|
Name |
Accession |
Description |
Interval |
E-value |
| CNH |
smart00036 |
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2; |
1187-1483 |
1.05e-78 |
|
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
Pssm-ID: 214481 Cd Length: 302 Bit Score: 262.67 E-value: 1.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1187 DMNCTLPFSDQ--VVLVGTEEGLYALNVLK--NSLTHIPGIGAVFQIYIIKDLEKLLMIAGE---ERALCLVDVKKVKQS 1259
Cdd:smart00036 2 TAKWNHPITCDgkWLLVGTEEGLYVLNISDqpGTLEKLIGRRSVTQIWVLEENNVLLMISGKkpqLYSHPLSALVEKKEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1260 LAQSHLPAQPDVSPNiFEAVKGCHLFAAGKIENSLCICAAMPSKVVIL-RYNDNLSKYCIR-----KEIETSEPCSCIHF 1333
Cdd:smart00036 82 LGSARLVIRKNVLTK-IPDVKGCHLCAVVNGKRSLFLCVALQSSVVLLqWYNPLKKFKLFKskflfPLISPVPVFVELVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1334 TNY---SILIGTNKfYEIDMKQYTLDeFLDKNDHSLAPAVFASSSNSFPVSIVQANsagqreEYLLCFHEFGVFVDSYG- 1409
Cdd:smart00036 161 SSFerpGICIGSDK-GGGDVVQFHES-LVSKEDLSLPFLSEETSLKPISVVQVPRD------EVLLCYDEFGVFVNLYGk 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 1410 RRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSLGSPARAylEIPNPRYLGPaiSSGAIYLASSY 1483
Cdd:smart00036 233 RRSRNPILHWEFMPESFAYHSPYLLAFHDNGIEIRSIKTGELLQELADR--ETRKIRLLGS--SDRKILLSSSP 302
|
|
| CNH |
pfam00780 |
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ... |
1195-1447 |
3.45e-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 Unpublished observations.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: 230.60 E-value: 3.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1195 SDQVVLVGTEEGLYALNV-LKNSLTHIPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKkvkqSLAQSHLPAQPDVSP 1273
Cdd:pfam00780 1 GGQNLLLGTEEGLYVLNRsGPREPVRIIDKKRVTQLAVLEEFNLLLLLSGKDKRLYVYPLS----ALDSREENDRKDAAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1274 NIFEAVKGCHLFAAGKIENSLCICAAMPSKVVILRYNDNLS-KYCIRKEIETSEPCSCIHFTNYSILIGTNKFYE-IDMK 1351
Cdd:pfam00780 77 NKLPETKGCHFFKVGRHSNGRFLVVAVKRTIKLLEWYEPLLdKFRKFKEFYLPSPPVSIELLKSKLCVGCAKGFEiVSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1352 QYTLDEFLdkndhsLAPAVFASSSNSFPVSIVQANsagqREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREP 1431
Cdd:pfam00780 157 SKATESLL------TSLLFANRQENLKPLAVVRLD----RSEFLLCYNEFGVYVNLQGRRSRPWEIEWEGAPEAVAYLYP 226
|
250
....*....|....*.
gi 1039770408 1432 YLFVTHFNSLEVIEIQ 1447
Cdd:pfam00780 227 YLLAFHDNFIEIRDVE 242
|
|
| CRIK |
cd20814 |
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ... |
938-993 |
4.00e-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: 136.61 E-value: 4.00e-38
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 938 HNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLP 993
Cdd:cd20814 1 HNIPHRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTCGLP 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
202-792 |
5.50e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.03 E-value: 5.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 202 AEQQLKIQELQEKLEKAvkastEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLE 281
Cdd:COG1196 209 AEKAERYRELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 282 VHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLA 361
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 362 ANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEkishqdhsdksRLLELETRLREVSLEHEEQKLE 441
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE-----------ALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 442 LKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeEEIQALTAHRDEIQRKFDALRnsctvitdLEE 521
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL-----------EEAALLEAALAELLEELAEAA--------ARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 522 QLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTT---- 597
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagr 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 598 CTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKA 677
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 678 EILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQ 757
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590
....*....|....*....|....*....|....*
gi 1039770408 758 EALDRADLLKTERSDLEYQLENIQVLYSHEKVKME 792
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-859 |
5.36e-22 |
|
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: 103.98 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 72 EDDKALQLLHDIREQSRKLQEIKEQ--------------EYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAA 137
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERYKELKAElrelelallvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 138 EEFKRKANECQHKLmkvvshpprgdsggtalddlhkmqghagltsakdqgkpevgeYSKLEKINAEQQlKIQELQEKLEK 217
Cdd:TIGR02168 277 SELEEEIEELQKEL------------------------------------------YALANEISRLEQ-QKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 218 AVKASTEATELLQNIRQAKERAERELEKLHNREDSSEgikkklVEAEELEEKHREAQVSAQHLEVHLKQKEQHYE----- 292
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLEtlrsk 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 293 -----EKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQK-----AMINAMDSKIRSLEQRIVELSEANKLAA 362
Cdd:TIGR02168 388 vaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 363 NSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKiSHQDHSDKSRLLEL-------ETRLrEVSLEH 435
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELisvdegyEAAI-EAALGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 436 EEQKLELKRQLTELQL--SLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSC 513
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 514 TVITDLEEQLNQLTEDNAELNnqNFYLSKQLDEASG--------ANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSA 585
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYR--IVTLDGDLVRPGGvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 586 PDLQT-----MEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQR 660
Cdd:TIGR02168 704 RKELEeleeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 661 ITESRQVVELAVKEHKA---EILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAK 737
Cdd:TIGR02168 784 IEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 738 LQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIqvlySHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKK 817
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1039770408 818 GLFSRRKEDPALPTQVPLQ-YNELKLALEKEKARCAELEEALQ 859
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEAlENKIEDDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-774 |
1.18e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNRE--------DSSEGIKKKLVEAE 264
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelaRLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 265 ELEEKHREAQVSAQHLEvhlkQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEkgkILSEQKAMINAMDSKI 344
Cdd:COG1196 313 ELEERLEELEEELAELE----EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 345 RSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIshqdhsdkSRLLEL 424
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE--------AELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 425 ETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteLEETTAEAEEEIQALTAHRDEIQR 504
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK--AALLLAGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 505 KFDALRNSctvitDLEEQLNQLTEDNAELNNQNFYLSKQLDEASG--ANDEIVQLRSEVDHLRREITEREMQLTSQKQAQ 582
Cdd:COG1196 536 YEAALEAA-----LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 583 LSAPDLQTMEAlkttctmLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFEcRVRELQRMLDTEKQSRARADQRIT 662
Cdd:COG1196 611 ADARYYVLGDT-------LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA-GGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 663 ESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQM 742
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1039770408 743 DLQKNHIFRLTQGLQE-------ALD-------RADLLKTERSDLE 774
Cdd:COG1196 763 EELERELERLEREIEAlgpvnllAIEeyeeleeRYDFLSEQREDLE 808
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-873 |
4.67e-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: 94.35 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 199 KINAEQQLKIQELQEKLEKAVKAS-----TEATELLQNIRQAKERAERELE----KLHNREDSSEGIKKKLVEAEELEEK 269
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 270 HREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQ 349
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 350 RIVELSEANKlaansslftqrnmkAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLr 429
Cdd:TIGR02168 366 ELEELESRLE--------------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 430 evsleHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeeeiQALTAHRDEIQRkfdaL 509
Cdd:TIGR02168 431 -----EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE--------------QALDAAERELAQ----L 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 510 RNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASgandEIVQLRSEvdhLRREITE-----REMQLTSQKQAQLS 584
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS----ELISVDEG---YEAAIEAalggrLQAVVVENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 585 APDLQTmEALKTTCTMLEEQVL---DLEALNDELLEKERQWEAWRSVLGDEKSQFEcrvRELQRMLD-----------TE 650
Cdd:TIGR02168 561 AIAFLK-QNELGRVTFLPLDSIkgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLR---KALSYLLGgvlvvddldnaLE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 651 KQSRARADQRIT-------ESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLemnaRSLQQKLET 723
Cdd:TIGR02168 637 LAKKLRPGYRIVtldgdlvRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL----RKELEELEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 724 ERELKQRLLEEqakLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLEniqvLYSHEKVKMEGTISQQTKLID 803
Cdd:TIGR02168 713 ELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE----ELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 804 FLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAA 873
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-705 |
7.34e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 57 SLKRSLEQARmevsqeddKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLA 136
Cdd:COG1196 204 PLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 137 AEEFKRKANECQHKLMKVVShpprgdsggtalddlhkmqghagltsakdqgkpevgEYSKLEKINAEQQLKIQELQEKLE 216
Cdd:COG1196 276 LEELELELEEAQAEEYELLA------------------------------------ELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 217 KAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEgikKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIK 296
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 297 VLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQE 376
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 377 EMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLE------LKRQLTELQ 450
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEaalaaaLQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 451 LSLQERESQLTALQAARAA---LESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLT 527
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 528 EDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSApdlqtmealkttctmLEEQVLD 607
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE---------------LEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 608 LEALNDELLEKERQWEAWRSVLGDEKSQFE-CRVRELQRMLDTEKQSRARADQRITE--SRQVVELAVKEHKAEI----- 679
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEaEREELLEELLEEEELLEEEALEELPEppDLEELERELERLEREIealgp 781
|
650 660
....*....|....*....|....*....
gi 1039770408 680 ---LALQQaLKEQKLKAESLSDKLNDLEK 705
Cdd:COG1196 782 vnlLAIEE-YEELEERYDFLSEQREDLEE 809
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-571 |
9.67e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.12 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLhnredssegiKKKLVEAEELEEKHRE 272
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----------RKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIV 352
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 353 ELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVs 432
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL- 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 433 lehEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRqakteleettAEAEEEIQALTAHRDEIQRKFDALRNS 512
Cdd:TIGR02168 907 ---ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----------EEYSLTLEEAEALENKIEDDEEEARRR 973
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 513 ctvITDLEEQLNQLTEDN-------AELNNQNFYLSKQLDEASGAndeIVQLRSEVDHLRREITER 571
Cdd:TIGR02168 974 ---LKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKEDLTEA---KETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-774 |
1.42e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 5 EEAMMEQEMTRLHRRVSEVEAVLSQKEVElKASETQRSllEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIR 84
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKA--EDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 85 --EQSRKLQEIKEQEYQAQVEEMRlmmnQLEEdlvsARRrsdlYESELR-ESRLAAEEFKRKANECQHklmkvvSHPPRG 161
Cdd:PTZ00121 1189 kaEELRKAEDARKAEAARKAEEER----KAEE----ARK----AEDAKKaEAVKKAEEAKKDAEEAKK------AEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 162 DSGGTALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKI-------NAEQQLKIQELQEKLEKAVKASteatELLQNIRQ 234
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKkkadeakKAEEKKKADEAKKKAEEAKKAD----EAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 235 AKERAERELEKLHNREDSSEGIKKklveaeELEEKHREAQVSAQHLEVHLKQKEqhyEEKIKVldNQIKKDLADKESLEN 314
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKA------EAEAAADEAEAAEEKAEAAEKKKE---EAKKKA--DAAKKKAEEKKKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 315 MMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVElsEANKLAANSSLFTQRNMKAQEEMISELRQQKfylETQAG 394
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 395 KLEAQNRKLEE--QLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESqltalQAARAALEs 472
Cdd:PTZ00121 1471 KADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA-----DEAKKAEE- 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 473 qLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvitdleEQLNQLTEDNAELNNQNFYLSKQLDEASGAND 552
Cdd:PTZ00121 1545 -KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA--------EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 553 EIVQLRSEvdHLRREITEREMQLTSQKQaqlSAPDLQTMEALKTTctmLEEQVLDLEALNDELLEKERQWEAWRSVLGDE 632
Cdd:PTZ00121 1616 EEAKIKAE--ELKKAEEEKKKVEQLKKK---EAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 633 KSQFECRVRELQRMLDTEkQSRARADQRITESRQVVElAVKEHKAEILALQQALKEQKLKAESLsdKLNDLEKK---HAM 709
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKkiaHLK 1763
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 710 LEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLE 774
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
22-877 |
7.47e-17 |
|
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: 86.95 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 22 EVEAVLSQKEVElkasetqRSLLEQDLATYItecssLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEyqaq 101
Cdd:pfam02463 143 KIEIIAMMKPER-------RLEIEEEAAGSR-----LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 102 veemrlmmnqleedlvsarrrsdlyESELRESRLAAEEFKRKANECQHKLMKVVshpprgdsgGTALDDLHKMQGHAGLT 181
Cdd:pfam02463 207 -------------------------KKALEYYQLKEKLELEEEYLLYLDYLKLN---------EERIDLLQELLRDEQEE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 182 SAKDQGKPEVGEySKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLV 261
Cdd:pfam02463 253 IESSKQEIEKEE-EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 262 ----EAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAmI 337
Cdd:pfam02463 332 kekeEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL-L 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 338 NAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSD 417
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 418 KSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQER---------ESQLTALQAARAALESQLRQAKTELEETTAEA 488
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGrlgdlgvavENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 489 EEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSkqldEASGANDEIVQLRSEVDHLRREI 568
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK----VVEGILKDTELTKLKESAKAKES 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 569 TEREMQLTSQKQAQLSapdLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLD 648
Cdd:pfam02463 647 GLRKGVSLEEGLAEKS---EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 649 TEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKL---ETER 725
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkaqEEEL 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 726 ELKQRLLEEQAKLQQQMDLQKNH---------------IFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVK 790
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQeekikeeeleelaleLKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 791 -------MEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRI 863
Cdd:pfam02463 884 lkdelesKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
890
....*....|....
gi 1039770408 864 ELRSAREEAAHRKA 877
Cdd:pfam02463 964 RLLLAKEELGKVNL 977
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
193-729 |
3.57e-16 |
|
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: 84.30 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKEraerELEKlhnredssegiKKKLVEAEELEEKHRE 272
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE----ELEN-----------ELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEVHLK-QKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSE-QKAMINAMDSK---IRSL 347
Cdd:TIGR04523 190 DKIKNKLLKLELLlSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQLKDEQnkiKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 348 EQRIVELSEANKLAANsslfTQRNMKAQEEMISELRQQKF-----YLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLL 422
Cdd:TIGR04523 270 SEKQKELEQNNKKIKE----LEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 423 ELETRLREVSLEHEEQKLELKRQLTELQLSLQERES---QLTALQAARAALESQLRQAKteleETTAEAEEEIQALTAHR 499
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSykqEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEK 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 500 DEIQRKFDALRNSctvITDLEEQLNQLTEDNAEL----NNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQL 575
Cdd:TIGR04523 422 ELLEKEIERLKET---IIKNNSEIKDLTNQDSVKeliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 576 tsqkqaqlsapdlqtmEALKTTCTMLEEQVLDLEALNDELLEKERQWEAwrsvlgdEKSQFECRVRELQRMLDTEKQSRA 655
Cdd:TIGR04523 499 ----------------KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES-------EKKEKESKISDLEDELNKDDFELK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 656 RA---------DQRITESRQV----------VELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARS 716
Cdd:TIGR04523 556 KEnlekeidekNKEIEELKQTqkslkkkqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
570
....*....|....
gi 1039770408 717 LQQKLET-ERELKQ 729
Cdd:TIGR04523 636 IKSKKNKlKQEVKQ 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-723 |
3.97e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.72 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 2 LLGEEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLH 81
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 82 DIREQSRKLQEIKEQ--EYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHPP 159
Cdd:TIGR02168 324 QLEELESKLDELAEElaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 160 RGDSGGTALDDLHKMQGHAGLTSAKDQGKPEVGEYS-KLEKINAEqqlkIQELQEKLEKAVKASTEATELLQNIRQAKER 238
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaELEELEEE----LEELQEELERLEEALEELREELEEAEQALDA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 239 AERELEKLHNREDS-----------SEGIKKKLVEAEEL-------------EEKHREA-----QVSAQHLEV------- 282
Cdd:TIGR02168 480 AERELAQLQARLDSlerlqenlegfSEGVKALLKNQSGLsgilgvlselisvDEGYEAAieaalGGRLQAVVVenlnaak 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 283 ----HLKQKE----------QHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSL- 347
Cdd:TIGR02168 560 kaiaFLKQNElgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAk 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 348 ----EQRIVEL-----------SEANKLAANSSLFTQRN-------MKAQEEMISELRQQKFYLETQAGKLEAQNRKLEE 405
Cdd:TIGR02168 640 klrpGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREieeleekIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 406 QLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKR---QLTELQLSLQERESQLTALQAARAALESQLRQAKTELE 482
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 483 ETTAEAEEEIQALTAHRDEIQRKFDALRNSC-------TVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIV 555
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLErriaateRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 556 QLRSEVDHLRREItEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLE-KERQWEAWRSVLGDEKS 634
Cdd:TIGR02168 880 NERASLEEALALL-RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEA 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 635 QFECRVRELQRMldteKQSRARADQRITESRQVVELAVKEHKaEILALQQALKEQKlkaESLSDKLNDLEKkhAMLEMNA 714
Cdd:TIGR02168 959 LENKIEDDEEEA----RRRLKRLENKIKELGPVNLAAIEEYE-ELKERYDFLTAQK---EDLTEAKETLEE--AIEEIDR 1028
|
....*....
gi 1039770408 715 RSLQQKLET 723
Cdd:TIGR02168 1029 EARERFKDT 1037
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-864 |
6.55e-16 |
|
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: 83.53 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 287 KEQHYEEKIKVLDNQIKKDLADKESLEnmmqrheeeahekgKILSEQKAMINAMDSKIRSLEQRIVEL--------SEAN 358
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLD--------------KNLNKDEEKINNSNNKIKILEQQIKDLndklkknkDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 359 KLAANSSLFT------QRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREvs 432
Cdd:TIGR04523 100 KLNSDLSKINseikndKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 433 LEHEEQKLE-----LKRQLTELQLSL----------QERESQLTALQAARAALES---QLRQAKTELEETTAEAEEEIQA 494
Cdd:TIGR04523 178 LEKEKLNIQknidkIKNKLLKLELLLsnlkkkiqknKSLESQISELKKQNNQLKDnieKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 495 LTAHRDEIQRKFDA----LRNSCTVITDLEEQLNQLTEDNAELNNQnfylsKQLDEASGANDEIVQLRSEVDHLRREITE 570
Cdd:TIGR04523 258 LKDEQNKIKKQLSEkqkeLEQNNKKIKELEKQLNQLKSEISDLNNQ-----KEQDWNKELKSELKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 571 REMQLTSQKqaqlsapdlQTMEALKTTCTMLEeqvLDLEALNDELLEKERQWEAWRS---VLGDEKSQFECRVRELQRML 647
Cdd:TIGR04523 333 NNKIISQLN---------EQISQLKKELTNSE---SENSEKQRELEEKQNEIEKLKKenqSYKQEIKNLESQINDLESKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 648 DTEKQSRARADQRITESRQVVELAVKEH---KAEILALQQALKE-------QKLKAESLSDKLNDLEKKHAMLEMNARSL 717
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIerlKETIIKNNSEIKDltnqdsvKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 718 QQKLE-TERELKQRlLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQvlYSHEKVKMEGTIS 796
Cdd:TIGR04523 481 KQNLEqKQKELKSK-EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE--DELNKDDFELKKE 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 797 QQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIE 864
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-817 |
1.24e-15 |
|
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: 83.10 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDI--REQS 87
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIeeLEKE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 88 RKLQEIKEQEYQAQVEEMRlmmnQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVShpprgdsggtA 167
Cdd:pfam02463 344 LKELEIKREAEEEEEEELE----KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ----------L 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 168 LDDLHKMQGHAgLTSAKDQGKPEVGEyskLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLH 247
Cdd:pfam02463 410 LLELARQLEDL-LKEEKKEELEILEE---EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 248 NREDSSEgikKKLVEAEELEEKHREAqvsaqhLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKG 327
Cdd:pfam02463 486 LELLLSR---QKLEERSQKESKARSG------LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 328 KILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQL 407
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 408 EKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLtalqaarAALESQLRQAKTELEETTAE 487
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL-------AKEEILRRQLEIKKKEQREK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 488 AEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEasgandeiVQLRSEVDHLRRE 567
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE--------LSLKEKELAEERE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 568 ITEREMQLTSQKqaqlsapdlQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfECRVRELQRML 647
Cdd:pfam02463 782 KTEKLKVEEEKE---------EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL-ELKEEQKLEKL 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 648 DTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETEREL 727
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 728 KQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKlIDFLQA 807
Cdd:pfam02463 932 KYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK-KKLIRA 1010
|
810
....*....|
gi 1039770408 808 KMDQPAKKKK 817
Cdd:pfam02463 1011 IIEETCQRLK 1020
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-774 |
1.76e-15 |
|
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: 82.32 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKE--RAERELEKLHNREDSSEGIKKKLVEAEELEEKH 270
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 271 REAQVSAQHLEVHLKQKEQHYEEKIKVLDNQikKDLADKESLENMMQRHEEE---AHEKGKILSEQKAMINAMDSKIRSL 347
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ--SSIEEQRRLLQTLHSQEIHirdAHEVATSIREISCQQHTLTQHIHTL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 348 EQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETR 427
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 428 LRevSLEHEEQKLELKRQLTelqlslqERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFD 507
Cdd:TIGR00618 465 AQ--SLKEREQQLQTKEQIH-------LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 508 ALRNSCTVITDLEEQLNQLTEDNAELNNQ------NFYLSKQLDEASGANDEIV-QLRSEVDHLRREITEREMQLTSQKQ 580
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQmqeiqqSFSILTQCDNRSKEDIPNLqNITVRLQDLTEKLSEAEDMLACEQH 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 581 AQLSA--PDLQTMEALKTTCTMLEEQVLDLEALNDELLE--KERQWEAWRSVLGDEKSQFECRVRELQRMldtekQSRAR 656
Cdd:TIGR00618 616 ALLRKlqPEQDLQDVRLHLQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQLALQKM-----QSEKE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 657 ADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQA 736
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
570 580 590
....*....|....*....|....*....|....*....
gi 1039770408 737 KLQQQMDLQKNHIFRLTQGLQEALD-RADLLKTERSDLE 774
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREeDTHLLKTLEAEIG 809
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-568 |
2.55e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 9 MEQEMTRLHRRVSEVEAVLS----QKEV-----ELKASETQRSL---------LEQDLATYITECSSLKRSLEQARMEVS 70
Cdd:COG1196 184 TEENLERLEDILGELERQLEplerQAEKaeryrELKEELKELEAellllklreLEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 71 QEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRlmmnqLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHK 150
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELAR-----LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 151 LmkvvshpprgDSGGTALDDLHKMQGHAGLTSAKDQgkpevgeySKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQ 230
Cdd:COG1196 339 L----------EELEEELEEAEEELEEAEAELAEAE--------EALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 231 NIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLE--------------VHLKQKEQHYEEKIK 296
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEaeleeeeeallellAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 297 VLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQE 376
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 377 EMISELRQQK-----FYLETQAGKLEAQNRKLEEQLEK-----------------------------ISHQDHSDKSRLL 422
Cdd:COG1196 561 AAIEYLKAAKagratFLPLDKIRARAALAAALARGAIGaavdlvasdlreadaryyvlgdtllgrtlVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 423 ELETRLREVSLEHEEQkleLKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEI 502
Cdd:COG1196 641 TLAGRLREVTLEGEGG---SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 503 QRKFDALRNSCTVITDLEEQLNQLTEDNAElnnqnfyLSKQLDEASGANDEIVQLRSEVDHLRREI 568
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEEL-------LEEEALEELPEPPDLEELERELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
197-934 |
3.88e-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: 78.24 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 197 LEKINAEQQLKIQELQEKLekavkasTEATELLQN----IRQAKERAERELEKLHNREDSSEGIKKKlvEAEELEEKHRE 272
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRL-------NESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAMADIRRR--ESQSQEDLRNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEVHLKQKEQHYEEKikvlDNQIkkdladkESLENMMQRHEEEAHE-----------KGKILSEQKAM----- 336
Cdd:pfam15921 147 LQNTVHELEAAKCLKEDMLEDS----NTQI-------EQLRKMMLSHEGVLQEirsilvdfeeaSGKKIYEHDSMstmhf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 337 ----------INAMDSKIRSLEQRIVELSEA-NKLAANSS----LFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNR 401
Cdd:pfam15921 216 rslgsaiskiLRELDTEISYLKGRIFPVEDQlEALKSESQnkieLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 402 KLEEQLEKISHQDHSDKS----RLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQA 477
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 478 KTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQ-----------LTEDNAELNNQnfyLSKQLDE 546
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmevqrlealLKAMKSECQGQ---MERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 547 ASGANDEI-------VQLRSEVDHLRR---EITEREMQLTS-------------QKQAQLSAPD-------------LQT 590
Cdd:pfam15921 453 IQGKNESLekvssltAQLESTKEMLRKvveELTAKKMTLESsertvsdltaslqEKERAIEATNaeitklrsrvdlkLQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 591 MEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGD-----------------EKSQFECRVRELQRMLDTEKQS 653
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKIL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 654 RARADQRITE-SRQVVELAVKEHK-----AEILALQQALKEQKLK----AESLSDKLNDLEKKHAMLEMNARSLQQKLE- 722
Cdd:pfam15921 613 KDKKDAKIRElEARVSDLELEKVKlvnagSERLRAVKDIKQERDQllneVKTSRNELNSLSEDYEVLKRNFRNKSEEMEt 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 723 TERELKQRLLEEQAKLQQ------QMDLQKNHIFRLTQGLQEALD----RADLLKTERSDLEYQLENI---QVLYSHEKV 789
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQtrntlkSMEGSDGHAMKVAMGMQKQITakrgQIDALQSKIQFLEEAMTNAnkeKHFLKEEKN 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 790 KMegtiSQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPAlptqvplqynELKLALEKEKARCAELEEALQktRIELRSAR 869
Cdd:pfam15921 773 KL----SQELSTVATEKNKMAGELEVLRSQERRLKEKVA----------NMEVALDKASLQFAECQDIIQ--RQEQESVR 836
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 870 EEAAHR---KATDHP-HPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSR-RKESSTPEEFSRRLKE 934
Cdd:pfam15921 837 LKLQHTldvKELQGPgYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHsRKTNALKEDPTRDLKQ 906
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
215-792 |
8.62e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 215 LEKAVKASTEATELLQNIRQAKERAERELEklhnredSSEGIKKKLVEAE-ELEEKHREAQvsaqhlevHLKQKEQHYEE 293
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIK-------RTENIEELIKEKEkELEEVLREIN--------EISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 294 KIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKI---LSEQKAMINAMDSKIRSLEQRIVELSEANKLAansslftqR 370
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeekIRELEERIEELKKEIEELEEKVKELKELKEKA--------E 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 371 NMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIShqdhSDKSRLLELETRLREV-----SLEHEEQKLELKRQ 445
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELekrleELEERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 446 LTELQLSLQERESQLTALQAARAALEsqLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNS------CTVITDL 519
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 520 EEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREM--QLTSQKQaQLSAPDLQTMEALKTT 597
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEE-KLKKYNLEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 598 CTMLEEQVLDLEA----LNDELLEKErqweawrsvlgdeksQFECRVRELQRMLDTEKQSRARADQRITE----SRQVVE 669
Cdd:PRK03918 527 YEKLKEKLIKLKGeiksLKKELEKLE---------------ELKKKLAELEKKLDELEEELAELLKELEElgfeSVEELE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 670 LAVKEHKA---EILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQ-AKLQQQMDLQ 745
Cdd:PRK03918 592 ERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLEL 671
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1039770408 746 KNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIqvlyshEKVKME 792
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEER------EKAKKE 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-572 |
1.17e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 9 MEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQdLATYITECSSLKRSLEQarmEVSQEDDKALQLLHDIREQSR 88
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 89 KLQEIKEQEyqAQVEEMRlmmnQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKlmkvvshpprgdsggtaL 168
Cdd:PRK03918 274 EIEELEEKV--KELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-----------------I 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 169 DDLHKMQGHAG-LTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQE-KLEKAVKASTEATELLQNIRQAKERAERELEKL 246
Cdd:PRK03918 331 KELEEKEERLEeLKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 247 HNREDSSEGIKKKLVEA-EELEEKHREAQVSAQHLEvhlkqkEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHE 325
Cdd:PRK03918 411 TARIGELKKEIKELKKAiEELKKAKGKCPVCGRELT------EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 326 KGKILSEQKAMI--NAMDSKIRSLEQRIVELsEANKLAANSSLFTqrnmKAQEEMIsELRQQKFYLETQAGKLEAQNRKL 403
Cdd:PRK03918 485 LEKVLKKESELIklKELAEQLKELEEKLKKY-NLEELEKKAEEYE----KLKEKLI-KLKGEIKSLKKELEKLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 404 EEQLEKIshqdHSDKSRLLELETRLREVSLEHEEqklELKRQLTELQ------LSLQERESQLTALQAARAALESQLRQA 477
Cdd:PRK03918 559 AELEKKL----DELEEELAELLKELEELGFESVE---ELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 478 ktelEETTAEAEEEIQALTAHRDEIQRKFDalrnsctvitdlEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIvql 557
Cdd:PRK03918 632 ----FEELAETEKRLEELRKELEELEKKYS------------EEEYEELREEYLELSRELAGLRAELEELEKRREEI--- 692
|
570
....*....|....*
gi 1039770408 558 RSEVDHLRREITERE 572
Cdd:PRK03918 693 KKTLEKLKEELEERE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-877 |
1.57e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.26 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 202 AEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLhnredssegikkklveaeeleEKHREaqvsaqhle 281
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA---------------------ERYQA--------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 282 vhLKQKEQHYEEKIKVldNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEankla 361
Cdd:TIGR02169 216 --LLKEKREYEGYELL--KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 362 aNSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIshqdhsdKSRLLELETRLREVSLEHEEQKLE 441
Cdd:TIGR02169 287 -EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-------LAEIEELEREIEEERKRRDKLTEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 442 LKRQLTELQLSLQERESQLTALQAARAALeSQLRQAkteleettaeaeeeIQALTAHRDEIQRKFDAlrnsctvitdLEE 521
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDEL-KDYREK--------------LEKLKREINELKRELDR----------LQE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 522 QLNQLTEDNAELNNqnfylskqldEASGANDEIVQLRSEVDHLRREITEREMQLtSQKQAQLSAPDlQTMEALKTTCTML 601
Cdd:TIGR02169 414 ELQRLSEELADLNA----------AIAGIEAKINELEEEKEDKALEIKKQEWKL-EQLAADLSKYE-QELYDLKEEYDRV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 602 EEQvldLEALNDELLEKERQWEAWRS----------VLGDEKSQFECRVREL-----QRMLDTEKQSRARADQRITESRQ 666
Cdd:TIGR02169 482 EKE---LSKLQRELAEAEAQARASEErvrggraveeVLKASIQGVHGTVAQLgsvgeRYATAIEVAAGNRLNNVVVEDDA 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 667 VVELAV---KEHK---AEILALQQALKEQKLKAESLSDKLND-------------------------------------- 702
Cdd:TIGR02169 559 VAKEAIellKRRKagrATFLPLNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgk 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 703 ----------LEKKHAM---------LEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEA---- 759
Cdd:TIGR02169 639 yrmvtlegelFEKSGAMtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrki 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 760 ---LDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFS-RRKEDPALPTQVPL 835
Cdd:TIGR02169 719 geiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA 798
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1039770408 836 QYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKA 877
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-860 |
1.69e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 16 LHRRVSEVEAVLSQKEVElkASETQRSLLEQDLAtyitecsSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKE 95
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKE--ALERQKEAIERQLA-------SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 96 QEYQAQVEEMRlmmnQLEEDLVSARRRSDLYESELREsrlaAEEFKRKANEcqhklmkvvshpprgdsggtaldDLHKMQ 175
Cdd:TIGR02169 287 EEQLRVKEKIG----ELEAEIASLERSIAEKERELED----AEERLAKLEA-----------------------EIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 176 ghagltSAKDQGKPEVGEYSK-LEKINAEqqlkIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSE 254
Cdd:TIGR02169 336 ------AEIEELEREIEEERKrRDKLTEE----YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 255 GIKKKLVeaEELEEKHREAQVSAQHLEVhLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEahekgkiLSEQK 334
Cdd:TIGR02169 406 RELDRLQ--EELQRLSEELADLNAAIAG-IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE-------LYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 335 AMINAMDSKIRSLEQRIVELsEANKLAANSslfTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEE-----QLEK 409
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEA-EAQARASEE---RVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnRLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 410 ISHQDHSDKSRLLELETR----------LREVSLEHEEQKLELKRQLTELQLSLQERESQLtalqaaRAALESQLRQAKT 479
Cdd:TIGR02169 552 VVVEDDAVAKEAIELLKRrkagratflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY------EPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 480 ELEETTAEAEEEIQALTAHRDEIQRK-------FDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAND 552
Cdd:TIGR02169 626 VEDIEAARRLMGKYRMVTLEGELFEKsgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 553 EIVQLRSEVDHLRREItEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDe 632
Cdd:TIGR02169 706 ELSQELSDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND- 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 633 ksqfecrvreLQRMLDTEKQsraradQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEM 712
Cdd:TIGR02169 784 ----------LEARLSHSRI------PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 713 NARSLQQKLETERELKQRLLEEQAKLQQQmdlqknhifrltqgLQEALDRADLLKTERSDLEYQLENIQvlyshekvKME 792
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAA--------------LRDLESRLGDLKKERDELEAQLRELE--------RKI 905
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 793 GTISQQtklIDFLQAKMDQPAKKKKGLFSRRKE-DPALPTQVPlqYNELKLALEKEKARCAELEEALQK 860
Cdd:TIGR02169 906 EELEAQ---IEKKRKRLSELKAKLEALEEELSEiEDPKGEDEE--IPEEELSLEDVQAELQRVEEEIRA 969
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10-560 |
7.58e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRsllEQDLATyITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRK 89
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQR---EQARET-RDEADEVLEEHEERREELETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 90 LQEIKEQeyqaqVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVvshpprgdsggtald 169
Cdd:PRK02224 274 REELAEE-----VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC--------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 170 dlhkmqgHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKA----VKASTEATELLQNIRQAKERAERELEK 245
Cdd:PRK02224 334 -------RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAreavEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 246 LHNREDSSEgikkklveaeELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLD-------NQIKKDLADKESLENMMQR 318
Cdd:PRK02224 407 LGNAEDFLE----------ELREERDELREREAELEATLRTARERVEEAEALLEagkcpecGQPVEGSPHVETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 319 HEEEAHEkgkiLSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQR------NMKAQEEMISELRQQKFYLETQ 392
Cdd:PRK02224 477 VEELEAE----LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELiaerreTIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 393 AGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVS--------LEHEEQKLE-LKRQLTELQLSLQERESQLTAL 463
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllaaIADAEDEIErLREKREALAELNDERRERLAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 464 QAARAALES--------QLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCtvitdleEQLNQLTEDNAELNN 535
Cdd:PRK02224 633 RERKRELEAefdearieEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL-------EELEELRERREALEN 705
|
570 580
....*....|....*....|....*
gi 1039770408 536 QNFYLSKQLDEASGANDEIVQLRSE 560
Cdd:PRK02224 706 RVEALEALYDEAEELESMYGDLRAE 730
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
195-880 |
9.04e-13 |
|
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: 73.85 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 195 SKLEKINAEQQLKIQELQEKLEKAVKASTEAT---ELLQNIRQAKERAERELEKLHNREdssegiKKKLVEAEELEEKhr 271
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAEliiDLEELKLQELKLKEQAKKALEYYQ------LKEKLELEEEYLL-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 272 eaqvsaqhlevhLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRI 351
Cdd:pfam02463 228 ------------YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 352 VELSEANKLAANSSLFTQRNMKAQEEMI----SELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQdhsdKSRLLELETR 427
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKkkaeKELKKEKEEIEELEKELKELEIKREAEEEEEEEL----EKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 428 LREVSLEHEEQKLELKRQLTELQLSLQEREsqltaLQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFD 507
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKS-----EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 508 ALRNSCTVITDLEEQLNQLTEDNAELNNQ-------NFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQ 580
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKetqlvklQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 581 AQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQS-----RA 655
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIdpilnLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 656 RADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQ-----KLETERELKQR 730
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEltkelLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 731 LLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDF-LQAKM 809
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEeKEEEK 766
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 810 DQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDH 880
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE 837
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-620 |
1.11e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 58 LKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQeyqaqVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAA 137
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-----LEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 138 EEFKRKANECQHKLMKVvshpprgdsggtalddlhkmqghagltsakDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEK 217
Cdd:PRK03918 269 EELKKEIEELEEKVKEL------------------------------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 218 avkasteATELLQNIrqakeraERELEKLHNREDSSEGIKKKLveaEELEEKHREaqvsaqhlevhLKQKEQHYEEKIKV 297
Cdd:PRK03918 319 -------LEEEINGI-------EERIKELEEKEERLEELKKKL---KELEKRLEE-----------LEERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 298 LDN--QIKKDLADK--ESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEA-NKLAANSSLFTQRN- 371
Cdd:PRK03918 371 KEEleRLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkGKCPVCGRELTEEHr 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 372 ---MKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISH--QDHSDKSRLLELETRLREVSLEHEEQKLE----L 442
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEeyekL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 443 KRQLTEL---QLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEE-----------IQALtahrDEIQRKFDA 508
Cdd:PRK03918 531 KEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeleerLKEL----EPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 509 LRNSCTVITDLEEQLNQLTEDnaelnnqnfyLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDL 588
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEE----------LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
570 580 590
....*....|....*....|....*....|..
gi 1039770408 589 QTMEALKTTCTMLEEQVLDLEALNDELLEKER 620
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-876 |
1.47e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 291 YEEKIKVLDNQIKKDLADKESLENMMQRhEEEAHEKgkiLSEQKAMINAMDSKIRSLEQRIVELSEanKLAANSSLFtqR 370
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEEL---IKEKEKELEEVLREINEISSELPELRE--ELEKLEKEV--K 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 371 NMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIshqdhsdKSRLLELETRLREV-SLEHEEQK-LELKRQLTE 448
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL-------KKEIEELEEKVKELkELKEKAEEyIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 449 LQLSLQERESQLTALQAARAALESQLRQAKTELEEttaeaeeeIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTE 528
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEER--------LEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 529 DNAELNNQNF-YLSKQLDEASGAN----DEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEE 603
Cdd:PRK03918 377 LKKRLTGLTPeKLEKELEELEKAKeeieEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 604 QVLDLEALNDELLEkerqweawrsvLGDEKSQFECRVRELQRMLdtEKQSRARADQRITESRQVVELAVKEHKAEILA-- 681
Cdd:PRK03918 457 YTAELKRIEKELKE-----------IEEKERKLRKELRELEKVL--KKESELIKLKELAEQLKELEEKLKKYNLEELEkk 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 682 --LQQALKEQ--KLKAESLS-----DKLNDLEKKHAMLEMNARSLQQKLEterELKQRLLEEQAKLQQQMDLQknhifrl 752
Cdd:PRK03918 524 aeEYEKLKEKliKLKGEIKSlkkelEKLEELKKKLAELEKKLDELEEELA---ELLKELEELGFESVEELEER------- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 753 TQGLQEALDRADLLKTERSDLEYQLENIQVLYShEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDpalptq 832
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE------ 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039770408 833 vplQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRK 876
Cdd:PRK03918 667 ---EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| C1_MgcRacGAP |
cd20821 |
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ... |
940-994 |
2.00e-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: 63.19 E-value: 2.00e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 940 IPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPA 994
Cdd:cd20821 1 RPHRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPTS 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-873 |
6.95e-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: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 368 TQRNMKAQEEMISELRQQKFYLETQAGKLEaQNRKLEEQLEKISH-----QDHSDKSRLLELETRLREVSLEHEEQKLEL 442
Cdd:TIGR02168 184 TRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 443 KR---QLTELQLSLQERESQLTALQAA-------RAALESQLRQAK---TELEETTAEAEEEIQALTAHRDEIQRKFDAL 509
Cdd:TIGR02168 263 QEleeKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRerlANLERQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 510 RNsctVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEAsgaNDEIVQLRSEVDHLRREIT-----------------ERE 572
Cdd:TIGR02168 343 EE---KLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLRSKVAQLELQIAslnneierlearlerleDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 573 MQLTSQKQAQLSAPDLQTMEALKTTC----TMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFE---CRVRELQR 645
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELeeleEELEELQEELERLEEALEELREELEEAEQALDAAERELAqlqARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 646 MLD------------TEKQSR---------------------------ARADQRITESRQVVELAV---KEH---KAEIL 680
Cdd:TIGR02168 497 LQEnlegfsegvkalLKNQSGlsgilgvlselisvdegyeaaieaalgGRLQAVVVENLNAAKKAIaflKQNelgRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 681 AL--------QQALKEQKLKAESLSDKLNDLEKKHAMLEMN----------ARSLQQKLETERELKQR------------ 730
Cdd:TIGR02168 577 PLdsikgteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGyrivtldgdlvr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 731 ---------------LLE---EQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKV--- 789
Cdd:TIGR02168 657 pggvitggsaktnssILErrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdla 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 790 -------KMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTR 862
Cdd:TIGR02168 737 rleaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
650
....*....|.
gi 1039770408 863 IELRSAREEAA 873
Cdd:TIGR02168 817 EEAANLRERLE 827
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-873 |
1.05e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 542 KQLDEASGA----NDEIVQLRSEVDHLRR--EITEREMQLTSQK---QAQLSAPDLQTMEA-LKTTCTMLEEQVLDLEAL 611
Cdd:TIGR02168 179 RKLERTRENldrlEDILNELERQLKSLERqaEKAERYKELKAELrelELALLVLRLEELREeLEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 612 NDELLEKERQWEAWRsvlgDEKSQFECRVRELQRMLDTEKQSRARADQRI---TESRQVVELAVKEHKAEILALQQALKE 688
Cdd:TIGR02168 259 TAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEISRLEQQKqilRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 689 QKLKAESLSDKLNDLEKKHAMLEM---NARSLQQKLETERELKQRLLEEQ----AKLQQQMDLQKNHIFRLTQGLQEALD 761
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAeleELEAELEELESRLEELEEQLETLrskvAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 762 RADLLKTERSDLEYQLENIQVLYSHEKVkmegtisqqtklidflqakmdqpAKKKKGLFSRRKEDPALPTQvplqynelk 841
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAEL-----------------------EELEEELEELQEELERLEEA--------- 462
|
330 340 350
....*....|....*....|....*....|..
gi 1039770408 842 laLEKEKARCAELEEALQKTRIELRSAREEAA 873
Cdd:TIGR02168 463 --LEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-734 |
1.24e-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: 69.75 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 198 EKINAEQQLKIQElQEKLEKAVKASTEATELLQNI--RQAKERAERELEKLHNRE---DSSEGIKKKLVEAEELEekhre 272
Cdd:pfam05483 130 EKVSLKLEEEIQE-NKDLIKENNATRHLCNLLKETcaRSAEKTKKYEYEREETRQvymDLNNNIEKMILAFEELR----- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEVHLKQKEQHyeEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGK----ILSEQKAMINAMDSKIRSLE 348
Cdd:pfam05483 204 VQAENARLEMHFKLKEDH--EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKdltfLLEESRDKANQLEEKTKLQD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 349 QRIVELSEAN----------KLAANSSLFTQRNMKA---------------QEEMISELRQQKFY-------LETQAGKL 396
Cdd:pfam05483 282 ENLKELIEKKdhltkelediKMSLQRSMSTQKALEEdlqiatkticqlteeKEAQMEELNKAKAAhsfvvteFEATTCSL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 397 EAQNRKLEEQLEKISHQ------DHSDKSRLLELETRL---REVSLEH------EEQKL------------ELKRQLTEL 449
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQlkiitmELQKKSSELEEMTKFknnKEVELEElkkilaEDEKLldekkqfekiaeELKGKEQEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 450 QLSLQERES-------QLTALQAARAALESQLRQAKTELEETTAEAEEeiqaLTAHRDEIQRKFDALRNSCtviTDLEEQ 522
Cdd:pfam05483 442 IFLLQAREKeihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE----LTAHCDKLLLENKELTQEA---SDMTLE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 523 LNQLTEDnaeLNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQL-----TSQKQAQLSAPDL----QTMEA 593
Cdd:pfam05483 515 LKKHQED---IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkckldKSEENARSIEYEVlkkeKQMKI 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 594 LKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQ---------SRARADQRITE- 663
Cdd:pfam05483 592 LENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeeiidnyQKEIEDKKISEe 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 664 --------SRQVVELAVK---------EHK-AEILALQQALKEQ---------------KLKAESLSDKLNDLEKKHAML 710
Cdd:pfam05483 672 klleevekAKAIADEAVKlqkeidkrcQHKiAEMVALMEKHKHQydkiieerdselglyKNKEQEQSSAKAALEIELSNI 751
|
650 660
....*....|....*....|....
gi 1039770408 711 EMNARSLQQKLETERELKQRLLEE 734
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLKME 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-743 |
1.30e-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: 69.71 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 6 EAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEddkalqllhdiRE 85
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE-----------RK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 86 QSRKLQEikeqEYQAQVEEMRLMMNQLEEDLVSARRRSDlyesELRESRLAAEEFKRKANECQHKLMKVVSHPPRGDSGG 165
Cdd:TIGR02169 351 RRDKLTE----EYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 166 TALddlhkmqgHAGLTSAKDQgkpevgeYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEK 245
Cdd:TIGR02169 423 ADL--------NAAIAGIEAK-------INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 246 LHNREDSSEGiKKKLVEAEELEEKHREAQVSAQHLEVH-----LKQKEQHYEEKIKV-----LDNQIKKDLADKESLENM 315
Cdd:TIGR02169 488 LQRELAEAEA-QARASEERVRGGRAVEEVLKASIQGVHgtvaqLGSVGERYATAIEVaagnrLNNVVVEDDAVAKEAIEL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 316 MQRHE------------EEAHEKGKILSEQKAMINAMDskIRSLEQRIvelSEANKLAANSSLFTQRNMKAQEEMIselr 383
Cdd:TIGR02169 567 LKRRKagratflplnkmRDERRDLSILSEDGVIGFAVD--LVEFDPKY---EPAFKYVFGDTLVVEDIEAARRLMG---- 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 384 qqKFYLETQAGKLeaqnrkleeqLEKI-SHQDHSDKSRLLELETR-LREVSLEHEEQKLELKRQLTELQLSLQERESQLT 461
Cdd:TIGR02169 638 --KYRMVTLEGEL----------FEKSgAMTGGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 462 ALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDnaelnnqnfyls 541
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED------------ 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 542 kqldeasgandeIVQLRSEVDHLRREITEREMQltsQKQAQlsapdlqtMEALKTTCTMLEEQVLDLEA-LNDELLEKEr 620
Cdd:TIGR02169 774 ------------LHKLEEALNDLEARLSHSRIP---EIQAE--------LSKLEEEVSRIEARLREIEQkLNRLTLEKE- 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 621 qweawrsvLGDEKSQfecrvRELQRMLDTEKQSRARADQritesrqvvelaVKEHKAEILALQQALKEQKLKAESLSDKL 700
Cdd:TIGR02169 830 --------YLEKEIQ-----ELQEQRIDLKEQIKSIEKE------------IENLNGKKEELEEELEELEAALRDLESRL 884
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1039770408 701 NDLEKKHAMLEMNARSLQQK---LETERE-LKQRLLEEQAKLQQQMD 743
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKieeLEAQIEkKRKRLSELKAKLEALEE 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-567 |
1.60e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 9 MEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSR 88
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 89 KLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKvvshpprgdsggTAL 168
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL------------EEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 169 DDLHKmqghAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHN 248
Cdd:COG1196 427 EEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 249 REDSSEGIKKKLVE----------AEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQR 318
Cdd:COG1196 503 YEGFLEGVKAALLLaglrglagavAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 319 HEEEAHEKGKILSEQKAMINAMDSKIRSLE---QRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGK 395
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADaryYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 396 LEAQNRKLEEQLEKISHQDhsdkSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLR 475
Cdd:COG1196 663 TGGSRRELLAALLEAEAEL----EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 476 QAKTELEETTAEAEEEIQALTAHRDEIQRKfdalrnsctvITDLEEQLNQL-------TEDNAELNNQNFYLSKQLDEAS 548
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERE----------LERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLE 808
|
570
....*....|....*....
gi 1039770408 549 GANDEIVQLRSEVDHLRRE 567
Cdd:COG1196 809 EARETLEEAIEEIDRETRE 827
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
607-877 |
3.24e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 607 DLEALNDELLEKERQWEAwrsvLGDEKSQFEcRVRELQRMLDT-EKQSRARADQRITESRQVVELAVKEHKAEILALQQ- 684
Cdd:COG1196 187 NLERLEDILGELERQLEP----LERQAEKAE-RYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAe 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 685 ------ALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQE 758
Cdd:COG1196 262 laeleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 759 ALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDpalptqvpLQYN 838
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE--------EALL 413
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039770408 839 ELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKA 877
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-575 |
3.41e-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: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 18 RRVSEVEAVLSQKEVELKAS----ETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEI 93
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 94 KEQeyqaqveEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAeEFKRKANECQHKLMKVVshpprgdsggtalddlhk 173
Cdd:pfam15921 397 KEQ-------NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA-LLKAMKSECQGQMERQM------------------ 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 174 mqghagltsAKDQGKPEVGE-----YSKLEKINAEQQLKIQELQEK---LEKAVKASTEATELLQNIRQAKERAERELEK 245
Cdd:pfam15921 451 ---------AAIQGKNESLEkvsslTAQLESTKEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITK 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 246 LHNREDssegikKKLVEAEEL--EEKH-REAQVSAQHLEVHLKQKEQhyeeKIKVLDNQIkkdladkeslENMMQ---RH 319
Cdd:pfam15921 522 LRSRVD------LKLQELQHLknEGDHlRNVQTECEALKLQMAEKDK----VIEILRQQI----------ENMTQlvgQH 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 320 --------------EEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELS-EANKLAANSSlftqRNMKAqeemISELRQ 384
Cdd:pfam15921 582 grtagamqvekaqlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGS----ERLRA----VKDIKQ 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 385 QKFYLETQAGKLEAQNRKLEEQLEKishqdhsdksrlleLETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQ 464
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEV--------------LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 465 AARA-ALESQLRQAKTeleettaeaeeeiqaLTAHRDEIqrkfDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQ 543
Cdd:pfam15921 720 GSDGhAMKVAMGMQKQ---------------ITAKRGQI----DALQSK---IQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
570 580 590
....*....|....*....|....*....|....*.
gi 1039770408 544 LD----EASGANDEIVQLRSEVDHLRREITEREMQL 575
Cdd:pfam15921 778 LStvatEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-793 |
6.64e-11 |
|
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: 67.51 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 203 EQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSsegikkkLVEAEE----LEEKHREAQVSAQ 278
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETEL-------CAEAEEmrarLAARKQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 279 HLEVHLKQKEqhyeEKIKVLDNQIKKDLADKESLENmmQRHEEEAhekgkilSEQKAMIN--AMDSKIRSLEQRIVELSE 356
Cdd:pfam01576 79 ELESRLEEEE----ERSQQLQNEKKKMQQHIQDLEE--QLDEEEA-------ARQKLQLEkvTTEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 357 ANklaansslftqrnmkaqeemiSELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLR---EVSL 433
Cdd:pfam01576 146 QN---------------------SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 434 EHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETtaeaeeeiqalTAHRDEIQRKfdalrnsc 513
Cdd:pfam01576 205 ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEE-----------TAQKNNALKK-------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 514 tvITDLEEQLNQLTEDnaeLNNQNFYLSKQLDEASGANDEIVQLRSEV-DHLrrEITEREMQLTSQKQAQLSapdlQTME 592
Cdd:pfam01576 266 --IRELEAQISELQED---LESERAARNKAEKQRRDLGEELEALKTELeDTL--DTTAAQQELRSKREQEVT----ELKK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 593 ALKTTCTMLEEQVLD--------LEALNDELLEKER---QWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQri 661
Cdd:pfam01576 335 ALEEETRSHEAQLQEmrqkhtqaLEELTEQLEQAKRnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG-- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 662 tesrQVVELAVKEHKAEILALQQALKEQKLKAE--SLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRllEEQAKLQ 739
Cdd:pfam01576 413 ----QLQELQARLSESERQRAELAEKLSKLQSEleSVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKLN 486
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 740 -----QQMDLQKNhifrltqGLQEALDRADllkTERSDLEYQLENIQVLYSHEKVKMEG 793
Cdd:pfam01576 487 lstrlRQLEDERN-------SLQEQLEEEE---EAKRNVERQLSTLQAQLSDMKKKLEE 535
|
|
| C1_ScPKC1-like_rpt2 |
cd20823 |
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ... |
938-995 |
7.36e-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: 7.36e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 938 HNIPHRFNVGLNMRATKCAVCLDTVHFGR-QASKCLECQVMCHPKCSTCLPATCGLPAE 995
Cdd:cd20823 1 HRIPHRFEPFTNLGANWCCHCGQMLPLGRkQIRKCTECGKTAHAQCAHLVPNFCGLSME 59
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
403-872 |
8.14e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 403 LEEQLEKISHQDHSDksRLLELETRLREVS--LEH-EEQKLELKRQLTELQLSLQERESQLTALQAARAALEsQLRQAKT 479
Cdd:PRK02224 192 LKAQIEEKEEKDLHE--RLNGLESELAELDeeIERyEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 480 ELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTV----ITDLEEQLNQLTEDNAE----LNNQNFYLSKQLDEASGAN 551
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadAEAVEARREELEDRDEElrdrLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 552 DEIVQLRSEVDHLRREITEREMQLTSQKQA------QLSAPDLQtMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAW 625
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAvedrreEIEELEEE-IEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 626 RSVLGDEKSQFECRVRELQRMLDTEKQSRAraDQRITESRQVVELAVKEHKAEILALQqaLKEQKLKAESLSDKLN---- 701
Cdd:PRK02224 428 EAELEATLRTARERVEEAEALLEAGKCPEC--GQPVEGSPHVETIEEDRERVEELEAE--LEDLEEEVEEVEERLEraed 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 702 --DLEKKHAMLEMNARSLQQKLET-------ERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSD 772
Cdd:PRK02224 504 lvEAEDRIERLEERREDLEELIAErretieeKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 773 LEYQLENIqvlyshekvkmeGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRkedpalptqvplqyNELKLALEKEKARCA 852
Cdd:PRK02224 584 LKERIESL------------ERIRTLLAAIADAEDEIERLREKREALAELN--------------DERRERLAEKRERKR 637
|
490 500
....*....|....*....|.
gi 1039770408 853 ELEEALQKTRIE-LRSAREEA 872
Cdd:PRK02224 638 ELEAEFDEARIEeAREDKERA 658
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
30-589 |
9.47e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 66.85 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 30 KEV--ELKASETQRSLLEQDLATYITECSSLKRSLEQarmevsqeDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRL 107
Cdd:PRK01156 172 KDVidMLRAEISNIDYLEEKLKSSNLELENIKKQIAD--------DEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 108 MMNQLEEdlvsarrrSDLYESELR--ESRLAAEEFKR-KANECQHKLMKVVSHPprgdsggtALDDLHKMQGHAGLtsak 184
Cdd:PRK01156 244 LSSLEDM--------KNRYESEIKtaESDLSMELEKNnYYKELEERHMKIINDP--------VYKNRNYINDYFKY---- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 185 dqgKPEVGEYSK-LEKINAEqqlkIQELQEKLEKAvkasteatELLQNIRQAKERAERELEKLHNREDSSEGIKKKLV-- 261
Cdd:PRK01156 304 ---KNDIENKKQiLSNIDAE----INKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNsy 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 262 --EAEELEEKHREAQVSAQHLEVHLKQKEQHYE---EKIKVLDNQIKKDLADKES-LENMMQR------HEEEAHEKGKI 329
Cdd:PRK01156 369 lkSIESLKKKIEEYSKNIERMSAFISEILKIQEidpDAIKKELNEINVKLQDISSkVSSLNQRiralreNLDELSRNMEM 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 330 LSEQKAM----INAMDSKIRSLEQRIVElsEANKLAANSSlFTQRNMKAQEEMISELRQQKFYLET-QAGKLEAQNRKLE 404
Cdd:PRK01156 449 LNGQSVCpvcgTTLGEEKSNHIINHYNE--KKSRLEEKIR-EIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 405 E---QLEKISHQDHSDKSRLL---ELETRLREVSLEHEEQKL-----------------------ELKRQLTELQLSLQE 455
Cdd:PRK01156 526 SaraDLEDIKIKINELKDKHDkyeEIKNRYKSLKLEDLDSKRtswlnalavislidietnrsrsnEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 456 RESQLTALQAAraaLESQLRQAKTELEETTAEAEEeIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNN 535
Cdd:PRK01156 606 IEIGFPDDKSY---IDKSIREIENEANNLNNKYNE-IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIED 681
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 536 QNFYLSKQLDEA----SGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQ 589
Cdd:PRK01156 682 NLKKSRKALDDAkanrARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| C1 |
smart00109 |
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
942-990 |
1.77e-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: 1.77e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1039770408 942 HRFNVGLNMRATKCAVCLDTVHFGR-QASKCLECQVMCHPKCSTCLPATC 990
Cdd:smart00109 1 HKHVFRTFTKPTFCCVCRKSIWGSFkQGLRCSECKVKCHKKCADKVPKAC 50
|
|
| C1 |
cd00029 |
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
942-990 |
1.85e-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: 57.53 E-value: 1.85e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1039770408 942 HRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd00029 1 HRFVPTTFSSPTFCDVCGKLIwGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
57-815 |
1.89e-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: 66.13 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 57 SLKRSLEQARMEVSQEDDKALQLLHDIREQSRkLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESE--LRESR 134
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTerLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 135 LAAEEFKRKANECQHKLMKVVSHPPRGDSG----GTALDDLHK-----MQGHAGLTSAKDQ-GKPE-----VGEYskLEK 199
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyQQALDVQQTraiqyQQAVQALEKARALcGLPDltpenAEDY--LAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 200 INAEQQL---KIQELQEKLEKAVKASTE---ATELLQNIRQAKERAE---------RELEKLHNREDSSEGIKKKLVEAE 264
Cdd:COG3096 446 FRAKEQQateEVLELEQKLSVADAARRQfekAYELVCKIAGEVERSQawqtarellRRYRSQQALAQRLQQLRAQLAELE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 265 ELEEKHREAQVSAQHLEVHLKQKEQHYEEkikvLDNQikkdladKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKI 344
Cdd:COG3096 526 QRLRQQQNAERLLEEFCQRIGQQLDAAEE----LEEL-------LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 345 RSLEQRivelsEANKLAANSSLFTQRNMKAQE----EMISELRQQKFYLETQA----GKLEAQNRKLEEQLEKISHQDHS 416
Cdd:COG3096 595 KELAAR-----APAWLAAQDALERLREQSGEAladsQEVTAAMQQLLEREREAtverDELAARKQALESQIERLSQPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 417 DKSRLLELETRLREV--SLEHEEQKLE-----------------------LKRQLTELQ-----LSLQER------ESQL 460
Cdd:COG3096 670 EDPRLLALAERLGGVllSEIYDDVTLEdapyfsalygparhaivvpdlsaVKEQLAGLEdcpedLYLIEGdpdsfdDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 461 TALQAARAAL----ESQLRQAKTELEET--TAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLtednaeln 534
Cdd:COG3096 750 DAEELEDAVVvklsDRQWRYSRFPEVPLfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQF-------- 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 535 nqnfyLSKQLDEASGANDE--IVQLRSEVDHLRREITEREMQLTSQKQAQLSA-PDLQTMEALKTTCTMLEEQVL----- 606
Cdd:COG3096 822 -----VGGHLAVAFAPDPEaeLAALRQRRSELERELAQHRAQEQQLRQQLDQLkEQLQLLNKLLPQANLLADETLadrle 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 607 DLEALNDELLEKER----------QWEAWRSVLGDEKSQFEcrvrELQRMLDTEKQSRARADQRI---TESRQVVELAVK 673
Cdd:COG3096 897 ELREELDAAQEAQAfiqqhgkalaQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSY 972
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 674 EHKAEIL----ALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHi 749
Cdd:COG3096 973 EDAVGLLgensDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA- 1051
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 750 frltqglqEALDRAdllKTERSDLEYQLeniqvlyshekVKMEGTISQQTKLIDFLQAKMDQPAKK 815
Cdd:COG3096 1052 --------EAEERA---RIRRDELHEEL-----------SQNRSRRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
312-548 |
2.15e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.42 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 312 LENMMQRHEEEAHEKGKILSEQkamINAMDSKIRSLEQRIVELSEANKLAAnsslfTQRNMKAQEEMISELRQQKFYLET 391
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQ---LPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 392 QAGKLEAQNRKLEEQLEKISHQ--DHSDKSRLLELETRLREvsleheeqkleLKRQLTELQLSLQERESQLTALQAARAA 469
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDAlpELLQSPVIQQLRAQLAE-----------LEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 470 LESQLRQAkteLEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDnAELNNQNF-YLSKQLDEAS 548
Cdd:COG3206 303 LRAQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE-VEVARELYeSLLQRLEEAR 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5-472 |
2.18e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 5 EEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLE--QDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHD 82
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 83 IREQ-------SRKLQEIKEQEYQAQVEEMRL--------MMNQLEEDLVSARRRSDLYESELRESRLaaEEFKRKANEC 147
Cdd:PRK03918 326 IEERikeleekEERLEELKKKLKELEKRLEELeerhelyeEAKAKKEELERLKKRLTGLTPEKLEKEL--EELEKAKEEI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 148 QHKLMKVVSHPPRGDSGG----TALDDLHKMQGHAGLTSAkdqgkpEVGEYSKLEkINAEQQLKIQELQEKLEKAVKAST 223
Cdd:PRK03918 404 EEEISKITARIGELKKEIkelkKAIEELKKAKGKCPVCGR------ELTEEHRKE-LLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 224 EATELLQNIRQAKERaERELEKLHNREDSSEGIKKKL--VEAEELEEKHREAQvsaqhlevHLKQKEQHYEEKIKVLdnq 301
Cdd:PRK03918 477 KLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLkkYNLEELEKKAEEYE--------KLKEKLIKLKGEIKSL--- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 302 iKKDLADKESLENMMQRHEEEAHEKGKILSE-QKAMINAMDSKIRSLEQRIVELSEANK---LAANSSLFTQRNMKAQEE 377
Cdd:PRK03918 545 -KKELEKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNeylELKDAEKELEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 378 MISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKS-RLLELETRLREVslehEEQKLELKRQLTELQLSLQER 456
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELReEYLELSRELAGL----RAELEELEKRREEIKKTLEKL 699
|
490
....*....|....*.
gi 1039770408 457 ESQLTALQAARAALES 472
Cdd:PRK03918 700 KEELEEREKAKKELEK 715
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
370-774 |
2.32e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 370 RNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISH--QDHSDKSRLLELETRLREVSlEHEEQKLELKRQLT 447
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELE-ALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 448 ELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLT 527
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE---LEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 528 EDNAELNNQ--NFYLSKQLDEA-------------SGAND----------EIVQLRSEVDHLRREITEREMQLTSQKQAQ 582
Cdd:COG4717 227 EELEQLENEleAAALEERLKEArlllliaaallalLGLGGsllsliltiaGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 583 LSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVL-----GDEKSQFECRVRELQRMLDTEK-QSRAR 656
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAGvEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 657 ADQRITESRQVVELavkehKAEILALQQALKEQKLKAESLSDKLNDlekkhAMLEMNARSLQQKLETERELKQRLLEEQA 736
Cdd:COG4717 387 LRAALEQAEEYQEL-----KEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039770408 737 KLQQQMDLQKNhifrlTQGLQEALDRADLLKTERSDLE 774
Cdd:COG4717 457 ELEAELEQLEE-----DGELAELLQELEELKAELRELA 489
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
244-746 |
2.33e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 65.69 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 244 EKLHNREDSSEGIKKKLveaEELEEKHREAQVSAQHLEVHLKQKEQHYeekikvldNQIKKDLADKESLENMMQRHEEEA 323
Cdd:PRK01156 190 EKLKSSNLELENIKKQI---ADDEKSHSITLKEIERLSIEYNNAMDDY--------NNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 324 HEkgkiLSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQeemISELRQQKFYLETQAGKLEAQNRKL 403
Cdd:PRK01156 259 KT----AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKND---IENKKQILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 404 EEqLEKISHQDHSDKSRLLELETRLREVSLEH-----------------EEQKLELKRQLTELQLSLQERESQLTALQAA 466
Cdd:PRK01156 332 SV-LQKDYNDYIKKKSRYDDLNNQILELEGYEmdynsylksieslkkkiEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 467 RAALESQLRQakteLEETTAEAEEEIQALTAHRDEIQRKFDAL--RNSCTVI-TDL-EEQLNQLTED-NAELNNQNFYLS 541
Cdd:PRK01156 411 LNEINVKLQD----ISSKVSSLNQRIRALRENLDELSRNMEMLngQSVCPVCgTTLgEEKSNHIINHyNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 542 KQLDEASGANDEIVQLRSEVDHL------------------RREITEREMQLTSQKQAQLSAP---------DLQTMEAL 594
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLeseeinksineynkiesaRADLEDIKIKINELKDKHDKYEeiknrykslKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 595 KTTCTMLEEQV--LDLEALNDELLEKERQWEAWRSVLG-------DEKSQFECRVRELQRMLDT--EKQSRARADQRITE 663
Cdd:PRK01156 567 RTSWLNALAVIslIDIETNRSRSNEIKKQLNDLESRLQeieigfpDDKSYIDKSIREIENEANNlnNKYNEIQENKILIE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 664 SRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETER----ELKQRLLEEQAKLQ 739
Cdd:PRK01156 647 KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRtrinELSDRINDINETLE 726
|
....*..
gi 1039770408 740 QQMDLQK 746
Cdd:PRK01156 727 SMKKIKK 733
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
13-756 |
3.28e-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: 65.38 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 13 MTRLHRRVSEVEAVLSQKEVELkasETQrsLLEQDLATYITECSSLKRSLEQARMEVSQE---DDKALQLLHDIREQSRK 89
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQL---LTL--CTPCMPDTYHERKQVLEKELKHLREALQQTqqsHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 90 LQEIKE---QEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHPPrgdsggT 166
Cdd:TIGR00618 259 QQLLKQlraRIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA------A 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 167 ALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKL 246
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 247 HNREDSSEGIKKKLVEAE---ELEEKHREA-QVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKdLADKEsleNMMQRHEEE 322
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKkqqELQQRYAELcAAAITCTAQCEKLEKIHLQESAQSLKEREQQ-LQTKE---QIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 323 AHEKGKILSEQKaminamdSKIRSLEQRIVELSEANKLAANSSLFTQRnmkaqeemISELRQQKFYLETQAGKLEAQNRK 402
Cdd:TIGR00618 489 KAVVLARLLELQ-------EEPCPLCGSCIHPNPARQDIDNPGPLTRR--------MQRGEQTYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 403 LEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELE 482
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 483 ETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQL---NQLTEDNAE-LNNQNFYLSKQLDEASGANDEIVQLR 558
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlasRQLALQKMQsEKEQLTYWKEMLAQCQTLLRELETHI 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 559 SEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERqweawrsvLGDEKSQFEC 638
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ--------TGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 639 RVRELQRMLDTEKQSRARADQRITESRQVVELAVKehkAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQ 718
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN---LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730 740 750
....*....|....*....|....*....|....*...
gi 1039770408 719 QKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGL 756
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEI 900
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
193-755 |
6.92e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELeklhnredssegikkklveaEELEEKHRE 272
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------------------EELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEvHLKQKEQHYEEKIKVldnqikkdladKESLENMMQRHEEeahekgkiLSEQKAMINAMDSKIRSLEQRIV 352
Cdd:COG4717 114 LREELEKLE-KLLQLLPLYQELEAL-----------EAELAELPERLEE--------LEERLEELRELEEELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 353 ELSEA-NKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIS--HQDHSDKSRLLELETRLR 429
Cdd:COG4717 174 ELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneLEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 430 EVSLEHEeqklelkrqLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDAL 509
Cdd:COG4717 254 IAAALLA---------LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 510 RNSCTVITDLEEqlnqltednaelnnqnfylsKQLDEASGANDEIVQLRSEVDHLRREIteREMQLTSQKQAQLSAPDLQ 589
Cdd:COG4717 325 LAALGLPPDLSP--------------------EELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 590 TMEALKTTCTMLEEQV---LDLEALNDELLEKERQWEAWRSVLGDEksqfecrvrELQRMLDTEKQSRARADQRITESRQ 666
Cdd:COG4717 383 DEEELRAALEQAEEYQelkEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELRE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 667 vvELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAklqqqmdlqk 746
Cdd:COG4717 454 --ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERA---------- 521
|
570
....*....|
gi 1039770408 747 NHIF-RLTQG 755
Cdd:COG4717 522 SEYFsRLTDG 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-779 |
7.43e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 321 EEAHEKGKILSEQKAM---INAMDSKIRSLEQRIVELSEAnkLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLE 397
Cdd:COG4913 238 ERAHEALEDAREQIELlepIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 398 AQNRKLEEQLEKISHQ-DHSDKSRLLELETRLREVSLEHEEQK---LELKRQLTELQLSLQERESQLTALQAARAALESQ 473
Cdd:COG4913 316 ARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 474 LRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVI--------TDLEEQLN-------------QLTEDNAE 532
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllalrDALAEALGldeaelpfvgeliEVRPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 533 --------LNNQNFYL---SKQLDEASGANDEIvqlrsevdHLRREITEREMQLTSQKQAQLSAPD---LQTMEALKTTC 598
Cdd:COG4913 476 wrgaiervLGGFALTLlvpPEHYAAALRWVNRL--------HLRGRLVYERVRTGLPDPERPRLDPdslAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 599 TM-LEEQ---------VLDLEALNDE---------------LLEKERQWEAWRS-VLG----DEKSQFECRVRELQRMLD 648
Cdd:COG4913 548 RAwLEAElgrrfdyvcVDSPEELRRHpraitragqvkgngtRHEKDDRRRIRSRyVLGfdnrAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 649 T--EKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEqklkAESLSDKLNDLEKKHAMLemnaRSLQQKLETERE 726
Cdd:COG4913 628 EaeERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE----IAELEAELERLDASSDDL----AALEEQLEELEA 699
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 727 LKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRAD-LLKTERSDLEYQLEN 779
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELRALLEE 753
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-879 |
1.24e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 181 TSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKAsteatellQNIRQAKErAERELEKLHNREDSSEGIKKKL 260
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA--------EEARKAED-ARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 261 VEAEELEEKHREAQvsAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQ--RHEEEAHEKGKILSEQKAMIN 338
Cdd:PTZ00121 1161 EDARKAEEARKAED--AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEeaRKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 339 AMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEE-MISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSD 417
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 418 KSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTA 497
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 498 HRDEIQRKFDALRNSCTVITDLEEqlnqlTEDNAELNNQNFYLSKQLDEASGANDeiVQLRSEVDHLRREITEREMQLTS 577
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE-----AKKKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 578 QKQAQLSAPDLQTMEALKTTCtmlEEQVLDLEALNDELLEKERQWEAWRSvlgDEKSQFEcRVRELQRMLDTEKQSRARA 657
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKA---EEAKKKADEAKKAAEAKKKADEAKKA---EEAKKAD-EAKKAEEAKKADEAKKAEE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 658 DQRITESRQVVELAVKEHKAEILALQQAlKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAK 737
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 738 LQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEgtisqqtklidflQAKMDQPAKKKK 817
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-------------EAKKAEEDEKKA 1690
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 818 GLFSRRKEDPALPTQvplqynELKLALEKEKARCAEL--EEALQKTRIELRSAREEAAHRKATD 879
Cdd:PTZ00121 1691 AEALKKEAEEAKKAE------ELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
81-781 |
1.38e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 81 HDIREQSRKLQEIK------EQEYQAQVEEMRLMMNQL---------EEDLVSARRRsdLYES-----ELRESRLAAEEF 140
Cdd:PRK04863 307 YRLVEMARELAELNeaesdlEQDYQAASDHLNLVQTALrqqekieryQADLEELEER--LEEQnevveEADEQQEENEAR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 141 KRKANECQHKLMKVVSHPPRgdsggtALDDLHKM-----QGHAGLTSAKDQ-GKPEVgEYSKLEKINAEQQLKIQELQEK 214
Cdd:PRK04863 385 AEAAEEEVDELKSQLADYQQ------ALDVQQTRaiqyqQAVQALERAKQLcGLPDL-TADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 215 L----------EKAVKASTEATELLQNI----------RQAKErAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQ 274
Cdd:PRK04863 458 LlsleqklsvaQAAHSQFEQAYQLVRKIagevsrseawDVARE-LLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 275 vsaQHLEVHLKQKEQHYEEKIKVLDNQikkdladkESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVEL 354
Cdd:PRK04863 537 ---RLLAEFCKRLGKNLDDEDELEQLQ--------EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 355 seankLAANSSLFTQRNMKAQE----EMISELRQQKFYLETQA----GKLEAQNRKLEEQLEKISHQDHSDKSRLLELET 426
Cdd:PRK04863 606 -----LAAQDALARLREQSGEEfedsQDVTEYMQQLLERERELtverDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 427 RLREVSLE--HEEQKLE-----------------------LKRQLTELQ-----LSLQE------RESQLTALQAARAAL 470
Cdd:PRK04863 681 RFGGVLLSeiYDDVSLEdapyfsalygparhaivvpdlsdAAEQLAGLEdcpedLYLIEgdpdsfDDSVFSVEELEKAVV 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 471 ----ESQLRQAKTELEET--TAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTednaelnNQNFYLSKQL 544
Cdd:PRK04863 761 vkiaDRQWRYSRFPEVPLfgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFI-------GSHLAVAFEA 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 545 DEasgaNDEIVQLRSEVDHLRREITEREMQLTSQKQAqlsapdlqtMEALKTTCTMLEE-----QVLDLEALNDELLEKE 619
Cdd:PRK04863 834 DP----EAELRQLNRRRVELERALADHESQEQQQRSQ---------LEQAKEGLSALNRllprlNLLADETLADRVEEIR 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 620 RQWEAWR--------------------SVLGDEKSQFEcrvrELQRMLDTEKQSRARADQRI---TESRQVVELAVKEHK 676
Cdd:PRK04863 901 EQLDEAEeakrfvqqhgnalaqlepivSVLQSDPEQFE----QLKQDYQQAQQTQRDAKQQAfalTEVVQRRAHFSYEDA 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 677 AEILA----LQQALKEQKLKAESLSDKLNDLEKKHA--MLEMNAR------SLQQKLETERELKQRL----------LEE 734
Cdd:PRK04863 977 AEMLAknsdLNEKLRQRLEQAEQERTRAREQLRQAQaqLAQYNQVlaslksSYDAKRQMLQELKQELqdlgvpadsgAEE 1056
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1039770408 735 QAKLQQQmdlqknhifRLTQGLQEALDRADLLKTERSDLEYQLENIQ 781
Cdd:PRK04863 1057 RARARRD---------ELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
|
| ROM1 |
COG5422 |
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ... |
1195-1446 |
1.75e-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: 62.99 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1195 SDQVVLVGTEEGLYALNVLKNS--------LTHIPGIGavfQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLp 1266
Cdd:COG5422 868 SGRKLLTGTNKGLYISNRKDNVnrfnkpidLLQEPNIS---QIIVIEEYKLMLLLSDKKLYSCPLDVIDASTEENVKKS- 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1267 aqpDVSPNIFEAVK-----GCHLFAAGKiENSLCICAAMPSKVVILRYNDN------LSKYCIRKEIETSEPCScIHFTN 1335
Cdd:COG5422 944 ---RIVNGHVSFFKqgfcnGKRLVCAVK-SSSLSATLAVIEAPLALKKNKSgnlkkaLTIELSTELYVPSEPLS-VHFLK 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1336 YSILIGTNKFYEI-DMKQYTLDEFLDKNDHSlaPAVFASSSNSFPVSIVQANSagqreEYLLCFHEFGVFVDSYGRRSRT 1414
Cdd:COG5422 1019 NKLCIGCKKGFEIvSLENLRTESLLNPADTS--PLFFEKKENTKPIAIFRVSG-----EFLLCYSEFAFFVNDQGWRKRT 1091
|
250 260 270
....*....|....*....|....*....|...
gi 1039770408 1415 DDL-KWSRLPLAFAYREPYlfVTHFNSlEVIEI 1446
Cdd:COG5422 1092 SWIfHWEGEPQEFALSYPY--ILAFEP-NFIEI 1121
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-739 |
2.38e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 192 GEYSKLekINA---EQQ------LKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEK-----LHNREDSSEGIK 257
Cdd:PRK02224 138 GEVNKL--INAtpsDRQdmiddlLQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkeekdLHERLNGLESEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 258 KKL-VEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEkIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAM 336
Cdd:PRK02224 216 AELdEEIERYEEQREQARETRDEADEVLEEHEERREE-LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 337 INAM-------DSKIRSLEQRIVELsEANKLAANSSLFTQR-NMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLE 408
Cdd:PRK02224 295 RDDLlaeagldDADAEAVEARREEL-EDRDEELRDRLEECRvAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 409 KISHQDHSDKSRLLELETRLRE---------VSLEHEEQKLELKRQ-LTELQLSLQERESQLTALQAARAALESQLRQAK 478
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEElrerfgdapVDLGNAEDFLEELREeRDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 479 TELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQL-----TEDNAE-LNNQNFYLSKQLDEASGAND 552
Cdd:PRK02224 454 CPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveAEDRIErLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 553 E----IVQLRSEVDHLRREITEREMQLTSQK-QAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRS 627
Cdd:PRK02224 534 EkrerAEELRERAAELEAEAEEKREAAAEAEeEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 628 vlgdeksqfecRVRELQRMldtEKQSRARADQRITESRqvvELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKH 707
Cdd:PRK02224 614 -----------KREALAEL---NDERRERLAEKRERKR---ELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570 580 590
....*....|....*....|....*....|..
gi 1039770408 708 AMLEMNARSLQQKLETERELKQRLLEEQAKLQ 739
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
403-872 |
2.43e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 403 LEEQLEKISHQDHSDKSRLLELE-TRLREVSLEHEEQKlELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTEL 481
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 482 EETTAEAEeeIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQ------------NFYLSKQLDEASG 549
Cdd:COG4717 126 QLLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslatEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 550 ANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTcTMLEEQVLDLEALNDELLEKERQWEAWRSVL 629
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 630 GdeksqfecrvrelqRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKham 709
Cdd:COG4717 283 L--------------GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR--- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 710 lemnARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHI-----FRltqGLQEALDRADLLKTERSDLEYQLENI---- 780
Cdd:COG4717 346 ----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVedeeeLR---AALEQAEEYQELKEELEELEEQLEELlgel 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 781 -QVLYSHEKVKMEGTISQQTKLIDFLQAKMDQpAKKKKGLFSRRKEDpaLPTQVPLQynELKLALEKEKARCAELEE--- 856
Cdd:COG4717 419 eELLEALDEEELEEELEELEEELEELEEELEE-LREELAELEAELEQ--LEEDGELA--ELLQELEELKAELRELAEewa 493
|
490
....*....|....*.
gi 1039770408 857 ALQKTRIELRSAREEA 872
Cdd:COG4717 494 ALKLALELLEEAREEY 509
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
229-782 |
2.75e-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: 62.16 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 229 LQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQ-HLEVHLKQKEQHYEEKI-------KVLDN 300
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSaELNQLLRTLDDQWKEKRdelngelSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 301 QIKKDLADKESLENMMQRHEEEAHEKGKI-----------LSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLftQ 369
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDADIETAAAdqeqlpswqseLENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDI--A 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 370 RNMKAQEEMISELRQQKFYLETQAGKLEAQ-NRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEqklelKRQLTE 448
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL-----LLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 449 LQLSLQERESQLTALQAARAALESQLRQAKTELEettaeaeeeiQALTAHRDEIQRkfdalrnsctvitdLEEQLNQLTE 528
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRRD----------QASEALRQASRR--------------LEERQSALDE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 529 dnaelnnqnfyLSKQLDEASGANDEIvqLRSEV----DHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEEQ 604
Cdd:pfam12128 525 -----------LELQLFPQAGTLLHF--LRKEApdweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRID 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 605 VLDLEALNDELLEKERQWEawrSVLGDEKS---QFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILA 681
Cdd:pfam12128 592 VPEWAASEEELRERLDKAE---EALQSAREkqaAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 682 LQQALKEQKLKAE----SLSDKLNDLEKKH-AMLEMNARSLQ----QKLETERELKQRLLEEQAKLQQQMDLQKNHIFRL 752
Cdd:pfam12128 669 KNKALAERKDSANerlnSLEAQLKQLDKKHqAWLEEQKEQKReartEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAE 748
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1039770408 753 TQGLQEALDRaDL------------LKTERSDLEYQLENIQV 782
Cdd:pfam12128 749 LKALETWYKR-DLaslgvdpdviakLKREIRTLERKIERIAV 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-579 |
3.43e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 202 AEQQLKIQELQEKLEKAVKasteateLLQNIRQAKERAEREL-EKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHL 280
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLdELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 281 EVHLKQKEQHYEEKIKVLDnQIKKDLADKESLENMMQRHEE--EAHEKGKILSEQKAMINAMDSKIRSLEQRIVELsean 358
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEARLREI---- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 359 klaansslftqrnmkaqEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKIshqdhsdKSRLLELETRLREvsleheeq 438
Cdd:TIGR02169 818 -----------------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNGKKEE-------- 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 439 kleLKRQLTELQLSLQERESQLTALQAARAALESQLRQAKT----------ELEETTAEAEEEIQALTAHRDEIQRKFDA 508
Cdd:TIGR02169 866 ---LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERkieeleaqieKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 509 LRNSCT---VITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQK 579
Cdd:TIGR02169 943 DEEIPEeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
203-666 |
3.65e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 203 EQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAE--ELEEKHREAQVSAQHL 280
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREieRLERELEERERRRARL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 281 EVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSeANKL 360
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP-ARLL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 361 AANSSLFTQRNMKAQE--------EMISE-----------LRQQKF--------------------------YLETQAGK 395
Cdd:COG4913 444 ALRDALAEALGLDEAElpfvgeliEVRPEeerwrgaiervLGGFALtllvppehyaaalrwvnrlhlrgrlvYERVRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 396 LEAQNRKLEEQ--LEKISHQDHSDKSRLL-ELETRLREVSLEHEEQKLELKRQLT-ELQLSL------------------ 453
Cdd:COG4913 524 PDPERPRLDPDslAGKLDFKPHPFRAWLEaELGRRFDYVCVDSPEELRRHPRAITrAGQVKGngtrhekddrrrirsryv 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 454 --QERESQLTALQAARAALESQLRQAKteleettaeaeEEIQALTAHRDEIQRKFDALRNSCTV-------------ITD 518
Cdd:COG4913 604 lgFDNRAKLAALEAELAELEEELAEAE-----------ERLEALEAELDALQERREALQRLAEYswdeidvasaereIAE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 519 LEEQLNQLTEDNAELNNqnfyLSKQLDEasgANDEIVQLRSEVDHLRREITEREMQLTS-QKQAQLSAPDLQTMEALKTt 597
Cdd:COG4913 673 LEAELERLDASSDDLAA----LEEQLEE---LEAELEELEEELDELKGEIGRLEKELEQaEEELDELQDRLEAAEDLAR- 744
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 598 ctmlEEQVLDLEALNDELLEKERQWEAwrsvlgdeksqfecrVRELQRMLDTEKQSRARADQRITESRQ 666
Cdd:COG4913 745 ----LELRALLEERFAAALGDAVEREL---------------RENLEERIDALRARLNRAEEELERAMR 794
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
9-594 |
3.95e-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: 61.52 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 9 MEQEMTRLHRRVSEVEAVLSQKEVELKASETQ---RSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIRE 85
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 86 QSRKLQEIKEQEYQAQVeemrlmmnqleedlvsarrrsdlyeSELRESRLAAEEFKR----KANECQHKLMKVVSHPPRG 161
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQ-------------------------IHLQETRKKAVVLARllelQEEPCPLCGSCIHPNPARQ 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 162 DSGGTALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAER 241
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 242 ELEKLHNREDssegikkKLVEAEELEEKHREAQVSAQHLEVHLKQKEQhyeekikvldNQIKKDLADKESLENMMQRHEE 321
Cdd:TIGR00618 599 LTEKLSEAED-------MLACEQHALLRKLQPEQDLQDVRLHLQQCSQ----------ELALKLTALHALQLTLTQERVR 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 322 EAHEKGKILSEQKAMIN-----AMDSKIRSLEQRIVELSEANKLaansslftqrnMKAQEEMISELR----QQKFYLETQ 392
Cdd:TIGR00618 662 EHALSIRVLPKELLASRqlalqKMQSEKEQLTYWKEMLAQCQTL-----------LRELETHIEEYDrefnEIENASSSL 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 393 AGKLEAQNRKLEEQLEKISHQdhsdKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALES 472
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQ----ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 473 QLRQAKTELEETTAEAEEEIQaltAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAND 552
Cdd:TIGR00618 807 EIGQEIPSDEDILNLQCETLV---QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQ 883
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 553 EIVQLRSEV----------DHLRREITEREMQLTSQKQAQLSAPDLQTMEAL 594
Cdd:TIGR00618 884 IKIQFDGDAlikflheitlYANVRLANQSEGRFHGRYADSHVNARKYQGLAL 935
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
192-892 |
8.17e-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: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 192 GEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIR--QAKERAERELEKLHNREDSSEGIKKKLVEAEELEEK 269
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHgkAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 270 hREAQVSAQHLEVHLKQKEQHYEEKIKvLDNQIKKDLADKESLENMMQRHEEE------AHEKGKILSEQKAMINaMDSK 343
Cdd:TIGR00618 232 -REALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETqerinrARKAAPLAAHIKAVTQ-IEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 344 IRSLEQRIVElseanKLAANSSLFTQRNMKAQEEmiSELRQQKFYLETqagkLEAQNRKLEEQLEK-ISHQDHSDKSRLL 422
Cdd:TIGR00618 309 AQRIHTELQS-----KMRSRAKLLMKRAAHVKQQ--SSIEEQRRLLQT----LHSQEIHIRDAHEVaTSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 423 ELETRLREVSLEHEEQKLEL----KRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAH 498
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSlckeLDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 499 RDEIQRKFDALRNSctviTDLEEQLNQLTEDNAElnnqnfylSKQLDEasgandeivQLRSEVDHLRREITEREMQLTSQ 578
Cdd:TIGR00618 458 KIHLQESAQSLKER----EQQLQTKEQIHLQETR--------KKAVVL---------ARLLELQEEPCPLCGSCIHPNPA 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 579 K-QAQLSAPDLQTMEALKTTCTMLEEQVLDLEAlndellekerqweawrsvlgdeksqfecrvrelqrMLDTEKQSRARA 657
Cdd:TIGR00618 517 RqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH-----------------------------------QLTSERKQRASL 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 658 DQRITESRQvvelavkehkaEILALQQALKEQKLKAESLSDKLNDLEKkhaMLEMNARSLQQKLETERELKQRLLEEQAK 737
Cdd:TIGR00618 562 KEQMQEIQQ-----------SFSILTQCDNRSKEDIPNLQNITVRLQD---LTEKLSEAEDMLACEQHALLRKLQPEQDL 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 738 LQQQMDLQKnhifrLTQGLQEALDRadlLKTERSDLEYQLENIQVLYSHEKVKMEGTISQqtKLIDFLQAKMDQPAKKKK 817
Cdd:TIGR00618 628 QDVRLHLQQ-----CSQELALKLTA---LHALQLTLTQERVREHALSIRVLPKELLASRQ--LALQKMQSEKEQLTYWKE 697
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 818 GL----FSRRKEDPALPTQVPlQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQ 892
Cdd:TIGR00618 698 MLaqcqTLLRELETHIEEYDR-EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
301-779 |
1.07e-08 |
|
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: 60.14 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 301 QIKKDLADKEsLENMMQRHEEE--AHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKlaansslftqrnmkaqeEM 378
Cdd:pfam05557 13 QLQNEKKQME-LEHKRARIELEkkASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR-----------------EQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 379 ISELRQQKFYLETQAGKLEAQnrklEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLE---LKRQLTELQLSLQE 455
Cdd:pfam05557 75 AELNRLKKKYLEALNKKLNEK----ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSEleeLQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 456 RE---SQLTALQAARAALESQLR--QAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRnsctvitDLEEQLNQLTEDN 530
Cdd:pfam05557 151 AEqlrQNLEKQQSSLAEAEQRIKelEFEIQSQEQDSEIVKNSKSELARIPELEKELERLR-------EHNKHLNENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 531 AELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREmqltsqKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEA 610
Cdd:pfam05557 224 LLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWV------KLAQDTGLNLRSPEDLSRRIEQLQQREIVLKE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 611 LNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRI---TESRQVVELAVKEHKAEiLALQQALK 687
Cdd:pfam05557 298 ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVlllTKERDGYRAILESYDKE-LTMSNYSP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 688 EQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQ-----KNHIFRLTQGLQEALDR 762
Cdd:pfam05557 377 QLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAdpsysKEEVDSLRRKLETLELE 456
|
490
....*....|....*..
gi 1039770408 763 ADLLKTERSDLEYQLEN 779
Cdd:pfam05557 457 RQRLREQKNELEMELER 473
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-743 |
1.84e-08 |
|
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: 59.42 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 22 EVEAVLSQKEVELKASETQ---RSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSR-------KLQ 91
Cdd:pfam01576 300 ELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKrnkanleKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 92 EIKEQEYQAQVEEMRLMMNQLEEdlvSARRRSDLyESELRESRLAAEEFKRKANECQHKLMKVVSHPprgDSGGTALDDL 171
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQD---SEHKRKKL-EGQLQELQARLSESERQRAELAEKLSKLQSEL---ESVSSLLNEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 172 ----HKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQE-----LQEKLEKAVKASTEATELLQNIRQAKERAERE 242
Cdd:pfam01576 453 egknIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEdernsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 243 LEKLHNREDSSEGIKKKLV-EAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQ-------------IKKDLAD 308
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLQrELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQrqlvsnlekkqkkFDQMLAE 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 309 KESLENMMQ----RHEEEAHEK-GKILSEQKAMINAMDSKirsleqriVELSEANKLaansslftqrnMKAQ-EEMIS-- 380
Cdd:pfam01576 613 EKAISARYAeerdRAEAEAREKeTRALSLARALEEALEAK--------EELERTNKQ-----------LRAEmEDLVSsk 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 381 --------ELRQQKFYLETQAGKLEAQNRKLEEQLekishQDHSDKSRLLELETRLREVSLEH---------EEQKLELK 443
Cdd:pfam01576 674 ddvgknvhELERSKRALEQQVEEMKTQLEELEDEL-----QATEDAKLRLEVNMQALKAQFERdlqardeqgEEKRRQLV 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 444 RQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQAL---TAHRDEIQRKFDALRNSCTVI---- 516
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLkklQAQMKDLQRELEEARASRDEIlaqs 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 517 -------TDLEEQLNQLTEDNA------------------ELNNQNFYLSKQLDEASGANDEIVQLRSEvdhLRREITER 571
Cdd:pfam01576 829 kesekklKNLEAELLQLQEDLAaserarrqaqqerdeladEIASGASGKSALQDEKRRLEARIAQLEEE---LEEEQSNT 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 572 EMQLTSQKQAQLSAPDLQT-MEALKTTCTMLEEQVLDLEALNDELLEKERQWE-AWRSVLGDEKSQFECRVRELQRMLDT 649
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTeLAAERSTSQKSESARQQLERQNKELKAKLQEMEgTVKSKFKSSIAALEAKIAQLEEQLEQ 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 650 EKQSRARADQRITEsrqvvelavKEHKAEILALQqaLKEQKLKAESLSDKLndlEKKHAMLemnaRSLQQKLETERELKQ 729
Cdd:pfam01576 986 ESRERQAANKLVRR---------TEKKLKEVLLQ--VEDERRHADQYKDQA---EKGNSRM----KQLKRQLEEAEEEAS 1047
|
810
....*....|....
gi 1039770408 730 RLLEEQAKLQQQMD 743
Cdd:pfam01576 1048 RANAARRKLQRELD 1061
|
|
| C1_KSR |
cd20812 |
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ... |
940-991 |
2.08e-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: 51.56 E-value: 2.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 940 IPHRFNVGLNMRATkCAVCLDTVHFGRqasKCLECQVMCHPKCSTCLPATCG 991
Cdd:cd20812 1 IKHRFSKKLFMRQT-CDYCHKQMFFGL---KCKDCKYKCHKKCAKKAPPSCG 48
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-728 |
2.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKalqlLHDIREQSRK 89
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA----IAGIEAKINE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 90 LQEIKEqEYQAQVEEMRLMMNQLEEDLVSARRRS-------DLYESELRESR--LAAEEFKRKANECQHKLMKVVSHPPR 160
Cdd:TIGR02169 439 LEEEKE-DKALEIKKQEWKLEQLAADLSKYEQELydlkeeyDRVEKELSKLQreLAEAEAQARASEERVRGGRAVEEVLK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 161 GDSGGtalddLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLeKAVKAStEATEL-LQNIRQakerA 239
Cdd:TIGR02169 518 ASIQG-----VHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELL-KRRKAG-RATFLpLNKMRD----E 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 240 ERELEKLHnrEDSSEGIKKKLVeaeELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADK---------- 309
Cdd:TIGR02169 587 RRDLSILS--EDGVIGFAVDLV---EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsra 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 310 -ESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEAnklaansslftqrnMKAQEEMISELRQQKFY 388
Cdd:TIGR02169 662 pRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE--------------LSDASRKIGEIEKEIEQ 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 389 LETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVslehEEQKLELKRQLTELQLSL-----QERESQLTAL 463
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLshsriPEIQAELSKL 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 464 QAARAALESQLRQAKTELEETTAEAEEEiqaltahRDEIQRKFDALRnsctvitDLEEQLNQLTEDNAELNNQNFYLSKQ 543
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYL-------EKEIQELQEQRI-------DLKEQIKSIEKEIENLNGKKEELEEE 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 544 LDEASGAndeIVQLRSEVDHLRREITEREMQLTSQKQAQlsapdlqtmEALKTTCTMLEEQVLDL----EALNDELLEKE 619
Cdd:TIGR02169 870 LEELEAA---LRDLESRLGDLKKERDELEAQLRELERKI---------EELEAQIEKKRKRLSELkaklEALEEELSEIE 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 620 RQWEAWRSVLGDEKSqfecrvrelqrmLDTEKQSRARADQRITESRQVVELAVKEHkaeilalqqalkeqklkaESLSDK 699
Cdd:TIGR02169 938 DPKGEDEEIPEEELS------------LEDVQAELQRVEEEIRALEPVNMLAIQEY------------------EEVLKR 987
|
730 740
....*....|....*....|....*....
gi 1039770408 700 LNDLEKKHAMLEMNARSLQQKLETERELK 728
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
10-776 |
2.85e-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: 58.90 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEA---VLSQKEVELKASETQRSLLEQdlatyITECSSLKRSLEQARMEVSQEDDkALQLLHDIREQ 86
Cdd:TIGR00606 318 ERELVDCQRELEKLNKerrLLNQEKTELLVEQGRLQLQAD-----RHQEHIRARDSLIQSLATRLELD-GFERGPFSERQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 87 SRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHPPRGDSGG- 165
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSd 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 166 ----------TALDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINAEQQLKIQEL---QEKLEKAVKASTEATELLQNI 232
Cdd:TIGR00606 472 rileldqelrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQMEMLTKDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 233 RQAKERAERELEKL----HNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLEvhlkQKEQHYEEKIKVLDNQIKK---- 304
Cdd:TIGR00606 552 RKIKSRHSDELTSLlgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE----QNKNHINNELESKEEQLSSyedk 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 305 --DLADKESLENMMQRHEEEAHEKGKilseQKAMINAmdsKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISEL 382
Cdd:TIGR00606 628 lfDVCGSQDEESDLERLKEEIEKSSK----QRAMLAG---ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 383 RQQKFYLETQAGKLEAQNRKLEEQLEKI--------SHQDHSDKsRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQ 454
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrqSIIDLKEK-EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 455 ERES------QLTALQAARAALESQLRQ-AKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSC----TVITDLEEQL 523
Cdd:TIGR00606 780 EEESakvcltDVTIMERFQMELKDVERKiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIelnrKLIQDQQEQI 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 524 NQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREIteremqltSQKQAQLSaPDLQTMEalkttctmlee 603
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREI--------KDAKEQDS-PLETFLE----------- 919
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 604 qvlDLEALNDELLEKERQweawrsvlgdEKSQFECRVRELQRMLDTEKQSRARADQRITESRqvvELAVKEHKAEILALQ 683
Cdd:TIGR00606 920 ---KDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK---DDYLKQKETELNTVN 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 684 QALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKL----------ETERELKQRLLE-----------EQAKLQQQM 742
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlrkrenelkEVEEELKQHLKEmgqmqvlqmkqEHQKLEENI 1063
|
810 820 830
....*....|....*....|....*....|....
gi 1039770408 743 DLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQ 776
Cdd:TIGR00606 1064 DLIKRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
204-410 |
3.22e-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: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 204 QQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNR-EDSSEGIKKKLVEAEELEEKHREAQVSAQHLEV 282
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 283 HLKQKEQHYEEKIKVLDNQIKKDL-------ADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELS 355
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 356 EANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKI 410
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
396-743 |
4.90e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 57.38 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 396 LEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEeqklELKRQLTELQLSLQERESQLTALQAARAALESQLR 475
Cdd:pfam19220 25 LKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYG----KLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 476 QAKTELEETTAeaeeeiqaltahrdeiqrkfdALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASgandeiv 555
Cdd:pfam19220 101 EAEAAKEELRI---------------------ELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 556 QLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLE-EQVLD-----LEALNDELLEK-------ERQW 622
Cdd:pfam19220 153 KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAElETQLDatrarLRALEGQLAAEqaereraEAQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 623 EAWRSVLGDEKSQFECRVRELQ-RMLDTEK---QSRARADQRiTESRQVVELAVKEHKAEILALQQALKEQKLKAESLSD 698
Cdd:pfam19220 233 EEAVEAHRAERASLRMKLEALTaRAAATEQllaEARNQLRDR-DEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQ 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039770408 699 KLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMD 743
Cdd:pfam19220 312 QFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIA 356
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
1023-1142 |
5.11e-08 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 52.56 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1023 LHLEGWMKVPRNNKRGqqGWDRKYIVLEGSKVLIYDNEAREAGQRPVeefelclpdGDVSIHGAVgASELANTAKADVPY 1102
Cdd:pfam00169 1 VVKEGWLLKKGGGKKK--SWKKRYFVLFDGSLLYYKDDKSGKSKEPK---------GSISLSGCE-VVEVVASDSPKRKF 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039770408 1103 ILKMESHPHTtcwPGRTLYLLAPSFPDKQRWVTALESVVA 1142
Cdd:pfam00169 69 CFELRTGERT---GKRTYLLQAESEEERKDWIKAIQSAIR 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
662-873 |
6.50e-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: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 662 TESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQ 741
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 742 MDLQKNHIFRLTQGLQ------------------EALDRADLLKTERSDLEYQLENIQvlysHEKVKMEGTISQQTKLID 803
Cdd:COG4942 99 LEAQKEELAELLRALYrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 804 FLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAA 873
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-559 |
7.12e-08 |
|
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: 57.49 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 9 MEQEMTRLHRRVSEVEAvlSQKEVELKASETQRSLleQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSR 88
Cdd:pfam01576 494 LEDERNSLQEQLEEEEE--AKRNVERQLSTLQAQL--SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 89 KLQEIKEQeYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLA----AEEFKRKANECQHKLMKVVSHPPRGDSG 164
Cdd:pfam01576 570 KLEKTKNR-LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAIsaryAEERDRAEAEAREKETRALSLARALEEA 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 165 GTALDDLHKMQGH-----AGLTSAKDQGKPEVGEYSKlEKINAEQQLKIQELQ-EKLEKAVKASTEATELLQ-NIRQAKE 237
Cdd:pfam01576 649 LEAKEELERTNKQlraemEDLVSSKDDVGKNVHELER-SKRALEQQVEEMKTQlEELEDELQATEDAKLRLEvNMQALKA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 238 RAERELeklHNREDSSEGIKKKLV------EAEELEEKHREAQVSA--QHLEVHLKQKEQHYEEKIKVLDNQIKKdLADK 309
Cdd:pfam01576 728 QFERDL---QARDEQGEEKRRQLVkqvrelEAELEDERKQRAQAVAakKKLELDLKELEAQIDAANKGREEAVKQ-LKKL 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 310 ESLENMMQRHEEEAHekgkiLSEQKAMINAMDS--KIRSLEQRIVELSEanKLAANSSLFTQRNM---KAQEEMI----- 379
Cdd:pfam01576 804 QAQMKDLQRELEEAR-----ASRDEILAQSKESekKLKNLEAELLQLQE--DLAASERARRQAQQerdELADEIAsgasg 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 380 -SELRQQKFYLETQAGKLEAQNRklEEQLEKISHQDHSDKSRLL--ELETRL---REVSLEHEEQKLELKRQLTELQLSL 453
Cdd:pfam01576 877 kSALQDEKRRLEARIAQLEEELE--EEQSNTELLNDRLRKSTLQveQLTTELaaeRSTSQKSESARQQLERQNKELKAKL 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 454 QERESQ--------LTALQAARAALESQLRQ--------AKTELEETTAEAEEEIQALTAHRDEIQRKfDALRNSCTVIT 517
Cdd:pfam01576 955 QEMEGTvkskfkssIAALEAKIAQLEEQLEQesrerqaaNKLVRRTEKKLKEVLLQVEDERRHADQYK-DQAEKGNSRMK 1033
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1039770408 518 DLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAND----EIVQLRS 559
Cdd:pfam01576 1034 QLKRQLEEAEEEASRANAARRKLQRELDDATESNEsmnrEVSTLKS 1079
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
186-582 |
8.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 186 QGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLhnredssegikkKLVEAEE 265
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL------------SLATEEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 266 LEEKHREAQvsaqhlevHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAH-EKGKILSEQKAMINAMDSKI 344
Cdd:COG4717 194 LQDLAEELE--------ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 345 RSLEQRIVELSEANKL-AANSSLFTQRNMKAQEEMISELRQqkfyLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLE 423
Cdd:COG4717 266 GSLLSLILTIAGVLFLvLGLLALLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 424 LETRLREV-----SLEHEEQKLELKRQLTELQLSLQ--------------ERESQLTALQAARAALESQLRQAKTELEEt 484
Cdd:COG4717 342 LLDRIEELqellrEAEELEEELQLEELEQEIAALLAeagvedeeelraalEQAEEYQELKEELEELEEQLEELLGELEE- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 485 taeaeeeiQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQldeasganDEIVQLRSEVDHL 564
Cdd:COG4717 421 --------LLEALDEEELEEELEELEEE---LEELEEELEELREELAELEAELEQLEED--------GELAELLQELEEL 481
|
410
....*....|....*...
gi 1039770408 565 RREITEREMQLTSQKQAQ 582
Cdd:COG4717 482 KAELRELAEEWAALKLAL 499
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
427-762 |
9.22e-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: 57.27 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 427 RLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAkteleettAEAEEEIQALTAHRDEIQRKF 506
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA--------SDHLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 507 DALrnsctviTDLEEQLNQLTEDNAELNNQnfyLSKQLDEASGANDEIVQLRSEVDHLRREIterEMQLTSQKQAQlsap 586
Cdd:COG3096 354 EDL-------EELTERLEEQEEVVEEAAEQ---LAEAEARLEAAEEEVDSLKSQLADYQQAL---DVQQTRAIQYQ---- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 587 dlQTMEALKTTCTMLEEQVLDLEALNDELLE-KERQWEAWRSVLGDE---------KSQFECRVRELQRMLDTEKQSRA- 655
Cdd:COG3096 417 --QAVQALEKARALCGLPDLTPENAEDYLAAfRAKEQQATEEVLELEqklsvadaaRRQFEKAYELVCKIAGEVERSQAw 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 656 -RADQRITESRQVVELAVKEH--KAEILALQQALKEQKlKAESLsdkLNDLEKKHA-------MLEMNARSLQQKLETER 725
Cdd:COG3096 495 qTARELLRRYRSQQALAQRLQqlRAQLAELEQRLRQQQ-NAERL---LEEFCQRIGqqldaaeELEELLAELEAQLEELE 570
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039770408 726 ELKQRLLEEQAKLQQQMDLQKNHIFRLTQ------GLQEALDR 762
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALER 613
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
234-477 |
1.15e-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: 55.93 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 234 QAKERAERELEKLHNRedssegIKKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQhyeeKIKVLDNQIKKdladkesLE 313
Cdd:COG4942 20 DAAAEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALAR----RIRALEQELAA-------LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 314 NMMQRHEEEAHEKGKILSEQKAMINAMdskIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQA 393
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 394 GKLEAQNRKLEEQlekishqdhsdKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQ 473
Cdd:COG4942 160 AELAALRAELEAE-----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....
gi 1039770408 474 LRQA 477
Cdd:COG4942 229 IARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-788 |
1.21e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 542 KQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSapdlQTMEALKTTCTMLEEQVLDLEALNDELLEKERQ 621
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE----AELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 622 WE-AWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRItesrQVVELAVKEHKAEILALQQALKEQKLKAESLSDKl 700
Cdd:COG4913 328 LEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL----AALGLPLPASAEEFAALRAEAAALLEALEEELEA- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 701 ndlekkhamlemnarsLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDR-ADLLKTERSDLEYQLEN 779
Cdd:COG4913 403 ----------------LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEALGLDEAELPFVGEL 466
|
....*....
gi 1039770408 780 IQVLYSHEK 788
Cdd:COG4913 467 IEVRPEEER 475
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
56-478 |
1.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 56 SSLKRSLEQARMEVSQEDDKALQL-LHDIREQSRKLQEIKEQEyqAQVEEMRLMMNQLEEDLVSARRRSDLYESELR--E 132
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKE--EEYAELQEELEELEEELEELEAELEELREELEklE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 133 SRLAAEEFKRKANECQHKLmkvvshpprgDSGGTALDDL-HKMQGHAGLTSAKDQGKPEVGEYSklEKINAEQQLKIQEL 211
Cdd:COG4717 123 KLLQLLPLYQELEALEAEL----------AELPERLEELeERLEELRELEEELEELEAELAELQ--EELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 212 QEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHR-------------------- 271
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallglggslls 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 272 -----------EAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKEsLENMMQRHEEEAHEKGKILSEQKAMINAM 340
Cdd:COG4717 271 liltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 341 DSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKfyletqagkleaQNRKLEEQLEKISHQdhsdksr 420
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE------------EYQELKEELEELEEQ------- 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 421 lLELETRLREVSLEHEEQKlELKRQLTELQLSLQERESQLTALQAARAALESQLRQAK 478
Cdd:COG4717 411 -LEELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
1023-1142 |
1.83e-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: 50.62 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1023 LHLEGWMKVPRNNKRGqqGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELClpdgDVSIhgavgaSELANTAKADVPY 1102
Cdd:smart00233 1 VIKEGWLYKKSGGGKK--SWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLS----GCTV------REAPDPDSSKKPH 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039770408 1103 ILKMeshphtTCWPGRTLYLLAPSFPDKQRWVTALESVVA 1142
Cdd:smart00233 69 CFEI------KTSDRKTLLLQAESEEEREKWVEALRKAIA 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
361-586 |
1.88e-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: 55.16 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 361 AANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKL 440
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 441 ELKRQLTELQ-----LSLQERESQLTALQAARAALESQ-----LRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALR 510
Cdd:COG4942 98 ELEAQKEELAellraLYRLGRQPPLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 511 nscTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASganDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAP 586
Cdd:COG4942 178 ---ALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-722 |
2.04e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 210 ELQEKLEKAvkasTEATELLQNIRQAKERAERELEKLHNREDSSEGIK-----KKLVEAEELEEKHREAQVSAQHLEVHL 284
Cdd:COG4913 239 RAHEALEDA----REQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 285 KQKEQHYEEKIKVLDNQIKK-DLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAAN 363
Cdd:COG4913 315 EARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 364 SSlftqrnmkaqEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREvSLEHEEQKL--- 440
Cdd:COG4913 395 AL----------EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE-ALGLDEAELpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 441 -ELkrqlteLQLSLQERESQLTA-----------------LQAARAALES-QLRQAKTELEETTAEAEEEIQALTAH--- 498
Cdd:COG4913 464 gEL------IEVRPEEERWRGAIervlggfaltllvppehYAAALRWVNRlHLRGRLVYERVRTGLPDPERPRLDPDsla 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 499 --------------RDEIQRKFD--------ALRNSCTVIT-----------------DLEEQLNQLTEDNAELNNQnfy 539
Cdd:COG4913 538 gkldfkphpfrawlEAELGRRFDyvcvdspeELRRHPRAITragqvkgngtrhekddrRRIRSRYVLGFDNRAKLAA--- 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 540 LSKQLDEAsgaNDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKE 619
Cdd:COG4913 615 LEAELAEL---EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 620 RQWEAWRSvlgdEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDK 699
Cdd:COG4913 692 EQLEELEA----ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
570 580
....*....|....*....|...
gi 1039770408 700 LNDLEKKHAMLEMNARSLQQKLE 722
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELE 790
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
502-743 |
2.43e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 502 IQRKFDALRNSctvITDLEEQLNQLTE--DNAELNNQNFYLSKQL----DEASGANDEIVQLRSEVDHLRREITEREMQL 575
Cdd:COG3206 166 LELRREEARKA---LEFLEEQLPELRKelEEAEAALEEFRQKNGLvdlsEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 576 tSQKQAQLSAPDLQTMEALKTTctmleeqvlDLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTEKQSRA 655
Cdd:COG3206 243 -AALRAQLGSGPDALPELLQSP---------VIQQLRAQLAELEAELAELSARYTPNHPD----VIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 656 RADQRITESRQVvelAVKEHKAEILALQQALKEQKLKAESLSDKLNDLekkhamlemnaRSLQQKLETERELKQRLLE-- 733
Cdd:COG3206 309 QEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL-----------RRLEREVEVARELYESLLQrl 374
|
250
....*....|
gi 1039770408 734 EQAKLQQQMD 743
Cdd:COG3206 375 EEARLAEALT 384
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
75-815 |
2.47e-07 |
|
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: 55.82 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 75 KALQLLHDIRE-QSRKLQEIKE-----QEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELresrlaaEEFKRKANECQ 148
Cdd:TIGR00606 186 KALETLRQVRQtQGQKVQEHQMelkylKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL-------DPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 149 HKLMKVVShpprgdsggtaLDDlhkmqghagltsakdqgkpevgEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATEL 228
Cdd:TIGR00606 259 HNLSKIMK-----------LDN----------------------EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 229 LQNIRQAKERaerelEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLEVhlkQKEQHYEEKIK----VLDNQIKK 304
Cdd:TIGR00606 306 LYHNHQRTVR-----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQL---QADRHQEHIRArdslIQSLATRL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 305 DLaDKESLENMMQRHEEEAHEKGKILSEQKA-----MINAMDSKIRSLEQRIVELSEANKLAANSslfTQRNMKAQEEMI 379
Cdd:TIGR00606 378 EL-DGFERGPFSERQIKNFHTLVIERQEDEAktaaqLCADLQSKERLKQEQADEIRDEKKGLGRT---IELKKEILEKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 380 SELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELEtRLREVSLEHEeqKLELKRQLTELQLSLQERE-- 457
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL-KKEVKSLQNE--KADLDRKLRKLDQEMEQLNhh 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 458 ----SQLTALQAARAALESQLRQAKTELEETTAEAEEEI-------QALTAHRDEIQRKFDALRNSCTVITDLEEQLNQL 526
Cdd:TIGR00606 531 tttrTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkkqleDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 527 TEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREM-------------QLTSQKQA--QLSAPDLQTM 591
Cdd:TIGR00606 611 NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMlagatavysqfitQLTDENQSccPVCQRVFQTE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 592 EALKTTCTMLEEQVL----DLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLD-TEKQSRARADQRITESRQ 666
Cdd:TIGR00606 691 AELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNkLQKVNRDIQRLKNDIEEQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 667 VVELAV---KEHKAEIL--------ALQQALKEQKLKAESLSDKLN--DLEKKHAMLEMNARSLQQKLET---ERELKQR 730
Cdd:TIGR00606 771 ETLLGTimpEEESAKVCltdvtimeRFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTvvsKIELNRK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 731 LLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTErsdLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMD 810
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ---LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
....*
gi 1039770408 811 QPAKK 815
Cdd:TIGR00606 928 LISSK 932
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
233-644 |
3.15e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 233 RQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQ---HLEVHLKQKEQHYEEKIKVL--DNQIKKDLA 307
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEaesDLEQDYQAASDHLNLVQTALrqQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 308 DKESLENMMqrheEEAHEKGKILSEQKAMINAmdsKIRSLEQRIVELseANKLAAnsslfTQRNMKAQEEMISELRQQKF 387
Cdd:PRK04863 356 DLEELEERL----EEQNEVVEEADEQQEENEA---RAEAAEEEVDEL--KSQLAD-----YQQALDVQQTRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 388 YLE-----TQAGKLEAQNrkLEEQLEKISHQDHSDKSRLLELETRLR--EVSLEHEEQKLELKRQLT-ELqlslqEREsq 459
Cdd:PRK04863 422 ALErakqlCGLPDLTADN--AEDWLEEFQAKEQEATEELLSLEQKLSvaQAAHSQFEQAYQLVRKIAgEV-----SRS-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 460 lTALQAARAALEsQLRQAKTELEETtaeaeeeiQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFY 539
Cdd:PRK04863 493 -EAWDVARELLR-RLREQRHLAEQL--------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 540 LSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDlqtmeALKTTCTMLEEQVLD---LEALNDELL 616
Cdd:PRK04863 563 LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD-----ALARLREQSGEEFEDsqdVTEYMQQLL 637
|
410 420
....*....|....*....|....*...
gi 1039770408 617 EKERQWEAWRSVLGDEKSQFECRVRELQ 644
Cdd:PRK04863 638 ERERELTVERDELAARKQALDEEIERLS 665
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
193-478 |
3.27e-07 |
|
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: 54.96 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEqqLKIQELQEKLEKAVKASTEATELLQNIRQAKERAeRELEKLHNREDSSEGIKKKLVEAEEleekhre 272
Cdd:COG5185 254 KLEKLVEQNTD--LRLEKLGENAESSKRLNENANNLIKQFENTKEKI-AEYTKSIDIKKATESLEEQLAAAEA------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 aqvsaqhlEVHLKQKEQHYEEKIKVLDNQIKKdlaDKESLENMMQRHEEEAHEKGKI--LSEQKAMINAMDSKIRSLEQR 350
Cdd:COG5185 324 --------EQELEESKRETETGIQNLTAEIEQ---GQESLTENLEAIKEEIENIVGEveLSKSSEELDSFKDTIESTKES 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 351 IVELSEANKLAANSSLFT-QRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQdhSDKSRLLELETRLR 429
Cdd:COG5185 393 LDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMRE--ADEESQSRLEEAYD 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1039770408 430 EVSLEHEEQKLELKRQLTELQLSLQEresQLTALQAARAALESQLRQAK 478
Cdd:COG5185 471 EINRSVRSKKEDLNEELTQIESRVST---LKATLEKLRAKLERQLEGVR 516
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
58-742 |
3.99e-07 |
|
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: 55.23 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 58 LKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQeyqaqVEEMRLMMNQLEEDLVSARRRSDlYESELRESRLAA 137
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNT-----LESAELRLSHLHFGYKSDETLIA-SRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 138 EEFKRKANECQhklMKVVSHPPRGDSGgTALDDLHKMQGHagLTSAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEK 217
Cdd:pfam12128 288 LNQLLRTLDDQ---WKEKRDELNGELS-AADAAVAKDRSE--LEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 218 AVKASTEA----TELLQNIRQA-KERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHY- 291
Cdd:pfam12128 362 RLKALTGKhqdvTAKYNRRRSKiKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYr 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 292 -EEKIKVLDNQIKKDLADKESLENMMQRHEEeahekgkilseqkamINAMDSKIrsleqrivELSEANKLAANSSLFTQR 370
Cdd:pfam12128 442 lKSRLGELKLRLNQATATPELLLQLENFDER---------------IERAREEQ--------EAANAEVERLQSELRQAR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 371 nmKAQEEMISELRQQKFYLETQAGKLEAqnrkLEEQLEKISH-------------QDHSDK--SRLLELETRLREVSLEH 435
Cdd:pfam12128 499 --KRRDQASEALRQASRRLEERQSALDE----LELQLFPQAGtllhflrkeapdwEQSIGKviSPELLHRTDLDPEVWDG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 436 EEQ--------KLELKR----QLTELQLSLQERESQL-TALQAAR---AALESQLRQAKTELEETTAEAEEEIQALTAHR 499
Cdd:pfam12128 573 SVGgelnlygvKLDLKRidvpEWAASEEELRERLDKAeEALQSARekqAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 500 DEIQRKFDALRNsctvitdLEEQLNQLTEDNAELNNQNFylsKQLDEASGANDEIVQLRSEvdHLRREITEREMQLTSQK 579
Cdd:pfam12128 653 LDLRRLFDEKQS-------EKDKKNKALAERKDSANERL---NSLEAQLKQLDKKHQAWLE--EQKEQKREARTEKQAYW 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 580 QAQLSAPDLQtMEALKTTCTMLEEQvldLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRaradQ 659
Cdd:pfam12128 721 QVVEGALDAQ-LALLKAAIAARRSG---AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRR----Q 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 660 RITESRQVVELAVKEHKaeilalqQALKEQKLKAESlsdKLNDLEKKHAMLEMNARSLQQKLETER----ELKQRLLEEQ 735
Cdd:pfam12128 793 EVLRYFDWYQETWLQRR-------PRLATQLSNIER---AISELQQQLARLIADTKLRRAKLEMERkaseKQQVRLSENL 862
|
....*..
gi 1039770408 736 AKLQQQM 742
Cdd:pfam12128 863 RGLRCEM 869
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
214-783 |
7.73e-07 |
|
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: 54.28 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 214 KLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEE 293
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 294 ---KIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQ-KAMINAMDSKIRSLEQRIVELseanklaansslftQ 369
Cdd:TIGR00606 260 nlsKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlNDLYHNHQRTVREKERELVDC--------------Q 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 370 RNMKAQEEMISELRQQKFYLETQAGKLeaqnrkleeQLEKISHQDHSDK--SRLLELETRLREVSLEHEEQKLELKRQLT 447
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRL---------QLQADRHQEHIRArdSLIQSLATRLELDGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 448 ELQLSLQERESQLTALQAARaaLESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLT 527
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCAD--LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 528 EDNAELNNQNFYLSKqLDEasgaNDEIVQLRSEVDHLRREITE--REMQLTSQKQAQLS--APDLQTMEALKTTCTMLEE 603
Cdd:TIGR00606 475 ELDQELRKAERELSK-AEK----NSLTETLKKEVKSLQNEKADldRKLRKLDQEMEQLNhhTTTRTQMEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 604 QVLDLEALNDELL-------EKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRItESRQVVELAVKEHK 676
Cdd:TIGR00606 550 QIRKIKSRHSDELtsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 677 AEILALQqalkEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERE-------LKQRLLEEQAKLQQqmdlqknHI 749
Cdd:TIGR00606 629 FDVCGSQ----DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpVCQRVFQTEAELQE-------FI 697
|
570 580 590
....*....|....*....|....*....|....
gi 1039770408 750 FRLTQGLQEALDRADLLKTERSDLEYQLENIQVL 783
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
307-510 |
7.82e-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: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 307 ADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQk 386
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 387 fyLETQAGKLEAQNRKL-----EEQLEKISHQDHSDKS------------RLLELETRLREVSLEHEEQKLELKRQLTEL 449
Cdd:COG4942 99 --LEAQKEELAELLRALyrlgrQPPLALLLSPEDFLDAvrrlqylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 450 QLSLQERESQLTALQAARAALESQLRQAKteleETTAEAEEEIQALTAHRDEIQRKFDALR 510
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-742 |
9.54e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 2 LLGEEAMMEQEMTRLHRRVSEVEAVLSQKEVELKA-------SETQRSLLEQDLATYITECSSLKRSLEQARM------- 67
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAalarleeETAQKNNALKKIRELEAQISELQEDLESERAarnkaek 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 68 ----------------EVSQEDDKALQLLHDIREQS----RKLQEIKEQEYQAQVEEMRLMMNQ----LEEDLVSARR-R 122
Cdd:pfam01576 293 qrrdlgeelealktelEDTLDTTAAQQELRSKREQEvtelKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRnK 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 123 SDLYES----ELRESRLAAE-----------EFKRKANECQ-HKLMKVVSHPPRGDSggTALDDLHKMQGH-----AGLT 181
Cdd:pfam01576 373 ANLEKAkqalESENAELQAElrtlqqakqdsEHKRKKLEGQlQELQARLSESERQRA--ELAEKLSKLQSElesvsSLLN 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 182 SAKDQGKPEVGEYSKLE-KINAEQQLKIQELQEKLEKA--VKASTEATELLQNIRQAKERAERELEK-LHNREDSSEGIK 257
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLEsQLQDTQELLQEETRQKLNLStrLRQLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDMK 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 258 KKLVE----AEELEEKHREAQVSAQHLEVHLKQKEQHYE--EKIKV-LDNQIKKDLADKESLENMMQRHEEEAHEKGKIL 330
Cdd:pfam01576 531 KKLEEdagtLEALEEGKKRLQRELEALTQQLEEKAAAYDklEKTKNrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 331 SEQKAMINAM-------DSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQ----EEMIS----------ELRQQKFYL 389
Cdd:pfam01576 611 AEEKAISARYaeerdraEAEAREKETRALSLARALEEALEAKEELERTNKQLraemEDLVSskddvgknvhELERSKRAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 390 ETQAGKLEAQNRKLEEQLekishQDHSDKSRLLELETRLREVSLEH---------EEQKLELKRQLTELQLSLQERESQL 460
Cdd:pfam01576 691 EQQVEEMKTQLEELEDEL-----QATEDAKLRLEVNMQALKAQFERdlqardeqgEEKRRQLVKQVRELEAELEDERKQR 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 461 TALQAARAALESQLRQAKTELEETTAEAEEEIQAL---TAHRDEIQRKFDALRNSCTVI-----------TDLEEQLNQL 526
Cdd:pfam01576 766 AQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLkklQAQMKDLQRELEEARASRDEIlaqskesekklKNLEAELLQL 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 527 TEDNA------------------ELNNQNFYLSKQLDEASGANDEIVQLRSEvdhLRREITEREMQLTSQKQAQLSAPDL 588
Cdd:pfam01576 846 QEDLAaserarrqaqqerdeladEIASGASGKSALQDEKRRLEARIAQLEEE---LEEEQSNTELLNDRLRKSTLQVEQL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 589 QT-MEALKTTCTMLEEQVLDLEALNDELLEKERQWE-AWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQ--RITES 664
Cdd:pfam01576 923 TTeLAAERSTSQKSESARQQLERQNKELKAKLQEMEgTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKlvRRTEK 1002
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 665 R-QVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQM 742
Cdd:pfam01576 1003 KlKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
318-755 |
1.44e-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: 53.42 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 318 RHEEEAHEK-GKILSEQKAMINAMDsKIRSLEQRIVELS-EANKLAANSSLFTQRNMKAQEE---MISELRQQKfYLETQ 392
Cdd:COG3096 275 RHANERRELsERALELRRELFGARR-QLAEEQYRLVEMArELEELSARESDLEQDYQAASDHlnlVQTALRQQE-KIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 393 AGKLEAQNRKLEEQLEKISHQDhsdkSRLLELETRLREVSLEHEEqkleLKRQLTELQLSLQERESQLTALQAARAALEs 472
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAA----EQLAEAEARLEAAEEEVDS----LKSQLADYQQALDVQQTRAIQYQQAVQALE- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 473 qlrQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRnsctvitDLEEQLNqLTEDNAELNNQNFYLSKQLD---EASG 549
Cdd:COG3096 424 ---KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVL-------ELEQKLS-VADAARRQFEKAYELVCKIAgevERSQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 550 ANDEIVQLRSE----------VDHLRREITEREMQLTSQKQAQLSAPDLQTMEALK-TTCTMLEEQVLDLEALNDELLEK 618
Cdd:COG3096 493 AWQTARELLRRyrsqqalaqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 619 ERQWEAWRSVLGDEKSQFECRVRELqrmldtekqsRARADQRITESRQVVELAvkEHKAEILALQQALKEQklkaeslsd 698
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKEL----------AARAPAWLAAQDALERLR--EQSGEALADSQEVTAA--------- 631
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 699 klndlekkhamlemnarsLQQKLETERELKQ---RLLEEQAKLQQQmdlqknhIFRLTQG 755
Cdd:COG3096 632 ------------------MQQLLEREREATVerdELAARKQALESQ-------IERLSQP 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-570 |
1.58e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 11 QEMTRLHRRVSEVEAVLSQkeVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQS-RK 89
Cdd:COG4913 262 ERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 90 LQEIKEQeyqaqveemrlmMNQLEEDLVSARRRSDLYESELRESRLA----AEEFKRKANECQHKLmkvvshpprgdsgg 165
Cdd:COG4913 340 LEQLERE------------IERLERELEERERRRARLEALLAALGLPlpasAEEFAALRAEAAALL-------------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 166 TALDDLHKmQGHAGLTSAKDQGKPEVGEYSKLEK-INAEQQLK------IQELQEKLEKAVKASTE----ATELLQnIRQ 234
Cdd:COG4913 394 EALEEELE-ALEEALAEAEAALRDLRRELRELEAeIASLERRKsniparLLALRDALAEALGLDEAelpfVGELIE-VRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 235 AKERAERELEK-LHNR------EDSSEGIKKKLVEAEELEEKHREAQVSAQHLEVHLKQ-KEQHYEEKIKVLDNQ----I 302
Cdd:COG4913 472 EEERWRGAIERvLGGFaltllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRlDPDSLAGKLDFKPHPfrawL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 303 KKDLADK------ESLENM-----------MQRHEEEAHEKG-KILSEQKAMI---NAmdSKIRSLEQRIVELseankla 361
Cdd:COG4913 552 EAELGRRfdyvcvDSPEELrrhpraitragQVKGNGTRHEKDdRRRIRSRYVLgfdNR--AKLAALEAELAEL------- 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 362 ansslftQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDhsdksRLLELETRLREVSLEHEEQKlE 441
Cdd:COG4913 623 -------EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER-----EIAELEAELERLDASSDDLA-A 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 442 LKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeEEIQALTAHRDEIQRKFDAlrnscTVITDLEE 521
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE-----------EELDELQDRLEAAEDLARL-----ELRALLEE 753
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1039770408 522 QLNQLTEDNAElnnqnfylsKQLDEAsgANDEIVQLRSEVDHLRREITE 570
Cdd:COG4913 754 RFAAALGDAVE---------RELREN--LEERIDALRARLNRAEEELER 791
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
333-605 |
1.70e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.13 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 333 QKAMINAMDSKIRSLEQRIVELSEANKLaansslftQRNMKAQEEMISELRQQKFYLETQAGKLEAQ--NRKLEEQLEKI 410
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAKQY--------QQVIDNFPKLSAELRQQLNNERDEPRSVPPNmsTDALEQEILQV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 411 SHQdHSDKSRLLELET-RLREVS---LEHEEQKLELKRQLTELQLSLQERESQLTAL-QAARAAL--ESQLRQAKTELEE 483
Cdd:PRK10929 115 SSQ-LLEKSRQAQQEQdRAREISdslSQLPQQQTEARRQLNEIERRLQTLGTPNTPLaQAQLTALqaESAALKALVDELE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 484 TTAEAEEEIQALTAHRDEI-QRKFDALRNSctvITDLEEQLNQLTEDNAElnnQNFYLSKQLDEASG--ANDEIVQLRse 560
Cdd:PRK10929 194 LAQLSANNRQELARLRSELaKKRSQQLDAY---LQALRNQLNSQRQREAE---RALESTELLAEQSGdlPKSIVAQFK-- 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 561 vdhLRREITE------REMQLTSQKQAQLSAPDLQTMEALKTtctmLEEQV 605
Cdd:PRK10929 266 ---INRELSQalnqqaQRMDLIASQQRQAASQTLQVRQALNT----LREQS 309
|
|
| C1_1 |
pfam00130 |
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
937-992 |
1.92e-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: 1.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770408 937 HHNIPHRFNvglnmRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCGL 992
Cdd:pfam00130 1 HHFVHRNFK-----QPTFCDHCGEFLwGLGKQGLKCSWCKLNVHKRCHEKVPPECGC 52
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
653-930 |
2.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 653 SRARADQRITESRQvvelAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLET-ERELKQR- 730
Cdd:COG3883 10 TPAFADPQIQAKQK----ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 731 -LLEEQAKLQQQMDLQKNHIFRLT--QGLQEALDRADLLKTErsdleyqleniqvlyshekvkmegtISQQTKLIDFLQA 807
Cdd:COG3883 86 eELGERARALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKI-------------------------ADADADLLEELKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 808 KMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPA 887
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1039770408 888 TARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSR 930
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-325 |
2.04e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 2 LLGEEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKR---SLEQARMEVSQEDDKALQ 78
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 79 LLHDIREQSRKLQE----IKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELrESRLAAEEFKRKanECQHKLMKV 154
Cdd:TIGR02169 766 RIEELEEDLHKLEEalndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-NRLTLEKEYLEK--EIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 155 VSHPPRGDSGGTALDDLHKMQGHAGLTSAKDQGKPE--VGEYSKLEKINAEQQLKIQELQEKLEKAvKASTEATELLQNI 232
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdlESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 233 RQAK-ERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLE-VHLKQKEQHYEEKIKVLDNQIKKD--LAD 308
Cdd:TIGR02169 922 LKAKlEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpVNMLAIQEYEEVLKRLDELKEKRAklEEE 1001
|
330
....*....|....*..
gi 1039770408 309 KESLENMMQRHEEEAHE 325
Cdd:TIGR02169 1002 RKAILERIEEYEKKKRE 1018
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
547-875 |
2.35e-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: 52.53 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 547 ASGANDEIVQL-----RSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALkttctMLEEQVLDLEALNDELLEKERQ 621
Cdd:pfam12128 204 AILEDDGVVPPksrlnRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESA-----ELRLSHLHFGYKSDETLIASRQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 622 wEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLN 701
Cdd:pfam12128 279 -EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 702 DLEKKHAMLEMNARSLQQKLETEREL-KQRLLEEQAKLQQQMDLQKNHIFRltqglQEALDRADLLKTErSDLEYQLENI 780
Cdd:pfam12128 358 NLEERLKALTGKHQDVTAKYNRRRSKiKEQNNRDIAGIKDKLAKIREARDR-----QLAVAEDDLQALE-SELREQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 781 QVLYSHEKVKMEGTISQQTKLIDFLQAkmdqpakkkkglfsrrkeDPALPTQVPLQYNELKLALEKEKARCAELEeALQK 860
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLRLNQATA------------------TPELLLQLENFDERIERAREEQEAANAEVE-RLQS 492
|
330
....*....|....*
gi 1039770408 861 TRIELRSAREEAAHR 875
Cdd:pfam12128 493 ELRQARKRRDQASEA 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-610 |
2.87e-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: 51.69 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 374 AQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVslehEEQKLELKRQLTELQLSL 453
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 454 QERESQLTALqaaRAALESQLRQAKTELEETTAeaeeeiqALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAEL 533
Cdd:COG4942 93 AELRAELEAQ---KEELAELLRALYRLGRQPPL-------ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770408 534 NNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQlsapdLQTMEALKTTCTMLEEQVLDLEA 610
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL-----AAELAELQQEAEELEALIARLEA 234
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-744 |
4.05e-06 |
|
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: 51.71 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 2 LLGEEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSL---KRSLEQARMEVSQEddkalq 78
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLskeRKLLEERISEFTSN------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 79 lLHDIREQSRKLQEIKEQeYQAQVEEMRLMMNQLE---EDLVSARRRSDLYESELRES----RLAAEEFK----RKANEC 147
Cdd:pfam01576 168 -LAEEEEKAKSLSKLKNK-HEAMISDLEERLKKEEkgrQELEKAKRKLEGESTDLQEQiaelQAQIAELRaqlaKKEEEL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 148 QHKLMKVvshPPRGDSGGTALDDLHKMQGHagLTSAKDQGKPEVGEYSKLEK----------------------INAEQQ 205
Cdd:pfam01576 246 QAALARL---EEETAQKNNALKKIRELEAQ--ISELQEDLESERAARNKAEKqrrdlgeelealkteledtldtTAAQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 206 LKIQELQE--KLEKAVKASTEATEL-LQNIRQAKERAEREL-EKLHNREDSSEGIKK-KLVEAEELEEKHREAQVsaqhl 280
Cdd:pfam01576 321 LRSKREQEvtELKKALEEETRSHEAqLQEMRQKHTQALEELtEQLEQAKRNKANLEKaKQALESENAELQAELRT----- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 281 evhLKQKEQHYEEKIKVLDNQikkdLADKESLENMMQRHEEEAHEKgkiLSEQKAMINAMDSKIRSLEQRIVELSEankl 360
Cdd:pfam01576 396 ---LQQAKQDSEHKRKKLEGQ----LQELQARLSESERQRAELAEK---LSKLQSELESVSSLLNEAEGKNIKLSK---- 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 361 aANSSLFTQrnMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEK-------ISHQDHSDKSRLLELETRLREVSL 433
Cdd:pfam01576 462 -DVSSLESQ--LQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEeeeakrnVERQLSTLQAQLSDMKKKLEEDAG 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 434 ---EHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETtaeaeeeiQALTAHRDEIQRKFD-AL 509
Cdd:pfam01576 539 tleALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ--------RQLVSNLEKKQKKFDqML 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 510 RNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEI----VQLRSEVDHLrreiteremqLTSQKQAQLSA 585
Cdd:pfam01576 611 AEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELertnKQLRAEMEDL----------VSSKDDVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 586 PDL--------QTMEALKTTCTMLEEQvldLEALNDELLEKERQWEAW----------RSVLGDEK-SQFECRVRELQRM 646
Cdd:pfam01576 681 HELerskraleQQVEEMKTQLEELEDE---LQATEDAKLRLEVNMQALkaqferdlqaRDEQGEEKrRQLVKQVRELEAE 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 647 LDTEKQSRARAdqriTESRQVVELAVKEHKAEILALQQ----ALKEQKLKAESLSDKLNDLEKKHAMLEmnaRSLQQKLE 722
Cdd:pfam01576 758 LEDERKQRAQA----VAAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRD---EILAQSKE 830
|
810 820
....*....|....*....|..
gi 1039770408 723 TERELKQRlleEQAKLQQQMDL 744
Cdd:pfam01576 831 SEKKLKNL---EAELLQLQEDL 849
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
5-459 |
4.18e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 5 EEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQ-RSLLEQDLATYITeCSSLKRSLEQARMEVSQEDD--KAL---- 77
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnKRLWDRDTGNSIT-IDHLRRELDDRNMEVQRLEAllKAMksec 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 78 -----QLLHDIREQSRKLQEIkeQEYQAQVEEMRLMMNQLEEDLVSA--------------------------------- 119
Cdd:pfam15921 443 qgqmeRQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKkmtlessertvsdltaslqekeraieatnaeit 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 120 --RRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHPPRGDSGGTALDDLHKMQGHAGLTSA-----KDQGKPEVG 192
Cdd:pfam15921 521 klRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGamqveKAQLEKEIN 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 ----EYSKLEKINAEQQLKIQELQEK-----LEKaVKASTEATELLQNIRQAKERAERELEKLHN-REDSSEGIKKKLVE 262
Cdd:pfam15921 601 drrlELQEFKILKDKKDAKIRELEARvsdleLEK-VKLVNAGSERLRAVKDIKQERDQLLNEVKTsRNELNSLSEDYEVL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 263 AEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLdnqikkdladkESLENMMQRHEEEAHEKGKILSEQKAMINAMDS 342
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL-----------KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 343 KIRSLEQrivELSEANKlaANSSLFTQRNMKAQEemISELRQQKFYLETQAGKLEAQNRKLEEqlekishqdhsdksRLL 422
Cdd:pfam15921 749 KIQFLEE---AMTNANK--EKHFLKEEKNKLSQE--LSTVATEKNKMAGELEVLRSQERRLKE--------------KVA 807
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1039770408 423 ELETRLREVSLEHEEQKLELKRQLTE-----LQLSLQERESQ 459
Cdd:pfam15921 808 NMEVALDKASLQFAECQDIIQRQEQEsvrlkLQHTLDVKELQ 849
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
493-722 |
4.40e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 493 QALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLDEAsgaNDEIVQLRSEVDHLRREITERE 572
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQE---IAELEKELAALKKEEKALLKQLAALERRIAAL---ARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 573 MQLtSQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTEKQ 652
Cdd:COG4942 90 KEI-AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 653 SRaradQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLE 722
Cdd:COG4942 165 LR----AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
201-867 |
4.98e-06 |
|
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: 51.36 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 201 NAEQQLKIQELQEKLekavKASTEATELLQNIRQAKERAEREleKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHL 280
Cdd:pfam10174 69 NQHLQLTIQALQDEL----RAQRDLNQLLQQDFTTSPVDGED--KFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 281 EVHLKQKEQHYEEKikvlDNQIKKDLADKESlENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKl 360
Cdd:pfam10174 143 ELRIETQKQTLGAR----DESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELH- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 361 aansslftQRNMKAQE-EMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQ-DHSDKSRllELETRLREVSLEHEEQ 438
Cdd:pfam10174 217 --------RRNQLQPDpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNgLLHTEDR--EEEIKQMEVYKSHSKF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 439 kleLKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTaeaeeeiQALTAHRDE---IQRKFDALRNSC-- 513
Cdd:pfam10174 287 ---MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLK-------ESLTAKEQRaaiLQTEVDALRLRLee 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 514 --TVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEAsgaNDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSapdLQTM 591
Cdd:pfam10174 357 keSFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVK---ERKINVLQKKIENLQEQLRDKDKQLAGLKERVKS---LQTD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 592 EALKTTCtmleeqvldLEALNDELLEKERQWEAWRsvlgdEKSQFECRVR--ELQRMLDTEKQSRARAD--QRITESRQV 667
Cdd:pfam10174 431 SSNTDTA---------LTTLEEALSEKERIIERLK-----EQREREDRERleELESLKKENKDLKEKVSalQPELTEKES 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 668 VELAVKEHkAEILALQQALKEQKLKA---------ESLSDKLNDLEKKHAMlEMNARSLQQKLETERELKQ---RLLEEQ 735
Cdd:pfam10174 497 SLIDLKEH-ASSLASSGLKKDSKLKSleiaveqkkEECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQevaRYKEES 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 736 AKLQQQMDlqknhifRLTQGLQEAldradllKTERSDLEYQLENIQVLYSHEkvkmegtISQQTKLIDflQAKMDQPAKK 815
Cdd:pfam10174 575 GKAQAEVE-------RLLGILREV-------ENEKNDKDKKIAELESLTLRQ-------MKEQNKKVA--NIKHGQQEMK 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 816 KKGLfsrRKEDPALPTQVPLQYNELKLALEkekarcaELEEALQKTRIELRS 867
Cdd:pfam10174 632 KKGA---QLLEEARRREDNLADNSQQLQLE-------ELMGALEKTRQELDA 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-571 |
5.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 15 RLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATyitecssLKRSLEQARMEVSQEDDKAL-QLLHDIREQSRKLQEI 93
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDA-------LREELDELEAQIRGNGGDRLeQLEREIERLERELEER 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 94 KE--QEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKvvshpprgdsggtALDDL 171
Cdd:COG4913 358 ERrrARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR-------------ELREL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 172 hkmqgHAGLTSAKDQGKPevgeysklekINAEQqlkiQELQEKLEKAVKASTE----ATELLQnIRQAKERAERELEK-L 246
Cdd:COG4913 425 -----EAEIASLERRKSN----------IPARL----LALRDALAEALGLDEAelpfVGELIE-VRPEEERWRGAIERvL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 247 HNR------EDSSEGIKKKLVEAEELEEKHREAQVSAQHLEVHLKQ-KEQHYEEKIKVLDNQ----IKKDLADK------ 309
Cdd:COG4913 485 GGFaltllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRlDPDSLAGKLDFKPHPfrawLEAELGRRfdyvcv 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 310 ESLENM-----------MQRHEEEAHEKG---KILSEQ------KAMINAMDSKIRSLEQRIVELSEANKLAANSslftQ 369
Cdd:COG4913 565 DSPEELrrhpraitragQVKGNGTRHEKDdrrRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAE----L 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 370 RNMKAQEEMISELRQQKFYlETQAGKLEAQNRKLEEQLEKIShqdhSDKSRLLELETRLREVSLEH---EEQKLELKRQL 446
Cdd:COG4913 641 DALQERREALQRLAEYSWD-EIDVASAEREIAELEAELERLD----ASSDDLAALEEQLEELEAELeelEEELDELKGEI 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 447 TELQLSLQERESQLTALQAA------------RAALESQLRQAKTELEETTAEAEEEiQALTAHRDEIQRKFDALRN--- 511
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRleaaedlarlelRALLEERFAAALGDAVERELRENLE-ERIDALRARLNRAEEELERamr 794
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 512 ---------SCTVITDLE------EQLNQLTEDNAELNNQNFylSKQLDEASgaNDEIVQLRSEVDHLRREITER 571
Cdd:COG4913 795 afnrewpaeTADLDADLEslpeylALLDRLEEDGLPEYEERF--KELLNENS--IEFVADLLSKLRRAIREIKER 865
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
547-818 |
5.97e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 547 ASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDlqtmealkttctmleeqvlDLEALNDELLEKERQweawr 626
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK-------------------QLAALERRIAALARR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 627 svlgdeksqfecrVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKK 706
Cdd:COG4942 71 -------------IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 707 HAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKnhifRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSH 786
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
250 260 270
....*....|....*....|....*....|..
gi 1039770408 787 EKVKMEGTISQQTKLIDFLQAKMDQPAKKKKG 818
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
516-747 |
6.57e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 516 ITDLEEQLNQLTEDNAELNNQnfyLSKQLDEASGANDEIVQLRSEVDHLRREI--TEREMQLTSQKQAQLSAPdlqtMEA 593
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKE---LAALKKEEKALLKQLAALERRIAALARRIraLEQELAALEAELAELEKE----IAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 594 LKTTctmLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLdtekQSRARADQRITESRQVVELAVK 673
Cdd:COG4942 95 LRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 674 EHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKN 747
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
198-868 |
7.98e-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: 51.11 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 198 EKInAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERE--------------LEKLHNREDSSEGIKKKLVEA 263
Cdd:COG3096 347 EKI-ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslksqladyqqaLDVQQTRAIQYQQAVQALEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 264 EELEEKHREAQVSAQHLEVHLKQKEQHYEEKikVLDNQIKKDLAD--KESLENMMQRHE--------EEAHEKGKIL--- 330
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAKEQQATEE--VLELEQKLSVADaaRRQFEKAYELVCkiageverSQAWQTARELlrr 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 331 -SEQKAMI---NAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQ---EEMISELRQQKFYLETQAGKLEAQNRKL 403
Cdd:COG3096 504 yRSQQALAqrlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQAAEAVEQRSEL 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 404 EEQLEKISHQDHSDKSR---LLELETRLREVSlEHEEQKLELKRQLTELQLSLQERESQLTA----LQAARAALESQLRQ 476
Cdd:COG3096 584 RQQLEQLRARIKELAARapaWLAAQDALERLR-EQSGEALADSQEVTAAMQQLLEREREATVerdeLAARKQALESQIER 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 477 AKTELEETTAEAEEEIQALTAH-----RDEIQRK----FDAL----RNScTVITDLE---EQLNQLT---------EDNA 531
Cdd:COG3096 663 LSQPGGAEDPRLLALAERLGGVllseiYDDVTLEdapyFSALygpaRHA-IVVPDLSavkEQLAGLEdcpedlyliEGDP 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 532 ELNNQNFYLSKQLDEASGANDEIVQLR----SEVDHLRR-------EITEREMQLTSQKQAQLSApDLQTMEALKTTCTM 600
Cdd:COG3096 742 DSFDDSVFDAEELEDAVVVKLSDRQWRysrfPEVPLFGRaarekrlEELRAERDELAEQYAKASF-DVQKLQRLHQAFSQ 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 601 LEEQVLDLEALNDEllekerqwEAWRSVLGDEKSQFEcrvRELQRMLDTEKQSRARADQ---RITESRQVVELAVKEHKA 677
Cdd:COG3096 821 FVGGHLAVAFAPDP--------EAELAALRQRRSELE---RELAQHRAQEQQLRQQLDQlkeQLQLLNKLLPQANLLADE 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 678 EILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEeqakLQQQMDLQKNHIFRLTQGLQ 757
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQ 965
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 758 --EAL---DRADLLkTERSD----LEYQLENIQVLYSHEKVKMEGtisQQTKLIDFLQAKMDQPAK---KKKGLFSRRKE 825
Cdd:COG3096 966 rrPHFsyeDAVGLL-GENSDlnekLRARLEQAEEARREAREQLRQ---AQAQYSQYNQVLASLKSSrdaKQQTLQELEQE 1041
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 826 DPALPTQVP--------LQYNELKLALEKEKARCAELEEALQKTRIELRSA 868
Cdd:COG3096 1042 LEELGVQADaeaeerarIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
17-444 |
9.20e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 17 HRRVSEVEAVLSQKEVELKASETQRSLLEqDLATYITECSSLKRSLEQARMEVsQEDDKALQLLHDIREQSRKLQEIKEQ 96
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRYDDLNNQIL-ELEGYEMDYNSYLKSIESLKKKI-EEYSKNIERMSAFISEILKIQEIDPD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 97 EYQAQVEEMRLMMNQLEEDLVSARRRSDlyesELRESRlaaEEFKRKANECQHKLMKVVSHPPRGDSGGTALDDlHKMQG 176
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIR----ALRENL---DELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-HYNEK 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 177 HAGLTSAKDQGKPEVgeysklEKINaEQQLKIQELQEKLEKAvkastEATELLQNIRQAKErAERELEKLHNREDSsegI 256
Cdd:PRK01156 478 KSRLEEKIREIEIEV------KDID-EKIVDLKKRKEYLESE-----EINKSINEYNKIES-ARADLEDIKIKINE---L 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 257 KKKLVEAEELEEKHReaqvsAQHLEVhLKQKEQHYEEKIKVLD-----------NQIKKDLADKESlenmmqRHEEEAHE 325
Cdd:PRK01156 542 KDKHDKYEEIKNRYK-----SLKLED-LDSKRTSWLNALAVISlidietnrsrsNEIKKQLNDLES------RLQEIEIG 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 326 KGKILSEQKAMINAMDSKIRSLEQRIVELsEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEE 405
Cdd:PRK01156 610 FPDDKSYIDKSIREIENEANNLNNKYNEI-QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRK 688
|
410 420 430
....*....|....*....|....*....|....*....
gi 1039770408 406 QLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKR 444
Cdd:PRK01156 689 ALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
494-872 |
1.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 494 ALTAHRDEIQRKFDAlrNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREM 573
Cdd:PRK02224 188 SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 574 QLTSqkqaqlsapDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQS 653
Cdd:PRK02224 266 TIAE---------TEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 654 -----------RARADQRITESRQVVELAvKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLE 722
Cdd:PRK02224 337 aqahneeaeslREDADDLEERAEELREEA-AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 723 TERELKQRLLEEQAKLQQQMDLQKNHIfRLTQGLQEA---------------LDRADLLKTERSDLEYQLENIQVlyshE 787
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERV-EEAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEE----E 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 788 KVKMEGTISQQTKLIDfLQAKMDQPAKKKKGLFSRRKEDPAlptqvplQYNELKLALEKEKARCAELEEALQKTRIELRS 867
Cdd:PRK02224 491 VEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRE-------TIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
....*
gi 1039770408 868 AREEA 872
Cdd:PRK02224 563 AEEEA 567
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-708 |
1.21e-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: 49.38 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 437 EQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeeeiQALTAHRDEIQrkfdalrnsctvi 516
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE--------------RRIAALARRIR------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 517 tDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEivQLRSevdHLRREITEREMQLTSQKQAQLSAPDLQTMEALKT 596
Cdd:COG4942 73 -ALEQELAALEAELAELEKEIAELRAELEAQKEELAE--LLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 597 TctmLEEQVLDLEALNDELLEKERQWEAWRsvlgdeksqfecrvRELQRMLDTEKQSRARADQRITESRQVvelaVKEHK 676
Cdd:COG4942 147 A---RREQAEELRADLAELAALRAELEAER--------------AELEALLAELEEERAALEALKAERQKL----LARLE 205
|
250 260 270
....*....|....*....|....*....|..
gi 1039770408 677 AEILALQQALKEQKLKAESLSDKLNDLEKKHA 708
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1499-1590 |
1.26e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1499 ESGTEQHRVPSTSRSSPNKRGPP--TYNEHITKR--------------VASSPAPPEGPSHPREPSTPHRYRDREGRTEL 1562
Cdd:PTZ00449 527 KEGEEGEHEDSKESDEPKEGGKPgeTKEGEVGKKpgpakehkpskiptLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRP 606
|
90 100 110
....*....|....*....|....*....|
gi 1039770408 1563 RRDKSPGRP--LEREKSPGRMLSTRRERSP 1590
Cdd:PTZ00449 607 TRPKSPKLPelLDIPKSPKRPESPKSPKRP 636
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
207-455 |
1.40e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.10 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 207 KIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNR----EDSSEGIKKKLVEA-EELEEKHREAQVSAQHLE 281
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRiqllEEELERTEERLAEAlEKLEEAEKAADESERGRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 282 VhLKQKEQHYEEKIKVLDNQIKKdladkeslenmMQRHEEEAHEKGKILSEQKAMINA----MDSKIRSLEQRIVELSEA 357
Cdd:pfam00261 82 V-LENRALKDEEKMEILEAQLKE-----------AKEIAEEADRKYEEVARKLVVVEGdlerAEERAELAESKIVELEEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 358 NKLAANSSlftqRNMKAQEEMISElRQQKFyletqagklEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEE 437
Cdd:pfam00261 150 LKVVGNNL----KSLEASEEKASE-REDKY---------EEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEA 215
|
250
....*....|....*...
gi 1039770408 438 QKLELKRQLTELQLSLQE 455
Cdd:pfam00261 216 EKEKYKAISEELDQTLAE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-536 |
1.45e-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: 49.38 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 333 QKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISH 412
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 413 QDHSDKSRLLEL-------ETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETT 485
Cdd:COG4942 98 ELEAQKEELAELlralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 486 AEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQ 536
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
327-763 |
1.60e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 49.61 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 327 GKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQ 406
Cdd:COG5281 3 ALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 407 LEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQlslQERESQLTALQAARAALESQLRQAKTELEETTA 486
Cdd:COG5281 83 ALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAA---AAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 487 EAEEEIQALTAHRDEIQRKFDALRNSctvitDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRR 566
Cdd:COG5281 160 AAAAAAAAAAAAAAAAAAALAAASAA-----AAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 567 EITEREMQLTSQKQAQLSapDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfecRVRELQRM 646
Cdd:COG5281 235 AALAAASAAAQALAALAA--AAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQA---LAAAAAAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 647 LDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDlekkhAMLEMNARSLQQKLETERE 726
Cdd:COG5281 310 AAQLAAAAAAAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALE-----AAAAAAAAELAAAGDWAAG 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 1039770408 727 LKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRA 763
Cdd:COG5281 385 AKAALAEYADSATNVAAQVAQAATSAFSGLTDALAGA 421
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
194-572 |
1.90e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 194 YSKLEKINAEQQLKIqELQEKLEKAVKASTEateLLQNIRQAKER------AERELEKLHNREDSSEGIKKKLVEAEELE 267
Cdd:PRK04863 296 YTSRRQLAAEQYRLV-EMARELAELNEAESD---LEQDYQAASDHlnlvqtALRQQEKIERYQADLEELEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 268 EkhrEAQVSAQHLEVHLKQKEQHYEEkikvldnqIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSL 347
Cdd:PRK04863 372 E---EADEQQEENEARAEAAEEEVDE--------LKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 348 EQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQN-----RKLEEQLEKISHQDhsdkSRLL 422
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEawdvaRELLRRLREQRHLA----EQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 423 ELETRLREVSLEHEEQKlELKRQLTELQLSLQ---ERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHR 499
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQ-RAERLLAEFCKRLGknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 500 DEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITERE 572
Cdd:PRK04863 596 QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
|
|
| C1_SpBZZ1-like |
cd20824 |
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ... |
941-991 |
1.98e-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: 1.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 941 PHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCG 991
Cdd:cd20824 1 PHNFKPHSFSIPTKCDYCGEKIwGLSKKGLSCKDCGFNCHIKCELKVPPECP 52
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
196-448 |
2.09e-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: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 196 KLEKINA--EQQLKIQELQEKLEKAVKASTEATELLQNIRQAK---ERAERELEKLHNREDSSEgIKKKLVEAE------ 264
Cdd:TIGR01612 1471 KIKKDNAtnDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKelfEQYKKDVTELLNKYSALA-IKNKFAKTKkdseii 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 265 --ELEEKHREAQVSAQHLEVHLKQKEQhyeEKIKVLDNQIKKDLADKESLEnmMQRHEEEAHEKGKILSEQKAMINAMDS 342
Cdd:TIGR01612 1550 ikEIKDAHKKFILEAEKSEQKIKEIKK---EKFRIEDDAAKNDKSNKAAID--IQLSLENFENKFLKISDIKKKINDCLK 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 343 KIRSLEQRIVELS---EANKLAANSSlftqrNMKAQEEMISELRQQKFYLETQAGKLEaqnrKLEEQLEKISHQ-DHSDK 418
Cdd:TIGR01612 1625 ETESIEKKISSFSidsQDTELKENGD-----NLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDvDQHKK 1695
|
250 260 270
....*....|....*....|....*....|
gi 1039770408 419 SRLLELETRLREVSLEHEEqKLELKRQLTE 448
Cdd:TIGR01612 1696 NYEIGIIEKIKEIAIANKE-EIESIKELIE 1724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10-269 |
2.28e-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: 48.61 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRK 89
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 90 LQE-IKEQEYQAQVEEMRLMMNQleEDLVSARRRSDLYESELRESRLAAEEFKRKANEcqhklmkvvshpprgdsggtal 168
Cdd:COG4942 106 LAElLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAE---------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 169 ddlhkmqghagLTSAKDQgkpevgeyskLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHN 248
Cdd:COG4942 162 -----------LAALRAE----------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260
....*....|....*....|.
gi 1039770408 249 REDSSEGIKKKLVEAEELEEK 269
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
246-871 |
2.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 246 LHNREDSSEGIKKklvEAEELEEKHREAQVSAqhlevhLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHE 325
Cdd:PRK02224 182 LSDQRGSLDQLKA---QIEEKEEKDLHERLNG------LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 326 kgkilseqkaminamdskIRSLEQRIVELSEanKLAAnsslfTQRNMKAQEEMISELRQQKFYLETQagkleaqnrkLEE 405
Cdd:PRK02224 253 ------------------LETLEAEIEDLRE--TIAE-----TEREREELAEEVRDLRERLEELEEE----------RDD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 406 QLEKISHQDHSDKSRLLELEtrlrevslEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETT 485
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARRE--------ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 486 aeaeeeiqaltahrDEIQRKFDALRNSCTVITDLEEQLNQLTE--DNAELnnqnfylskQLDEASGANDEivqLRSEVDH 563
Cdd:PRK02224 370 --------------SELEEAREAVEDRREEIEELEEEIEELRErfGDAPV---------DLGNAEDFLEE---LREERDE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 564 LRreitEREMQLTSqkqaqlsapDLQTMEalkttcTMLEEqvldlealNDELLEKERQWEAWRSVLG----DEKSQFECR 639
Cdd:PRK02224 424 LR----EREAELEA---------TLRTAR------ERVEE--------AEALLEAGKCPECGQPVEGsphvETIEEDRER 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 640 VRELQRMLDTEKQSRARADQRITESRQVVELAVK----EHKAEilALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNAR 715
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierlEERRE--DLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 716 SLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIfrltqglqEALDRADLLKTERSDLEYQLENIQvlyshEKVKMEGTI 795
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERI--------ESLERIRTLLAAIADAEDEIERLR-----EKREALAEL 621
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 796 SQQTKliDFLQAKMDqpakKKKGLFSRRKEDpalptqvplqynelklALEKEKARCAELEEALQKTRIELRSAREE 871
Cdd:PRK02224 622 NDERR--ERLAEKRE----RKRELEAEFDEA----------------RIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
476-754 |
2.58e-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: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 476 QAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANdEIV 555
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEE---LEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVN-ELL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 556 QLRSEVDHLRREITEREMQLT------SQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEawrsvl 629
Cdd:pfam15905 142 KAKFSEDGTQKKMSSLSMELMklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKI------ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 630 gDEKSQFECRVRELQRMldteKQSRARADQRITESRQVVELAvKEHKAEILALQQALKEqklKAESLSDKLNDLEKKHAM 709
Cdd:pfam15905 216 -EEKSETEKLLEYITEL----SCVSEQVEKYKLDIAQLEELL-KEKNDEIESLKQSLEE---KEQELSKQIKDLNEKCKL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039770408 710 LEmnaRSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQ 754
Cdd:pfam15905 287 LE---SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
284-477 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 284 LKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMIN----AMDSKIRSLEQRIVELSEANK 359
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerreELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 360 LAANSSL--FTQRN------MKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEkishqdhsdksrllELETRLREV 431
Cdd:COG3883 108 LLGSESFsdFLDRLsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA--------------ELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039770408 432 slehEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQA 477
Cdd:COG3883 174 ----EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
238-757 |
2.85e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 238 RAERE--LEKLHN-REDSSEGIKKKLVEAEELEEKHREA-QVSAQHLEVHLkqkEQHYEEKIKVLD---NQIKKDLADKE 310
Cdd:PRK04863 781 RAAREkrIEQLRAeREELAERYATLSFDVQKLQRLHQAFsRFIGSHLAVAF---EADPEAELRQLNrrrVELERALADHE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 311 SLEnmmQRHEEEAhekgKILSEQKAMINAMDSKIR-----SLEQRIVELSEANKLAANSSLFTQRNMKA----------- 374
Cdd:PRK04863 858 SQE---QQQRSQL----EQAKEGLSALNRLLPRLNlladeTLADRVEEIREQLDEAEEAKRFVQQHGNAlaqlepivsvl 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 375 --QEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLL----ELETRLREVSLEHEEQKLELKRQLTE 448
Cdd:PRK04863 931 qsDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLaknsDLNEKLRQRLEQAEQERTRAREQLRQ 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 449 LQLSLQERESQLTALQAARAALESQLRQAKTELEET-TAEAEEEIQALTAHRDEIQrkfDALRNSCTVITDLEEQLnQLT 527
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgVPADSGAEERARARRDELH---ARLSANRSRRNQLEKQL-TFC 1086
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 528 EdnAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITER--EMQLTSQKQAQLSAPDLQTMeALKttctmleeqv 605
Cdd:PRK04863 1087 E--AEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAYLSADELRSM-SDK---------- 1153
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 606 lDLEAL------NDELLEKERQWEAWRSVlgDEKSQFECRVRELQRmldtekqSRARADqrITESRQVVElavkehkaei 679
Cdd:PRK04863 1154 -ALGALrlavadNEHLRDVLRLSEDPKRP--ERKVQFYIAVYQHLR-------ERIRQD--IIRTDDPVE---------- 1211
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 680 lALQQalkeqklkaesLSDKLNDLEKkhamlEMNARslQQKLETERElkqrllEEQAKLQQQMDLQKNHIFRLTQGLQ 757
Cdd:PRK04863 1212 -AIEQ-----------MEIELSRLTE-----ELTSR--EQKLAISSE------SVANIIRKTIQREQNRIRMLNQGLQ 1264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-497 |
2.88e-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: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIV 352
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 353 ELSEA-NKLAA----NSSLFTQRNMKAQEEMISELRQQKFYLETQAgklEAQNRKLEEQLEkishqdhsDKSRLLELETR 427
Cdd:COG3883 83 ERREElGERARalyrSGGSVSYLDVLLGSESFSDFLDRLSALSKIA---DADADLLEELKA--------DKAELEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 428 LREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTA 497
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
380-866 |
2.88e-05 |
|
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: 48.95 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 380 SELRQQKFYLETQAGKLEAQNRKLEE---QLEKISH------QDHSDKSR-----------LLELETRLREVSLEHEEQK 439
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAIQElqfENEKVSLkleeeiQENKDLIKennatrhlcnlLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 440 LELKRQLTELQLSLqerESQLTALQAARAalesQLRQAKTELEETTAEAEEEIQALtahRDEIQRKFDALRNSCTVItdl 519
Cdd:pfam05483 179 EETRQVYMDLNNNI---EKMILAFEELRV----QAENARLEMHFKLKEDHEKIQHL---EEEYKKEINDKEKQVSLL--- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 520 eeqLNQLTEDNAELNNQNFYLSK------QLDEASGANDE-IVQLRSEVDHLRREITEREMQLTSQKQAQLS-APDLQTm 591
Cdd:pfam05483 246 ---LIQITEKENKMKDLTFLLEEsrdkanQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKAlEEDLQI- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 592 eALKTTCTMLEEQVLDLEALNDE-------LLEKERQWEAWRSVLGDEKSQFECRVRELqRMLDTEKQSRARADQRITES 664
Cdd:pfam05483 322 -ATKTICQLTEEKEAQMEELNKAkaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 665 RQVVELAVKEHKaEILALQQALKEQKLKAESLSDKLNDLEKKHAML----EMNARSLQQKLETERELKQRLLEEQAKLQQ 740
Cdd:pfam05483 400 KNNKEVELEELK-KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 741 QMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQqtklIDFLQAKMDQpakkkkglf 820
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ----IENLEEKEMN--------- 545
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1039770408 821 sRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELR 866
Cdd:pfam05483 546 -LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
45-780 |
3.03e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 45 EQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQeiKEQEYQAQVEEMRLMMnqleedlvsARRRSD 124
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ--AETELCAEAEEMRARL---------AARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 125 LYE--SELrESRLAAEEfkrkanECQHKLMkvvshpprgdsggtalDDLHKMQGHAGLTSAKDQGKPEVGEYSKLEKINA 202
Cdd:pfam01576 73 LEEilHEL-ESRLEEEE------ERSQQLQ----------------NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 203 EQQLK--------IQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSegikkklveAEELEEKHREAQ 274
Cdd:pfam01576 130 EAKIKkleedillLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---------ISDLEERLKKEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 275 VSAQHLEVHLKQKEQHYEEkikvLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVEL 354
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTD----LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 355 SEanklaansSLFTQRNMKAQEEmiselrQQKFYLETQagkLEAQNRKLEEQLEKISHQDHSDKSR---LLELETRLREV 431
Cdd:pfam01576 277 QE--------DLESERAARNKAE------KQRRDLGEE---LEALKTELEDTLDTTAAQQELRSKReqeVTELKKALEEE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 432 SLEHEEQKLELKR----QLTELQLSLQERESQLTALQAARAALESQ----------LRQAKTELEETTAEAEEEIQALTA 497
Cdd:pfam01576 340 TRSHEAQLQEMRQkhtqALEELTEQLEQAKRNKANLEKAKQALESEnaelqaelrtLQQAKQDSEHKRKKLEGQLQELQA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 498 HRDEIQRkfdalrnsctVITDLEEQLNQLTednAELNNqnfyLSKQLDEASGANdeiVQLRSEVDHLRREITEREMQLTS 577
Cdd:pfam01576 420 RLSESER----------QRAELAEKLSKLQ---SELES----VSSLLNEAEGKN---IKLSKDVSSLESQLQDTQELLQE 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 578 QKQAQLSapdlqtmeaLKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARA 657
Cdd:pfam01576 480 ETRQKLN---------LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 658 DQRITESRQvvELAVKEHKAEILA-----LQQALKEQKLKAESLSDKLNDLEKKHamlemnaRSLQQKLETERELKQRLL 732
Cdd:pfam01576 551 QRELEALTQ--QLEEKAAAYDKLEktknrLQQELDDLLVDLDHQRQLVSNLEKKQ-------KKFDQMLAEEKAISARYA 621
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1039770408 733 EEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENI 780
Cdd:pfam01576 622 EERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
428-754 |
3.25e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 428 LREVSLEHEEQKLeLKRQLTELQLSLQERESQ---LTALQAARAALESQLRQAKTEleettaeaeeeIQALTAHRDEIQR 504
Cdd:PRK11281 48 LNKQKLLEAEDKL-VQQDLEQTLALLDKIDRQkeeTEQLKQQLAQAPAKLRQAQAE-----------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 505 KfdalRNSCTVITDLEEQLNQLTEDNAELNNqnfylskqldEASGANDEIVQLRSEVDHLRREITE---REMQLTSQK-- 579
Cdd:PRK11281 116 E----TLSTLSLRQLESRLAQTLDQLQNAQN----------DLAEYNSQLVSLQTQPERAQAALYAnsqRLQQIRNLLkg 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 580 ----QAQLSAPDLQTMEAlkttctmleEQVLdLEALNDEllekERQWEAWRSVLGDeksqfecrVRELQRMLDTEKQsrA 655
Cdd:PRK11281 182 gkvgGKALRPSQRVLLQA---------EQAL-LNAQNDL----QRKSLEGNTQLQD--------LLQKQRDYLTARI--Q 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 656 RADQRITESRQVV---ELAVKEHKAEilALQQALKEQKLKAESLsdklndlekkhamlemnarsLQQKLETERELKQRLL 732
Cdd:PRK11281 238 RLEHQLQLLQEAInskRLTLSEKTVQ--EAQSQDEAARIQANPL--------------------VAQELEINLQLSQRLL 295
|
330 340
....*....|....*....|....*
gi 1039770408 733 EEQAKLQQ--QMDLQ-KNHIFRLTQ 754
Cdd:PRK11281 296 KATEKLNTltQQNLRvKNWLDRLTQ 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-508 |
3.34e-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: 47.23 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 339 AMDSKIRSLEQRIVELSEAnklaansslftqrnmkaqeemISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDK 418
Cdd:COG1579 14 ELDSELDRLEHRLKELPAE---------------------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 419 SRLLELETRLREVS-------LEHEEQKLELKRQLTE-LQLSLQER----ESQLTALQAARAALESQLRQAKTELEETTA 486
Cdd:COG1579 73 ARIKKYEEQLGNVRnnkeyeaLQKEIESLKRRISDLEdEILELMERieelEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|..
gi 1039770408 487 EAEEEIQALTAHRDEIQRKFDA 508
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP 174
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
501-810 |
3.37e-05 |
|
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: 48.42 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 501 EIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFY----LSKQLDEasgandEIVQLRSEVDHLRREITEREMQLT 576
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGenaeSSKRLNE------NANNLIKQFENTKEKIAEYTKSID 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 577 SQKQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQF--ECRVRELQRMLDTEKQSR 654
Cdd:COG5185 307 IKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 655 ARADQRITESRQVVELAVKEHKAeilALQQALKEQKLKAESLSDKLNDLEKKhamlemNARSLQQKLETERELKQRLLEE 734
Cdd:COG5185 387 ESTKESLDEIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSS------NEEVSKLLNELISELNKVMREA 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 735 QAKLQQQMDLQKNHIFRltqGLQEALDRADLlktERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMD 810
Cdd:COG5185 458 DEESQSRLEEAYDEINR---SVRSKKEDLNE---ELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLK 527
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
11-384 |
3.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 11 QEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATY--ITECSSLKRSLEQARMEVSQEDDKALQL---LHDIRE 85
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELeerLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 86 QSRKLQEIKEQEYQAQVEEMRLM----------MNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMK-- 153
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaa 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 154 -----------------VVSHPPRGDSGGTALDDLHKMQ---------GHAGLTSAKDQGKPEVGEYSKLEKINAEQQLK 207
Cdd:COG4717 241 leerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 208 IQELQEKLEKAVKAS-TEATELLQNIRQAK------ERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHL 280
Cdd:COG4717 321 LEELLAALGLPPDLSpEELLELLDRIEELQellreaEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 281 EVHLKQKEQHYEEKIKVLDNQIkkDLADKESLENMMQRHEEEahekgkiLSEQKAMINAMDSKIRSLEQRIVELSEANKL 360
Cdd:COG4717 401 KEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEE-------LEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|....
gi 1039770408 361 AansslftqRNMKAQEEMISELRQ 384
Cdd:COG4717 472 A--------ELLQELEELKAELRE 487
|
|
| C1_CeDKF1-like_rpt2 |
cd20798 |
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ... |
941-992 |
5.83e-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: 5.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 941 PHRFNVGLNMRATKCAVClDTVHFG--RQASKCLECQVMCHPKCSTCLPATCGL 992
Cdd:cd20798 1 PHTLAEHNYKKPTVCKVC-DKLLVGlvRQGLKCRDCGVNVHKKCASLLPSNCRL 53
|
|
| PH_ROCK |
cd01242 |
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ... |
1024-1069 |
5.83e-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: 43.88 E-value: 5.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1039770408 1024 HLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPV 1069
Cdd:cd01242 2 RLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPI 47
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6-478 |
6.83e-05 |
|
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: 47.91 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 6 EAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQD-----------LATYITECSSLKRSL------------ 62
Cdd:pfam12128 296 DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdietaaadqeqLPSWQSELENLEERLkaltgkhqdvta 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 63 --EQARMEVSQEDDKALQLLHD----IREQSRKLQEIKEQEYQAQVEEMRLMMNQ------------------------- 111
Cdd:pfam12128 376 kyNRRRSKIKEQNNRDIAGIKDklakIREARDRQLAVAEDDLQALESELREQLEAgklefneeeyrlksrlgelklrlnq 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 112 ----------------------------------LEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMkvvsh 157
Cdd:pfam12128 456 atatpelllqlenfderierareeqeaanaeverLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLF----- 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 158 PPRG--------------DSGGTALDD--LHKMQGHAGLTSAKDQGKPEVGEYS-KLEKINAEQQLKI-QELQEKLEKAV 219
Cdd:pfam12128 531 PQAGtllhflrkeapdweQSIGKVISPelLHRTDLDPEVWDGSVGGELNLYGVKlDLKRIDVPEWAASeEELRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 220 KASTEATELLQNIRQAKERAERELEKLHNRE-DSSEGIKKKLVEAEELEEKHREAQVSAQH-LEVHLKQKEQH---YEEK 294
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREEtFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKDSANERlnsLEAQ 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 295 IKVLDNQIKKDLA--DKESLENMMQRHEeeahekgkilsEQKAMINAMDSKIRSLEQRIVELSEANKlAANSSLFTQ--R 370
Cdd:pfam12128 691 LKQLDKKHQAWLEeqKEQKREARTEKQA-----------YWQVVEGALDAQLALLKAAIAARRSGAK-AELKALETWykR 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 371 NMKAQ---EEMISELRQQKFYLETqagKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLT 447
Cdd:pfam12128 759 DLASLgvdPDVIAKLKREIRTLER---KIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA 835
|
570 580 590
....*....|....*....|....*....|.
gi 1039770408 448 ELQLSLQERESQLTALQAARAALESQLRQAK 478
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| C1_aPKC |
cd20794 |
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ... |
943-991 |
7.39e-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: 7.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1039770408 943 RFNvglnmRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCG 991
Cdd:cd20794 9 RFN-----RRAVCAYCSDRIwGLGRQGYKCINCKLLVHKKCHKLVKVACG 53
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
230-476 |
7.57e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 230 QNIRQAKERAERELEKLhnrEDSSEGIKKKLVEAEELEEKHREaqvsaQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADK 309
Cdd:COG3206 164 QNLELRREEARKALEFL---EEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 310 ESLENMMQRHEEEAHEKGKILSEQKAminamDSKIRSLEQRIVELSEanKLAANSSLFTQRN--MKAQEEMISELRQQkf 387
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEA--ELAELSARYTPNHpdVIALRAQIAALRAQ-- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 388 yletqagkLEAQNRKLEEQLEkishqdhsdkSRLLELETRLREVSLEHEEQKLELKRqltelqlsLQERESQLTALQAAR 467
Cdd:COG3206 307 --------LQQEAQRILASLE----------AELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREV 360
|
....*....
gi 1039770408 468 AALESQLRQ 476
Cdd:COG3206 361 EVARELYES 369
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
185-328 |
7.63e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 185 DQGKPEVGEYSKLEKINAEQqlKIQELQEKLEKAVKAST-EATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEA 263
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKE--EIHKLRNEFEKELRERRnELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 264 EE-LEEKHREAQVSAQHLEVHLKQ-----KEQHYEEKIKVLDNQIKKDLAdkesleNMMQRHEEEAHEKGK 328
Cdd:PRK12704 123 QQeLEKKEEELEELIEEQLQELERisgltAEEAKEILLEKVEEEARHEAA------VLIKEIEEEAKEEAD 187
|
|
| PH_MRCK |
cd01243 |
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ... |
1026-1141 |
7.66e-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: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 1026 EGWMKVPrnnKRG--QQGWDRKYIVLEGSKVLIYD-NEAREAGQRPVEEFELCLPDGDVSIhGAVGASELANTAKADVPY 1102
Cdd:cd01243 15 EGYVRVP---KPGgvKKGWQRQFAVVCDFKLFLFDiSEDKASQPSQVASQVLDMRDEEFSV-SSVLASDVIHANKKDIPC 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039770408 1103 ILKME-SHPHTTCWPGRTLyLLAPSFPDKQRWVTALESVV 1141
Cdd:cd01243 91 IFRVSaSQLAPPSLKFSLL-MLADSENEKQKWVDALNELH 129
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
427-763 |
7.76e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 427 RLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEEttaeaeeeIQALTAHRDEIQRKF 506
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNL--------VQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 507 DALrnsctviTDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEI------VQLRSEVDHLRREITEREMQLTSQKQ 580
Cdd:PRK04863 355 ADL-------EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladYQQALDVQQTRAIQYQQAVQALERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 581 AQLSAPDLqTMEALKTtctMLEEQVLDLEALNDELLEKERQWeawrSVLGDEKSQFECRVRELQRMLDTEKQSRAR--AD 658
Cdd:PRK04863 428 QLCGLPDL-TADNAED---WLEEFQAKEQEATEELLSLEQKL----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 659 QRITESRQVVELAVKEH--KAEILALQQALKEQKlKAESLsdkLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQA 736
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQqlRMRLSELEQRLRQQQ-RAERL---LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340
....*....|....*....|....*..
gi 1039770408 737 KLQQQMDLQKNHIFRLTQGLQEALDRA 763
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARA 602
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
640-894 |
8.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 640 VRELqrMLDtEKQSRARAD------QRITESRQVVELAVKEHKA--EILALQQALKEQKLKAESLSDKLNDLEKKHAMLE 711
Cdd:COG4913 213 VREY--MLE-EPDTFEAADalvehfDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 712 MNArsLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEA-LDRADLLKTERSDLEYQLENIqvlyshekvk 790
Cdd:COG4913 290 LEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEER---------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 791 mEGTISQQTKLIDFLQAKMDQPAKkkkGLFSRRKEDPALPTQVPLQYNELKLALekekarcAELEEALQKTRIELRSARE 870
Cdd:COG4913 358 -ERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEAL-------AEAEAALRDLRRELRELEA 426
|
250 260
....*....|....*....|....
gi 1039770408 871 EAAHRKATDHPHPSTPATARQQIA 894
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALA 450
|
|
| C1_Munc13-1 |
cd20858 |
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ... |
940-990 |
8.30e-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: 8.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 940 IPHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20858 6 TPHNFEVWTATTPTYCYECEGLLwGIARQGMRCTECGVKCHEKCQDLLNADC 57
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
658-815 |
8.54e-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: 45.69 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 658 DQRITESRQvvelAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLEterELKQRLLE---- 733
Cdd:COG1579 16 DSELDRLEH----RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNvrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 734 -EQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQP 812
Cdd:COG1579 89 kEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
...
gi 1039770408 813 AKK 815
Cdd:COG1579 169 AAK 171
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
205-529 |
8.84e-05 |
|
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: 46.98 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 205 QLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSE-GIKKKLVEAEEL--EEKHREAQVSAqhLE 281
Cdd:pfam19220 47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEaALREAEAAKEELriELRDKTAQAEA--LE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 282 VHLKQ---KEQHYEEKIKVLDNQIK---KDLADKES-LENMMQRH---EEEAHEKGKILSEQKAMINAMDSKIRSLEQRI 351
Cdd:pfam19220 125 RQLAAeteQNRALEEENKALREEAQaaeKALQRAEGeLATARERLallEQENRRLQALSEEQAAELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 352 ------VELSEANKLAANSSlfTQRNMKAQEEMISELRQQKfylETQAGKLEAQNRKLE--EQLekishqdhsdksrLLE 423
Cdd:pfam19220 205 datrarLRALEGQLAAEQAE--RERAEAQLEEAVEAHRAER---ASLRMKLEALTARAAatEQL-------------LAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 424 LETRLRevslEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRdeiq 503
Cdd:pfam19220 267 ARNQLR----DRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKD---- 338
|
330 340
....*....|....*....|....*.
gi 1039770408 504 rkfDALRNSCTVITDLEEQLNQLTED 529
Cdd:pfam19220 339 ---AALERAEERIASLSDRIAELTKR 361
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
564-701 |
1.14e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 564 LRREITEREMQLtSQKQAQLSapDLQTMEAL-KTTCTMLEEQVLDLEA-LNDELLEKERqWEAWRSVLGDEKSQFECRVR 641
Cdd:PRK09039 44 LSREISGKDSAL-DRLNSQIA--ELADLLSLeRQGNQDLQDSVANLRAsLSAAEAERSR-LQALLAELAGAGAAAEGRAG 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 642 ELQRMLDTEKQSRARADQRITE-SRQVVELavkehKAEILALQQAL-------KEQKLKAESLSDKLN 701
Cdd:PRK09039 120 ELAQELDSEKQVSARALAQVELlNQQIAAL-----RRQLAALEAALdasekrdRESQAKIADLGRRLN 182
|
|
| C1_nPKC_theta-like_rpt2 |
cd20837 |
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
942-990 |
1.18e-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: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 942 HRFNVGLNMRATKCAVClDTVHFG--RQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20837 1 HRFKVYNYMSPTFCDHC-GSLLWGlfRQGLKCEECGMNVHHKCQKKVANLC 50
|
|
| C1_aPKC_iota |
cd21094 |
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ... |
942-993 |
1.28e-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: 1.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 942 HRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCGLP 993
Cdd:cd21094 3 HTFQAKRFNRRAHCAICTDRIwGLGRQGYKCINCKLLVHKKCHKLVTIECGRH 55
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
211-475 |
1.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 211 LQEKLEKAVKASTEATELLQNIRQAKERAERELEKLhnredssegikkklveaeeleekhreaqvSAQHLEVHLKQKEQH 290
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----------------------------RQKNGLVDLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 291 YEEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAminamDSKIRSLEQRIVELSEanKLAANSSLFTQR 370
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEA--ELAELSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 371 N--MKAQEEMISELRQQkfyLETQAGKLEAQnrkLEEQLEKISHQDHSDKSRLLELETRLREVSlEHEEQKLELKRQLTE 448
Cdd:COG3206 290 HpdVIALRAQIAALRAQ---LQQEAQRILAS---LEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEV 362
|
250 260
....*....|....*....|....*..
gi 1039770408 449 LQLSLQERESQLTALQAARAALESQLR 475
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
550-743 |
1.72e-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: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 550 ANDEIVQLRSEVDHLRREITEREMQLtSQKQAQLSapdlQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVL 629
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAEL-DALQAELE----ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 630 GDeksqfecRVRELQR------MLDTEKQSRARAD--QRITESRQVVElavkeHKAEILALQQALKEQ-KLKAESLSDKL 700
Cdd:COG3883 89 GE-------RARALYRsggsvsYLDVLLGSESFSDflDRLSALSKIAD-----ADADLLEELKADKAElEAKKAELEAKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039770408 701 NDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMD 743
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
539-783 |
1.88e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 539 YLSKQLDEASGANDEIVQ-LRSEVDHLRREITEREMQLTS-QKQAQLSAPDLQTMEALKTTcTMLEEQVLDLEAlndELL 616
Cdd:COG3206 161 YLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQL-SELESQLAEARA---ELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 617 EKERQWEAWRSVLGDEKSQF-----ECRVRELQRMLDTEKQSRARADQRITE-SRQVVELavkehKAEILALQQALKEQK 690
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELSARYTPnHPDVIAL-----RAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 691 LKAeslsdkLNDLEKKHAMLEMNARSLQQKLEterELKQRLLEEQAKLQQQMDLQKNhIFRLTQGLQEALDRADLLKTER 770
Cdd:COG3206 312 QRI------LASLEAELEALQAREASLQAQLA---QLEARLAELPELEAELRRLERE-VEVARELYESLLQRLEEARLAE 381
|
250
....*....|...
gi 1039770408 771 SdleYQLENIQVL 783
Cdd:COG3206 382 A---LTVGNVRVI 391
|
|
| C1_MTMR-like |
cd20828 |
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ... |
938-991 |
1.93e-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: 1.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 938 HNIPHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATCG 991
Cdd:cd20828 2 FTQPHNFEPHSFVTPTNCDYCLQILwGIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
207-476 |
2.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 207 KIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNRED-SSEGIKKKLVEAE--ELEEKHREAQVSAQHLEvH 283
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEySWDEIDVASAEREiaELEAELERLDASSDDLA-A 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 284 LKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRHEEEahekgkilseqkaminamdskIRSLEQRIVELSEANKLAAN 363
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---------------------LDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 364 SSLFTQRNMKAQEEMISELRQQkfyLETQAGKLEAQNRKLEEQLEKI----SHQDHSDKSRL----------LELETRLR 429
Cdd:COG4913 749 ALLEERFAAALGDAVERELREN---LEERIDALRARLNRAEEELERAmrafNREWPAETADLdadleslpeyLALLDRLE 825
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039770408 430 EVSL-EHEEQkleLKRQLTElqLSLQERESQLTALQAARAALESQLRQ 476
Cdd:COG4913 826 EDGLpEYEER---FKELLNE--NSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| C1_PKD2_rpt2 |
cd20843 |
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ... |
940-990 |
2.80e-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: 2.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 940 IPHRFNVGLNMRATKCAVCLDTVH-FGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20843 10 VPHTFVIHSYTRPTVCQFCKKLLKgLFRQGLQCKDCKFNCHKRCATRVPNDC 61
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
171-464 |
3.11e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 171 LHKMQGHAGLTSAKDQGKPEVGEYSKLEKiNAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERA----ERELEKL 246
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQERLRQ-EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 247 hnredssegikkklveaeELEEKHREAQvsaqhlevHLKQKEQHYE-EKIKVLDNqikkdLADKESLENMMQRHEEEAHE 325
Cdd:pfam17380 354 ------------------RQEERKRELE--------RIRQEEIAMEiSRMRELER-----LQMERQQKNERVRQELEAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 326 KGKILSEQKAminamdskiRSLEQRIVELSEANKLAANSSlftQRNMKAQEEMISElrqqkfylETQAGKLEAQNRklEE 405
Cdd:pfam17380 403 KVKILEEERQ---------RKIQQQKVEMEQIRAEQEEAR---QREVRRLEEERAR--------EMERVRLEEQER--QQ 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 406 QLEKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQ 464
Cdd:pfam17380 461 QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
447-777 |
3.28e-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: 45.27 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 447 TELQLSLQERESQLTALQAARAALESQLRQAKTEleettaeaeeeiqaltahRDEIQRKFDALRNSctvITDLEEQLNQL 526
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRD------------------REQWERQRRELESR---VAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 527 TEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQAQLSAPDLQTMEALKTTCTMLEEQV- 605
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 606 -----LDLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTEKQSRARADQRITESRQVvelavkehKAEIL 680
Cdd:pfam07888 173 rkqlqAKLQQTEEELRSLSKEFQELRNSLAQRDTQ----VLQLQDTITTLTQKLTTAHRKEAENEAL--------LEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 681 ALQQALKEQKLKAESLSDKLNDL--EKKHAMLEMNARSLQ------QKLETE---RELKQRLLEEQAKLQQQMDLQKNHI 749
Cdd:pfam07888 241 SLQERLNASERKVEGLGEELSSMaaQRDRTQAELHQARLQaaqltlQLADASlalREGRARWAQERETLQQSAEADKDRI 320
|
330 340
....*....|....*....|....*...
gi 1039770408 750 FRLTQGLQEALDRADLLKTERSDLEYQL 777
Cdd:pfam07888 321 EKLSAELQRLEERLQEERMEREKLEVEL 348
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
192-313 |
3.34e-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: 44.15 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 192 GEYSKLEKINAEQQLKIQELQEKLEKAvkasteaTELLQNIRQAKE--RAERELEKLHNR-EDSSEGIKKKLVEAEELEE 268
Cdd:COG1579 52 TELEDLEKEIKRLELEIEEVEARIKKY-------EEQLGNVRNNKEyeALQKEIESLKRRiSDLEDEILELMERIEELEE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039770408 269 KHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLE 313
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
208-343 |
3.40e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 208 IQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSS-----EGIKKKLVEA-EELEEKHREAQVSAQhlE 281
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaeKEAQQAIKEAkKEADEIIKELRQLQK--G 599
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 282 VHLKQKEQHYEEKIKVLDNQIKKdlADKESLENMMQRHEEEAHEKGKILS-EQKAMINAMDSK 343
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEK--KEKKKKKQKEKQEELKVGDEVKYLSlGQKGEVLSIPDD 660
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
194-776 |
3.71e-04 |
|
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: 45.12 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 194 YSKLEKINAEQQLKIQELQEKLEKAvkasteatELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEE-LEEKHRE 272
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHKRARI--------ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEaLREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 273 AQVSAQHLEVHLKQKEQHY--EEKIKVLDNQIKKDLAD-KESLENMMQRHEEEAHEKGKI---LSEQKAMINAMDSKIRS 346
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKEsqLADAREVISCLKNELSElRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 347 L----------EQRIVELSEANKLAANSSLFTqRNMKAQEEMISElrqqkfyLETQAGKLEAQNRKLEEQLEKIS---HQ 413
Cdd:pfam05557 158 LekqqsslaeaEQRIKELEFEIQSQEQDSEIV-KNSKSELARIPE-------LEKELERLREHNKHLNENIENKLllkEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 414 DHSDKSRLLELE-TRLREVSLEHEEQKLELKrqLTELQLSLQERESQLTALQAARAALEsQLRQAKTELEETTAEAEEEI 492
Cdd:pfam05557 230 VEDLKRKLEREEkYREEAATLELEKEKLEQE--LQSWVKLAQDTGLNLRSPEDLSRRIE-QLQQREIVLKEENSSLTSSA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 493 QALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNNQNFYLSKQLDeasgandeivQLRSEVDHLRREITERE 572
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKK---IEDLNKKLKRHKALVRRLQRRVLLLTKERD----------GYRAILESYDKELTMSN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 573 mqlTSQKQaqlsapdLQTMEAlkttctmLEEQVLDLEALNDELlekerqweawrsvlgdeksqfECRVRELQRMLDTEKQ 652
Cdd:pfam05557 374 ---YSPQL-------LERIEE-------AEDMTQKMQAHNEEM---------------------EAQLSVAEEELGGYKQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 653 SRARADQRITESRQVVELA-VKEHKAEILALQQALKEQKLKAESLSDKLNDLEkkhamLEMNARSLQQKLETER------ 725
Cdd:pfam05557 416 QAQTLERELQALRQQESLAdPSYSKEEVDSLRRKLETLELERQRLREQKNELE-----MELERRCLQGDYDPKKtkvlhl 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770408 726 ------ELKQRLLEEQAKLQQQMDLQKnhifRLTQGLQEALDRADLLKTERSDLEYQ 776
Cdd:pfam05557 491 smnpaaEAYQQRKNQLEKLQAEIERLK----RLLKKLEDDLEQVLRLPETTSTMNFK 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
514-742 |
4.02e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 514 TVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASG----ANDEIVQLRSEVDHLRREITEREMQLtSQKQAQLSApDLQ 589
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEeyneLQAELEALQAEIDKLQAEIAEAEAEI-EERREELGE-RAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 590 TMEALKTTCTMLEeQVLDLEALNDELlekeRQWEAWRSVLGDEKSQFEcRVRELQRMLDTEKQSRARADQRITESRQVVE 669
Cdd:COG3883 94 ALYRSGGSVSYLD-VLLGSESFSDFL----DRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 670 LAVKEhkaeilaLQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQM 742
Cdd:COG3883 168 AAKAE-------LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| C1_Munc13-2-like |
cd20859 |
protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar ... |
936-990 |
4.20e-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: 4.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 936 MHHNIPHRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20859 14 ISCTTPHNFEVWTATTPTYCYECEGLLwGIARQGMRCSECGVKCHEKCQDLLNADC 69
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
197-531 |
4.76e-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: 44.68 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 197 LEKINAEQQLKIQELQeklekavKASTEATELLQNIRQAKERAEReLEKLhnrEDSSEGIKKKL---------VEAEE-- 265
Cdd:pfam05622 92 LEKEVLELQHRNEELT-------SLAEEAQALKDEMDILRESSDK-VKKL---EATVETYKKKLedlgdlrrqVKLLEer 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 266 ----------LEEKHREAQVSAQHLEVHLKQ-KEQHyeekiKVLDNQIKKdlADKESLE--NMMQRHEEEAHEKGKILSE 332
Cdd:pfam05622 161 naeymqrtlqLEEELKKANALRGQLETYKRQvQELH-----GKLSEESKK--ADKLEFEykKLEEKLEALQKEKERLIIE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 333 QKAMINAMDS-KIRSLEQRivELSEANKLAANSSLfTQRNMkAQEEMISELRQQKFYLETQAGKL-EAQNRKLEEQLEKI 410
Cdd:pfam05622 234 RDTLRETNEElRCAQLQQA--ELSQADALLSPSSD-PGDNL-AAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTEL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 411 SHQDHSDKSRLLELETRLRevslEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettaEAEE 490
Cdd:pfam05622 310 QQLLEDANRRKNELETQNR----LANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH--------EAQS 377
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039770408 491 EIQALTAHRDEIQRKFDAlrNSCTVITDLEEQLNQLTEDNA 531
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDS--NLAQKIDELQEALRKKDEDMK 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
238-615 |
5.05e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 238 RAERE--LEKLHnredssegikkklVEAEELEEKHREA---------------QVSAQHLEVHLkqkEQHYEEKIKVLDN 300
Cdd:COG3096 780 RAAREkrLEELR-------------AERDELAEQYAKAsfdvqklqrlhqafsQFVGGHLAVAF---APDPEAELAALRQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 301 QIKKDLADKESLENMMQRHEEEAHEkgkiLSEQKAMINAMDSKI-----RSLEQRIVELSEANKLAANSSLFTQRNMKAQ 375
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQ----LKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQEAQAFIQQHGKAL 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 376 ---EEMIS----------ELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLL----ELETRLREVSLEHEEQ 438
Cdd:COG3096 920 aqlEPLVAvlqsdpeqfeQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLgensDLNEKLRARLEQAEEA 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 439 KLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTA-HRDEIQRKFDALRNSCtviT 517
Cdd:COG3096 1000 RREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARiRRDELHEELSQNRSRR---S 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 518 DLEEQLnQLTEdnAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITER--EMQLTSQKQAQLSAPDLQTM--EA 593
Cdd:COG3096 1077 QLEKQL-TRCE--AEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNdvERRLHRRELAYLSADELRSMsdKA 1153
|
410 420
....*....|....*....|..
gi 1039770408 594 LKTtctmLEEQVLDLEALNDEL 615
Cdd:COG3096 1154 LGA----LRLAVADNEHLRDAL 1171
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
33-478 |
5.42e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 33 ELKASETQRSLLEQDLATYITECSSLKRSlEQARMEVSQEDDKALQLlhDIREQSRKLQEIKEQEYQAQVEemrlmmnqL 112
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRT-EQQRLEKNEDQLKIITM--ELQKKSSELEEMTKFKNNKEVE--------L 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 113 EE-DLVSARRRSDLYESELRESrlAAEEFKRKANECQHKLMkvvshpprgdsggTALDDLHKMQGHAGLTSAKDQgkpev 191
Cdd:pfam05483 408 EElKKILAEDEKLLDEKKQFEK--IAEELKGKEQELIFLLQ-------------AREKEIHDLEIQLTAIKTSEE----- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 192 gEYSKlekinaeqqlKIQELQEKLEKAVKASTEATE-----LLQNIRQAKERAERELEKLHNREDSSEGIKKK---LVEA 263
Cdd:pfam05483 468 -HYLK----------EVEDLKTELEKEKLKNIELTAhcdklLLENKELTQEASDMTLELKKHQEDIINCKKQEermLKQI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 264 EELEEKhreaqvsaqhlEVHLKQKEQHYEEKIKVLDNQIKKDLADKEslENmMQRHEEEAHEKGKILSEQKAMINAMDSK 343
Cdd:pfam05483 537 ENLEEK-----------EMNLRDELESVREEFIQKGDEVKCKLDKSE--EN-ARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 344 IRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELR------QQKFYLETQAGKLEAQNRKLEEQ--LEKISH-QD 414
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelasaKQKFEEIIDNYQKEIEDKKISEEklLEEVEKaKA 682
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 415 HSDKSRLLELETRLR------EVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAK 478
Cdd:pfam05483 683 IADEAVKLQKEIDKRcqhkiaEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIK 752
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
227-523 |
5.49e-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: 44.50 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 227 ELLQNIRQAKERAERELEKLHNREDSSEGIKKK----LVEAEELEEKHREAQVSAQHLEVHLKQKEQHYE---EKIKVLD 299
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEkdalLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkERAKKAG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 300 NQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSeaNKLAAnsslfTQRNMKAQEEMI 379
Cdd:pfam07888 164 AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTT-----AHRKEAENEALL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 380 SELRQQKFYLETQAGKLEAQNRKLEEQlekISHQDHS----DKSRL--LELETRLREVSLEHEEQKLELKRQLTELQLSL 453
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEELSSM---AAQRDRTqaelHQARLqaAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 454 QERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQL 523
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQL 383
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
232-401 |
5.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 232 IRQAKERAERELEklhNREDSSEGIKK-KLVEA--------EELEEKHREAQVSAQHLEVHLKQKEQHYEEkikvldnqi 302
Cdd:PRK12704 33 IKEAEEEAKRILE---EAKKEAEAIKKeALLEAkeeihklrNEFEKELRERRNELQKLEKRLLQKEENLDR--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 303 KKDLADKEslENMMQRHEEEAHEKGKILSEQKAMInamDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISEL 382
Cdd:PRK12704 101 KLELLEKR--EEELEKKEKELEQKQQELEKKEEEL---EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLI 175
|
170
....*....|....*....
gi 1039770408 383 RQqkfyLETQAgKLEAQNR 401
Cdd:PRK12704 176 KE----IEEEA-KEEADKK 189
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
648-807 |
5.80e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 648 DTEKQSRARADQRITESRQVVELAVKE---HKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQ------ 718
Cdd:PHA02562 202 KNIEEQRKKNGENIARKQNKYDELVEEaktIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmy 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 719 ----------QKLETERELKQRLLEEQAKLQQQMDLQKNHIfrltQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEk 788
Cdd:PHA02562 282 ekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAI----DELEEIMDEFNEQSKKLLELKNKISTNKQSLITL- 356
|
170
....*....|....*....
gi 1039770408 789 vkmEGTISQQTKLIDFLQA 807
Cdd:PHA02562 357 ---VDKAKKVKAAIEELQA 372
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-508 |
5.93e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 195 SKLEKINAEQQL---KIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNredssegikkklvEAEELEEKHR 271
Cdd:COG4372 66 EELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------------ERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 272 EAQVSAQHLEVHLKQKEqhyeEKIKVLDNQIKKDLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRI 351
Cdd:COG4372 133 QLEAQIAELQSEIAERE----EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 352 VELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREV 431
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770408 432 SLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDA 508
Cdd:COG4372 289 EEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-277 |
5.94e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 5 EEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLatyitECSSLKRSLEQARMEVSQEDDKALQLLHDIR 84
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 85 EQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKvvshppRGDSG 164
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE------LKAKL 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 165 GTALDDLhkmqghAGLTSAKDQGKPEVGEYSKLEKInaeqQLKIQELQEKLEKAVKASTEAtellqnIRQAKERAER--E 242
Cdd:TIGR02169 927 EALEEEL------SEIEDPKGEDEEIPEEELSLEDV----QAELQRVEEEIRALEPVNMLA------IQEYEEVLKRldE 990
|
250 260 270
....*....|....*....|....*....|....*.
gi 1039770408 243 LEKLHNR-EDSSEGIKKKLveaEELEEKHREAQVSA 277
Cdd:TIGR02169 991 LKEKRAKlEEERKAILERI---EEYEKKKREVFMEA 1023
|
|
| C1_dGM13116p-like |
cd20831 |
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ... |
953-990 |
6.79e-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: 6.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1039770408 953 TKCAVCLDTV--HFGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20831 17 PSCAVCNKLIpgRFGKQGYQCRDCGLICHKRCHVKVETHC 56
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
215-478 |
7.10e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 215 LEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVE-AEELEEKHREAQVSAQHLEVHLKQKEQHYEE 293
Cdd:pfam04108 2 LSSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKvREGLEKVLNELKKDFKQLLKDLDAALERLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 294 KIKVLDNQI------------KK--DLADKESLENM---MQRHEEEAHEKGKILSEQkamINAMDSKIRSLEQRIVELSE 356
Cdd:pfam04108 82 TLDKLRNTPvepalppgeekqKTllDFIDEDSVEILrdaLKELIDELQAAQESLDSD---LKRFDDDLRDLQKELESLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 357 ANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHE 436
Cdd:pfam04108 159 PSESISLIPTLLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039770408 437 ------EQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAK 478
Cdd:pfam04108 239 rlqkllEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEK 286
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
354-574 |
8.03e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 354 LSEANKLaaNSSLftqrnMKAQEEMISELRQQKFYLETQagkLEAQNRKLEEQlEKISHQDHSDKSrllELETRLREVSL 433
Cdd:PHA02562 165 LSEMDKL--NKDK-----IRELNQQIQTLDMKIDHIQQQ---IKTYNKNIEEQ-RKKNGENIARKQ---NKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 434 EHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAK--------------------------TELEETTAE 487
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctqqisegpdriTKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 488 AEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGA----NDEIVQLRSEVDH 563
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnAEELAKLQDELDK 390
|
250
....*....|.
gi 1039770408 564 LRREITEREMQ 574
Cdd:PHA02562 391 IVKTKSELVKE 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
6-299 |
8.21e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 6 EAMMEQEmTRLHRRVSEVEAVLSQKevelKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIRE 85
Cdd:pfam07888 143 QRVLERE-TELERMKERAKKAGAQR----KEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 86 QSRKLQEIKEQEyqAQVEEMRLMMNQLEEDLVSARRRSDLYESELREsrlaaeefkrkanecqhklmkvvshpprgdsgg 165
Cdd:pfam07888 218 LTQKLTTAHRKE--AENEALLEELRSLQERLNASERKVEGLGEELSS--------------------------------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 166 talddlhkmqghagLTSAKDQGKPEVGEySKLEKINAEQQLKIQELQEKLEKAvKASTEATELLQNIRQAKERAER---E 242
Cdd:pfam07888 263 --------------MAAQRDRTQAELHQ-ARLQAAQLTLQLADASLALREGRA-RWAQERETLQQSAEADKDRIEKlsaE 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 243 LEKLHNR--EDSSEGIKKKLVEAEE-------LEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLD 299
Cdd:pfam07888 327 LQRLEERlqEERMEREKLEVELGREkdcnrvqLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
448-816 |
8.58e-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: 43.91 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 448 ELQLSLQERESQLTALQAARAALESQLRQAKteleettaeaeeeiqaltahrdEIQRKFDALRNSCTVIT----DLEEQL 523
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQ----------------------ERLDQLESGDDSGTPGGkkylLLQKQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 524 NQLTEDN--------------AELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRrEITER----EMQLTSQKQaqlsa 585
Cdd:pfam05622 69 EQLQEENfrletarddyrikcEELEKEVLELQHRNEELTSLAEEAQALKDEMDILR-ESSDKvkklEATVETYKK----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 586 pDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVLGDEKSQfecrVRELQRMLDTE-----------KQSR 654
Cdd:pfam05622 143 -KLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQ----VQELHGKLSEEskkadklefeyKKLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 655 A------RADQRITESRQVVELAVKE-----------HKAEILALQQALKEQKLKAESLS----DKLNDLEKKHAMLEMN 713
Cdd:pfam05622 218 EklealqKEKERLIIERDTLRETNEElrcaqlqqaelSQADALLSPSSDPGDNLAAEIMPaeirEKLIRLQHENKMLRLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 714 AR--------SLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLEniQVLYS 785
Cdd:pfam05622 298 QEgsyrerltELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLE--KLHEA 375
|
410 420 430
....*....|....*....|....*....|.
gi 1039770408 786 HEKvkmegtISQQTKLIDFLQAKMDQPAKKK 816
Cdd:pfam05622 376 QSE------LQKKKEQIEELEPKQDSNLAQK 400
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
10-825 |
9.36e-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: 44.27 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQarmEVSQEDDKALQLLHDIREQsrk 89
Cdd:TIGR01612 806 DEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKE---KIDSEHEQFAELTNKIKAE--- 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 90 LQEIKEQEYQAQVEEMRLMMNQ----LEEDL--VSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVVSHPPRGDS 163
Cdd:TIGR01612 880 ISDDKLNDYEKKFNDSKSLINEinksIEEEYqnINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNL 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 164 ggtaLDDLHKMQGHAGLTSAKDQGKPEVGEYS--KLEKINAEQQLKIQELQEKLEKAvKAST------EATELLQNIRQA 235
Cdd:TIGR01612 960 ----IEKSYKDKFDNTLIDKINELDKAFKDASlnDYEAKNNELIKYFNDLKANLGKN-KENMlyhqfdEKEKATNDIEQK 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 236 KERAERELEKLH-----NREDSSEGIKKKLVEAEELEEKH--REAQVSAQHLEvHLKQKEQHY-------EEKIKVLD-- 299
Cdd:TIGR01612 1035 IEDANKNIPNIEiaihtSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFN-EIKEKLKHYnfddfgkEENIKYADei 1113
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 300 NQIKKDLadkeslENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQrivelsEANKLAANSSLftQRNMKAQEEMI 379
Cdd:TIGR01612 1114 NKIKDDI------KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED------VADKAISNDDP--EEIEKKIENIV 1179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 380 SELRQQKfYLETQAGKLEAQNRKLEE---QLEKISHQDHSDKSRLLEL-------ETRLREVSLEHEEQKLElkrQLTEL 449
Cdd:TIGR01612 1180 TKIDKKK-NIYDEIKKLLNEIAEIEKdktSLEEVKGINLSYGKNLGKLflekideEKKKSEHMIKAMEAYIE---DLDEI 1255
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 450 QLSLQERESQLTALQAARAALESqlrqakteleettaeaeeeiqaLTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTED 529
Cdd:TIGR01612 1256 KEKSPEIENEMGIEMDIKAEMET----------------------FNISHDDDKDHHIISKKHDENISDIREKSLKIIED 1313
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 530 NAELNNQNFY---LSKQLDEASGANDEIVQLRSEVDHL-------------------RREITEREMQLTSQ--------- 578
Cdd:TIGR01612 1314 FSEESDINDIkkeLQKNLLDAQKHNSDINLYLNEIANIynilklnkikkiidevkeyTKEIEENNKNIKDEldkseklik 1393
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 579 -----------KQAQLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRSVL------GDEKSQFECRVR 641
Cdd:TIGR01612 1394 kikddinleecKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLfkniemADNKSQHILKIK 1473
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 642 -------------ELQRMLDTEKQSRARADQRITESRQVVELaVKEHKAEILALQQALKEQKLK---AESLSDK---LND 702
Cdd:TIGR01612 1474 kdnatndhdfninELKEHIDKSKGCKDEADKNAKAIEKNKEL-FEQYKKDVTELLNKYSALAIKnkfAKTKKDSeiiIKE 1552
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 703 LEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQ----MDLQKNhifrlTQGLQEALDRADLLKTERSDLEYQLE 778
Cdd:TIGR01612 1553 IKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSnkaaIDIQLS-----LENFENKFLKISDIKKKINDCLKETE 1627
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 779 NIQvlyshEKVKMEGTISQQTKL------IDFLQAKMDQPAKKKKGLFSRRKE 825
Cdd:TIGR01612 1628 SIE-----KKISSFSIDSQDTELkengdnLNSLQEFLESLKDQKKNIEDKKKE 1675
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
182-409 |
1.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 182 SAKDQGKPEVGEYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEgikkklv 261
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 262 eaEELEEKHREAQVS---AQHLEVhlkqkeqhyeekikVLDNQIKKDLADKESLENMMQRHEeeahekGKILSEQKAMIN 338
Cdd:COG3883 86 --EELGERARALYRSggsVSYLDV--------------LLGSESFSDFLDRLSALSKIADAD------ADLLEELKADKA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 339 AMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEK 409
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
234-654 |
1.18e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 234 QAKERAERE-LEKLHNRedssegIKKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKikvldNQikkDLADKESL 312
Cdd:PRK10246 418 HAEQRPLRQrLVALHGQ------IVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEK-----TQ---QLADVKTI 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 313 EnmmqrheeEAHEKGKILSEQKAMINAMDS--KIRSLEQRIVELSEANKLAANsslftQRNMKAQEEMISELRQQKFYLE 390
Cdd:PRK10246 484 C--------EQEARIKDLEAQRAQLQAGQPcpLCGSTSHPAVEAYQALEPGVN-----QSRLDALEKEVKKLGEEGAALR 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 391 tqaGKLEAqnrkLEEQLekisHQDHSDKSRLLELETRLRE----------VSL-------------EHEEQKLELKRQLT 447
Cdd:PRK10246 551 ---GQLDA----LTKQL----QRDESEAQSLRQEEQALTQqwqavcaslnITLqpqddiqpwldaqEEHERQLRLLSQRH 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 448 ELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQR------KFDALRNSCTVITDLEE 521
Cdd:PRK10246 620 ELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSwqqrqnELTALQNRIQQLTPLLE 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 522 QLNQLTEDNAELNnqnfylSKQLDEASGANDEIVQLRSEVDHLRREITErEMQLTSQKQAQLSApdlqtmeALKTTCtmL 601
Cdd:PRK10246 700 TLPQSDDLPHSEE------TVALDNWRQVHEQCLSLHSQLQTLQQQDVL-EAQRLQKAQAQFDT-------ALQASV--F 763
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 602 EEQVLDLEALNDEllEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSR 654
Cdd:PRK10246 764 DDQQAFLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHR 814
|
|
| C1_MRCKalpha |
cd20864 |
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ... |
942-995 |
1.38e-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: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 942 HRFNVGLNMRATKCAVCLD-TVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAE 995
Cdd:cd20864 3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKAPSVCPIPPE 57
|
|
| C1_TNS1_v |
cd20888 |
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ... |
942-989 |
1.44e-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: 1.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 942 HRFNVGLNMRATKCAVCLDTVhfGRQASKCLECQVMCHPKC-----STCLPAT 989
Cdd:cd20888 6 HTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCeakvaTPCVPAV 56
|
|
| C1_MRCK |
cd20809 |
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ... |
942-993 |
1.45e-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: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 942 HRFNVGLNMRATKCAVClDTVHFG--RQASKCLECQVMCHPKCSTCLPATCGLP 993
Cdd:cd20809 1 HKFIVRTFSTPTKCNHC-TSLMVGlvRQGLVCEVCGYACHVSCADKAPQVCPVP 53
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
208-785 |
1.46e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 208 IQELQEKLEKavkasteatELLQNIRQAKERAERELEkLHNREDSSEGIKKK----------LVEAEELEEKHREAQV-- 275
Cdd:COG5022 819 IIKLQKTIKR---------EKKLRETEEVEFSLKAEV-LIQKFGRSLKAKKRfsllkketiyLQSAQRVELAERQLQElk 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 276 ----SAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLENMMQRH--EEEAHEKGKILSEQKAMINAMDSKIRSLEQ 349
Cdd:COG5022 889 idvkSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPELNKLHEVESKLKE 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 350 RIVELSEANKlaANSSLFTQRNmKAQEEM------ISELRQQKFYLETQAGKLEAQNRKLEE--QLEKISHQDHSDKSRL 421
Cdd:COG5022 969 TSEEYEDLLK--KSTILVREGN-KANSELknfkkeLAELSKQYGALQESTKQLKELPVEVAElqSASKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 422 LELEtrlrEVSLEHEEQKLELKRQLTELQLslqERESQLTalqaaraaLESQLRQAKTELEETTAEAEEEIQALTahrde 501
Cdd:COG5022 1046 KPLQ----KLKGLLLLENNQLQARYKALKL---RRENSLL--------DDKQLYQLESTENLLKTINVKDLEVTN----- 1105
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 502 iqRKFDALRNSCTVITDLEEQLNqLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQA 581
Cdd:COG5022 1106 --RNLVKPANVLQFIVAQMIKLN-LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL 1182
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 582 QLSApdlqtmeALKTTCTMLEEQVLDLEalnDELLEKERQ-WEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRAR--AD 658
Cdd:COG5022 1183 YQSA-------LYDEKSKLSSSEVNDLK---NELIALFSKiFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKkfDT 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 659 QRITESRQVVELAVKehkaeilaLQQALKEQKLKAESLSDKLNDLEKKHAM-----LEMNARSLQQKLETERELKQRLLE 733
Cdd:COG5022 1253 PASMSNEKLLSLLNS--------IDNLLSSYKLEEEVLPATINSLLQYINVglfnaLRTKASSLRWKSATEVNYNSEELD 1324
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 734 EQAKLQQQMDLQKNhifrltqgLQEALDRADLLKTERSDLEYQLENIQVLYS 785
Cdd:COG5022 1325 DWCREFEISDVDEE--------LEELIQAVKVLQLLKDDLNKLDELLDACYS 1368
|
|
| C1_ScPKC1-like_rpt1 |
cd20822 |
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ... |
937-990 |
1.63e-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: 38.04 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 937 HHNIPHRF-NVglnmraTKCAVCLDtvHFGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20822 3 HKFVQKQFyQI------MRCAVCGE--FLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
202-464 |
1.94e-03 |
|
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: 42.49 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 202 AEQQLKIQELQEKLEKAVKASTEATELLQNIR-QAKERAERElEKLHNREDSSEGIKKKLVEAeeLEEKhREAQVSAQHL 280
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESKDQKELEKEIRaLVQERGEQD-KRLQALEEELEKVEAKLNAA--VREK-TSLSASVASL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 281 EVHLKQKEQHYE-EKIKVLDNQIKKDLaDKESLENMMQRHEEEAHEKG----------------KILSEQKAMINAMDSK 343
Cdd:pfam15905 128 EKQLLELTRVNElLKAKFSEDGTQKKM-SSLSMELMKLRNKLEAKMKEvmakqegmegklqvtqKNLEHSKGKVAQLEEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 344 IRSLEQ-RIVELSEANKLAAnsslFTQRNMKAQEEMIS---ELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKS 419
Cdd:pfam15905 207 LVSTEKeKIEEKSETEKLLE----YITELSCVSEQVEKyklDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039770408 420 RLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQ 464
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
193-313 |
2.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSS------------------- 253
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyealqke 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770408 254 -EGIKKKLVEAE----ELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLE 313
Cdd:COG1579 98 iESLKRRISDLEdeilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
492-611 |
2.11e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 492 IQALTahrDEIQRKFDALRNSCT-VITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAN--DEIVQLRSEVDHLRREI 568
Cdd:cd22656 119 IKALL---DDLLKEAKKYQDKAAkVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIarKEIKDLQKELEKLNEEY 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039770408 569 TER---EMQLTSQKQAQLSApDLQTMEALKTTCTMLEEQVLDLEAL 611
Cdd:cd22656 196 AAKlkaKIDELKALIADDEA-KLAAALRLIADLTAADTDLDNLLAL 240
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
657-793 |
2.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 657 ADQRITESRQVVELAVKEHKAEILALQQALKEqklKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQA 736
Cdd:PRK12704 62 AKEEIHKLRNEFEKELRERRNELQKLEKRLLQ---KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770408 737 KLQQQMDlqknHIFRLTQglQEAldRADLLKTERSDLEYQlenIQVLY--SHEKVKMEG 793
Cdd:PRK12704 139 EQLQELE----RISGLTA--EEA--KEILLEKVEEEARHE---AAVLIkeIEEEAKEEA 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
556-885 |
2.47e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 556 QLRSEVDHLRREItEREMQLTSQKQAQLSAPDLQ-TMEALKTTCTMLEEQVLDLEALNDELLEKERqweawrsVLGDEKS 634
Cdd:pfam17380 300 RLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQaAIYAEQERMAMERERELERIRQEERKRELER-------IRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 635 QFECRVRELQRMLDTEKQSRARADQRITESRQvVELAVKEHkaeilalQQALKEQKLKAESLSDKlndlekkhamlEMNA 714
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARK-VKILEEER-------QRKIQQQKVEMEQIRAE-----------QEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 715 RSLQ-QKLETERELK-QRLLEEQAKLQQQMDlqknhifRLTQglQEALDRADLLKTERSDLEYQL---ENIQVLYSHEKV 789
Cdd:pfam17380 433 RQREvRRLEEERAREmERVRLEEQERQQQVE-------RLRQ--QEEERKRKKLELEKEKRDRKRaeeQRRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 790 KMEGTISQQTKLiDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPL----QYNELKLALEKEKARCaeleEALQKTRIEL 865
Cdd:pfam17380 504 RKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRL----EAMEREREMM 578
|
330 340
....*....|....*....|
gi 1039770408 866 RSAREEAAHRKATDHPHPST 885
Cdd:pfam17380 579 RQIVESEKARAEYEATTPIT 598
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
68-618 |
2.57e-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: 42.73 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 68 EVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVsarrrsDLYESELRESRLAAEEFKRKANEC 147
Cdd:TIGR01612 1230 KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETF------NISHDDDKDHHIISKKHDENISDI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 148 QHKLMKVVshppRGDSGGTALDDLHKMQGHAGLTSAKDQGkpEVGEYskLEKI-NAEQQLKIQELQEKLEKAVKASTEAT 226
Cdd:TIGR01612 1304 REKSLKII----EDFSEESDINDIKKELQKNLLDAQKHNS--DINLY--LNEIaNIYNILKLNKIKKIIDEVKEYTKEIE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 227 ELLQNIRQAKERAERELEKLhnREDSS-EGIKKKL---VEAEELEEKHREAQVSAQHL-------EVHLKQKEQHYE--- 292
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKLIKKI--KDDINlEECKSKIestLDDKDIDECIKKIKELKNHIlseesniDTYFKNADENNEnvl 1453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 293 ---EKIKVLDNQ------IKKDLADKESLENMMQRHE---------EEAHEKGKILSEQKAMINAMDSKIRSLEQRIVEL 354
Cdd:TIGR01612 1454 llfKNIEMADNKsqhilkIKKDNATNDHDFNINELKEhidkskgckDEADKNAKAIEKNKELFEQYKKDVTELLNKYSAL 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 355 SEANKLAansslftqRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEqlEKISHQD---HSDKSrlleletrlrev 431
Cdd:TIGR01612 1534 AIKNKFA--------KTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKK--EKFRIEDdaaKNDKS------------ 1591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 432 sleheeqklelKRQLTELQLSLQERESQLTALQAARAALESQLRQAkteleettaeaeeeiqaltahrDEIQRKFDALR- 510
Cdd:TIGR01612 1592 -----------NKAAIDIQLSLENFENKFLKISDIKKKINDCLKET----------------------ESIEKKISSFSi 1638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 511 -NSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREIterEMQLTsQKQAQLSAPDLQ 589
Cdd:TIGR01612 1639 dSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNY---EIGII-EKIKEIAIANKE 1714
|
570 580 590
....*....|....*....|....*....|....*.
gi 1039770408 590 TMEALKTTCTMLEEQVL------DLEALN-DELLEK 618
Cdd:TIGR01612 1715 EIESIKELIEPTIENLIssfntnDLEGIDpNEKLEE 1750
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
437-737 |
2.58e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 437 EQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKteleettAEAEEEIQALTAHRDEIQRKFDALRnsctvi 516
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA-------EKRDELNAQVKELREEAQELREKRD------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 517 tDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREIT--EREMQ---LTSQKQAQLsapdlqtM 591
Cdd:COG1340 68 -ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIErlEWRQQtevLSPEEEKEL-------V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 592 EALKTTCTMLEEqVLDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQrITESRqvvela 671
Cdd:COG1340 140 EKIKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE-LRKEA------ 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770408 672 vKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEmnarslQQKLETERELKQRLLEEQAK 737
Cdd:COG1340 212 -DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR------KKQRALKREKEKEELEEKAE 270
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
193-758 |
2.62e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 193 EYSKLEKINAEQQLKIQELQEKLEKAVKASTE--------ATELLQNIRQAKERAERELEKLHNREDSS----------- 253
Cdd:pfam07111 87 ETSLQQKMRLEAQAMELDALAVAEKAGQAEAEglraalagAEMVRKNLEEGSQRELEEIQRLHQEQLSSltqaheealss 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 254 -----EGIKKKLV--------EAEELEEKHREAQVsaqhLEVHLKQKEQHYEEKIKVLDNqIKKDLADKESLENMMQRHE 320
Cdd:pfam07111 167 ltskaEGLEKSLNsletkragEAKQLAEAQKEAEL----LRKQLSKTQEELEAQVTLVES-LRKYVGEQVPPEVHSQTWE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 321 EEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLaansslftqrnmkaQEEMISELRQQKFYLETQAGKleaqn 400
Cdd:pfam07111 242 LERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAL--------------QEEELTRKIQPSDSLEPEFPK----- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 401 rkleeqleKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKRQLTELQlslqereSQLTALQAARAALESQLrQAKTE 480
Cdd:pfam07111 303 --------KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ-------EQVTSQSQEQAILQRAL-QDKAA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 481 LEETTAEAEEEIQAltahrdEIQRKFDALRNSCTVITDLEEQL----NQLTEDNAELNNQNFYLSKQLDEASGANDEIVQ 556
Cdd:pfam07111 367 EVEVERMSAKGLQM------ELSRAQEARRRQQQQTASAEEQLkfvvNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 557 LRSEVdHLRREITEREMQLTSQKQAQ----LSAPDLQTMEALKTTCTMLEEQVLDLE-ALNDELLEKE-----RQWEAWR 626
Cdd:pfam07111 441 AVRKV-HTIKGLMARKVALAQLRQEScpppPPAPPVDADLSLELEQLREERNRLDAElQLSAHLIQQEvgrarEQGEAER 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 627 SVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAES-----LSD--- 698
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETrlreqLSDtkr 599
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 699 KLNDLEKKHAMLEMNARSLQQKLETERELKQ---RLLEEQAKLQQQmdlqknhifRLTQGLQE 758
Cdd:pfam07111 600 RLNEARREQAKAVVSLRQIQHRATQEKERNQelrRLQDEARKEEGQ---------RLARRVQE 653
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
492-695 |
2.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 492 IQALTAHRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNnqnfylsKQLDEAsgaNDEIVQLRSEVDHLRREITER 571
Cdd:COG3883 25 LSELQAELEAAQAELDALQAE---LEELNEEYNELQAELEALQ-------AEIDKL---QAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 572 --------------EMQLTSQKQA----------QLSAPDLQTMEALKTTCTMLEEQVLDLEALNDELLEKERQWEAWRS 627
Cdd:COG3883 92 aralyrsggsvsylDVLLGSESFSdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 628 VLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAES 695
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
195-478 |
2.67e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 195 SKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAereLEKLHNREDSSEGIKKKLVEAEELEEKHREAQ 274
Cdd:PRK04778 112 SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL---LANRFSFGPALDELEKQLENLEEEFSQFVELT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 275 VSAQHLEVH---LKQKE-----QHYEEKIKVLDNQIKKDLADK-ESLENMMQRHEEEAH--EKGKILSEqkamINAMDSK 343
Cdd:PRK04778 189 ESGDYVEAReilDQLEEelaalEQIMEEIPELLKELQTELPDQlQELKAGYRELVEEGYhlDHLDIEKE----IQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 344 IRSLEQRIVEL-----SEANKLAANS-----SLFtQRNMKAQEEMISELRQQKFYLEtqagKLEAQNRKLEEQLEKISHQ 413
Cdd:PRK04778 265 IDENLALLEELdldeaEEKNEEIQERidqlyDIL-EREVKARKYVEKNSDTLPDFLE----HAKEQNKELKEEIDRVKQS 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 414 ---DHSDKSRLLELETRLREvsleheeqkleLKRQLTELQLSLQERESQLTALQAARAALESQLRQAK 478
Cdd:PRK04778 340 ytlNESELESVRQLEKQLES-----------LEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIE 396
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
5-476 |
3.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 5 EEAMMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDL------ATYITECSSLKRSLEQARMEVSQEDDKAL- 77
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAv 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 78 --QLLHDIREQSRKLQEIKEQEYQAQvEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFkrkanecqhklmkvv 155
Cdd:TIGR00606 665 ysQFITQLTDENQSCCPVCQRVFQTE-AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--------------- 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 156 shpprgdsggtalddLHKMQGHAGLTSAKDQGKPEVGEysKLEKINAEQQLKIQEL--QEKLEKAVKASTEATE------ 227
Cdd:TIGR00606 729 ---------------LGLAPGRQSIIDLKEKEIPELRN--KLQKVNRDIQRLKNDIeeQETLLGTIMPEEESAKvcltdv 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 228 -LLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLEVHLK--QKEQHYEEKIKVLDNQIKK 304
Cdd:TIGR00606 792 tIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKliQDQQEQIQHLKSKTNELKS 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 305 DLADKESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSlfTQRNMKAQEE---MISE 381
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK--ETSNKKAQDKvndIKEK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 382 LRQQKFYLET-----QAGKlEAQNRKLEEQLEKISHQDHSDKSRLLELETRLREVSLEHEEQKleLKRQLTELQLSLQER 456
Cdd:TIGR00606 950 VKNIHGYMKDienkiQDGK-DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRKR 1026
|
490 500
....*....|....*....|
gi 1039770408 457 ESQLTALQAARAALESQLRQ 476
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQ 1046
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
58-326 |
3.60e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 58 LKRSLEQARMEVSQEDDKalqlLHDIREQSRKLQEiKEQEYQAQVEEMRLMMNQLEEdlvsarRRSDLYEsELRESRLAA 137
Cdd:COG1340 13 LEEKIEELREEIEELKEK----RDELNEELKELAE-KRDELNAQVKELREEAQELRE------KRDELNE-KVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 138 EEFKRKANECQHKLMKVVSHPPRGDSGGTALDDLHKmqghagltsakdqgkpevgEYSKLEK--------INAEQQL--K 207
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRK-------------------EIERLEWrqqtevlsPEEEKELveK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 208 IQELQEKLE---KAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLV-----------EAEELEEKHREA 273
Cdd:COG1340 142 IKELEKELEkakKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIelykeadelrkEADELHKEIVEA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 274 QVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLE-NMMQRHEEEAHEK 326
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEkEELEEKAEEIFEK 275
|
|
| C1_PKD_rpt2 |
cd20796 |
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ... |
941-990 |
3.74e-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: 3.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 941 PHRFNVGLNMRATKCAVCLDTVH-FGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20796 1 PHTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
318-740 |
3.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 318 RHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELS-EANKLAANSSLFTQRNMKAQEE---MISELRQQKfYLETQA 393
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMArELAELNEAESDLEQDYQAASDHlnlVQTALRQQE-KIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 394 GKLEAQNRKLEEQLEKISHQDhsdkSRLLELETRLREVslehEEQKLELKRQLTELQLSLQeresqltaLQAARAaleSQ 473
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEAD----EQQEENEARAEAA----EEEVDELKSQLADYQQALD--------VQQTRA---IQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 474 LRQAKteleettaeaeeeiQALtahrDEIQR--KFDALrnsctVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGAN 551
Cdd:PRK04863 416 YQQAV--------------QAL----ERAKQlcGLPDL-----TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 552 DEIVQ----LRSEVDHLRRE-----ITEREMQLTSQKQAQLSAPDLQTmeALKTTCTMLEEQVlDLEALNDELLEKERQW 622
Cdd:PRK04863 473 SQFEQayqlVRKIAGEVSRSeawdvARELLRRLREQRHLAEQLQQLRM--RLSELEQRLRQQQ-RAERLLAEFCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 623 EAWRSVLGDEKSQFECRVRELqrmldteKQSRARADQRITESRQVVElavkEHKAEIlalqQALKEQKLKAESLSDKLND 702
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESL-------SESVSEARERRMALRQQLE----QLQARI----QRLAARAPAWLAAQDALAR 614
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 703 L-EKKHAMLEMNAR---SLQQKLETEREL----------KQRLLEEQAKLQQ 740
Cdd:PRK04863 615 LrEQSGEEFEDSQDvteYMQQLLERERELtverdelaarKQALDEEIERLSQ 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
673-800 |
4.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 673 KEHKAEILAlQQALKEQKLKAESLsdklndleKKHAMLEMNARSLQQKLETERELKQRLLEEQA---KLQQQMDLQKNHI 749
Cdd:PRK12704 32 KIKEAEEEA-KRILEEAKKEAEAI--------KKEALLEAKEEIHKLRNEFEKELRERRNELQKlekRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1039770408 750 FRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEgTISQQTK 800
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE-RISGLTA 152
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
206-358 |
4.14e-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: 41.96 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 206 LKIQ-ELQEKLEKAVKASTEATELL--------QNIRQAKERAERElEKLHNREDSSEGIKK-----KLVE-----AEEL 266
Cdd:TIGR01612 561 HEIKkELEEENEDSIHLEKEIKDLFdkyleiddEIIYINKLKLELK-EKIKNISDKNEYIKKaidlkKIIEnnnayIDEL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 267 eekhreAQVSAQHLEVHLKQKEQHYEeKIKVLDNQIKKDLADK--ESLENMMQRHEEEAHEKGKILSEQKAMINAMDSKI 344
Cdd:TIGR01612 640 ------AKISPYQVPEHLKNKDKIYS-TIKSELSKIYEDDIDAlyNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKI 712
|
170
....*....|....
gi 1039770408 345 RSLEQRIVELSEAN 358
Cdd:TIGR01612 713 QNMETATVELHLSN 726
|
|
| C1_TNS2 |
cd20887 |
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ... |
941-993 |
4.27e-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: 37.07 E-value: 4.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 941 PHRFNVGLNMRATKCAVCLDTVhfGRQASKCLECQVMCHPKCSTCLPATCGLP 993
Cdd:cd20887 2 PHSFKEKTFKKKRACAVCREPV--GGQGLVCRVCKVASHKKCEAKVTSACQPP 52
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
368-575 |
4.41e-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: 40.27 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 368 TQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQL---EKISHQDHSDKSRLLELETRLREVSLEHEEQKLELKR 444
Cdd:pfam15619 2 TQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQkrqEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 445 QLTELQLSLQERESQLTALQAARAALEsQLRQAKTEleettaeaeeeiqaltAHRDEIQRKFDALRNsctvITDLEEQLN 524
Cdd:pfam15619 82 KERDLERKLKEKEAELLRLRDQLKRLE-KLSEDKNL----------------AEREELQKKLEQLEA----KLEDKDEKI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039770408 525 QLTEDNAELNNQNF--YLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQL 575
Cdd:pfam15619 141 QDLERKLELENKSFrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
78-278 |
4.45e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 78 QLLHDIREQSRKLQEIKEQE--YQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKVV 155
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 156 ---------SHPPRGDSGGTALDDLHKMQGHAGLTSA-KDQGKpevgeysKLEKINAEQQLKIQELQEKLEKAVKASTEA 225
Cdd:COG4942 111 ralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPArREQAE-------ELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039770408 226 TELLQNIRQAKERAERELEKLHNREDSSEG-IKKKLVEAEELEEKHREAQVSAQ 278
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAA 237
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
444-875 |
5.04e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 444 RQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITD----- 518
Cdd:PRK10929 2 RLIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNfpkls 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 519 --LEEQLNQLTED---------NAELNNQNFYLSKQLDEASGandeivQLRSEVDHLrREITEREMQLTSQKQA---QLS 584
Cdd:PRK10929 82 aeLRQQLNNERDEprsvppnmsTDALEQEILQVSSQLLEKSR------QAQQEQDRA-REISDSLSQLPQQQTEarrQLN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 585 APDlQTMEALKTTCTMLEE-QVLDLEAlndellekerqweawrsvlgdEKSQFECRVRELQrmldtekQSRARADQRITE 663
Cdd:PRK10929 155 EIE-RRLQTLGTPNTPLAQaQLTALQA---------------------ESAALKALVDELE-------LAQLSANNRQEL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 664 SRQVVELAVKEHkAEILALQQALKEQklkaeslsdkLNDLEKKHA--------MLEMNA----RSLQQKLETERELKQrL 731
Cdd:PRK10929 206 ARLRSELAKKRS-QQLDAYLQALRNQ----------LNSQRQREAeralesteLLAEQSgdlpKSIVAQFKINRELSQ-A 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 732 LEEQAklqQQMDL----QK---NHIFRLTQGLQ----------------EALdRADLLKTERSDLEYQLENIQVLYSHEK 788
Cdd:PRK10929 274 LNQQA---QRMDLiasqQRqaaSQTLQVRQALNtlreqsqwlgvsnalgEAL-RAQVARLPEMPKPQQLDTEMAQLRVQR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 789 VKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFsrrkeDPALPTQVPL------QYNELKLALEKEKARCAELEEALQKTR 862
Cdd:PRK10929 350 LRYEDLLNKQPQLRQIRQADGQPLTAEQNRIL-----DAQLRTQRELlnsllsGGDTLILELTKLKVANSQLEDALKEVN 424
|
490
....*....|...
gi 1039770408 863 ielrsareEAAHR 875
Cdd:PRK10929 425 --------EATHR 429
|
|
| C1_Munc13 |
cd20807 |
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ... |
942-990 |
6.18e-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: 6.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1039770408 942 HRFNVGLNMRATKCAVCLDTV-HFGRQASKCLECQVMCHPKCSTCLPATC 990
Cdd:cd20807 1 HNFEVWTATTPTYCYECEGLLwGIARQGVRCTECGVKCHEKCKDLLNADC 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10-246 |
7.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 10 EQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQ---------DLATYITECSS-----------------LKRSLE 63
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAEleaelerldassddlaaLEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 64 QARMEVSQEDDKALQLLHDIREQSRKLQEIKEQ--EYQAQVEEMRLMMNQLEEDLVSARRRS---DLYESELRE---SRL 135
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEEldELQDRLEAAEDLARLELRALLEERFAAalgDAVERELREnleERI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 136 AAEefKRKANECQHKLMKVVSH-----PPRGDSGGTALDDLHKMQGHagltsakdqgkpevgeYSKLEKINAEqqlkiqE 210
Cdd:COG4913 776 DAL--RARLNRAEEELERAMRAfnrewPAETADLDADLESLPEYLAL----------------LDRLEEDGLP------E 831
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039770408 211 LQEKLEKAVKASTEA--TELLQNIRQAKERAERELEKL 246
Cdd:COG4913 832 YEERFKELLNENSIEfvADLLSKLRRAIREIKERIDPL 869
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
244-465 |
7.45e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 244 EKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQHLEvHLKQKEQHYEEKIKVLDNQIKKDLADKEslenmmqrheeea 323
Cdd:PLN02939 94 DDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLE-DLVGMIQNAEKNILLLNQARLQALEDLE------------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 324 hekgKILSEQKAMinamDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQkfyLETQAGKLEAqnrkL 403
Cdd:PLN02939 160 ----KILTEKEAL----QGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIR---GATEGLCVHS----L 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039770408 404 EEQLEKISHQDHSDKSRLLELETRLREVSlEHEEQKLELKRQLTELQLSLQERESQLTALQA 465
Cdd:PLN02939 225 SKELDVLKEENMLLKDDIQFLKAELIEVA-ETEERVFKLEKERSLLDASLRELESKFIVAQE 285
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
417-743 |
8.02e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 417 DKSRLLELETRLREVSL-EHEEQKLELKRQLTEL-QLSLQERESQLTALQAARAALESQLRQAkteleettaeaeeeiqa 494
Cdd:pfam00038 18 DKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNL----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 495 ltahRDEIQRkfdaLRNSctvitdLEEQLNQLTEDNAELNNqnfyLSKQLDEASGANdeiVQLRSEVDHLRREIT----- 569
Cdd:pfam00038 81 ----RLAAED----FRQK------YEDELNLRTSAENDLVG----LRKDLDEATLAR---VDLEAKIESLKEELAflkkn 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 570 -EREMqltSQKQAQLSAPDLQtMEALKTTCTMLEEQVLDLEALNDELLEKERQweawrsvlgDEKSQFECRVRELQRMLD 648
Cdd:pfam00038 140 hEEEV---RELQAQVSDTQVN-VEMDAARKLDLTSALAEIRAQYEEIAAKNRE---------EAEEWYQSKLEELQQAAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 649 TEKQSRARADQRITESRQVVElavkehkaeilALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETE-REL 727
Cdd:pfam00038 207 RNGDALRSAKEEITELRRTIQ-----------SLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAElQET 275
|
330
....*....|....*.
gi 1039770408 728 KQRLLEEQAKLQQQMD 743
Cdd:pfam00038 276 RQEMARQLREYQELLN 291
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
657-774 |
8.26e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 657 ADQRITESrqvvELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHamlEMNARSLQQKLETERELKQRllEEQA 736
Cdd:pfam02841 195 TDQALTAK----EKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSY---QEHVKQLIEKMEAEREQLLA--EQER 265
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039770408 737 KLQQQMDLQKNhifRLTQGLQEaldRADLLKTERSDLE 774
Cdd:pfam02841 266 MLEHKLQEQEE---LLKEGFKT---EAESLQKEIQDLK 297
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
257-780 |
8.34e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 257 KKKLVEAEELEEKHREAQVSAQHLEVHLKQK---------EQHYE-------EKIKVLDNQIKKDLADKESLENMMQR-- 318
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKekenihlreELHRRnqlqpdpAKTKALQTVIEMKDTKISSLERNIRDle 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 319 ------------HEEEAHEKGKILSEQKAMINAMDSKIRSLEQrivELS--EANKLAANSSLFTQRNM------------ 372
Cdd:pfam10174 254 devqmlktngllHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQ---ELSkkESELLALQTKLETLTNQnsdckqhievlk 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 373 -----KAQEEMI--SELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDH--SDKSRLLELETR-----------LREVS 432
Cdd:pfam10174 331 esltaKEQRAAIlqTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGeiRDLKDMLDVKERkinvlqkkienLQEQL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 433 LEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALEsqlrqakteleettaeaeEEIQALTAHRD-EIQRKFDALRN 511
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE------------------RIIERLKEQRErEDRERLEELES 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 512 SCTVITDLEEQLNQLtedNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREItEREMQLTSQKQAQLsaPDLQTM 591
Cdd:pfam10174 473 LKKENKDLKEKVSAL---QPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV-EQKKEECSKLENQL--KKAHNA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 592 EALKTTCTMLEEQVldlealndELLEKERQWEAWRSvlgdEKSQFEC-RVRELQRMLDTEKQSRaraDQRITEsrqvvel 670
Cdd:pfam10174 547 EEAVRTNPEINDRI--------RLLEQEVARYKEES----GKAQAEVeRLLGILREVENEKNDK---DKKIAE------- 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 671 avkehkAEILALQQaLKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQ--RLLEEQAKLQQQMDLQKNH 748
Cdd:pfam10174 605 ------LESLTLRQ-MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQleELMGALEKTRQELDATKAR 677
|
570 580 590
....*....|....*....|....*....|..
gi 1039770408 749 IFRLTQGLQEaldRADLLKTERSDLEYQLENI 780
Cdd:pfam10174 678 LSSTQQSLAE---KDGHLTNLRAERRKQLEEI 706
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
194-355 |
9.55e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.00 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 194 YSKLEKINAEQ--QLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLH--NREDSSEGIKKKLVEA-EELEE 268
Cdd:PRK06669 6 FKRSNVINKEKlkTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIeeAEEDAFEIVEAAEEEAkEELLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 269 KHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADK---ESLENMMQRHEEEAHEKGKILSEqkaMINAMDSKIR 345
Cdd:PRK06669 86 KTDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEgyeKGREEGLEEVRELIEQLNKIIEK---LIKKREEILE 162
|
170
....*....|
gi 1039770408 346 SLEQRIVELS 355
Cdd:PRK06669 163 SSEEEIVELA 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
73-278 |
9.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 73 DDKALQLLHDIREQSRKLQEIKEQ--EYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELresrlaaEEFKRKANECQHK 150
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEldALQAELEELNEEYNELQAELEALQAEIDKLQAEI-------AEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 151 LMKVVSHPPRGDSGGTAL----------DDLHKMQghaGLTSAKDQGKPEVGEYSKLEKINAEQQlkiQELQEKLEKAVK 220
Cdd:COG3883 88 LGERARALYRSGGSVSYLdvllgsesfsDFLDRLS---ALSKIADADADLLEELKADKAELEAKK---AELEAKLAELEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770408 221 ASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEELEEKHREAQVSAQ 278
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
398-706 |
9.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 398 AQNRKLEEQLEKISHQDHSDKSrlleLETRLREvsLEHEEQKLELKRQLTELQLSLQER-ESQLTALQAARaalesqlrq 476
Cdd:PHA02562 150 PARRKLVEDLLDISVLSEMDKL----NKDKIRE--LNQQIQTLDMKIDHIQQQIKTYNKnIEEQRKKNGEN--------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 477 akteleettaeaeeeiqaltahRDEIQRKFDALRNSctvITDLEEQLNQLTEDNAELNnqnfylsKQLDEASGA----ND 552
Cdd:PHA02562 215 ----------------------IARKQNKYDELVEE---AKTIKAEIEELTDELLNLV-------MDIEDPSAAlnklNT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 553 EIVQLRSEVDHLRREITERE--------MQLTSQKQAQLSapDLQT-MEALKTTCTMLEEQVLDLEALNDELLEKERqwe 623
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIKMYEkggvcptcTQQISEGPDRIT--KIKDkLKELQHSLEKLDTAIDELEEIMDEFNEQSK--- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770408 624 awrsvlgdeksqfecRVRELQRMLDTEKQSRARADQRITESRQVVELAVKE---HKAEILALQQALKEqklkaesLSDKL 700
Cdd:PHA02562 338 ---------------KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDK-------IVKTK 395
|
....*.
gi 1039770408 701 NDLEKK 706
Cdd:PHA02562 396 SELVKE 401
|
|
|