERQWEAWRSVLGD 677
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ---DYQAASDHLnlvQTALRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 678 eksqfecrVRELQRMLDTEKQSRARADQRITESRQVVELA---VKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHA 754
Cdd:PRK04863 357 --------LEELEERLEEQNEVVEEADEQQEENEARAEAAeeeVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 755 ML---EMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQ------------EALDRADLLKTERSDL 819
Cdd:PRK04863 429 LCglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevsrsEAWDVARELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 820 EYQLENIQVLYSHEKvKMEGTISQQTKLIDFLQAkmdqpAKKKkglFSRRKEDPALPTQVPLQYNELKLALEKEKARCAE 899
Cdd:PRK04863 509 RHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAE-----FCKR---LGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340
....*....|....*....|..
gi 1907160229 900 LEEALQKTRIELRSAREEAAHR 921
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAAR 601
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
81-661 |
3.44e-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: 42.35 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 81 EVSQEDDKALQLLHDIREQSRKLQEIKEQEyQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKanEC 160
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKS-ENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKK--NI 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 161 QHKLMKVVSHPPRGDSGGTALDDLHKMQghagLTSAKDQGKpevgeySKLEKINAEQqlkiqelqEKLEKAVKASTEATE 240
Cdd:TIGR01612 1189 YDEIKKLLNEIAEIEKDKTSLEEVKGIN----LSYGKNLGK------LFLEKIDEEK--------KKSEHMIKAMEAYIE 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 241 LLQNIRQAKERAERELeklhnredSSEGIKKKLVEAEERRHSlenKVKRLETMERRENRLKDDIQTKSEQIQQ------- 313
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEM--------GIEMDIKAEMETFNISHD---DDKDHHIISKKHDENISDIREKSLKIIEdfseesd 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 314 MADKILELEEKHREAQVSAQHLEVHLKQ------------------KEQHYEEKIKVLDNQIKKDLADKESLENMMQRHE 375
Cdd:TIGR01612 1320 INDIKKELQKNLLDAQKHNSDINLYLNEianiynilklnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 376 EEAHEKGKILSEQKAM-INAMDSKIRSLEQRIVE-----------LSEANK----------LAANSSLFTQRNMK--AQE 431
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKdIDECIKKIKELKNHILSeesnidtyfknADENNEnvlllfknieMADNKSQHILKIKKdnATN 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 432 EM---ISELRQQKfyleTQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKleLKRQLTELQLSL 508
Cdd:TIGR01612 1480 DHdfnINELKEHI----DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAK--TKKDSEIIIKEI 1553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 509 QERESQLTaLQAARAalESQLRQAKTELEETTAEAEEEIQALTAHRDeIQRKFDALRNSCTVITDLEEQLNQ-LTEDNAe 587
Cdd:TIGR01612 1554 KDAHKKFI-LEAEKS--EQKIKEIKKEKFRIEDDAAKNDKSNKAAID-IQLSLENFENKFLKISDIKKKINDcLKETES- 1628
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907160229 588 lnnqnfyLSKQLDEASgandeivqlrseVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDEL 661
Cdd:TIGR01612 1629 -------IEKKISSFS------------IDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEI 1683
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
612-791 |
4.37e-03 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 41.58 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 612 LRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLE-----EQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFEcRV 686
Cdd:TIGR03007 202 YYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEpvllaGSSVANSELDGRIEALEKQLDALRLRYTDKHPDVI-AT 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 687 RELQRMLDTEKQSRARADQRITESR-------QVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEmn 759
Cdd:TIGR03007 281 KREIAQLEEQKEEEGSAKNGGPERGeianpvyQQLQIELAEAEAEIASLEARVAELTARIERLESLLRTIPEVEAELT-- 358
|
170 180 190
....*....|....*....|....*....|....
gi 1907160229 760 arSLQQKLETERELKQRLLE--EQAKLQQQMDLQ 791
Cdd:TIGR03007 359 --QLNRDYEVNKSNYEQLLTrrESAEVSKQMEVQ 390
|
|
| C1_PKD_rpt2 |
cd20796 |
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ... |
987-1036 |
4.69e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410346 Cd Length: 54 Bit Score: 36.88 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 987 PHRFNVGLNMRATKCAVCLDTVH-FGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20796 1 PHTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
300-496 |
4.80e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 300 LKDDIQTKS-------EQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQ 372
Cdd:PHA02562 179 LNQQIQTLDmkidhiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 373 R----------------HEEEAHEKGKI-------LSEQKAMINAMDSKIRSLEQRIVELSEA-NKLAANSSLFTQRNMK 428
Cdd:PHA02562 259 KlntaaakikskieqfqKVIKMYEKGGVcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAiDELEEIMDEFNEQSKK 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 429 AQeEMISELRQQKfyleTQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLE 496
Cdd:PHA02562 339 LL-ELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| C1_TNS2 |
cd20887 |
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ... |
987-1039 |
4.80e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410437 Cd Length: 53 Bit Score: 36.68 E-value: 4.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 987 PHRFNVGLNMRATKCAVCLDTVhfGRQASKCLECQVMCHPKCSTCLPATCGLP 1039
Cdd:cd20887 2 PHSFKEKTFKKKRACAVCREPV--GGQGLVCRVCKVASHKKCEAKVTSACQPP 52
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
205-331 |
5.13e-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: 40.29 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 205 GEYSKLEKINAEQQLKIQELQEKLEKavkasteATELLQNIRQAKE--RAERELEKLHNREDSSEgikKKLVEAEERRHS 282
Cdd:COG1579 52 TELEDLEKEIKRLELEIEEVEARIKK-------YEEQLGNVRNNKEyeALQKEIESLKRRISDLE---DEILELMERIEE 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907160229 283 LENKVKRLET-MERRENRLKDDIQTKSEQIQQMADKILELEEKhREAQVS 331
Cdd:COG1579 122 LEEELAELEAeLAELEAELEEKKAELDEELAELEAELEELEAE-REELAA 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
719-846 |
5.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 719 KEHKAEILAlQQALKEQKLKAESLsdklndleKKHAMLEMNARSLQQKLETERELKQRLLEEQA---KLQQQMDLQKNHI 795
Cdd:PRK12704 32 KIKEAEEEA-KRILEEAKKEAEAI--------KKEALLEAKEEIHKLRNEFEKELRERRNELQKlekRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907160229 796 FRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEgTISQQTK 846
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE-RISGLTA 152
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
347-529 |
5.32e-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: 40.29 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 347 EEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRivelseanklaanssLFTQRN 426
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---------------LGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 427 MKAQEEMISELRqqkfYLETQAGKLEAQNRKLEEQLEkishqdhsdksrllELETRLREVSLEHEEQKLELKRQLTELQL 506
Cdd:COG1579 88 NKEYEALQKEIE----SLKRRISDLEDEILELMERIE--------------ELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|...
gi 1907160229 507 SLQERESQLTALQAARAALESQL 529
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
220-349 |
5.43e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 220 KIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIK----KKLVEA-EERRHSLENKVKRLETME 294
Cdd:smart00787 152 NLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDptelDRAKEKlKKLLQEIMIKVKKLEELE 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907160229 295 RRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEK 349
Cdd:smart00787 232 EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
10-376 |
5.50e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 10 KELQDSQDKCHKMEQEMTRLHRRVS--------EVEAVLSQKEVELKASETQRSlleqDLATYITECSSLKRSLEQARME 81
Cdd:PLN03229 376 IAINENMDELGKMDTEELLKHRMLKfrkiggfqEGVPVDPERKVNMKKREAVKT----PVRELEGEVEKLKEQILKAKES 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 82 VSQEDDKALQllhdirEQSRKLQEIKEQEYQAQVEEMRLM--MNQLEEDLVSARRRSDLYESELresrlaAEEFKRKANE 159
Cdd:PLN03229 452 SSKPSELALN------EMIEKLKKEIDLEYTEAVIAMGLQerLENLREEFSKANSQDQLMHPVL------MEKIEKLKDE 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 160 CQHKLmkvvSHPPRGDSGGTALDDLHKMQGHAGLTSAKDQG---KPEVGEYSKLEKINAEQQLKIQELQEKLEKAvKAST 236
Cdd:PLN03229 520 FNKRL----SRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAeklKAEINKKFKEVMDRPEIKEKMEALKAEVASS-GASS 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 237 EAT---ELLQNIRQAKERAERELEKLHNRED-SSEGIKKKLVEAEERR--HSLENKVKRLetmerrenrlKDDIQTKSEQ 310
Cdd:PLN03229 595 GDElddDLKEKVEKMKKEIELELAGVLKSMGlEVIGVTKKNKDTAEQTppPNLQEKIESL----------NEEINKKIER 664
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 311 IQQMADKILELEEKHREAQVSAQHLEVHLKqkeqhyeEKIKVLDNQIKKDLADKESLENMMQRHEE 376
Cdd:PLN03229 665 VIRSSDLKSKIELLKLEVAKASKTPDVTEK-------EKIEALEQQIKQKIAEALNSSELKEKFEE 723
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
240-340 |
5.94e-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: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 240 ELLQNIRQAKERAERELEKLhnREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKIL 319
Cdd:COG0542 411 EELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|.
gi 1907160229 320 ELEEKHREAQVSAQHLEVHLK 340
Cdd:COG0542 489 ELEKELAELEEELAELAPLLR 509
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
472-789 |
6.03e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 472 DKSRLLELETRLREVSL-EHEEQKLELKRQLTEL-QLSLQERESQLTALQAARAALESQLRQAkteleettaeaeeeiqa 549
Cdd:pfam00038 18 DKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNL----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 550 ltahRDEIQRkfdaLRNSctvitdLEEQLNQLTEDNAELNNqnfyLSKQLDEASGANDE----IVQLRSEVDHLRR---- 621
Cdd:pfam00038 81 ----RLAAED----FRQK------YEDELNLRTSAENDLVG----LRKDLDEATLARVDleakIESLKEELAFLKKnhee 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 622 EITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQweawrsvlgDEKSQFECRVRELQRMLDTEKQSRA 701
Cdd:pfam00038 143 EVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNRE---------EAEEWYQSKLEELQQAAARNGDALR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 702 RADQRITESRQVVElavkehkaeilALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETE-RELKQRLLEE 780
Cdd:pfam00038 214 SAKEEITELRRTIQ-----------SLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAElQETRQEMARQ 282
|
....*....
gi 1907160229 781 QAKLQQQMD 789
Cdd:pfam00038 283 LREYQELLN 291
|
|
| C1_Munc13 |
cd20807 |
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ... |
988-1036 |
6.30e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene family encodes a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-1 is a component of presynaptic active zones in which it acts as an essential synaptic vesicle priming protein. Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410357 Cd Length: 53 Bit Score: 36.30 E-value: 6.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907160229 988 HRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 1036
Cdd:cd20807 1 HNFEVWTATTPTYCYECEGLLwGIARQGVRCTECGVKCHEKCKDLLNADC 50
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
611-931 |
6.87e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 611 QLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQvldlealndELLEKERQWEAWRSVLGDEKSQFE------- 683
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ---------ERMAMERERELERIRQEERKRELErirqeei 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 684 ----CRVRELQRMLDTEKQSRARADQRITESRQvVELAVKEHkaeilalQQALKEQKLKAESLSDKlndlekkhamlEMN 759
Cdd:pfam17380 371 ameiSRMRELERLQMERQQKNERVRQELEAARK-VKILEEER-------QRKIQQQKVEMEQIRAE-----------QEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 760 ARSLQ-QKLETERELK-QRLLEEQAKLQQQMDlqknhifRLTQglQEALDRADLLKTERSDLEYQL---ENIQVLYSHEK 834
Cdd:pfam17380 432 ARQREvRRLEEERAREmERVRLEEQERQQQVE-------RLRQ--QEEERKRKKLELEKEKRDRKRaeeQRRKILEKELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 835 VKMEGTISQQTKLiDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPL----QYNELKLALEKEKARCaeleEALQKTRIE 910
Cdd:pfam17380 503 ERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRL----EAMEREREM 577
|
330 340
....*....|....*....|.
gi 1907160229 911 LRSAREEAAHRKATDHPHPST 931
Cdd:pfam17380 578 MRQIVESEKARAEYEATTPIT 598
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
203-822 |
8.04e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 203 EVGEYSKLEKINaEQQLKIQELQEKLEKAVKASTEatellqnirqakeraerELEKLHNREDSSEGIKKKLVEAEERRHS 282
Cdd:COG5022 949 EYVKLPELNKLH-EVESKLKETSEEYEDLLKKSTI-----------------LVREGNKANSELKNFKKELAELSKQYGA 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 283 LENKVKRLETMERRENRLKDDIQTKSEqiqqmadkilELEEKHREAQVsaQHLEVHLKQKEQHYEEKIKVLDNQIkkdla 362
Cdd:COG5022 1011 LQESTKQLKELPVEVAELQSASKIISS----------ESTELSILKPL--QKLKGLLLLENNQLQARYKALKLRR----- 1073
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 363 dkeslenmmqrheeeahEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANklAANSSLFTQRNMKAqeemiselrQQKF 442
Cdd:COG5022 1074 -----------------ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRN--LVKPANVLQFIVAQ---------MIKL 1125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 443 YLETQAGKLEAQNRKLEEQLEKishqdhSDKSRLLELETRLREVSLEHEEQKLELKRQltelqlsLQERESQLTALQAAR 522
Cdd:COG5022 1126 NLLQEISKFLSQLVNTLEPVFQ------KLSVLQLELDGLFWEANLEALPSPPPFAAL-------SEKRLYQSALYDEKS 1192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 523 AALESQLRQAKTELeettaeaeeeiqaltahrDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEA 602
Cdd:COG5022 1193 KLSSSEVNDLKNEL------------------IALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPA 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 603 SGANDEIVQLRSEVDHLR----REITEREMQLTSQKQTM-----EALKTTCTMLEEQVLDLEALNDELLEkerQWeawrs 673
Cdd:COG5022 1255 SMSNEKLLSLLNSIDNLLssykLEEEVLPATINSLLQYInvglfNALRTKASSLRWKSATEVNYNSEELD---DW----- 1326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 674 vlgdeksqfeCRVRELQRmLDTEKQSraradqrITESRQVVELAVK--EHKAEILALQQALKE---QKLKAE-SLSDKLN 747
Cdd:COG5022 1327 ----------CREFEISD-VDEELEE-------LIQAVKVLQLLKDdlNKLDELLDACYSLNPaeiQNLKSRyDPADKEN 1388
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 748 DLEKKHaMLEMNARSLQQKLETERELKQRLleeQAKLQQQMDLQKNHIFRLTQGLQ--EALDR--ADLLKTERSDLEYQ 822
Cdd:COG5022 1389 NLPKEI-LKKIEALLIKQELQLSLEGKDET---EVHLSEIFSEEKSLISLDRNSIYkeEVLSSlsALLTKEKIALLDRK 1463
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
269-456 |
8.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 269 IKKKLVEAEERRhslenkVKRLETMERRENRLKDDIqtKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEE 348
Cdd:PRK12704 29 AEAKIKEAEEEA------KRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 349 kikvldnqiKKDLADKEslENMMQRHEEEAHEKGKILSEQKAMInamDSKIRSLEQRIVELSEANKLAANSSLFTQRNMK 428
Cdd:PRK12704 101 ---------KLELLEKR--EEELEKKEKELEQKQQELEKKEEEL---EELIEEQLQELERISGLTAEEAKEILLEKVEEE 166
|
170 180
....*....|....*....|....*...
gi 1907160229 429 AQEEMISELRQqkfyLETQAgKLEAQNR 456
Cdd:PRK12704 167 ARHEAAVLIKE----IEEEA-KEEADKK 189
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
508-664 |
8.79e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.14 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 508 LQERESQLTALQAA-RAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTvitDLEEQLNQLTEDNA 586
Cdd:pfam08614 12 LLDRTALLEAENAKlQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRG---ELAQRLVDLNEELQ 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160229 587 ELNNQNFYLSKQLDEASganDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEK 664
Cdd:pfam08614 89 ELEKKLREDERRLAALE---AERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRELVER 163
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
423-630 |
9.67e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.12 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 423 TQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQL---EKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKR 499
Cdd:pfam15619 2 TQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQkrqEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 500 QLTELQLSLQERESQLTALQAARAALEsQLRQAKTEleettaeaeeeiqaltAHRDEIQRKFDALRNsctvITDLEEQLN 579
Cdd:pfam15619 82 KERDLERKLKEKEAELLRLRDQLKRLE-KLSEDKNL----------------AEREELQKKLEQLEA----KLEDKDEKI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907160229 580 QLTEDNAELNNQNF--YLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQL 630
Cdd:pfam15619 141 QDLERKLELENKSFrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
427-789 |
9.71e-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: 40.65 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 427 MKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEkishqdhsdksrllELETRLREVSLEHEEqkleLKRQLTELQL 506
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVA--------------ELKEELRQSREKHEE----LEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 507 SLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNA 586
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 587 ELNNQNFYLSKQLDEASganDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDEL----- 661
Cdd:pfam07888 189 SLSKEFQELRNSLAQRD---TQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELssmaa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 662 LEKERQWEAWRSVLgdEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKE-----QK 736
Cdd:pfam07888 266 QRDRTQAELHQARL--QAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerEK 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160229 737 LKAESLSDKLNDL----EKKHAMLEMNA--RSLQQKLETERELKQRLLEEQAKLQQQMD 789
Cdd:pfam07888 344 LEVELGREKDCNRvqlsESRRELQELKAslRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
492-707 |
9.81e-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: 39.52 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 492 EQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeeeiQALTAHRDEIQrkfdalrnsctvi 571
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALE--------------ARLEAAKTELE------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 572 tDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGaNDEIVQLRSEVDHLRREITEREMQLtsqKQTMEAlkttctmleeqv 651
Cdd:COG1579 56 -DLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEIESLKRRISDLEDEI---LELMER------------ 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907160229 652 ldLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRI 707
Cdd:COG1579 119 --IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
732-923 |
9.89e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 732 LKEQKLKAE---SLSDKLNDLEKKHAMLEMnaRSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIfrltQGLQEALDR 808
Cdd:COG1196 205 LERQAEKAEryrELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 809 ADLLKTERSDLEYQLENiqvlyshEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPAlptqvplqynELKL 888
Cdd:COG1196 279 LELELEEAQAEEYELLA-------ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----------ELEE 341
|
170 180 190
....*....|....*....|....*....|....*
gi 1907160229 889 ALEKEKARCAELEEAlQKTRIELRSAREEAAHRKA 923
Cdd:COG1196 342 LEEELEEAEEELEEA-EAELAEAEEALLEAEAELA 375
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
301-667 |
9.91e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 40.48 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 301 KDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHE 380
Cdd:COG2770 264 KDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 381 KGKILSEQKAMINAMDSKIRSLEQRIVELSEAnklaansslftQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEE 460
Cdd:COG2770 344 LLLAADLLLALALAALLLLLALELLLEAELLV-----------LLALEALALEAELAAVLALLAALAAALLLLELALEEL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 461 QLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETT 540
Cdd:COG2770 413 VLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLL 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160229 541 AEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLR 620
Cdd:COG2770 493 EEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALL 572
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907160229 621 REITEREMQLTSQKQTMEALKTTCTMLEEQVLDLEALNDELLEKERQ 667
Cdd:COG2770 573 LAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEV 619
|
|
|