|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
976-1087 |
9.82e-32 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 119.96 E-value: 9.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 976 AVRMGAGSSIIENLQSQLKLREGEISHLQLEISNLEKTRSIMSEELVKLTNQNDELEEKVKEIPKLRVQLRDLDQRYNTI 1055
Cdd:pfam12325 4 TSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETT 83
|
90 100 110
....*....|....*....|....*....|..
gi 158186663 1056 LQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1087
Cdd:pfam12325 84 LELLGEKSEEVEELKADVEDLKEMYREQVQQL 115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-1087 |
4.31e-14 |
|
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: 77.40 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 452 EFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTM 531
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 532 KEELASRLNSSQ-TADLLKEKDEQIQGLMEEGEKLSKQqlhnsnmIKKLRAKDKDNESviaklkkKAKELEEELQHLRQV 610
Cdd:TIGR02168 322 EAQLEELESKLDeLAEELAELEEKLEELKEELESLEAE-------LEELEAELEELES-------RLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 611 LDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREM 690
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 691 KAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDylRHEISELQQRLQEAENRNQELSQSVS----- 765
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSELISVDEGYEAAIEaalgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 766 ------------------------------------------STTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLG-- 801
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflkqnelgrvtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 802 -------ESQTLLAAAVERERAATEE-LLANK---IQMSSVESQNALL--RQENSRLQAQLESEKNKLRKLEDENSRYQV 868
Cdd:TIGR02168 626 lvvddldNALELAKKLRPGYRIVTLDgDLVRPggvITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 869 ELENLKDEYV---RTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKEHKPFSVSSTPTMSRSSSLSGVD--- 942
Cdd:TIGR02168 706 ELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeie 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 943 -----MAGLQTSFLSQDESHDHSFGPMS-TSASGSNLYEAV-----RMGAGSSIIENLQSQLKLREGEISHLQLEISNLE 1011
Cdd:TIGR02168 786 eleaqIEQLKEELKALREALDELRAELTlLNEEAANLRERLeslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 1012 KTRSIMSEELVKLTNQNDELEEKVKEI----PKLRVQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1087
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLrselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
622-920 |
2.47e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 622 RENIKKLNSVVERQEKDLGRLQVDMN------ELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEE 695
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 696 LSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAaRKEDYLRHEISELQQRLQEAENRNQELSQSVSSttrpLLRQI 775
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEEELEE----LEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 776 ENLQATLGSQTSSWEMLEKNLSdrlgESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNK 855
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158186663 856 LRKLEDENSRYQ---VELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKE 920
Cdd:COG1196 416 LERLEEELEELEealAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
442-920 |
1.72e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 442 LEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKER 521
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 522 DTAKKEMKTMKEELASRLN---------SSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAK 592
Cdd:COG1196 312 RELEERLEELEEELAELEEeleeleeelEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 593 LKKKAKELEEELQHLRQVLDGKEEVEK------QHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRE 666
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERleeeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 667 LTDLHKANAAKDSEVQEAALRREMK--AKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAA----------- 733
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLleAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqni 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 734 --RKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLG--SQTSSWEMLEKNLSDRLGES---QTL 806
Cdd:COG1196 552 vvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLvaSDLREADARYYVLGDTLLGRtlvAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 807 LAAAVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKD-EYVRTLEEAR 885
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLaEEEEERELAE 711
|
490 500 510
....*....|....*....|....*....|....*
gi 158186663 886 KEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKE 920
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
462-1091 |
3.70e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 462 ETQLLSLSKEKALLEEaYDNLKDEMFRVKEESSSISslKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKEELAS-RLN 540
Cdd:COG1196 199 ERQLEPLERQAEKAER-YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEElRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 541 SSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNEsviaklkkkakeleEELQHLRQVLDGKEEVEKQ 620
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE--------------EELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 621 HRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELtdLHKANAAKDSEVQEAALRREMKAKEELSGAL 700
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 701 EKAQEEARQQQETLALQVGDLRLALQRAEQAAAR---KEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIEN 777
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 778 LQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELLAnkiqmssVESQNALLRQENSRLQAQLESEKNKLR 857
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-------AALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 858 KLEdensryqvELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLkekehkpfsvsstptmSRSSS 937
Cdd:COG1196 573 RAT--------FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL----------------GRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 938 LSGVDMAGLQTsflsqdESHDHSFGPMSTSASGSNLYEAVRMGAGSSIIENLQSQLKLREGEISHLQLEISNLEKTRSIM 1017
Cdd:COG1196 629 AARLEAALRRA------VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158186663 1018 SEELVKLTNQNDELEEKVKEIPKLRVQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQR 1091
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
454-752 |
5.81e-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: 70.47 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 454 LNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTM-- 531
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELea 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 532 -KEELASRLNSSQTAdlLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQV 610
Cdd:TIGR02168 762 eIEELEERLEEAEEE--LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 611 LDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEA--ALRR 688
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrrELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158186663 689 EMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQE 752
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
455-920 |
8.32e-12 |
|
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: 69.66 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 455 NEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKEE 534
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 535 lasRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDGK 614
Cdd:TIGR04523 196 ---LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 615 -------------------------EEVEKQHRENI-KKLNSVVERQEKDLGRLQVDMNELEEKsrstqaaLDSAYRELT 668
Cdd:TIGR04523 273 qkeleqnnkkikelekqlnqlkseiSDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKI-------ISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 669 DLHKANAAKDSEVQEaaLRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDylrhEISELQQ 748
Cdd:TIGR04523 346 QLKKELTNSESENSE--KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE----QIKKLQQ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 749 RLQEAENRNQELSQSVS---STTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLlaaaVERERAATEELLANK 825
Cdd:TIGR04523 420 EKELLEKEIERLKETIIknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI----KQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 826 IQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARK---EKTLLSSQLEMERMKV 902
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKEIDEKNKEIEELKQ 575
|
490 500
....*....|....*....|
gi 158186663 903 EQE--RKKTIFTQETLKEKE 920
Cdd:TIGR04523 576 TQKslKKKQEEKQELIDQKE 595
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
491-876 |
1.57e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 491 EESSSISSLKdeftQRIAEAERKaqlackerdtakkeMKTMKEELAsRLNssqtaDLLKEKDEQIQGLMEEGEKLSK-QQ 569
Cdd:COG1196 162 EEAAGISKYK----ERKEEAERK--------------LEATEENLE-RLE-----DILGELERQLEPLERQAEKAERyRE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 570 LhnsnmikKLRAKDKDNESVIAKLkkkakeleeelQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNEL 649
Cdd:COG1196 218 L-------KEELKELEAELLLLKL-----------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 650 EEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSGALEKAQEEARQQQETLALQvgDLRLALQRAE 729
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE--EAEEELEEAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 730 QAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRpLLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAA 809
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158186663 810 AVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDE 876
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
443-896 |
8.30e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 443 EQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERD 522
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 523 TAKKEMKTMKEELASRLNS-SQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELE 601
Cdd:COG1196 376 EAEEELEELAEELLEALRAaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 602 EELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEV 681
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 682 QEAALRREMKA--------------------KEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRH 741
Cdd:COG1196 536 YEAALEAALAAalqnivveddevaaaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 742 EISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEEL 821
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 822 LANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVR-------TLEEARKEKTLLSSQ 894
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppDLEELERELERLERE 775
|
..
gi 158186663 895 LE 896
Cdd:COG1196 776 IE 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
673-909 |
1.09e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 673 ANAAKDSEVQEAALRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQaaarkedylrhEISELQQRLQE 752
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----------ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 753 AENRNQELSQSVSSTTRPLLRQIENLQaTLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVE 832
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158186663 833 SQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVEQERKKT 909
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
542-615 |
1.73e-10 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 58.09 E-value: 1.73e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158186663 542 SQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDGKE 615
Cdd:pfam12329 1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
387-922 |
1.83e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 387 SEEAELEESGRSATPVNCDQPDTLASPTPVNVGPSAS-GPAAEDGEAAENHPKAPQLEQEDVGKTVEFLNEKLE-KRETQ 464
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEeARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 465 LLSLSKEKAllEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKK---EMKTMKEELASRLNS 541
Cdd:PTZ00121 1319 EAKKKAEEA--KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 542 SQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDGKEEVE--K 619
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeaK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 620 QHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEvqEAALRREMKAKEELSGA 699
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 700 LEKAQEEARQQQETLALQVGDLRLALQRAEQA----AARKEDYLRHEISELQQRLQEAENRNQELSQSVSsttrplLRQI 775
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE------LKKA 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 776 ENLQATLgSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELlANKIQMSSVESQNALLRQENSRLQAQLESEKNK 855
Cdd:PTZ00121 1629 EEEKKKV-EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158186663 856 LRKLEDENSRYQVELENLKDEYVRTLEEARKEKTllSSQLEMERMKVEQERKKTIftQETLKEKEHK 922
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEEKKKI--AHLKKEEEKK 1769
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
526-1087 |
1.06e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 526 KEMKTMKEELASRLNSSQTAD-LLKEKDEQIQGLMEEGEKLSKQqlhnsnmIKKLRAKDKDNESVIAKLKKKAKELEEEL 604
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDkNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 605 QHLRQVLDGKE----EVEKQHREN---IKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDlhKANAAK 677
Cdd:TIGR04523 113 KNDKEQKNKLEvelnKLEKQKKENkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN--IQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 678 DSEVQEAALRREM---KAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAE 754
Cdd:TIGR04523 191 KIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 755 NRNQELSQSVS--STTRPLLRQIENLQATLGSQTSswEMLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVE 832
Cdd:TIGR04523 271 EKQKELEQNNKkiKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 833 SQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEyVRTLEEARKEKTLLSSQLEMERMKVEQERKKtift 912
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKEL---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 913 qetlKEKEHKPFSVSSTPTMSRSSSLSGVDmaglqTSFLSQDESHDhsfgpmstsasgsnlyeavrmgagsSIIENLQSQ 992
Cdd:TIGR04523 424 ----LEKEIERLKETIIKNNSEIKDLTNQD-----SVKELIIKNLD-------------------------NTRESLETQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 993 LKLREGEISHLQLEISNLEKTRSIMSEELVKLTNQNDELEEKVK----EIPKLRVQLRDLDQRYNTILQMYGEKAEEAEE 1068
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdltkKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
570
....*....|....*....
gi 158186663 1069 LRLDLEdvKNMYKTQIDEL 1087
Cdd:TIGR04523 550 DDFELK--KENLEKEIDEK 566
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-922 |
1.33e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 427 AEDGEAAENHPKAPQLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEayDNLKDEMFRVKEESSSISSLKDEfTQR 506
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE--EIRKFEEARMAHFARRQAAIKAE-EAR 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 507 IAEAERKAQLACKERDTAKKEMKTMKEELASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDN 586
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 587 ESVIAKLKKKAKELEEELQHlrqvldgKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRE 666
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKK-------KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 667 LTDLHKANAAKDSEVQEAALRREMKAKEElsgALEKAQEEARQQQEtLALQVGDLRLA--LQRAEQAAARKEDYLRHEIS 744
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAE---EAKKKAEEAKKADE-AKKKAEEAKKAdeAKKKAEEAKKKADEAKKAAE 1507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 745 ELQQ----RLQEAENRNQELSQSVSSTTRPLLRQIENLQAtlGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEE 820
Cdd:PTZ00121 1508 AKKKadeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 821 llANKIQMSSVESQNALLRQENSRLQAQL---ESEKNKLRKL--EDENSRYQVELENLKDEYVRTLEEARKEKTLLSSQL 895
Cdd:PTZ00121 1586 --AKKAEEARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
490 500
....*....|....*....|....*..
gi 158186663 896 EMERMKVEQERKKtifTQETLKEKEHK 922
Cdd:PTZ00121 1664 AEEAKKAEEDKKK---AEEAKKAEEDE 1687
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-760 |
6.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 466 LSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKEELAsrlnssQTA 545
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE------ELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 546 DLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNEsviaklkkkakeLEEELQHLRQVLDGKEEVEKQHRENI 625
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE------------ARLSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 626 KKLNSV---VERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAAlrremKAKEELSGALEK 702
Cdd:TIGR02169 812 ARLREIeqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE-----AALRDLESRLGD 886
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158186663 703 AQEEARQQQETLAlqvgdlrlALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQEL 760
Cdd:TIGR02169 887 LKKERDELEAQLR--------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
605-922 |
2.32e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 605 QHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQvdmnELEEKSRSTQAALDSAYRELTDLhkanaAKDSEVQEA 684
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKEL-----EARIEELEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 685 ALRREMKAKEELSGAL-----EKAQEEARQQQETLALQVGDLRlALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQE 759
Cdd:TIGR02169 773 DLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLR-EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 760 LSQsvssttrpllrQIENLQATLGSQTSSWEMLEKNLSDRLGEsqtlLAAAVERERAATEELLANKIQMSSVESQNALLR 839
Cdd:TIGR02169 852 IEK-----------EIENLNGKKEELEEELEELEAALRDLESR----LGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 840 QENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEyvRTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEK 919
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL--EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
...
gi 158186663 920 EHK 922
Cdd:TIGR02169 995 RAK 997
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
590-908 |
2.48e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 590 IAKLKKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTD 669
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 670 LhkanaakdsEVQEAALRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARkedyLRHEISELQQR 749
Cdd:TIGR02168 759 L---------EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----LNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 750 LQEAENRNQELSQSVssttRPLLRQIENLQATLGSQTSSWEMLEKNLSdrlgESQTLLAAAVERERAATEELLANKIQMS 829
Cdd:TIGR02168 826 LESLERRIAATERRL----EDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 830 SVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKD----EYVRTLEEARKEKTLLSSQLEMERMKVEQE 905
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
...
gi 158186663 906 RKK 908
Cdd:TIGR02168 978 ENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
431-1091 |
1.22e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 431 EAAENHPKAPQLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEA 510
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 511 ERKAQLACKERDTAKKEMKT---MKEELASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDne 587
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE-- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 588 svIAKLKKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQV---------------------DM 646
Cdd:TIGR02168 470 --LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggRL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 647 NEL-----------------EEKSRSTQAALDS-AYRELTDLHKANAAKDSEVQEAALRREmKAKEELSGA--------- 699
Cdd:TIGR02168 548 QAVvvenlnaakkaiaflkqNELGRVTFLPLDSiKGTEIQGNDREILKNIEGFLGVAKDLV-KFDPKLRKAlsyllggvl 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 700 ----LEKAQEEARQ--QQETLALQVGDL-----RLALQRAEQAAARKEdyLRHEISELQQRLQEAENRNQELSQ---SVS 765
Cdd:TIGR02168 627 vvddLDNALELAKKlrPGYRIVTLDGDLvrpggVITGGSAKTNSSILE--RRREIEELEEKIEELEEKIAELEKalaELR 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 766 STTRPLLRQIENLQATLGSQTSSWEMLEKNLSdRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENSRL 845
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 846 QAQLESEKNKLRKLEDENSRyqvELENLKDEYVRTLEEARKektlLSSQLEMERMKVEQERKKTIFTQETLKEKEHkpfs 925
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALRE---ALDELRAELTLLNEEAAN----LRERLESLERRIAATERRLEDLEEQIEELSE---- 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 926 vsstptmsrssslsgvDMAGLQTSFLSQDEShdhsfgpmstsasgsnlyeavrmgagssiIENLQSQLKLREGEISHLQL 1005
Cdd:TIGR02168 853 ----------------DIESLAAEIEELEEL-----------------------------IEELESELEALLNERASLEE 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 1006 EISNLEKTRSIMSEELVKLTNQNDELEEKVKEipkLRVQLRDLDQRYNTILQMYGEKAEE-AEELRLDLEDVKNMYKTQI 1084
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEE---LREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIE 964
|
....*..
gi 158186663 1085 DELLRQR 1091
Cdd:TIGR02168 965 DDEEEAR 971
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-764 |
1.52e-07 |
|
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: 55.84 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 443 EQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEaYDNLKDEMFRVK--------------------------EESSSI 496
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellkekealerqkeaierqlasleEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 497 SSLKDEFTQRIAEAERK-AQLACKERDTAKKEMKTMKEELAS-RLNSSQTADLLKEKDEQIQGLMEEGEK----LSKQQL 570
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGElEAEIASLERSIAEKERELEDAEERLAKleaeIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 571 HNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLrqvldgkEEVEKQHRENIKKLNSVVERQEKdlgrLQVDMNELE 650
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL-------EEVDKEFAETRDELKDYREKLEK----LKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 651 EKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEelsgalekaQEEARQQQETLALQVGDLRLALQRAEQ 730
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---------IKKQEWKLEQLAADLSKYEQELYDLKE 476
|
330 340 350
....*....|....*....|....*....|....
gi 158186663 731 AAARKEDylrhEISELQQRLQEAENRNQELSQSV 764
Cdd:TIGR02169 477 EYDRVEK----ELSKLQRELAEAEAQARASEERV 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
449-928 |
1.70e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 449 KTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDemfRVKEESSSISSLKdEFTQRIAEAERKAqlacKERDTAKKEM 528
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELE-EKVKELKELKEKA----EEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 529 KTMKEELAsrlNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKL---------------RAKDKDNESVIAKL 593
Cdd:PRK03918 303 EEYLDELR---EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELekrleeleerhelyeEAKAKKEELERLKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 594 KKKAKELEEELQHLRQVLDGKEEVEkqhrENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAaldsAYRELTDLHKA 673
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIE----EEISKITARIGELKKEIKELKKAIEELKKAKGKCPV----CGRELTEEHRK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 674 NAAKDsevQEAALRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLaLQRAEQAAARKEDYLRHEISELQQRLQEA 753
Cdd:PRK03918 452 ELLEE---YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEY 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 754 ENRNQELSQsVSSTTRPLLRQIENLQATlgsqTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELlankiqmssves 833
Cdd:PRK03918 528 EKLKEKLIK-LKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEEL------------ 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 834 qnallrqeNSRLQaQLESEKNKLRKLEDENSRYQVELENLKDEYvRTLEEARKEKTLLSSQLEMERMKVEQERKKtiFTQ 913
Cdd:PRK03918 591 --------EERLK-ELEPFYNEYLELKDAEKELEREEKELKKLE-EELDKAFEELAETEKRLEELRKELEELEKK--YSE 658
|
490
....*....|....*
gi 158186663 914 ETLKEKEHKPFSVSS 928
Cdd:PRK03918 659 EEYEELREEYLELSR 673
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
448-888 |
3.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 448 GKTVEFLNEKLEKRETQLlslsKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQL--ACKERDTAK 525
Cdd:COG4717 63 GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 526 KEMKTMKEELasrlnssqtaDLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDkdnesviaklkkkakeLEEELQ 605
Cdd:COG4717 139 AELAELPERL----------EELEERLEELRELEEELEELEAELAELQEELEELLEQL----------------SLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 606 HLRQVLDGKEEVEKQH---RENIKKLNSVVERQEKDLGRLQVDMNELEEKSR-----------STQAALDSAYRELTDL- 670
Cdd:COG4717 193 ELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLi 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 671 ------------------------HKANAAKDSEVQEAALRREMKAKE--ELSGALEKAQEEARQQQETLALQVGDLRLA 724
Cdd:COG4717 273 ltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 725 LQRAEQAAAR-KEDYLRHEISELQQR--------LQEAENRNQELSQsvssttrpLLRQIENLQATLGSQTSSWEML--- 792
Cdd:COG4717 353 LREAEELEEElQLEELEQEIAALLAEagvedeeeLRAALEQAEEYQE--------LKEELEELEEQLEELLGELEELlea 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 793 --EKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALlrqenSRLQAQLESEKNKLRKLEDENSRYQVEL 870
Cdd:COG4717 425 ldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL-----AELLQELEELKAELRELAEEWAALKLAL 499
|
490
....*....|....*...
gi 158186663 871 ENLKdeyvRTLEEARKEK 888
Cdd:COG4717 500 ELLE----EAREEYREER 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
441-914 |
7.23e-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: 53.64 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 441 QLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAE---RKAQLA 517
Cdd:pfam01576 123 QLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEerlKKEEKG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 518 CKERDTAKKEMKTMKEELASRLN--SSQTADL---LKEKDEQIQGLMeegEKLSKQQLHNSNMIKKLRAKDKdnesviak 592
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQIAelQAQIAELraqLAKKEEELQAAL---ARLEEETAQKNNALKKIRELEA-------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 593 lkkkakeleeelqhlrQVLDGKEEVEKQhreniKKLNSVVERQEKDLG-RLQVDMNELEEKSRSTQAALD---SAYRELT 668
Cdd:pfam01576 272 ----------------QISELQEDLESE-----RAARNKAEKQRRDLGeELEALKTELEDTLDTTAAQQElrsKREQEVT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 669 DLHKA--NAAKDSEVQEAALR-REMKAKEELSGALEKAQ------EEARQQQETLALQVGDLRLALQRAEQAAARKEDYL 739
Cdd:pfam01576 331 ELKKAleEETRSHEAQLQEMRqKHTQALEELTEQLEQAKrnkanlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 740 RHEISELQQRLQEAENRNQELSQSVSSttrpLLRQIENLQATLGSQTSSWEMLEKNLSDRlgESQtllaaavereRAATE 819
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSK----LQSELESVSSLLNEAEGKNIKLSKDVSSL--ESQ----------LQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 820 ELLANKI-QMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEY------VRTLEEARK----EK 888
Cdd:pfam01576 475 ELLQEETrQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLeedagtLEALEEGKKrlqrEL 554
|
490 500
....*....|....*....|....*..
gi 158186663 889 TLLSSQLEMERMKVEQ-ERKKTIFTQE 914
Cdd:pfam01576 555 EALTQQLEEKAAAYDKlEKTKNRLQQE 581
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-897 |
1.41e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 596 KAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEK-----------DLGRLQVDMNELEEKSRSTQAALDSAY 664
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 665 RELTDLHKANAAKDSEVQEaaLRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRH--- 741
Cdd:TIGR02168 253 EELEELTAELQELEEKLEE--LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEles 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 742 ----------------------------EISELQQRLQEAENRNQEL---SQSVSSTTRPLLRQIENLQATLGSQTSSWE 790
Cdd:TIGR02168 331 kldelaeelaeleekleelkeelesleaELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 791 MLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQM-SSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVE 869
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEElEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340
....*....|....*....|....*...
gi 158186663 870 LENLKDEYVRTLEEARKEKTLLSSQLEM 897
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
532-874 |
2.03e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 532 KEELAS-RLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQlhnsnmikKLRAKDKDNESVIAKLKKKAKELEEelQHLRQV 610
Cdd:TIGR02169 176 LEELEEvEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREYEGYELLKEKEALERQK--EAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 611 LDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNEL-EEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAAlRRE 689
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE-ERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 690 MKAKEELSGALEKAqEEARQQQETLALQvgdlRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTR 769
Cdd:TIGR02169 325 AKLEAEIDKLLAEI-EELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 770 ---PLLRQIENLQATLGSQTSSWEMLE---KNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQnallrqens 843
Cdd:TIGR02169 400 einELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE--------- 470
|
330 340 350
....*....|....*....|....*....|.
gi 158186663 844 rlqaqLESEKNKLRKLEDENSRYQVELENLK 874
Cdd:TIGR02169 471 -----LYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
429-800 |
2.87e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 429 DGEAAENHPKAPQLEQEdvgktVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIA 508
Cdd:PRK02224 355 EERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 509 EAERKAQLACKERDTAKKEMKTMK-EELASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKklRAKDkdne 587
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKcPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE--RAED---- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 588 sviaklkkkAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYREL 667
Cdd:PRK02224 504 ---------LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 668 TDLHKANAAKDSEVQE-AALRREMKAKEELSGALEKAQEEARQQQEtlalqvgdlrLALQRAEQAAARKE--DYLRHE-- 742
Cdd:PRK02224 575 AELNSKLAELKERIESlERIRTLLAAIADAEDEIERLREKREALAE----------LNDERRERLAEKRErkRELEAEfd 644
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186663 743 ---ISELQQRLQEAEnrnqELSQSVSSTTRPLLRQIENLQATLGSQTSSWEMLEkNLSDRL 800
Cdd:PRK02224 645 earIEEAREDKERAE----EYLEQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERR 700
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
687-905 |
3.18e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 687 RREMKAKEELsgalekaqEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLrheisELQQRLQEAENrnQELSQSVSS 766
Cdd:TIGR02169 170 RKKEKALEEL--------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-----ALLKEKREYEG--YELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 767 ttrpLLRQIENLQATLGSQTSSWEMLEKNLSDRLGES----QTLLAAAVERERAATEELLANKIQMSSVESQNALLRQEN 842
Cdd:TIGR02169 235 ----LERQKEAIERQLASLEEELEKLTEEISELEKRLeeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158186663 843 SRLQAQLESEKNKLRKLEDENSRYQVELENLKdeyvRTLEEARKEKTLLSSQ---LEMERMKVEQE 905
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELE----REIEEERKRRDKLTEEyaeLKEELEDLRAE 372
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-893 |
3.23e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 454 LNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKE 533
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 534 ELaSRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLrakdkdnESVIAKLKKKAKELEEELQHLRQVLDG 613
Cdd:TIGR04523 296 EI-SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 614 KE-EVEKQHREN------IKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEaaL 686
Cdd:TIGR04523 368 KQnEIEKLKKENqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD--L 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 687 RREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDylrhEISELQQRLQEAENRNQELSQSVSS 766
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK----ELKKLNEEKKELEEKVKDLTKKISS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 767 TTRPLlRQIENLQATLGSQTSS-------------WEMLEK-----------------NLSDRLGESQTLLAAAVERERA 816
Cdd:TIGR04523 522 LKEKI-EKLESEKKEKESKISDledelnkddfelkKENLEKeideknkeieelkqtqkSLKKKQEEKQELIDQKEKEKKD 600
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158186663 817 ATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKTLLSS 893
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
699-918 |
3.49e-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: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 699 ALEKAQEEARQQQETLALQVGDLRLALQRAEQaaarKEDYLRHEISELQQRLQEAENRNQELSQsvssttrpllrQIENL 778
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRALEQ-----------ELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 779 QATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQ---LESEKNK 855
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQaeeLRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158186663 856 LRKLEDENSRYQVELENLKDEYV---RTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKE 918
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
456-908 |
6.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 456 EKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAqlacKERDTAKKEMKTMKEEL 535
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 536 ASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLhnSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDG-- 613
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElk 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 614 ---------KEEVEKQHRENIKklnsvvERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEA 684
Cdd:PRK03918 433 kakgkcpvcGRELTEEHRKELL------EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 685 ALRREMKA--KEELsgalEKAQEEARQQQETLALQVGDLRLALQRAEQAAA--RKEDYLRHEISELQQRLQEAENRNQEL 760
Cdd:PRK03918 507 ELEEKLKKynLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDELEEELAELLKELEEL 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 761 SQSvssttrpllrQIENLQATLGSQTSSW-EMLE-KNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALL 838
Cdd:PRK03918 583 GFE----------SVEELEERLKELEPFYnEYLElKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158186663 839 RQENSrlQAQLESEKNKLRKLEDENSRYQVELENLK---DEYVRTLE------EARKEKTLLSSQLEMERMKVEQERKK 908
Cdd:PRK03918 653 EKKYS--EEEYEELREEYLELSRELAGLRAELEELEkrrEEIKKTLEklkeelEEREKAKKELEKLEKALERVEELREK 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
458-806 |
1.43e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 458 LEKRETQLLSLSK--EKAlleEAYDNLKDEmfrvkEESSSISSLKDEFTQRIAEAERKAQlackerdtAKKEMKTMKEEL 535
Cdd:TIGR02168 195 LNELERQLKSLERqaEKA---ERYKELKAE-----LRELELALLVLRLEELREELEELQE--------ELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 536 ASRLNssqtadllkEKDEQIQGLMEEGEKLSKQQLHnsnmikklrakdkdnesviaklkkkakeLEEELQHLRQVLDGKE 615
Cdd:TIGR02168 259 TAELQ---------ELEEKLEELRLEVSELEEEIEE----------------------------LQKELYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 616 EVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREmkAKEE 695
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE--ELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 696 LSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARkedyLRHEISELQQRLQEAEnrNQELSQSVSSTTRPLLRQI 775
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAE--LKELQAELEELEEELEELQ 453
|
330 340 350
....*....|....*....|....*....|....
gi 158186663 776 ---ENLQATLGSQTSSWEMLEKNLSDRLGESQTL 806
Cdd:TIGR02168 454 eelERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
448-922 |
1.59e-05 |
|
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: 49.20 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 448 GKTVEFLNEKLEKRETQLLSLSKEkalleEAYDNLKDEMFRVKEES-SSISSLKDEFTQRIAEAERKAQLACKERDTAKK 526
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPL-----DQYTQLALMEFAKKKSLhGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 527 EMKTMKEELAsrlNSSQTADLLKEKDEQIQglmeegEKLSKQQLhnsnmIKKLRAKDKDNESVIAKLKKKAKELEEELQH 606
Cdd:TIGR00618 227 ELKHLREALQ---QTQQSHAYLTQKREAQE------EQLKKQQL-----LKQLRARIEELRAQEAVLEETQERINRARKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 607 LRQVLDGK--EEVEKQHRENIKKLNSVVERQEKDL---GRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEV 681
Cdd:TIGR00618 293 APLAAHIKavTQIEQQAQRIHTELQSKMRSRAKLLmkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 682 QEAALRREMKAKEELSGALEKAQEEARQQQETLALQVG--DLRLALQRAEQ---AAARKEDYLRHEISELQQ-----RLQ 751
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAtiDTRTSAFRDLQgqlAHAKKQQELQQRYAELCAaaitcTAQ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 752 EAENRNQELSQSVSSTtRPLLRQIENLQaTLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELL---ANKIQM 828
Cdd:TIGR00618 453 CEKLEKIHLQESAQSL-KEREQQLQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDnpgPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 829 SSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVEQERKK 908
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490
....*....|....
gi 158186663 909 TIFTQETLKEKEHK 922
Cdd:TIGR00618 611 ACEQHALLRKLQPE 624
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
633-1069 |
2.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 633 ERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSGALEKAQEEARQQQE 712
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 713 TLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTR---PLLRQIENLQATLGSQTSSw 789
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEeleELEEELEQLENELEAAALE- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 790 EMLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMssVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVE 869
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL--VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 870 LENLKDEYvrTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKEHKpfsvsstptmsRSSSLSGVDMAGLQTs 949
Cdd:COG4717 321 LEELLAAL--GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-----------IAALLAEAGVEDEEE- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 950 FLSQDESHDHsfgpmstsasgsnlYEAVRmgagsSIIENLQSQLKLREGEISHLqLEISNLEKTRSIMSEELVKLTNQND 1029
Cdd:COG4717 387 LRAALEQAEE--------------YQELK-----EELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEE 446
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 158186663 1030 ELEEKVKEIPKLRVQLRDL--DQRYNTILQMYGEKAEEAEEL 1069
Cdd:COG4717 447 ELEELREELAELEAELEQLeeDGELAELLQELEELKAELREL 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
454-922 |
2.88e-05 |
|
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: 48.58 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 454 LNEKLEKRETQLLSLSKEKALLEEAYDNLKDemfRVKEESSSISSLKDEFTQRIAEAERKAQLackerdtakkeMKTMKE 533
Cdd:pfam15921 375 LDDQLQKLLADLHKREKELSLEKEQNKRLWD---RDTGNSITIDHLRRELDDRNMEVQRLEAL-----------LKAMKS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 534 ELASRLNSSQTAdlLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESviaklkkkakeLEEELQHLRQVLDG 613
Cdd:pfam15921 441 ECQGQMERQMAA--IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES-----------SERTVSDLTASLQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 614 KEEVEKQHRENIKKLNSVVERQEKDLGRLQVDmnelEEKSRSTQAALDSAYRELTDlhkanaaKDSEVQeaALRREMKAK 693
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMAE-------KDKVIE--ILRQQIENM 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 694 EELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRheisELQQRLQEAENRNQELSQSVSSTTRP--- 770
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR----ELEARVSDLELEKVKLVNAGSERLRAvkd 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 771 -------LLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENS 843
Cdd:pfam15921 651 ikqerdqLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 844 RLQAQLESEKNKLRKLedensryQVELENLKDeyvrTLEEARKEKTLL---SSQLEMERMKVEQERKKTIFTQETLKEKE 920
Cdd:pfam15921 731 GMQKQITAKRGQIDAL-------QSKIQFLEE----AMTNANKEKHFLkeeKNKLSQELSTVATEKNKMAGELEVLRSQE 799
|
..
gi 158186663 921 HK 922
Cdd:pfam15921 800 RR 801
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
434-922 |
3.42e-05 |
|
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: 48.04 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 434 ENHPKAPQLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERK 513
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 514 AQLACKERDTAKKEMKTMKEELASRLnsSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNsnmiKKLRAKDKDNESVIAKL 593
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEEL--EILEEEEESIELKQGKLTEEKEELEKQELKL----LKDELELKKSEDLLKET 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 594 KKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKA 673
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 674 NAAKDSEVQEAALRREMKAKEELSGALEKAQEEAR--------------QQQETLALQVGDLRLALQRAEQAAARKEDYL 739
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiavleidpilnlaQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 740 RHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATE 819
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 820 ELLANKIQMSSVESQNALLRQENSR---LQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEE----ARKEKTLLS 892
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKqkiDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEklkvEEEKEEKLK 797
|
490 500 510
....*....|....*....|....*....|
gi 158186663 893 SQLEMERMKVEQERKKTIFTQETLKEKEHK 922
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQE 827
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
441-710 |
3.44e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 441 QLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSS----ISSLKDEF---TQRIAEAERK 513
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeLTLLNEEAanlRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 514 AQLACKERDTAKKEMKTMKEELASrlNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKL 593
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 594 KKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLqvdMNELEEKSRSTQAALDSAYRELTDLHKA 673
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL---ENKIEDDEEEARRRLKRLENKIKELGPV 987
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 158186663 674 NAAKDSEVQEAALRRE---------MKAKEELSGALEKAQEEARQQ 710
Cdd:TIGR02168 988 NLAAIEEYEELKERYDfltaqkedlTEAKETLEEAIEEIDREARER 1033
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
519-1050 |
3.73e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 519 KERDTAKKEMKTMKEELASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVI-------- 590
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKImkldneik 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 591 ---AKLKKKAKELEEELQHLRQVLDGKEE----VEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSA 663
Cdd:TIGR00606 273 alkSRKKQMEKDNSELELKMEKVFQGTDEqlndLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 664 YRELTDLHKANAAKDSEVQEAALRREMKAKEE---LSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLR 740
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERgpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 741 HEISELQQRLQeaeNRNQELSQSVSStTRPLLRQIENLQATLGSQTSSWEMLEKNLSD-RLGESQTLLAAAVERERAATE 819
Cdd:TIGR00606 433 DEKKGLGRTIE---LKKEILEKKQEE-LKFVIKELQQLEGSSDRILELDQELRKAERElSKAEKNSLTETLKKEVKSLQN 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 820 ELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLE---DENSRYQVELENL------KDEYVRTLEEARKEKTL 890
Cdd:TIGR00606 509 EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEqirKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 891 LSSQLEMERMKVEQERKKTIFTQETLKEKEHKPFSVSSTPTMSRSSSLSGVDMAGL---------QTSFLSQDESHDHSF 961
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLkeeieksskQRAMLAGATAVYSQF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 962 GPMSTSASGSNLYEAVRM----GAGSSIIENLQSQLKLREGEISHLQLEISNLEKTRSIMseeLVKLTNQNDELEEKVKE 1037
Cdd:TIGR00606 669 ITQLTDENQSCCPVCQRVfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM---LGLAPGRQSIIDLKEKE 745
|
570
....*....|...
gi 158186663 1038 IPKLRVQLRDLDQ 1050
Cdd:TIGR00606 746 IPELRNKLQKVNR 758
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
607-802 |
4.51e-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: 46.18 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 607 LRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGR---LQVDMNELEEKSRSTQAALDSAYRELTDLHKAN--------- 674
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEvaaLNRRIQLLEEELERTEERLAEALEKLEEAEKAAdesergrkv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 675 ----AAKDSE--------------VQEAALRREMKAKEEL---SGALEKAQEEARQQQETLALQVGDLRLA------LQR 727
Cdd:pfam00261 83 lenrALKDEEkmeileaqlkeakeIAEEADRKYEEVARKLvvvEGDLERAEERAELAESKIVELEEELKVVgnnlksLEA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186663 728 AEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSsttrPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGE 802
Cdd:pfam00261 163 SEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQ----KLEKEVDRLEDELEAEKEKYKAISEELDQTLAE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
536-924 |
5.22e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 536 ASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDGKE 615
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 616 EVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEE 695
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 696 LSGALEKAQEEARQQQETLALQVGDLRLALQraEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQI 775
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALE--LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 776 ENLQATLgsQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNK 855
Cdd:pfam02463 889 ESKEEKE--KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158186663 856 LRKLEDENsryqvELENLKDEYVRTLEEARKEktllssqlEMERMKVEQERKKTIFTQETLKEKEHKPF 924
Cdd:pfam02463 967 LAKEELGK-----VNLMAIEEFEEKEERYNKD--------ELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
623-782 |
5.27e-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: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 623 ENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSG---- 698
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnhp 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 699 ALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQsvssttrpLLRQIENL 778
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--------LEREVEVA 363
|
....
gi 158186663 779 QATL 782
Cdd:COG3206 364 RELY 367
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
441-723 |
6.63e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 441 QLEQEDVGKTVEFLNEKLEKRETQLlslskekALLEEAYDNLKDE--MFRVKEESSSISSLKDEFTQRIAEAERKAQLAC 518
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKEL-------EEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 519 KERDTAKKEMKTMKEELASRLNSSQTADLLkekdEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKdkdnesviaklkkkak 598
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLR----AQLAELEAELAELSARYTPNHPDVIALRAQ---------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 599 eleeelqhlrqvldgKEEVEKQHRENIKKLnsvverqekdLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKAnaakd 678
Cdd:COG3206 300 ---------------IAALRAQLQQEAQRI----------LASLEAELEALQAREASLQAQLAQLEARLAELPEL----- 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158186663 679 sEVQEAALRREMKAKEELSGALEKAQEEARQQQetlALQVGDLRL 723
Cdd:COG3206 350 -EAELRRLEREVEVARELYESLLQRLEEARLAE---ALTVGNVRV 390
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
641-920 |
7.55e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 641 RLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEaaLRREMKAKEELSGALEKAQEEARQQQETLALQVGD 720
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 721 LRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRL 800
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 801 GESQTLlaaavereraatEELLANKIQmssvesqnallrqENSRLQAQLESEKN-----------KLRKLEDENSRYQVE 869
Cdd:TIGR02169 822 NRLTLE------------KEYLEKEIQ-------------ELQEQRIDLKEQIKsiekeienlngKKEELEEELEELEAA 876
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158186663 870 LENLKDEYV---RTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKE 920
Cdd:TIGR02169 877 LRDLESRLGdlkKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
622-876 |
9.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 622 RENIKKLNSV------VERQEKDLGRLQvdmnELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEE 695
Cdd:COG4913 231 VEHFDDLERAhealedAREQIELLEPIR----ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 696 LSGALEKAQEEARQQQETLalqvgdLRLALQRAEQAAARKEDyLRHEISELQQRLQEAENRNQELSQsvssttrpllrQI 775
Cdd:COG4913 307 LEAELERLEARLDALREEL------DELEAQIRGNGGDRLEQ-LEREIERLERELEERERRRARLEA-----------LL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 776 ENLQATLGSQTSSWEMLEKNLSDRLGESQTLLaaavereraateellankiqmSSVESQNALLRQENSRLQAQLESEKNK 855
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEEL---------------------EALEEALAEAEAALRDLRRELRELEAE 427
|
250 260
....*....|....*....|.
gi 158186663 856 LRKLEDENSRYQVELENLKDE 876
Cdd:COG4913 428 IASLERRKSNIPARLLALRDA 448
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-678 |
9.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 454 LNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKE 533
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 534 ELASRL-----NSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESViaklkkkAKELEEELQHLR 608
Cdd:COG4942 105 ELAELLralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------RAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 609 QVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKD 678
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
525-904 |
9.42e-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: 46.49 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 525 KKEMKTMKEELASRLNSSQTADLLKEKDEQIQGLMEEgEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEEL 604
Cdd:COG5185 178 KLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGN-LGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 605 QHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALD-SAYRELTDLHKANAAKDSEVQE 683
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESlEEQLAAAEAEQELEESKRETET 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 684 AALRREMKAKEELSGALEKaQEEARQQQETLALQVgDLRLALQRAEQAaarkEDYLRHEISELQQRLQEAENRNQELSQS 763
Cdd:COG5185 337 GIQNLTAEIEQGQESLTEN-LEAIKEEIENIVGEV-ELSKSSEELDSF----KDTIESTKESLDEIPQNQRGYAQEILAT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 764 VSSTTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAATEEllANKIQMSSVESQNALLRQENS 843
Cdd:COG5185 411 LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEE--AYDEINRSVRSKKEDLNEELT 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158186663 844 RLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTL-EEARKEKTLLSSQLEMERMKVEQ 904
Cdd:COG5185 489 QIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLkDFMRARGYAHILALENLIPASEL 550
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
523-869 |
1.35e-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: 45.88 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 523 TAKKEMKTMKEE--LASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQlhnSNMIKKLRAKDKDNESVIAKLKKKAKEL 600
Cdd:pfam17380 257 TVRYNGQTMTENefLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEK---EEKAREVERRRKLEEAEKARQAEMDRQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 601 EEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEkdLGRLQVDMNELEEKSRSTQAALDSAYRELtdlhkaNAAKDSE 680
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEERKRELERIRQEE--IAMEISRMRELERLQMERQQKNERVRQEL------EAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 681 VQEAALRREMKAKEELSGALEKAQEEARQQQetlalqvgdlrlaLQRAEQAAARKEDYLRHEISELQQ-----RLQEAEN 755
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQRE-------------VRRLEEERAREMERVRLEEQERQQqverlRQQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 756 RNQELSQSVSSTTRPLL---------RQIENLQATLGSQTSSWEMLEKNLSDRlgesQTLLAAAVERERAATEELLANKI 826
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAeeqrrkileKELEERKQAMIEEERKRKLLEKEMEER----QKAIYEEERRREAEEERRKQQEM 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 158186663 827 -QMSSVESQNALLRQENSRLQAqLESEKNKLRKL-EDENSRYQVE 869
Cdd:pfam17380 549 eERRRIQEQMRKATEERSRLEA-MEREREMMRQIvESEKARAEYE 592
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
575-940 |
2.72e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 575 MIKKLRAKDKDNESVIAKLKKKAKELEEElqhLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSR 654
Cdd:pfam02463 149 MMKPERRLEIEEEAAGSRLKRKKKEALKK---LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 655 STQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEEL--SGALEKAQEEARQQQETLALQVGDLRLALQRAEQAA 732
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 733 ARKEDYLRHEISELQQRLQEAENRNQELSQSVSsttrpllrQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVE 812
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE--------ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 813 RERAATEELLANKI---QMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKT 889
Cdd:pfam02463 378 KKKLESERLSSAAKlkeEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 158186663 890 LLSSQLEMERMKVEQERKKTIFTQETLKEKEHKPFSVSSTPTMSRSSSLSG 940
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
700-902 |
3.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 700 LEKAQEEARQQQETLALQVGDLRLALQRAEQAAAR-KEDY------------------LRHEISELQQRLQEAENRNQEL 760
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNglvdlseeaklllqqlseLESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 761 SQSVSSTTRPLLRQIEN-LQATLGSQTSSWEMLEKNLSDRLGES----QTLLAAAVERERAATEELlanKIQMSSVESQN 835
Cdd:COG3206 246 RAQLGSGPDALPELLQSpVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEA---QRILASLEAEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 836 ALLRQENSRLQAQLESEKNKLRKL---EDENSRYQVELENLKDEYVRTLeeARKEKTLLSSQLEMERMKV 902
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLL--QRLEEARLAEALTVGNVRV 390
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
605-914 |
3.68e-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: 44.73 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 605 QHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKD-LGRLQVDMNELEEKSRSTQAALDSayreltdlhkaNAAKDSEVQE 683
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDR-----------QAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 684 AALRREMKAkeELSGALEKAQEEARQQQETLALQVGDLRlALQRAEQAAARKEDYLRHEI-SELQQRLQEAENRnqelsq 762
Cdd:pfam17380 342 MAMEREREL--ERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQELeAARKVKILEEERQ------ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 763 svssttRPLLRQIENLQATLGSQTSSwemleknlsdRLGESQTLLAAAVERERAATEELLANKIQMSSvesqnaLLRQEN 842
Cdd:pfam17380 413 ------RKIQQQKVEMEQIRAEQEEA----------RQREVRRLEEERAREMERVRLEEQERQQQVER------LRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 843 SRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKTLLSSQL--------EMERMKVEQERKKTIFTQE 914
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEerqkaiyeEERRREAEEERRKQQEMEE 550
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
721-913 |
3.74e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 721 LRLALQRAEQAAARKEDYLRHEISELQQRLQEAEN-----RNQELSQSVSSTTRPLLRQIENL-------QATLGSQTSS 788
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefRQKNGLVDLSEEAKLLLQQLSELesqlaeaRAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 789 WEMLEKNLSDRLGESQTLLaaavereraATEELLANKIQMSSVESQNALLRQ---ENS----RLQAQLESEKNKLRKLED 861
Cdd:COG3206 242 LAALRAQLGSGPDALPELL---------QSPVIQQLRAQLAELEAELAELSArytPNHpdviALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158186663 862 EN-SRYQVELENLK---DEYVRTLEEARKE-KTLLSSQLEMERMKVEQERKKTIFTQ 913
Cdd:COG3206 313 RIlASLEAELEALQareASLQAQLAQLEARlAELPELEAELRRLEREVEVARELYES 369
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
441-920 |
3.78e-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: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 441 QLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKalleeayDNLKDEM-FRVKEESSSISSLKDEFTQRIAEAERKAQL--- 516
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEKMILAFEELRVQA-------ENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLlli 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 517 ACKERDTAKKEMKTMKEElaSRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQ----QLHNSNMIKKLRAKDKDNESVIAK 592
Cdd:pfam05483 248 QITEKENKMKDLTFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHLTKElediKMSLQRSMSTQKALEEDLQIATKT 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 593 LKKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVV----ERQEKDLGRLQVDMNELEEKSRSTQAAL---DSAYR 665
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLrteqQRLEKNEDQLKIITMELQKKSSELEEMTkfkNNKEV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 666 ELTDLHKANAAK----DSEVQEAALRREMKAKE-ELSGALEKAQEE----------ARQQQETLALQVGDLRLALQRAEQ 730
Cdd:pfam05483 406 ELEELKKILAEDekllDEKKQFEKIAEELKGKEqELIFLLQAREKEihdleiqltaIKTSEEHYLKEVEDLKTELEKEKL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 731 AAARKEDYLRHEISELQQRLQEAEN------RNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGESQ 804
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDmtlelkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 805 TLLAAAVERERAATEELLANKIQMSSVESQNALLR--------------QENSRLQAQLESEKNKLRKLEDENSRYQVEL 870
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKkqienknknieelhQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 158186663 871 ENLKDEYVRTLEEARKEktLLSSQLEMERMKVEQERKKTIFTQETLKEKE 920
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKE--IEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
606-870 |
7.20e-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: 43.58 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 606 HLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELE---EKSRSTQAALDSAYRELTDLHKANAAKDSEVQ 682
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkriRLLEKREAEAEEALREQAELNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 683 EAALRREMKakeelsgalekaQEEARQQQETLALQVGDLRLALQRAEQAAARKedylRHEISELQQRLQEAENRNQELSQ 762
Cdd:pfam05557 90 KKLNEKESQ------------LADAREVISCLKNELSELRRQIQRAELELQST----NSELEELQERLDLLKAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 763 ------SVSSTTRPLLRQIENLQATLGSQTsSWEMLEKNLSDRLGESQTLLAAAvereraatEELLANKIQMSSVESQNA 836
Cdd:pfam05557 154 lrqnleKQQSSLAEAEQRIKELEFEIQSQE-QDSEIVKNSKSELARIPELEKEL--------ERLREHNKHLNENIENKL 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 158186663 837 LLRQENSRLQAQLESE---KNKLRKLEDENSRYQVEL 870
Cdd:pfam05557 225 LLKEEVEDLKRKLEREekyREEAATLELEKEKLEQEL 261
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-769 |
9.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 427 AEDGEAAENHPKAPQLEQ-EDVGKTVEFLNEKLEKRETQLLSLSKEKAllEEAYDNLKDEMFRVKEESSSISSLKDEFTQ 505
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKA--EEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 506 RIAEAERKAQLACKERDTAKKEMKTMKEELASRlnssQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKD 585
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 586 NESVIAKLKKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYR 665
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 666 ELTDLHKANAAKDSEVQEAALRREMKAKEELSGALEKAQEEARQQQETlALQVGDLRLALQRAEQAAARKEDYLRHEISE 745
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEG-NLVINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
330 340
....*....|....*....|....
gi 158186663 746 LQQRLQEAENRNQELSQSVSSTTR 769
Cdd:PTZ00121 1849 FEKHKFNKNNENGEDGNKEADFNK 1872
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
628-918 |
1.27e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 628 LNSVVE--RQEKDLGRLQVDMNELEEKsrstqaaldsayreltdLHKANAAkdseVQEAALRREMKakEELSGALEKAQE 705
Cdd:PRK04863 337 LNLVQTalRQQEKIERYQADLEELEER-----------------LEEQNEV----VEEADEQQEEN--EARAEAAEEEVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 706 EARQQ----------QETLALQVGDLRLALQRAEQ-----------------AAARKEDYLRHEISELQQRLQEAENRNQ 758
Cdd:PRK04863 394 ELKSQladyqqaldvQQTRAIQYQQAVQALERAKQlcglpdltadnaedwleEFQAKEQEATEELLSLEQKLSVAQAAHS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 759 ELSQSVSS---------------TTRPLLRQIENLQAtLGSQTSSWEMLEKNLSDRLGESQTLLA-------------AA 810
Cdd:PRK04863 474 QFEQAYQLvrkiagevsrseawdVARELLRRLREQRH-LAEQLQQLRMRLSELEQRLRQQQRAERllaefckrlgknlDD 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 811 VERERAATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKTL 890
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY 632
|
330 340
....*....|....*....|....*...
gi 158186663 891 LSSQLEMERmKVEQERKKTIFTQETLKE 918
Cdd:PRK04863 633 MQQLLERER-ELTVERDELAARKQALDE 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
444-1079 |
1.31e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 444 QEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERK-AQLACKERD 522
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLlEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 523 TAKKEMKTMKEELAS-RLNSSQTADLLKEKDEQIQGLMEEGEK----LSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKA 597
Cdd:TIGR02169 284 LGEEEQLRVKEKIGElEAEIASLERSIAEKERELEDAEERLAKleaeIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 598 KELEEELQHLrqvldgkEEVEKQHRENIKKLNSVVERQEKdlgrLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAK 677
Cdd:TIGR02169 364 EELEDLRAEL-------EEVDKEFAETRDELKDYREKLEK----LKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 678 DSEVQEAALRREMKAKEelsgalekaQEEARQQQETLALQVGDLRLALQRAEQAAARKEDylrhEISELQQRLQEAENRN 757
Cdd:TIGR02169 433 EAKINELEEEKEDKALE---------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK----ELSKLQRELAEAEAQA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 758 QELSQSVSS-------------------------------------------------------------------TTRP 770
Cdd:TIGR02169 500 RASEERVRGgraveevlkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiellkrrkagraTFLP 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 771 L---------------------------------------------LRQIENLQATLGSQ---TSSWEMLEKN------- 795
Cdd:TIGR02169 580 LnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKYrmvTLEGELFEKSgamtggs 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 796 -------------------LSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKL 856
Cdd:TIGR02169 660 raprggilfsrsepaelqrLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 857 RKLEDENSRYQVELENLKDEyVRTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQ-ETLKEKEHKPFSVSSTPTMSRS 935
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 936 SSLSGVDMAGLQTSFLSQDESHDHSFGPMSTSASGSNLYEA-VRMGAGSSIIENLQSQLKLREGEISHLQLEISNLEKTR 1014
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186663 1015 SIMSEELVKLTNQNDELEEKVKEipkLRVQLRDLDQRYNTILQMYGEKAEEAEELrLDLEDVKNM 1079
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSE---LKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAE 959
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
829-1072 |
1.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 829 SSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQ-----VELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVE 903
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 904 QERKKTIFTQETLKEkehkpfsVSSTPTMSRSSSlsgvDMAGLQTSfLSQdeshdhsfgpmstsasgsnlyEAVRMGAGS 983
Cdd:COG3206 244 ALRAQLGSGPDALPE-------LLQSPVIQQLRA----QLAELEAE-LAE---------------------LSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 984 SIIENLQSQLKLREGEISH-LQLEISNLEKTRSIMSEELVKLTNQNDELEEKVKEIPKLRVQLRDLDQRYNTILQMYGEK 1062
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|
gi 158186663 1063 AEEAEELRLD 1072
Cdd:COG3206 371 LQRLEEARLA 380
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
426-714 |
1.74e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 426 AAEDGEAAENHPKAPQLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEE---AYDNLKDEMFRVKEESSSISSLKDE 502
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkkAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 503 FTQRIAEAERKAQLACKERDTAKKEMKTMKEELASRlnssqtADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAK 582
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK------AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 583 DKDNESVIAKLKKKAKELEEELQHlrqvldgKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDS 662
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKK-------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158186663 663 AYRELtdlhKANAAKDSEVQEAALRREMKAKEE-------LSGALEKAQEEARQQQETL 714
Cdd:PTZ00121 1726 EENKI----KAEEAKKEAEEDKKKAEEAKKDEEekkkiahLKKEEEKKAEEIRKEKEAV 1780
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
620-765 |
1.76e-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: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 620 QHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLhKANAAKDSEVQEA--------ALRREMK 691
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGNvrnnkeyeALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158186663 692 AKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVS 765
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
444-913 |
1.81e-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: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 444 QEDVGKTVEFLN-EKLEKRETQLLSLS--KEKALLEEAYDNLKDEMFRVKEEsssISSLKDEftqrIAEAERKAQLACKE 520
Cdd:TIGR01612 1061 EKEIGKNIELLNkEILEEAEINITNFNeiKEKLKHYNFDDFGKEENIKYADE---INKIKDD----IKNLDQKIDHHIKA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 521 RDTAKKEMKTMKEELASRLNssqtaDLLKEKDEQIQGlmEEGEKLSKQQlhnSNMIKKLRAKdkdnesviaklkkkakel 600
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQIN-----DLEDVADKAISN--DDPEEIEKKI---ENIVTKIDKK------------------ 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 601 eeelqhlrqvldgkeeveKQHRENIKKLNSVVERQEKD-----------------LGRLQVD-MNELEEKSRSTQAALDS 662
Cdd:TIGR01612 1186 ------------------KNIYDEIKKLLNEIAEIEKDktsleevkginlsygknLGKLFLEkIDEEKKKSEHMIKAMEA 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 663 AYRELTDLHKANAAKDSEVQ-EAALRREMKAKEELSGALEKAQEEARQQQETLAlqvgDLRLALQRAEQAAARKEDyLRH 741
Cdd:TIGR01612 1248 YIEDLDEIKEKSPEIENEMGiEMDIKAEMETFNISHDDDKDHHIISKKHDENIS----DIREKSLKIIEDFSEESD-IND 1322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 742 EISELQQRLQEAENRNQELSQSVSSTTRPL----LRQIENLQATLGSQTSSWEMLEKNLSDRLGESQTLLAAAVERERAA 817
Cdd:TIGR01612 1323 IKKELQKNLLDAQKHNSDINLYLNEIANIYnilkLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 818 T-----EELLANK-----IQmSSVESQNALLRQE---NSRLQAQLESEKNKL---RKLEDENSRYQVELENLKD------ 875
Cdd:TIGR01612 1403 EckskiESTLDDKdidecIK-KIKELKNHILSEEsniDTYFKNADENNENVLllfKNIEMADNKSQHILKIKKDnatndh 1481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 158186663 876 -----EYVRTLEEARKEKTllssqlEMERMKVEQERKKTIFTQ 913
Cdd:TIGR01612 1482 dfninELKEHIDKSKGCKD------EADKNAKAIEKNKELFEQ 1518
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
670-782 |
1.95e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 670 LHKANAAKDSEVQEAalRREMKAKEELsgALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQR 749
Cdd:PRK12704 33 IKEAEEEAKRILEEA--KKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110
....*....|....*....|....*....|...
gi 158186663 750 LQEAENRNQELSQsvssttrpLLRQIENLQATL 782
Cdd:PRK12704 109 EEELEKKEKELEQ--------KQQELEKKEEEL 133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
699-984 |
2.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 699 ALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDylrhEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENL 778
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA----ELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 779 QATlGSQTSSWEMLEknlsdrlgESQTLlaaavereraatEELLANKIQMSSVESQNALLRQENSRLQAQLESEKNKLRK 858
Cdd:COG3883 96 YRS-GGSVSYLDVLL--------GSESF------------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 859 LEDENSRYQVELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKEHKPFSVSSTPTMSRSSSL 938
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 158186663 939 SGVDMAGLQTSFLSQDESHDHSFGPMSTSASGSNLYEAVRMGAGSS 984
Cdd:COG3883 235 AAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
535-773 |
2.22e-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: 41.67 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 535 LASRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQqlhnsnmIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDGK 614
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 615 EEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRST----QAALDSAYRELTDLHKANAAKDSEVQE------- 683
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEElradlae 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 684 -AALRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQ 762
Cdd:COG4942 162 lAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 158186663 763 SVSSTTRPLLR 773
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
419-920 |
2.55e-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: 41.73 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 419 GPSASGPAAEDGEAAENHPKAPQLEQEDVGKTVEFLNEKLEKRETQLLSlskEKALLEEAYDNLKD--EMFRVKEESSSI 496
Cdd:pfam10174 100 SPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIET---QKQTLGARDESIKKllEMLQSKGLPKKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 497 SSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKEELASRL----NSSQTADL-----------------LKEKDEQI 555
Cdd:pfam10174 177 GEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNqlqpDPAKTKALqtviemkdtkisslernIRDLEDEV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 556 QGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQ 635
Cdd:pfam10174 257 QMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAK 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 636 EKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEaaLRREMKAKEELSGALEKAQEEARQQQETLA 715
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD--LKDMLDVKERKINVLQKKIENLQEQLRDKD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 716 LQVGDLR--------------LALQRAEQAAARKE---DYLRHEIS-ELQQRLQEAEN---RNQELSQSVSSTTRPLLRQ 774
Cdd:pfam10174 415 KQLAGLKervkslqtdssntdTALTTLEEALSEKEriiERLKEQRErEDRERLEELESlkkENKDLKEKVSALQPELTEK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 775 ---IENLQATLGSQTSSWEM-----------LEKNLSDRLGESQTLLAAAVERERAATEELLANKIQmsSVESQNALLRQ 840
Cdd:pfam10174 495 essLIDLKEHASSLASSGLKkdsklksleiaVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIR--LLEQEVARYKE 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 841 ENSRLQAQLESEKNKLRKLEDEnsryqvelENLKDEYVRTLEEAR----KEKTLLSSQLEMerMKVEQERKKTIFTQETL 916
Cdd:pfam10174 573 ESGKAQAEVERLLGILREVENE--------KNDKDKKIAELESLTlrqmKEQNKKVANIKH--GQQEMKKKGAQLLEEAR 642
|
....
gi 158186663 917 KEKE 920
Cdd:pfam10174 643 RRED 646
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
59-224 |
2.84e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.83 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 59 TSTWGLNSSSEPQSSPTAsqaitkPVRRTVVDESENFFSAFLSPSDVQTIQKSPVVSKPP---AKSQRPEEEVKSSLQEP 135
Cdd:pfam05109 414 TTTHKVIFSKAPESTTTS------PTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTvstADVTSPTPAGTTSGASP 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 136 SSPGQSRTSETAESEATDsacVSGETPAVGTPSPVPEGKREETASEESEGKVPTVRAKASESVVKVNTAEDVSPTStqSL 215
Cdd:pfam05109 488 VTPSPSPRDNGTESKAPD---MTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTP--AV 562
|
....*....
gi 158186663 216 TTETKDMAL 224
Cdd:pfam05109 563 TTPTPNATI 571
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
454-1092 |
3.30e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 454 LNEKLEKRETQLLSLSKEKALLEEAYDNLKDEmfRVKEESSSISSLKDEFTQRIAEAERKAQLACKERDTAKKEMKTMKE 533
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKL--ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 534 ELASRLNS-SQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESviaKLKKKAKeleeelqhlrqvld 612
Cdd:pfam02463 266 KLAQVLKEnKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK---EKKKAEK-------------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 613 gKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKA 692
Cdd:pfam02463 329 -ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 693 KE--ELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRP 770
Cdd:pfam02463 408 QLllELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 771 LLRQIENLQATLGSQTSSWEMLEKN--LSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNALLRQENSRLQAQ 848
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLlaLIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 849 LESEKNKLRKLEDENSRYQVELENLKDEYVRTLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETLKEKEHKPFSVSS 928
Cdd:pfam02463 568 RALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESG 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 929 TPTMsrSSSLSGVDMAGLQTSFLSQDESHDHSFGPMSTSASGSNLYEAVRMGAGSSIienLQSQLKLREGEISHLQLEIS 1008
Cdd:pfam02463 648 LRKG--VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 1009 NLEKTRSIMSEELVKLTNQNDELEEKVKEIPKLRVQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELL 1088
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
....
gi 158186663 1089 RQRL 1092
Cdd:pfam02463 803 LRAL 806
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
633-760 |
3.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 633 ERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSGALEKAQEEaRQQQE 712
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE-AEREE 736
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 158186663 713 TLALQVGDLRLALQRAEQAAARKEDylrheISELQQRLQEAENRNQEL 760
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPD-----LEELERELERLEREIEAL 779
|
|
| PHA03325 |
PHA03325 |
nuclear-egress-membrane-like protein; Provisional |
52-215 |
4.75e-03 |
|
nuclear-egress-membrane-like protein; Provisional
Pssm-ID: 223044 Cd Length: 418 Bit Score: 40.64 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 52 SVSGGWDTSTWGLNSSSEPQSSPTASQAITKPVRRTVVDESENFFSAFLSPSDVQTIQKSPVVSKPPAKSQRPEEEVKSS 131
Cdd:PHA03325 259 SSAFMLNSSLPTSAPKRRSRRAGAMRAAAGETADLADDDGSEHSDPEPLPASLPPPPVRRPRVKHPEAGKEEPDGARNAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 132 LQEPSSPGQSRTSETAESEATDSACVSGETPAVGTPSPVPEGKREETASEESEgkvPTVRAKASESvvkVNTAEDVSPTS 211
Cdd:PHA03325 339 AKEPAQPATSTSSKGSSSAQNKDSGSTGPGSSLAAASSFLEDDDFGSPPLDLT---TSLRHMPSPS---VTSAPEPPSIP 412
|
....
gi 158186663 212 TQSL 215
Cdd:PHA03325 413 LTYL 416
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
687-926 |
5.20e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 687 RREMKAKEELSGALEKAQEEARQQQETLAlQVGDLRLA--LQRAEQAAARKEDYLRHEISEL----QQRLQEAENRNQEL 760
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREKKLRETEE-VEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIylqsAQRVELAERQLQEL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 761 SQSVSSTT--RPLLRQIENLQATLGSQTSSWEMLEKNLSdrlgeSQTLLAAAVERERAATEELLANKIQMSSVESQnalL 838
Cdd:COG5022 888 KIDVKSISslKLVNLELESEIIELKKSLSSDLIENLEFK-----TELIARLKKLLNNIDLEEGPSIEYVKLPELNK---L 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 839 RQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKdEYVRTLEEARKEKTLLSSQLemERMKVEQERKKTIFTQETLKE 918
Cdd:COG5022 960 HEVESKLKETSEEYEDLLKKSTILVREGNKANSELK-NFKKELAELSKQYGALQEST--KQLKELPVEVAELQSASKIIS 1036
|
....*...
gi 158186663 919 KEHKPFSV 926
Cdd:COG5022 1037 SESTELSI 1044
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
614-904 |
5.79e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 614 KEEVEKQHREnikkLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQE---------- 683
Cdd:pfam07888 68 REQWERQRRE----LESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREleediktltq 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 684 ------AALRREMKAKEELSGALEKAQEEARQQQETLALQVGDLR---LALQRAEQAAARKEDY---LRHEISELQQRLQ 751
Cdd:pfam07888 144 rvlereTELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRslsKEFQELRNSLAQRDTQvlqLQDTITTLTQKLT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 752 EAENRNQELsqsvssttRPLLRQIENLQATLGSQTSSWEMLEKNLSDRLGE---SQTLLAAAVERERAATEELLANKIQM 828
Cdd:pfam07888 224 TAHRKEAEN--------EALLEELRSLQERLNASERKVEGLGEELSSMAAQrdrTQAELHQARLQAAQLTLQLADASLAL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 829 SSVESQNAllrQENSRLQAQLESEKNKLRKLEDE--------------NSRYQVELENLKDEYVRTLEEARKEKTLLSSQ 894
Cdd:pfam07888 296 REGRARWA---QERETLQQSAEADKDRIEKLSAElqrleerlqeermeREKLEVELGREKDCNRVQLSESRRELQELKAS 372
|
330
....*....|
gi 158186663 895 LEMERMKVEQ 904
Cdd:pfam07888 373 LRVAQKEKEQ 382
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
622-1091 |
6.52e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 622 RENIKKLNSVVERQEKDLGRLQVDMNELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSGALE 701
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 702 KAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQ------I 775
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 776 ENLQATLGSQTSSWEMLEKNL----------SDRLGESQTLLAAAVERERAATEELLA---------------------- 823
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELrqarkrrdqaSEALRQASRRLEERQSALDELELQLFPqagtllhflrkeapdweqsigk 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 824 ----------------------------------NKIQMSSVESQNALLRQENSRLQAQLESEKNKLRKLEDENSRYQVE 869
Cdd:pfam12128 554 vispellhrtdldpevwdgsvggelnlygvkldlKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 870 LENLKdeyvrtLEEARKEKTLLSSQLEMERMKVEQERKKTIFTQETlkeKEHKPFSVSSTPTMSRSSSLSGVDMAGLQTS 949
Cdd:pfam12128 634 LEKAS------REETFARTALKNARLDLRRLFDEKQSEKDKKNKAL---AERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 950 FlsQDESHDHSfgpMSTSASGSNLYEA--VRMGAGSSIIENLQSQLKlreGEISHLQLEISNLEKTRSIMSEELVKLTNQ 1027
Cdd:pfam12128 705 Q--KEQKREAR---TEKQAYWQVVEGAldAQLALLKAAIAARRSGAK---AELKALETWYKRDLASLGVDPDVIAKLKRE 776
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186663 1028 NDELEEKVKEIPKLRVQLRDLDQRYN-TILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQR 1091
Cdd:pfam12128 777 IRTLERKIERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR 841
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
442-652 |
6.98e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 442 LEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAERKAQLACKER 521
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 522 DTAKKEMKTMKEELAS-RLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNMIKKLRAKDKDNESVIAKLKKKAKEL 600
Cdd:TIGR04523 380 QSYKQEIKNLESQINDlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 158186663 601 EEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMNELEEK 652
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
438-568 |
8.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 438 KAPQLEQEDVGKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLK---------DEFTQRIA 508
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 509 EAERKAQLACKERDTAKKEMKTMKEELASRlnSSQTADLLKEKDEQIQGLMEEGEKLSKQ 568
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
607-1089 |
9.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 607 LRQVLDGKEEVEKQHRENIKKLNSVVERqekdlgrlqvdMNELEEKSRSTQAALDSAYRELTDLHK-ANAAKDSEVQEAA 685
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLRE-----------INEISSELPELREELEKLEKEVKELEElKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 686 LRREMKAKEELSGALEKAQEEARQQQETLALQVGDLRLALQRAEQAAARKEDYlrheiSELQQRLQEAENRNQELSQSVS 765
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY-----EEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 766 STTRpLLRQIENLQATLGSQTSSWEMLEKNLSdRLGESQTLLAAAVERERAAtEELLANKIQMSSVESQNALLRQENSRL 845
Cdd:PRK03918 325 GIEE-RIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEEL-ERLKKRLTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 846 QAQLESEK--NKLRKLEDENSRYQVELENLKDEYV------RTLEEARKEKTLLSSQLEMERmkVEQERKKTIFTQETLK 917
Cdd:PRK03918 402 EIEEEISKitARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTEEHRKELLEEYTAELKR--IEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 918 EKEHKPFSV-SSTPTMSRSSSLSgvdmaglqtSFLSQDESHDHSFGPMSTSASgSNLYEAVR-----MGAGSSIIENLQS 991
Cdd:PRK03918 480 KELRELEKVlKKESELIKLKELA---------EQLKELEEKLKKYNLEELEKK-AEEYEKLKeklikLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186663 992 QLKLREGEISHLQLEISNLEKTRSIMSEELVKLTNQN-DELEEKVKEIPKLR---VQLRDLDQRYNTILQMYGEKAEEAE 1067
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYneyLELKDAEKELEREEKELKKLEEELD 629
|
490 500
....*....|....*....|....*
gi 158186663 1068 ELRLDLEDVKN---MYKTQIDELLR 1089
Cdd:PRK03918 630 KAFEELAETEKrleELRKELEELEK 654
|
|
| |
