|
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 ... |
975-1089 |
2.92e-31 |
|
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: 118.42 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 975 LYDAVRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRY 1054
Cdd:pfam12325 1 SVSTSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRY 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1622908228 1055 NTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1089
Cdd:pfam12325 81 ETTLELLGEKSEEVEELKADVEDLKEMYREQVQQL 115
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
544-617 |
5.06e-16 |
|
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: 73.49 E-value: 5.06e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622908228 544 SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKE 617
Cdd:pfam12329 1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-803 |
6.47e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 464 EAQLLSLSKEKALLEEaYDNLKDEMFRVKEESSSISslKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELAT-RLN 542
Cdd:COG1196 199 ERQLEPLERQAEKAER-YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEElRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 543 SSETADLLKEKDEQIRGLMEEGEKLSKQQLHNsniikKLRAKDKENENmvaklnkkvKELEEELQHLKQVLDGKEEVEKQ 622
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARL-----EERRRELEERL---------EELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 623 HRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELtdLHKANAAKDSEAQEAALSREMKAKEELSAAL 702
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 703 EKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSS--TTRPLLRQIENL 780
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEElaEAAARLLLLLEA 499
|
330 340
....*....|....*....|...
gi 1622908228 781 QATLGSQTSSWEKLEKNLSDRLG 803
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-754 |
1.48e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.03 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 535
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ELATRLNS-SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLD 614
Cdd:TIGR02168 762 EIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 615 GKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEA--ALSREM 692
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrrELEELR 921
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622908228 693 KAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQE 754
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
456-742 |
2.42e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 535
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ELAtrlnssetadllkEKDEQIRGLMEEGEKLSKQQlhnsniiKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDG 615
Cdd:COG1196 324 ELA-------------ELEEELEELEEELEELEEEL-------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 616 KEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKanAAKDSEAQEAALSREMKAK 695
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622908228 696 EELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLR 742
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
461-924 |
4.94e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 461 EKREAQLLSLSKEKALLEEAYDNL--KDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEEL- 537
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAe 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 538 ATRLNSSET---ADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENE-NMVAKLNKKVKELEEELQHLKQVL 613
Cdd:PTZ00121 1368 AAEKKKEEAkkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 614 DGKEEVEKQHR-ENIKKLNSVVERQE--KDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSE----AQEA 686
Cdd:PTZ00121 1448 EAKKKAEEAKKaEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkADEA 1527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 687 ALSREMKAKEELSAALEKAQEEARQQQEtlaiqvgDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSV 766
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 767 SSTTRPL----LRQIEnlQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLlRQ 842
Cdd:PTZ00121 1601 YEEEKKMkaeeAKKAE--EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK-KA 1677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 843 ENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAiftQEAIKEKE 922
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA---EEAKKDEE 1754
|
..
gi 1622908228 923 RK 924
Cdd:PTZ00121 1755 EK 1756
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
454-1093 |
2.36e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 454 EFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNI 533
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 534 KEELATRLNSS-ETADLLKEKDEQIRGLMEEgeklskqqlhnsniIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQV 612
Cdd:TIGR02168 322 EAQLEELESKLdELAEELAELEEKLEELKEE--------------LESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 613 LDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREM 692
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 693 KAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylRHEISELQQRLQEAENRNQELSQSVS----- 767
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSELISVDEGYEAAIEaalgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 768 ------------------------------------------STTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLG-- 803
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflkqnelgrvtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 804 -------ESQTLLAAAVERERAATEE-LLANK---IQMSSMESQNSLL--RQENSRFQAQLESEKNRLCKLEDENNRYQV 870
Cdd:TIGR02168 626 lvvddldNALELAKKLRPGYRIVTLDgDLVRPggvITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 871 ELENLKDEYV---RTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKEKERKPFSVSSTPTMSRSSSISGVD--- 944
Cdd:TIGR02168 706 ELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeie 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 945 -----MAGLQTSFLSQDESHDhsfgpmSVSANGSNLYDAV------------RMGAGSSIIENLQSQLKLREGEITHLQL 1007
Cdd:TIGR02168 786 eleaqIEQLKEELKALREALD------ELRAELTLLNEEAanlrerleslerRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 1008 EIGNLEKTRSIMAEELVKLTN---------------------QNDELEEKVKEI----PKLRTQLRDLDQRYNTILQMYG 1062
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNerasleealallrseleelseELRELESKRSELrrelEELREKLAQLELRLEGLEVRID 939
|
730 740 750
....*....|....*....|....*....|..
gi 1622908228 1063 EKAEE-AEELRLDLEDVKNMYKTQIDELLRQR 1093
Cdd:TIGR02168 940 NLQERlSEEYSLTLEEAEALENKIEDDEEEAR 971
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
624-924 |
6.43e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 624 RENIKKLNSVVERQEKDLGRLQVDMD------ELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEE 697
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 698 LSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAaRKEDYLRHEISELQQRLQEAENRNQELSQSVSSttrpLLRQI 777
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEEELEE----LEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 778 ENLQATLGSQTSSWEKLEKNLSdrlgESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNR 857
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 858 LCKLEDENNRYQ---VELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKEKERK 924
Cdd:COG1196 416 LERLEEELEELEealAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
457-924 |
6.82e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.13 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 457 NEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEE 536
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 537 latRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKD----------------------------KEN 588
Cdd:TIGR04523 196 ---LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEInektteisntqtqlnqlkdeqnkikkqlSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 589 ENMVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHRENI-KKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYK 667
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEI---SDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 668 ELTDLHKANAAKDseaqeaalsREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEISE 747
Cdd:TIGR04523 350 ELTNSESENSEKQ---------RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE----QIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 748 LQQRLQEAENRNQELSQSVS---STTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLlaaaVERERAATEELL 824
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI----KQNLEQKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 825 ANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRK---EKTLLNSQLEMER 901
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKEIDEKNKEIEE 572
|
490 500
....*....|....*....|....*
gi 1622908228 902 MKVEQERKKAIFT--QEAIKEKERK 924
Cdd:TIGR04523 573 LKQTQKSLKKKQEekQELIDQKEKE 597
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
454-898 |
4.10e-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: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 454 EFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNI 533
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 534 KEELATRLNS-SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQV 612
Cdd:COG1196 385 AEELLEALRAaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 613 LDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREM 692
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 693 KA--------------------KEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRL 752
Cdd:COG1196 545 AAalqnivveddevaaaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 753 QEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSS 832
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622908228 833 MESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVR-------TLEETRKEKTLLNSQLE 898
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
586-898 |
1.08e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 586 KENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALdsa 665
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL--- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 666 yKELTDLHKANAAKDSEAQEAALSREMKaKEELSAALEKAQEEARQQQETLAIQVGDLRLaLQRTEQAAARKEDYLRHEI 745
Cdd:TIGR02168 757 -TELEAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 746 SELQQRLQEAENRNQELSQsvssttrpllrQIENLQATLGSQTSSWEKLEKNL---SDRLGESQTLLAAAVERERAATEE 822
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSE-----------DIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 823 LLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDE-NNRYQVELENLKDEYVRT---LEETRKEKTLLNSQLE 898
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIeddEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
523-878 |
1.37e-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: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 523 RDAAKKEIKNIKEELaTRLNssetaDLLKEKDEQIRGLMEEGEKLSKQQlhnsniikKLRAKDKENENMVAKLnkKVKEL 602
Cdd:COG1196 174 KEEAERKLEATEENL-ERLE-----DILGELERQLEPLERQAEKAERYR--------ELKEELKELEAELLLL--KLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 603 EEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTdlHKANAAKDSE 682
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA--RLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 683 AQEAALSREMKAKEElsaalEKAQEEarQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQEL 762
Cdd:COG1196 316 ERLEELEEELAELEE-----ELEELE--EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 763 SQSVSSTTRpLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQ 842
Cdd:COG1196 389 LEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622908228 843 ENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDE 878
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
509-808 |
2.78e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 509 IAEAEKKVQLACKERDAAKK--EIKNIKEELATRLnsseTADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDK 586
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERykELKAELRELELAL----LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 587 ENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAY 666
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 667 KELTDLHKANAAKdsEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARkedyLRHEIS 746
Cdd:TIGR02168 351 EELESLEAELEEL--EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622908228 747 ELQQRLQEAEnrNQELSQSVSSTTRPLLRQI---ENLQATLGSQTSSWEKLEKNLSDRLGESQTL 808
Cdd:TIGR02168 425 ELLKKLEEAE--LKELQAELEELEEELEELQeelERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
416-766 |
3.48e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 416 INEGHTVLDRVAEQCEPAESQPEALSEKEDVcKVTLtvefLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEES 495
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREY-EGYE----LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 496 SSISSLKDEFTQRIAEaekkvqLACKERDAAKKEIKNIKEELA-TRLNSSETADLLKEKDEQIRGLMEEgekLSKQQLHN 574
Cdd:TIGR02169 268 EEIEQLLEELNKKIKD------LGEEEQLRVKEKIGELEAEIAsLERSIAEKERELEDAEERLAKLEAE---IDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 575 SNIIKKLRAKDKEnenmVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHRENIKKLNSVVERQEKdlgrLQVDMDELEEK 654
Cdd:TIGR02169 339 EELEREIEEERKR----RDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEK----LKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 655 NRSIQAALDSAYKELTDLHkaNAAKDSEAQEAALSREMKAKEElsaalekAQEEARQQQETLAIQVGDLRLALQRTEQAA 734
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLN--AAIAGIEAKINELEEEKEDKAL-------EIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350
....*....|....*....|....*....|..
gi 1622908228 735 ARKEDylrhEISELQQRLQEAENRNQELSQSV 766
Cdd:TIGR02169 479 DRVEK----ELSKLQRELAEAEAQARASEERV 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
367-924 |
5.39e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 367 KTVESAEGKSEEVNETLVIPTEEAEMEESGRSATPVNCEQ---PDILVSSTPINEGHTVldRVAEQCEPAESQPEALSEK 443
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarkADELKKAEEKKKADEA--KKAEEKKKADEAKKKAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 444 EDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKER 523
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 524 DAAKK--EIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKE 601
Cdd:PTZ00121 1395 EAKKKaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 602 LEEELQHLKQVLDGK---EEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDEL---EEKNRSIQAALDSAYKELTDLHKA 675
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKKADELKKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 676 NAAKDSEAQEAAlSREMKAKEELSAALEKAqEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEA 755
Cdd:PTZ00121 1555 EELKKAEEKKKA-EEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 756 ENRNQELSQSVSSTTRP-LLRQIENLQATLGSQTSSWEKLEKNLSDRLGESqtllaaavereraatEELLANKIQMSSME 834
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---------------EEDEKKAAEALKKE 1697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 835 SQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKE----KTLLNSQLEMERMKVEQERKK 910
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekKKIAHLKKEEEKKAEEIRKEK 1777
|
570
....*....|....
gi 1622908228 911 AIFTQEAIKEKERK 924
Cdd:PTZ00121 1778 EAVIEEELDEEDEK 1791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
528-1089 |
1.02e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 528 KEIKNIKEELATRLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKDKENENMVAKLNKKVKELEEEL 606
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDkNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 607 QHLKQVLDGKE----EVEKQHREN---IKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANA-A 678
Cdd:TIGR04523 113 KNDKEQKNKLEvelnKLEKQKKENkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDkI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 679 KDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENR 758
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 759 NQELSQSVS--STTRPLLRQIENLQATLGSQTSswEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQ 836
Cdd:TIGR04523 273 QKELEQNNKkiKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 837 NSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEyVRTLEETRKEKTLLNSQLEMERMKVEQERKKaiftqe 916
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKEL------ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 917 aiKEKERKPFSVSSTPTMSRSSSISGVDmaglqTSFLSQDESHDhsfgpmsvsangsnlydavrmgagsSIIENLQSQLK 996
Cdd:TIGR04523 424 --LEKEIERLKETIIKNNSEIKDLTNQD-----SVKELIIKNLD-------------------------NTRESLETQLK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 997 LREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVK----EIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELR 1072
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdltkKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
570
....*....|....*..
gi 1622908228 1073 LDLEdvKNMYKTQIDEL 1089
Cdd:TIGR04523 552 FELK--KENLEKEIDEK 566
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
547-924 |
1.58e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 547 ADLLKEKDEQIRGLMEEGEKlskqqlhnsniIKKLRAKDKENEnmvaklnkkvKELEEELQHLKQVLDGKEEVEKQhren 626
Cdd:TIGR02168 147 SEIIEAKPEERRAIFEEAAG-----------ISKYKERRKETE----------RKLERTRENLDRLEDILNELERQ---- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 627 IKKLnsvvERQEKDLGRLQVDMDELEEKNRSIQAA-LDSAYKELTDLhkANAAKDSEAQEAALSREMKAKEELSAALEKA 705
Cdd:TIGR02168 202 LKSL----ERQAEKAERYKELKAELRELELALLVLrLEELREELEEL--QEELKEAEEELEELTAELQELEEKLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 706 QEEARQQQETLAIQVGDLRLALQRTE---QAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSStTRPLLRQIENLQA 782
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELESKLDELAEELAE-LEEKLEELKEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 783 TLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLckle 862
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL---- 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622908228 863 dennryqveLENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKEKERK 924
Cdd:TIGR02168 431 ---------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
437-930 |
1.69e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 437 PEALSEKEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKV 516
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 517 QLAcKERDAAKKEIKNIKEELATrlnssetadlLKEKDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKDKENENMVAKLN 596
Cdd:PRK03918 297 KLS-EFYEEYLDELREIEKRLSR----------LEEEINGIEERIKELEEKEER-------LEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 597 KKVKELEE------ELQHLKQVLDGK--EEVEKQHrENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAY-- 666
Cdd:PRK03918 359 ERHELYEEakakkeELERLKKRLTGLtpEKLEKEL-EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 667 -----KELTDLHKANAAKDSEAQeaaLSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLaLQRTEQAAARKEDYL 741
Cdd:PRK03918 438 cpvcgRELTEEHRKELLEEYTAE---LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 742 RHEISELQQRLQEAENRNQELSQsVSSTTRPLLRQIENLQAtLGSQTSSWEKLEKNLSDRLGEsqtlLAAAVERERAATE 821
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIK-LKGEIKSLKKELEKLEE-LKKKLAELEKKLDELEEELAE----LLKELEELGFESV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 822 ELLANKIQmssmesqnsllrqensrfqaQLESEKNRLCKLEDENNRYQVELENLKDEYvRTLEETRKEKTLLNSQLEMER 901
Cdd:PRK03918 588 EELEERLK--------------------ELEPFYNEYLELKDAEKELEREEKELKKLE-EELDKAFEELAETEKRLEELR 646
|
490 500
....*....|....*....|....*....
gi 1622908228 902 MKVEQERKKaiFTQEAIKEKERKPFSVSS 930
Cdd:PRK03918 647 KELEELEKK--YSEEEYEELREEYLELSR 673
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
675-911 |
2.49e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 675 ANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEISELQQRLQE 754
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 755 AENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLsdrlgesqTLLAAAVERERAATEELLANKIQMSSME 834
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--------QYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622908228 835 SQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKA 911
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
458-924 |
2.58e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 458 EKLEKREAQLLSLSKEKAL---LEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLAcKERDAAKKEIKNIK 534
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 535 EELATRLNSSETADLLKEKDEQIRGLM--EEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQV 612
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 613 LDG----KEEVEKQHRENIKklnsvvERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAAL 688
Cdd:PRK03918 435 KGKcpvcGRELTEEHRKELL------EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 689 SREMKA--KEELsaalEKAQEEARQQQETLAIQVGDLRLALQRTEQAAArkedyLRHEISELQQRLQEAENRNQELSQSV 766
Cdd:PRK03918 509 EEKLKKynLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-----LKKKLAELEKKLDELEEELAELLKEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 767 SSTTRPLLRQIENLQATLGSQTSSWEKLeKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSr 846
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS- 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 847 fQAQLESEKNRLCKLEDENNRYQVELENLK---DEYVRTLEETRKEKTllnsqlEMERMKVEQER-KKAIFTQEAIKEKE 922
Cdd:PRK03918 658 -EEEYEELREEYLELSRELAGLRAELEELEkrrEEIKKTLEKLKEELE------EREKAKKELEKlEKALERVEELREKV 730
|
..
gi 1622908228 923 RK 924
Cdd:PRK03918 731 KK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
580-924 |
3.52e-10 |
|
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: 64.32 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 580 KLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQvdmdELEEKNRSIQ 659
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 660 AALDSAYKELTDLhkanaAKDSEAQEAALSREMKAKEELSAAL-----EKAQEEARQQQETLAIQVGDLRlALQRTEQAA 734
Cdd:TIGR02169 751 QEIENVKSELKEL-----EARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLR-EIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 735 ARKEDYLRHEISELQQRLQEAENRNQELSQsvssttrpllrQIENLQATLGSQTSSWEKLEKNLSDRLGEsqtlLAAAVE 814
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEAALRDLESR----LGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 815 RERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEyvRTLEETRKEKTLLN 894
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL--EDVQAELQRVEEEI 967
|
330 340 350
....*....|....*....|....*....|
gi 1622908228 895 SQLEMERMKVEQERKKAIFTQEAIKEKERK 924
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
456-689 |
2.36e-09 |
|
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: 60.55 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 535
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ELATRL-----NSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKEnenmvakLNKKVKELEEELQHLK 610
Cdd:COG4942 105 ELAELLralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622908228 611 QVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALS 689
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
555-768 |
1.09e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 555 EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVV 634
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 635 ERQEKDLGRLQVDMDELEEKNRSI----QAALDSAYKELTDLHKANAAKDSEAQEaalsreMKAKEELSAALEKAQEEAR 710
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEE------LRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 711 QQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSS 768
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
476-1069 |
1.75e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 476 LLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDA-------AKKEIKNIKEELATRLNSSETAD 548
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAmadirrrESQSQEDLRNQLQNTVHELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 549 LLKEkdEQIRGLMEEGEKLSKQQLHNSNIIKKLRA-----------KDKENENMV--------AKLNKKVKELEEELQHL 609
Cdd:pfam15921 159 CLKE--DMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasgkKIYEHDSMStmhfrslgSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 610 K-QVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRL----QVDMDELEEKNRSIQAALDSAYKELTDLHkanaaKDSEAQ 684
Cdd:pfam15921 237 KgRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQ-----EQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 685 EAALSREMKAKEELSAALEKAQEEARQQQETlAIQVGDLRLALQRTEQAAARKE-DYLRHEI----SELQQRLQEAENRN 759
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYED-KIEELEKQLVLANSELTEARTErDQFSQESgnldDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 760 QELSQSVSSTTRPLLRQIENlqatlgsqTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELlanKIQMSSMESQNSL 839
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGN--------SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM---ERQMAAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 840 LRQENSrFQAQLESEKNRLCKLEDENNRYQVELENLK----------DEYVRTLEETRKEKTLLNSQLEMERMKVEQERK 909
Cdd:pfam15921 460 LEKVSS-LTAQLESTKEMLRKVVEELTAKKMTLESSErtvsdltaslQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 910 KAIFTQEAIKEKERKPFSVSSTPTMsrsssisgVDMAGLQTSFLSQ-DESHDHSFGPMSVS-ANGSNLYDAVRMGAGSSI 987
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKV--------IEILRQQIENMTQlVGQHGRTAGAMQVEkAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 988 IENLQSQLKLREGEITHLQLEignLEKTRSIMA--EELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKA 1065
Cdd:pfam15921 611 ILKDKKDAKIRELEARVSDLE---LEKVKLVNAgsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
....
gi 1622908228 1066 EEAE 1069
Cdd:pfam15921 688 EEME 691
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
458-1093 |
2.52e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.31 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 458 EKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISS-LKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEE 536
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 537 LaTRLNSS---------ETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKklRAKDKENENMVAKLNKKVKELEEELQ 607
Cdd:pfam12128 324 L-EALEDQhgafldadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVT--AKYNRRRSKIKEQNNRDIAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 608 HLKqvldgkEEVEKQHREnikkLNSVVERQEKDLgrlqvdMDELEEKNRSIQaalDSAYKELTDLHKANAAKDSEAQEAA 687
Cdd:pfam12128 401 KIR------EARDRQLAV----AEDDLQALESEL------REQLEAGKLEFN---EEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 688 LSREMKAKEELSAALEKAQEEARQQQEtlaiqvgdlrlALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVS 767
Cdd:pfam12128 462 LLLQLENFDERIERAREEQEAANAEVE-----------RLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 768 STTRPLLrqienlqATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATE------ELLANKIQMSSMESQNSLLR 841
Cdd:pfam12128 531 PQAGTLL-------HFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDVPEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 842 QENSRFQAQLESEKNRLCKLEDENNRYQVELENLKdeyvrtLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAikeK 921
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS------REETFARTALKNARLDLRRLFDEKQSEKDKKNKAL---A 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 922 ERKPFSVSSTPTMSRSSSISGVDMAGLQTSFlsQDESHDHSfgpMSVSANGSNLYDA--VRMGAGSSIIENLQSQLKlre 999
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQ--KEQKREAR---TEKQAYWQVVEGAldAQLALLKAAIAARRSGAK--- 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 1000 GEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYN-TILQMYGEKAEEAEELRLDLEDV 1078
Cdd:pfam12128 747 AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIERAISEL 826
|
650
....*....|....*
gi 1622908228 1079 KNMYKTQIDELLRQR 1093
Cdd:pfam12128 827 QQQLARLIADTKLRR 841
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
589-784 |
3.24e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 589 ENMVAKLNKKVKELEEELQHLKQ---VLDGKEEvEKQHRENIKKLNSvverqekDLGRLQVDMDELEEKNRSIQAALDSA 665
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQkngLVDLSEE-AKLLLQQLSELES-------QLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 666 YKELTDLHKANAAKDSEAQEAALSREMkakEELSA-------ALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKE 738
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAEL---AELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622908228 739 DYLRHEISELQQRLQEAENRNQELSQsvssttrpLLRQIENLQATL 784
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRR--------LEREVEVARELY 367
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
522-915 |
3.36e-08 |
|
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: 58.14 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 522 ERDAAKKEIKNIKEELATRLNSSETadlLKEKDE----QIRGLMEEGEKLSKQQLHNSNIikklRAKDKENENMVAKLNK 597
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEE---IKKKSEnyidEIKAQINDLEDVADKAISNDDP----EEIEKKIENIVTKIDK 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 598 KvKELEEELqhlKQVLDGKEEVEKQhRENIKKLNSVVERQEKDLGRLQVD-MDELEEKNRSIQAALDSAYKELTDLHKAN 676
Cdd:TIGR01612 1185 K-KNIYDEI---KKLLNEIAEIEKD-KTSLEEVKGINLSYGKNLGKLFLEkIDEEKKKSEHMIKAMEAYIEDLDEIKEKS 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 677 AAKDSE-AQEAALSREMKAKEELSAALEKAQEEARQQQETLAiqvgDLRLALQRTEQAAARKEDyLRHEISELQQRLQEA 755
Cdd:TIGR01612 1260 PEIENEmGIEMDIKAEMETFNISHDDDKDHHIISKKHDENIS----DIREKSLKIIEDFSEESD-INDIKKELQKNLLDA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 756 ENRNQELSQSVSSTTRPL----LRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAAT-----EELLAN 826
Cdd:TIGR01612 1335 QKHNSDINLYLNEIANIYnilkLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEEckskiESTLDD 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 827 K-----IQmSSMESQNSLLRQE---NSRFQAQLESEKNRLC---KLEDENNRYQVELENLKD----EYVRTLEETRKEKT 891
Cdd:TIGR01612 1415 KdidecIK-KIKELKNHILSEEsniDTYFKNADENNENVLLlfkNIEMADNKSQHILKIKKDnatnDHDFNINELKEHID 1493
|
410 420
....*....|....*....|....*
gi 1622908228 892 LLNS-QLEMERMKVEQERKKAIFTQ 915
Cdd:TIGR01612 1494 KSKGcKDEADKNAKAIEKNKELFEQ 1518
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
424-802 |
4.21e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 424 DRVAEQCEPAESQPEALSEKEDVCKVTLtvEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKD 503
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESEL--EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 504 EFTQRIAEAEKKVQLACKERDAAKKEIKNIK-EELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLr 582
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKcPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA- 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 583 akdkenenmvaklnKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAAL 662
Cdd:PRK02224 502 --------------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 663 DSAYKELTDLHKANAAKDSEAQEAALSREMKAK-EELSAALEKAQEEARQQQEtlaiqvgdlrLALQRTEQAAARKE--D 739
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLAAiADAEDEIERLREKREALAE----------LNDERRERLAEKRErkR 637
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 740 YLRHE-----ISELQQRLQEAEnrnqELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEkNLSDRL 802
Cdd:PRK02224 638 ELEAEfdearIEEAREDKERAE----EYLEQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERR 700
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
474-919 |
6.09e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 474 KALLEEAYDNLKDEMFRVKEESSSISSLK-DEFTQRIAEAEKKVQlACKERDAAKKEIKNIKEELATRLNSSETADLLKE 552
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 553 KDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHRENIKKLNS 632
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL---EQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 633 VVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSremkAKEELSAALEKAQEEARQQ 712
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA----ALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 713 QETLAIQVG-----DLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVS-STTRPLLRQIENLQATLgs 786
Cdd:COG4717 276 AGVLFLVLGllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELL-- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 787 qtSSWEKLEKNLsdRLGESQTLLAAAVERERAATEELLANKIQMSSMESQnslLRQENSRFQAQLESEKNRLCKLEDENN 866
Cdd:COG4717 354 --REAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE---LKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622908228 867 RYQV--ELENLK---DEYVRTLEETRKEKTLLNSQLEM-------ERMKVEQERKKAIFTQEAIK 919
Cdd:COG4717 427 EEELeeELEELEeelEELEEELEELREELAELEAELEQleedgelAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
454-1089 |
7.29e-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: 57.00 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 454 EFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKV-QLACKERDAAKKEIKN 532
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeELNKKIKDLGEEEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 533 IKEELAtrlnsSETADLLKEKDeQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQV 612
Cdd:TIGR02169 292 VKEKIG-----ELEAEIASLER-SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 613 LDGK----EEVEKQHRENIKKLNSVVERQEKdlgrLQVDMDELEEKNRSIQAALDSAYKELTDLHkaNAAKDSEAQEAAL 688
Cdd:TIGR02169 366 LEDLraelEEVDKEFAETRDELKDYREKLEK----LKREINELKRELDRLQEELQRLSEELADLN--AAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 689 SREMKAKEElsaalekAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEISELQQRLQEAENRNQELSQSVSS 768
Cdd:TIGR02169 440 EEEKEDKAL-------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK----ELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 769 TTRPLLRQIENLQATLG--SQTSSWEK-----LEKNLSDRL----------------------GESQTLLAAAVERERAA 819
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGtvAQLGSVGEryataIEVAAGNRLnnvvveddavakeaiellkrrkAGRATFLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 820 TEELLANK---------------------------IQMSSMESQNSLL----------------------------RQEN 844
Cdd:TIGR02169 589 DLSILSEDgvigfavdlvefdpkyepafkyvfgdtLVVEDIEAARRLMgkyrmvtlegelfeksgamtggsraprgGILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 845 SRFQ-AQLESEKNRLCKLEDENNRYQVEL---ENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKE 920
Cdd:TIGR02169 669 SRSEpAELQRLRERLEGLKRELSSLQSELrriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 921 KERKpfsvsstptmsrsssisgvdmaglqtsflsqdeshdhsfgpmsvsangsnlydavrmgagssiIENLQSQLKLREG 1000
Cdd:TIGR02169 749 LEQE---------------------------------------------------------------IENVKSELKELEA 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 1001 EITHLQLEIGNLEKT-----RSIMAEELVKLTNQNDELEEKVKEIpklRTQLRDLDQRYN--TILQMYGEKA-EEAEELR 1072
Cdd:TIGR02169 766 RIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRI---EARLREIEQKLNrlTLEKEYLEKEiQELQEQR 842
|
730
....*....|....*..
gi 1622908228 1073 LDLEDVKNMYKTQIDEL 1089
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENL 859
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
465-701 |
8.26e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 465 AQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATrlNSS 544
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 545 ETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIkKLRAKD-KENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQH 623
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLAL-LLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 624 RENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKanAAKDSEAQEAALSREMKAKEELSAA 701
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--EAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
521-775 |
9.26e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 521 KERDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVK 600
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 601 ELEEELQHLKQVLdgKEEVEKQHRENIKKLNSVVERQEkDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhkanaakd 680
Cdd:COG4942 94 ELRAELEAQKEEL--AELLRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAEL-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 681 sEAQEAALSREMKAKEelsaALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQ 760
Cdd:COG4942 163 -AALRAELEAERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*
gi 1622908228 761 ELSQSVSSTTRPLLR 775
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
550-734 |
1.01e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 550 LKEKDEQIRGLMEEGEKLSKQQLHNsniiKKLRAKDkENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKK 629
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKE----ALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 630 LNSVVERQEKDLGRLQVDMDELEEKNRSIQAaldsayKELTDLHKANAAKDSEAQEAALSR-EMKAKEELSAALEKAQEE 708
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIE------EQLQELERISGLTAEEAKEILLEKvEEEARHEAAVLIKEIEEE 181
|
170 180
....*....|....*....|....*...
gi 1622908228 709 ARQQQETLAIQVgdLRLALQR--TEQAA 734
Cdd:PRK12704 182 AKEEADKKAKEI--LAQAIQRcaADHVA 207
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
438-924 |
1.32e-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: 55.95 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 438 EALSEKEDVCKVTL--TVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKK 515
Cdd:pfam01576 116 EAARQKLQLEKVTTeaKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEER 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 516 VqlackerdaaKKEIKNIKE-ELATRLNSSETADLlkekDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAK 594
Cdd:pfam01576 196 L----------KKEEKGRQElEKAKRKLEGESTDL----QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 595 LNKKVKELEEELQHLKQVLdgkeEVEKQHRENikklnsvVERQEKDLG-RLQVDMDELEEKNRSIQAALDSAYK---ELT 670
Cdd:pfam01576 262 ALKKIRELEAQISELQEDL----ESERAARNK-------AEKQRRDLGeELEALKTELEDTLDTTAAQQELRSKreqEVT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 671 DLHKA--NAAKDSEAQEAALS-REMKAKEELSAALEKAQ------EEARQQQETLAIQVGDLRLALQRTEQAAARKEDYL 741
Cdd:pfam01576 331 ELKKAleEETRSHEAQLQEMRqKHTQALEELTEQLEQAKrnkanlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 742 RHEISELQQRLQEAENRNQELSQSVSSttrpLLRQIENLQATLGSQTSSWEKLEKNLS---DRLGESQTLLAAAVERERA 818
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSK----LQSELESVSSLLNEAEGKNIKLSKDVSsleSQLQDTQELLQEETRQKLN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 819 ATEELLANKIQMSSM--------------ESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYV-RTL 883
Cdd:pfam01576 487 LSTRLRQLEDERNSLqeqleeeeeakrnvERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEeKAA 566
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1622908228 884 EETRKEKTLLNSQLEMERMKVEQERKKAIFTqeAIKEKERK 924
Cdd:pfam01576 567 AYDKLEKTKNRLQQELDDLLVDLDHQRQLVS--NLEKKQKK 605
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
588-758 |
2.86e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 588 NENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQ---------EKDLGRLQVDMDELEEKN--- 655
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 656 RSIQAALDSAYKELTDLHKANAAKDSEAqeAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAA 735
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEI--GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
170 180
....*....|....*....|...
gi 1622908228 736 RKEDYLRHEISELQQRLQEAENR 758
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEE 788
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
456-924 |
4.11e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDE-MFRVKEESSSISSLKDE-------FTQRIAEAEKKVQLACKE----- 522
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSMyMRQLSDLESTVSQLRSElreakrmYEDKIEELEKQLVLANSEltear 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 523 --RDAAKKEIKNIKEELATRLnssetADLLKeKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVK 600
Cdd:pfam15921 363 teRDQFSQESGNLDDQLQKLL-----ADLHK-REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 601 ELEEELQ---------------------HLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVdmdELEEKNRSIQ 659
Cdd:pfam15921 437 AMKSECQgqmerqmaaiqgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA---SLQEKERAIE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 660 AA----------LDSAYKELTDL-----HKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQET--------- 715
Cdd:pfam15921 514 ATnaeitklrsrVDLKLQELQHLknegdHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTagamqveka 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 716 -LAIQVGDLRLALQRTEQAAARKEDYLRheisELQQRLQEAENRNQELSQSVSSTTRP----------LLRQIENLQATL 784
Cdd:pfam15921 594 qLEKEINDRRLELQEFKILKDKKDAKIR----ELEARVSDLELEKVKLVNAGSERLRAvkdikqerdqLLNEVKTSRNEL 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 785 GSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDE 864
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 865 NNRYQVELENLKDEYVRTLEETRKektllnsqLEMERMKVEQERKKAIFTQEAIKEKERK 924
Cdd:pfam15921 750 IQFLEEAMTNANKEKHFLKEEKNK--------LSQELSTVATEKNKMAGELEVLRSQERR 801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
616-944 |
4.66e-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: 54.30 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 616 KEEVEkQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELtdLHKANAAKDS----EAQEAALSRE 691
Cdd:TIGR02169 176 LEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEL--LKEKEALERQkeaiERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 692 MKAKEELSAALEKAQEEARQQQETLAIQVGDL----RLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELS---Q 764
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeiD 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 765 SVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSD---RLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLR 841
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 842 QENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEyVRTLEETRKEktlLNSQLEMERMKVEQERKKAIFTQEAIKEK 921
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQ---LAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340
....*....|....*....|...
gi 1622908228 922 ERKPFSVSSTPTMSRSSSISGVD 944
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
422-882 |
5.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 422 VLDRVAEQCEPAESQPEALSEKEDvCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSL 501
Cdd:COG4913 253 LLEPIRELAERYAAARERLAELEY-LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 502 KDEF-TQRIAEAEKKVQLACKERDAAKKEIKNIKEELAT-RLNSSETADLLKEKDEQIRGLMEEGEKLSKQqlhnsniik 579
Cdd:COG4913 332 IRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAEEFAALRAEAAALLEALEEELEA--------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 580 kLRAKDKENENMVAKLNKKVKELEEELQHLK-----------------------------------QVLDGKEE------ 618
Cdd:COG4913 403 -LEEALAEAEAALRDLRRELRELEAEIASLErrksniparllalrdalaealgldeaelpfvgeliEVRPEEERwrgaie 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 619 -----------VEKQH-RENIKKLNSV----------VERQEKDLGRLQVDMD----ELEEKNRSIQAALDSAYKELTDL 672
Cdd:COG4913 482 rvlggfaltllVPPEHyAAALRWVNRLhlrgrlvyerVRTGLPDPERPRLDPDslagKLDFKPHPFRAWLEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 673 HKANAAK--------------------------------------DSEAQEAALSREMKAKEELSAALEKAQEEARQQQE 714
Cdd:COG4913 562 VCVDSPEelrrhpraitragqvkgngtrhekddrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 715 TLAiqvgDLRLALQRTEQAAARKED--YLRHEISELQQRLQEAENRNQELSQsvssttrpLLRQIENLQATLGSQTSSWE 792
Cdd:COG4913 642 ALQ----ERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLAA--------LEEQLEELEAELEELEEELD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 793 KLE----------KNLSDRLGESQTLLAAAVERERAATEELLANKIqmssmesQNSLLRQENSRFQAQLEsekNRLCKLE 862
Cdd:COG4913 710 ELKgeigrlekelEQAEEELDELQDRLEAAEDLARLELRALLEERF-------AAALGDAVERELRENLE---ERIDALR 779
|
570 580
....*....|....*....|
gi 1622908228 863 DENNRYQVELENLKDEYVRT 882
Cdd:COG4913 780 ARLNRAEEELERAMRAFNRE 799
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
456-682 |
1.11e-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: 52.72 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 535
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 EL-ATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLD 614
Cdd:TIGR04523 392 QInDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 615 GKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSE 682
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
651-893 |
1.67e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 651 LEEknRSIQAALDSAYKELTDLHKA-NAAKDSEAQEAALSREMKAKEELSAALEKAqEEARQQQETLAIQVGDLRLALQR 729
Cdd:COG4913 218 LEE--PDTFEAADALVEHFDDLERAhEALEDAREQIELLEPIRELAERYAAARERL-AELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 730 TEQAAARKE-DYLRHEISELQQRLQEAENRNQELSQSVSS----TTRPLLRQIENLQATLGSQTSSWEKLEKNLsDRLGE 804
Cdd:COG4913 295 AELEELRAElARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALL-AALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 805 SQTLlaaavereraaTEELLANkiqmssmesqnslLRQENSRFQAQLESEKNRLckledENNRYQ--VELENLKDEyvrt 882
Cdd:COG4913 374 PLPA-----------SAEEFAA-------------LRAEAAALLEALEEELEAL-----EEALAEaeAALRDLRRE---- 420
|
250
....*....|.
gi 1622908228 883 LEETRKEKTLL 893
Cdd:COG4913 421 LRELEAEIASL 431
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
579-925 |
1.68e-06 |
|
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: 52.28 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 579 KKLRAKDKENENMVAKLNKKvkeLEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSI 658
Cdd:pfam02463 173 EALKKLIEETENLAELIIDL---EELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 659 QAALDSAYKELTDLHKANAAKDSEAQEAalSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKE 738
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEE--EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 739 DYL---RHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRlgeSQTLLAAAVER 815
Cdd:pfam02463 328 KELkkeKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK---EEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 816 ERAATEELLANKIQMSSMESQNSLLRQENSrfqAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTlLNS 895
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEE---EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET-QLV 480
|
330 340 350
....*....|....*....|....*....|
gi 1622908228 896 QLEMERMKVEQERKKAIFTQEAIKEKERKP 925
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
416-1081 |
1.79e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 416 INEGHTVLDRVAEQCEPaESQPEALSEKEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEES 495
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 496 SSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRlnsSETADLLKEKDEQIRG----LMEEGEKLSKQQ 571
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKLKREINELKReldrLQEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 572 LHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDEL 651
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 652 EEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETL-AIQVGDL------R 724
Cdd:TIGR02169 503 EERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLkRRKAGRAtflplnK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 725 LALQRTEQAAARKEDYLRHEIS--ELQQRLQEAEN---RNQELSQSVSsTTRPLLRQIE--------------------N 779
Cdd:TIGR02169 583 MRDERRDLSILSEDGVIGFAVDlvEFDPKYEPAFKyvfGDTLVVEDIE-AARRLMGKYRmvtlegelfeksgamtggsrA 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 780 LQATLGSQTSSWEKLEKnLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLC 859
Cdd:TIGR02169 662 PRGGILFSRSEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 860 KLEDENNRYQVELENLKDEyVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQ-EAIKEKERKPFSVSSTPTMSRSS 938
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQ 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 939 SISGVDMAGLQTSFLSQDESHDHSFGPMSVSANGSNLYDA-VRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRS 1017
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622908228 1018 IMAEELVKLTNQNDELEEKVKEipkLRTQLRDLDQRYNTILQMYGEKAEEAEELrLDLEDVKNM 1081
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSE---LKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAE 959
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
699-924 |
2.00e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 699 SAALEKAQEEARQQQETLAIQVGDLRLALQRTEQaaarKEDYLRHEISELQQRLQEAENRNQELSQsvssttrpllrQIE 778
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRALEQ-----------ELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 779 NLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRL 858
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622908228 859 CKLEDEnnryQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKEKERK 924
Cdd:COG4942 160 AELAAL----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
423-732 |
2.12e-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: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 423 LDRVAEQCEPAESQPEALSEKEDVCKVTLT-VEFLNEKLEKREAQL-LSLSKEKALLEEAYDNLKDEMFR-VKEESSSIS 499
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIEnVKSELKELEARIEELeEDLHKLEEALNDLEARLSHSRIPeIQAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 500 SLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELatrlnssetaDLLKEKDEQIRglmeegeklskQQLHNSNIik 579
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR----------IDLKEQIKSIE-----------KEIENLNG-- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 580 KLRAKDKEnenmVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQ 659
Cdd:TIGR02169 862 KKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 660 AALD---SAYKELTDLHKANAAKdsEAQEAALSR----EMKAKEELSAAlEKAQEEARQQQETLAIQVGDLRLALQRTEQ 732
Cdd:TIGR02169 938 DPKGedeEIPEEELSLEDVQAEL--QRVEEEIRAlepvNMLAIQEYEEV-LKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
585-1071 |
3.00e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 585 DKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLnsvvERQEKDLGRLQVDMDELEEKNRSIQAALDs 664
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 665 AYKELTDLHKANAAKDSEAQEA-ALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRH 743
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 744 EISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENlqatlgsqtsswEKLEKNLSDRLGESQTLLAAAVERERAATEEL 823
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE------------ERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 824 LANKIQMSSmeSQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYvrTLEETRKEKTLLNSQLEMERMK 903
Cdd:COG4717 275 IAGVLFLVL--GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--GLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 904 VEQERKKAIFTQEAIKEKERKpfsvsstptmsrsssisgvdmagLQTSFLSQDESHDHSFGpmsvsangSNLYDAVRMGA 983
Cdd:COG4717 351 ELLREAEELEEELQLEELEQE-----------------------IAALLAEAGVEDEEELR--------AALEQAEEYQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 984 GSSIIENLQSQLKLREGEITHLqLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDL--DQRYNTILQMY 1061
Cdd:COG4717 400 LKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQEL 478
|
490
....*....|
gi 1622908228 1062 GEKAEEAEEL 1071
Cdd:COG4717 479 EELKAELREL 488
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
482-922 |
3.13e-06 |
|
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: 51.26 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 482 DNLKDEM-FRVKEESSSISSLKDEFTQRIAEAEKKVQL---ACKERDAAKKEIKNIKEELATRLNSSEtaDLLKEKDEQI 557
Cdd:pfam05483 207 ENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLlliQITEKENKMKDLTFLLEESRDKANQLE--EKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 558 RGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDgkeEVEKQHRENIKKLNSVVERQ 637
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 638 EKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSE--------AQEAALSREMKAKEELSAALEKAQEEA 709
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEleelkkilAEDEKLLDEKKQFEKIAEELKGKEQEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 710 RQQQETLAIQVGDLRLALQRTEQAaarkEDYLRHEISELQQRLQEAENRN--------------QELSQSVSSTTRPL-- 773
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTS----EEHYLKEVEDLKTELEKEKLKNieltahcdklllenKELTQEASDMTLELkk 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 774 ---------------LRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNS 838
Cdd:pfam05483 518 hqediinckkqeermLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 839 LLR--------------QENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEktLLNSQLEMERMKV 904
Cdd:pfam05483 598 NLKkqienknknieelhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE--IEDKKISEEKLLE 675
|
490
....*....|....*...
gi 1622908228 905 EQERKKAIFTQEAIKEKE 922
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKE 693
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
464-721 |
3.53e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 464 EAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNS 543
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 544 SETADLLKEKDEQIRG------LMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKE 617
Cdd:COG3883 95 LYRSGGSVSYLDVLLGsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 618 EVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEE 697
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250 260
....*....|....*....|....
gi 1622908228 698 LSAALEKAQEEARQQQETLAIQVG 721
Cdd:COG3883 255 AGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
425-712 |
3.69e-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: 51.21 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 425 RVAEQCEPAESQPEALSEKEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDE 504
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 505 FTQRIAEAEKKVQLACKERDAAKKEIKNIKEELatrlnssetADLLKEKDEQIRGLMEEGEKLSKQqlhnSNIIKKLRAK 584
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESEL---------EALLNERASLEEALALLRSELEEL----SEELRELESK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 585 DKENENMVAKLNKKVKELEEELQHLKQVLDgkeevekqhrENIKKLNSVVERQEKDLGRLQVDMDELEEKnrsIQAALDS 664
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRID----------NLQERLSEEYSLTLEEAEALENKIEDDEEE---ARRRLKR 976
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622908228 665 AYKELTDLHKANAAKDSEAQEAA-----LSREM----KAKEELSAALEKAQEEARQQ 712
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKerydfLTAQKedltEAKETLEEAIEEIDREARER 1033
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
472-1089 |
3.91e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 472 KEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLK 551
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 552 EKD-EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKdkeneNMVAKLNKKVKELEEELQHLK-QVLDGKEEVEKQHRENIKK 629
Cdd:pfam15921 183 EGVlQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKgRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 630 LNSVVERQEKDLGRL----QVDMDELEEKNRSIQAALDSAYKELTDLHKanaakDSEAQEAALSREMKAKEELSAALEKA 705
Cdd:pfam15921 258 IELLLQQHQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQE-----QARNQNSMYMRQLSDLESTVSQLRSE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 706 QEEARQQQETlAIQVGDLRLALQRTEQAAARKE-DYLRHEI----SELQQRLQEAENRNQELSQSVSSTTRPLLRQIENl 780
Cdd:pfam15921 333 LREAKRMYED-KIEELEKQLVLANSELTEARTErDQFSQESgnldDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGN- 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 781 qatlgsqTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELlanKIQMSSMESQNSLLRQENSrFQAQLESEKNRLCK 860
Cdd:pfam15921 411 -------SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM---ERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 861 LEDEnnryqvelenlkdeyvrtleetrkektllnsqLEMERMKVEQERKKAIFTQEAIKEKERKPFSVSSTPTMSRSSsi 940
Cdd:pfam15921 480 VVEE--------------------------------LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR-- 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 941 sgVDMAGLQTSFLSQDESHdhsfgpmsvSANGSNLYDAVR--MGAGSSIIENLQSQLKLREGEITH-------LQLEIGN 1011
Cdd:pfam15921 526 --VDLKLQELQHLKNEGDH---------LRNVQTECEALKlqMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQ 594
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 1012 LEKTRSIMAEELVKLTNQNDELEEKVKEipkLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1089
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRE---LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
693-924 |
4.99e-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: 50.84 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 693 KAKEELsaalekaqEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLrheisELQQRLQEAENrnQELSQSVSSttrp 772
Cdd:TIGR02169 174 KALEEL--------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-----ALLKEKREYEG--YELLKEKEA---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 773 LLRQIENLQATLGSQTSSWEKLEKNLSDRLGES----QTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQ 848
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLeeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 849 AQLESEKNRLCKLEDENNRYQVELENLKdeyvRTLEETRKEKTLLNSQ-------LEMERMKVEQERKKAIFTQEAIKEK 921
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELE----REIEEERKRRDKLTEEyaelkeeLEDLRAELEEVDKEFAETRDELKDY 390
|
...
gi 1622908228 922 ERK 924
Cdd:TIGR02169 391 REK 393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
593-767 |
7.20e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 593 AKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLnsvverqEKDLGRLQVDMDELEEKNRSIQAALDSA--YKELT 670
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 671 dlhkanaakdseaqeaALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQ 750
Cdd:COG1579 93 ----------------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*..
gi 1622908228 751 RLQEAENRNQELSQSVS 767
Cdd:COG1579 157 ELEELEAEREELAAKIP 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
578-792 |
7.47e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 578 IKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRS 657
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 658 IQAALDSayKELTD-LHKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAAR 736
Cdd:COG3883 105 LDVLLGS--ESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622908228 737 KEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWE 792
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
456-1094 |
9.77e-06 |
|
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: 49.97 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEmfRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 535
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKL--ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ELATRLNS-SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKkvkELEEELQHLKQVLD 614
Cdd:pfam02463 266 KLAQVLKEnKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK---ELKKEKEEIEELEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 615 GKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKanaakdseaqeaaLSREMKA 694
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-------------EEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 695 KEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLL 774
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 775 RQIENLQATLGSQTSSWEKLEKNLS-DRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQEnsrfQAQLES 853
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLAlIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE----VEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 854 EKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEqERKKAIFTQEAIKEKERKPFSVSSTPT 933
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE-DDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 934 MSRSSSISGVDMAGLQTSFLSQDESHDHSFGPMSVSANGSNLYDAVRMGAGSSIIEN-LQSQLKLREGEITHLQLEIGNL 1012
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIkKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 1013 EKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQ 1092
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
..
gi 1622908228 1093 RL 1094
Cdd:pfam02463 805 AL 806
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
558-809 |
1.66e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 558 RGLMEEGEKLSKQQLHNS-NIIKKLRAKDKENENMVAKLN---KKVKELEEELQHLKQVLDgkEEVEKQHR-ENIKKLNS 632
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAqapAKLRQAQAELEALKDDND--EETRETLStLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 633 VVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHK-----ANAAKDSEAQEAALSREMKAKEELSAALEKAQE 707
Cdd:PRK11281 129 RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQrlqqiRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 708 EARQQQETLAIQVGDLrLALQRTEQAAarKEDYLRHEISELQ-----QRLQEAENRNQELSQS---VSSTTRPLL-RQIE 778
Cdd:PRK11281 209 DLQRKSLEGNTQLQDL-LQKQRDYLTA--RIQRLEHQLQLLQeainsKRLTLSEKTVQEAQSQdeaARIQANPLVaQELE 285
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622908228 779 N--------LQATLGSQTSSWEKLE-KNLSDRLGESQTLL 809
Cdd:PRK11281 286 InlqlsqrlLKATEKLNTLTQQNLRvKNWLDRLTQSERNI 325
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
530-926 |
1.72e-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: 49.20 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 530 IKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHL 609
Cdd:pfam02463 604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 610 KQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDsaYKELTDLHKANAAKDSEAQEAALS 689
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE--LKLLKQKIDEEEEEEEKSRLKKEE 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 690 REMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSST 769
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 770 TRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQA 849
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 850 QLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQ------------------------LEMERMKVE 905
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAkeelgkvnlmaieefeekeerynkDELEKERLE 1001
|
410 420
....*....|....*....|.
gi 1622908228 906 QERKKAIFTQEAIKEKERKPF 926
Cdd:pfam02463 1002 EEKKKLIRAIIEETCQRLKEF 1022
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
448-639 |
1.89e-05 |
|
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: 48.86 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 448 KVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKV---------QL 518
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 519 ACKERDAAKKEIKNIKEELATRLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNK 597
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622908228 598 KVKELEEELQHLKQVLDG----KEEVEKQHRENIKKLNSVVERQEK 639
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEirnkWPEIIKKIKESKTKIDDIIELMKD 684
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
458-796 |
2.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 458 EKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLK-DEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEE 536
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 537 LATRLNSSETADLLKEKDEQ-----IRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQ 611
Cdd:COG4717 229 LEQLENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 612 VLDGKEEVEKQHRENIKKLNSVVERQEKDlgrlqvdmdELEEKNRSIQAaLDSAYKELTDLHKANAAKDSEAQEAALSRE 691
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPE---------ELLELLDRIEE-LQELLREAEELEEELQLEELEQEIAALLAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 692 MKAK--EELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSvsst 769
Cdd:COG4717 379 AGVEdeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE---- 454
|
330 340
....*....|....*....|....*..
gi 1622908228 770 trplLRQIENLQATLGSQTSSWEKLEK 796
Cdd:COG4717 455 ----LAELEAELEQLEEDGELAELLQE 477
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
533-614 |
2.87e-05 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 47.76 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 533 IKEELATRlNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENM---VAKLNKKVKELEEELQHL 609
Cdd:PRK05431 14 VKEALAKR-GFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALiaeVKELKEEIKALEAELDEL 92
|
....*
gi 1622908228 610 KQVLD 614
Cdd:PRK05431 93 EAELE 97
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
458-690 |
3.00e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 458 EKLEKREAQLLSLSKEKALLE-EAYDNLKDEMFRVKEEsssISSLKDEFtQRIAEAEKKVQLACKERDAAKKEIKNIKEE 536
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELEKKaEEYEKLKEKLIKLKGE---IKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 537 LATRLNSSEtaDLLKEKDEQIRGLMEEGEKL--SKQQLHNS-NIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVL 613
Cdd:PRK03918 579 LEELGFESV--EELEERLKELEPFYNEYLELkdAEKELEREeKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 614 DGKE---------EVEKQH---RENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQaALDSAYKELTDLHKANAAKDS 681
Cdd:PRK03918 657 SEEEyeelreeylELSRELaglRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKYKA 735
|
....*....
gi 1622908228 682 EAQEAALSR 690
Cdd:PRK03918 736 LLKERALSK 744
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
594-800 |
4.25e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 594 KLNK-KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVverQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL 672
Cdd:PHA02562 170 KLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKK---NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 673 hkanaAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQE-------TLAIQVGDLRLALQRTEQAAARKE-DYLRHE 744
Cdd:PHA02562 247 -----VMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSlEKLDTA 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 745 ISELQQRLQEA--------------ENRNQELSQSVSSTTRpLLRQIENLQATLGSQTSSWEKLEKNLSD 800
Cdd:PHA02562 322 IDELEEIMDEFneqskkllelknkiSTNKQSLITLVDKAKK-VKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
639-808 |
4.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 639 KDLGRLQVDMDELEEKnRSIQAALDSAYKELTDLHKANAAKDSEAQEAAL---SREMKAKEELSAALEKAQEEARQQQET 715
Cdd:COG4913 235 DDLERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLwfaQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 716 LAIQVGDLRLALQRTEQAAA----RKEDYLRHEISELQQRLQEAENRNQELSQ-------SVSSTTRPLLRQIENLQATL 784
Cdd:COG4913 314 LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAALRAEAAALL 393
|
170 180
....*....|....*....|....
gi 1622908228 785 GSQTSSWEKLEKNLSDRLGESQTL 808
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
523-761 |
4.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 523 RDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDK--ENENMVAKL---NK 597
Cdd:COG4913 612 LAALEAELAELEEELA------EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLdasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 598 KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAA-LDSAYKELTDlhKAN 676
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALG--DAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 677 AAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAiqvGDLRLALQRTEQAAARKEDYLRHEISELQQRLQEAE 756
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLESLPEYLALLDRLEEDGLPEYEERFKELL 840
|
....*
gi 1622908228 757 NRNQE 761
Cdd:COG4913 841 NENSI 845
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
423-794 |
5.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 423 LDRVAEQCEPAESQPEALSEKEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLK 502
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 503 DE------------------FTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQ-----IRG 559
Cdd:COG4717 177 EEleelleqlslateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArllllIAA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 560 LMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEK 639
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 640 DLGRLQVD-MDELEEKNRSI-----QAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKE------ELSAALEKAQE 707
Cdd:COG4717 337 EELLELLDrIEELQELLREAeeleeELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQElkeeleELEEQLEELLG 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 708 EARQQQETLAIQVGDLRLALQRTEQAAARKE-DYLRHEISELQQRLQEAENrNQELSQsvssttrpLLRQIENLQATLGS 786
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELEEElEELREELAELEAELEQLEE-DGELAE--------LLQELEELKAELRE 487
|
....*...
gi 1622908228 787 QTSSWEKL 794
Cdd:COG4717 488 LAEEWAAL 495
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
545-913 |
7.83e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 545 ETADLLKEKDEQIRGlMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEElqhlkqvlDGKEEVEKQHR 624
Cdd:pfam17380 297 EQERLRQEKEEKARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE--------ERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 625 ENIkklnSVVERQEKDLGRLQVdmdELEEKNRSIQAALDsaykeltdlhkanAAKDSEAQEAALSREMKAKEELSAALEK 704
Cdd:pfam17380 368 EEI----AMEISRMRELERLQM---ERQQKNERVRQELE-------------AARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 705 AQEEARQQQetlaiqvgdlrlaLQRTEQAAARKEDYLRHEISELQQRLQeaenrnqelsqsvssttrpLLRQIENLQatl 784
Cdd:pfam17380 428 EQEEARQRE-------------VRRLEEERAREMERVRLEEQERQQQVE-------------------RLRQQEEER--- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 785 gsqtssweKLEKNLSDRLGESQTLLAAAVERERAatEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRlcKLEDE 864
Cdd:pfam17380 473 --------KRKKLELEKEKRDRKRAEEQRRKILE--KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR--REAEE 540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622908228 865 NNRYQVELENLK--DEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIF 913
Cdd:pfam17380 541 ERRKQQEMEERRriQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
442-669 |
9.01e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 442 EKEDVCKVTLTVEFLNEKLEKREaQLLSLSKEKALLEEAY--DNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVqla 519
Cdd:COG5022 837 EVEFSLKAEVLIQKFGRSLKAKK-RFSLLKKETIYLQSAQrvELAERQLQELKIDVKSISSLKLVNLELESEIIELK--- 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 520 ckeRDAAKKEIKN--IKEELATRL-------NSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENEN 590
Cdd:COG5022 913 ---KSLSSDLIENleFKTELIARLkkllnniDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNK 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 591 MVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHREN--IKKLNSVVERQEKDLGRLQvDMDELEEKNRSIQAALDSAYKE 668
Cdd:COG5022 990 ANSELKNFKKELAELSKQYGALQESTKQLKELPVEVaeLQSASKIISSESTELSILK-PLQKLKGLLLLENNQLQARYKA 1068
|
.
gi 1622908228 669 L 669
Cdd:COG5022 1069 L 1069
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
456-611 |
9.62e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLAC--KERDAAKKEIKNI 533
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 534 KEELAtrlnssetadllkEKDEQIRGLMEEGEKLSKQQlhnSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQ 611
Cdd:COG1579 102 KRRIS-------------DLEDEILELMERIEELEEEL---AELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
586-920 |
1.32e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 586 KENENMVAKLNKKvKELEEELQHLKQVLDgkeevekQHRENIKKlnsvVERQEKDLGRLQVDMDELEEKNRSIQAaldsa 665
Cdd:PRK11281 39 ADVQAQLDALNKQ-KLLEAEDKLVQQDLE-------QTLALLDK----IDRQKEETEQLKQQLAQAPAKLRQAQA----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 666 ykELTDLhKANAAKDSEAQEAALSRemkakEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAArkedylrhEI 745
Cdd:PRK11281 102 --ELEAL-KDDNDEETRETLSTLSL-----RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQA--------AL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 746 SELQQRLQEAENR--NQELSQSVSSTTRPLLRQIEnlQATLGSQTSSWEKLEKN---LSDrLGESQTLLAAAVERERAAT 820
Cdd:PRK11281 166 YANSQRLQQIRNLlkGGKVGGKALRPSQRVLLQAE--QALLNAQNDLQRKSLEGntqLQD-LLQKQRDYLTARIQRLEHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 821 EELLANKIqmssmeSQNSLLRQENSRFQAQLESEKNRLckleDENNRYQVELE-NLK-DEYVrtLEETRKektlLNsQLE 898
Cdd:PRK11281 243 LQLLQEAI------NSKRLTLSEKTVQEAQSQDEAARI----QANPLVAQELEiNLQlSQRL--LKATEK----LN-TLT 305
|
330 340
....*....|....*....|..
gi 1622908228 899 MERMKVEQERKKAIFTQEAIKE 920
Cdd:PRK11281 306 QQNLRVKNWLDRLTQSERNIKE 327
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
433-1076 |
1.37e-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: 46.12 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 433 AESQPEALSEKEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEA 512
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 513 EKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIK-KLRAKDKENENM 591
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKeEELELKSEEEKE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 592 VAKLNKKVKELEEELQHLKQVLDGKEEVE------KQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSI------Q 659
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEeesielKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvklqeqL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 660 AALDSAYKELTDLHKANAAKDSEAQEAALSREMK------------AKEELSAALEKAQEEARQQQETLAIQVGDLRLAL 727
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriisahgrlgDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 728 QRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQT 807
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 808 LLAAAVERERAATEELLANKI-QMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEET 886
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASlSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 887 RKEKTLLNSQLEmermkVEQERKKAIFTQEAIKEKERKPFSVSStpTMSRSSSISGVDMAGLQTSFLSQDESHDHSFGPM 966
Cdd:pfam02463 727 VQEAQDKINEEL-----KLLKQKIDEEEEEEEKSRLKKEEKEEE--KSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 967 SVSANGSNLYDAVRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTrsimAEELVKLTNQNDELEEKVKEIPKLRTQ 1046
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEELERLEEEITKEELLQELLLK 875
|
650 660 670
....*....|....*....|....*....|
gi 1622908228 1047 LRDLDQRYNTILQMYGEKAEEAEELRLDLE 1076
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEE 905
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
576-722 |
1.40e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 576 NIIKKLRA---KDKEN-ENMVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHREnikklnsvVERQekdlgrlqvdMDEL 651
Cdd:PRK00409 502 NIIEEAKKligEDKEKlNELIASLEELERELEQKAEEAEALL---KEAEKLKEE--------LEEK----------KEKL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 652 EEKNRSIQAALDSAYKELTDLHKANAA---KDSEAQEAALSREMKAKE------ELSAALEKAQEEAR-QQQETLAIQVG 721
Cdd:PRK00409 561 QEEEDKLLEEAEKEAQQAIKEAKKEADeiiKELRQLQKGGYASVKAHEliearkRLNKANEKKEKKKKkQKEKQEELKVG 640
|
.
gi 1622908228 722 D 722
Cdd:PRK00409 641 D 641
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
421-910 |
1.56e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 421 TVLDRVAEQCEPAESQPEALSEKEDVCKVTLtvefLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISS 500
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLNG----LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 501 LK---DEFTQRIAEAEKkvqlackERDAAKKEIKNIKEELATRlnssetadllkekDEQIRGLMEEGEKLSkqqlhnsni 577
Cdd:PRK02224 256 LEaeiEDLRETIAETER-------EREELAEEVRDLRERLEEL-------------EEERDDLLAEAGLDD--------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 578 ikklrAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRS 657
Cdd:PRK02224 307 -----ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 658 IQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKE---------ELSAALEKAQEEARQQQETLAiqVGDLRLALQ 728
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREErdelrereaELEATLRTARERVEEAEALLE--AGKCPECGQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 729 RTEQA--AARKEDYlRHEISELQQRLQEAENRNQELSQSVSSTTRplLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQ 806
Cdd:PRK02224 460 PVEGSphVETIEED-RERVEELEAELEDLEEEVEEVEERLERAED--LVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 807 TLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRyQVELENLKDEYVRtLEET 886
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-LAAIADAEDEIER-LREK 614
|
490 500
....*....|....*....|....
gi 1622908228 887 RKEKTLLNSQlEMERMKVEQERKK 910
Cdd:PRK02224 615 REALAELNDE-RRERLAEKRERKR 637
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
484-710 |
1.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 484 LKDEMFRVKEESSSISSLKDEFT------QRIAEAEKKVQL------ACKERDAAKKEIkNIKEELATRLN---SSETAD 548
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHFDdlerahEALEDAREQIELlepireLAERYAAARERL-AELEYLRAALRlwfAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 549 LLKEK----DEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENmvaklnKKVKELEEELQHLKQVLDGKEEVEKQHR 624
Cdd:COG4913 292 LLEAEleelRAELARLEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 625 ENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKEL-TDLHKANAAKDSEAQE-AAL--------SREMKA 694
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeAALRDLRRELRELEAEiASLerrksnipARLLAL 445
|
250
....*....|....*.
gi 1622908228 695 KEELSAALEKAQEEAR 710
Cdd:COG4913 446 RDALAEALGLDEAELP 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
550-910 |
1.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 550 LKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELqhlkqvldgkEEVEKQHREnIKK 629
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL----------EKLEKEVKE-LEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 630 LNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhkanaaKDSEAQEAALSREMKAKEELSAALEKAQEEA 709
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 710 RQQQETLAI---QVGDLRLALQRTEQAAARKEDyLRHEISELQQRLQEAENRNQELsqsvsSTTRPLLRQIENLQATLGS 786
Cdd:PRK03918 310 REIEKRLSRleeEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEERHELY-----EEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 787 QTSswEKLEKnlsdrlgesqtLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRfqaqLESEKNR--LCKLE-D 863
Cdd:PRK03918 384 LTP--EKLEK-----------ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE----LKKAKGKcpVCGRElT 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622908228 864 ENNRyqvelENLKDEYVRTLEETRKEKTLLN---SQLEMERMKVEQERKK 910
Cdd:PRK03918 447 EEHR-----KELLEEYTAELKRIEKELKEIEekeRKLRKELRELEKVLKK 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
458-764 |
1.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 458 EKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDeftqrIAEAEKKVQLACKERDAAKKEIKNIKeel 537
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----YSWDEIDVASAEREIAELEAELERLD--- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 538 atrlnssETADLLKEKDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKdkenenmVAKLNKKVKELEEELQHLKQVLDGKE 617
Cdd:COG4913 682 -------ASSDDLAALEEQLEELEAELEELEEE-------LDELKGE-------IGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 618 EVEKQH-RENIKKL--NSVVERQEKDLGRlqvdmdELEEKNRSIQAALDSAYKELTDLHKA------NAAKDSEAQEAAL 688
Cdd:COG4913 741 DLARLElRALLEERfaAALGDAVERELRE------NLEERIDALRARLNRAEEELERAMRAfnrewpAETADLDADLESL 814
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 689 SREMKAKEELSA-ALEKAQEEARQQQETLAIQ-VGDLRLAlqrteqaaarkedyLRHEISELQQRLQEAenrNQELSQ 764
Cdd:COG4913 815 PEYLALLDRLEEdGLPEYEERFKELLNENSIEfVADLLSK--------------LRRAIREIKERIDPL---NDSLKR 875
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
443-921 |
1.84e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 443 KEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDE---FTQRIAEAEKKVQLA 519
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 520 CKERDaakkEIKNIKEELATRLNSSETA-------------------DLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKK 580
Cdd:PRK01156 269 LEKNN----YYKELEERHMKIINDPVYKnrnyindyfkykndienkkQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 581 LRAKDkenenmvaKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQA 660
Cdd:PRK01156 345 KSRYD--------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 661 ALDSAYKELTDLhkaNAAKDSEAQ-EAALSREMKAKEELSA----ALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAA 735
Cdd:PRK01156 417 KLQDISSKVSSL---NQRIRALREnLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 736 RKEDYLRHEISeLQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLsdrlgesqtllaaaver 815
Cdd:PRK01156 494 DIDEKIVDLKK-RKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY----------------- 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 816 ERAATEELLANKIQMSSMESQNSLLRQENSRfqAQLESEKNRLCKLEDENNRYQVELENLK----------DEYVRTLEE 885
Cdd:PRK01156 556 KSLKLEDLDSKRTSWLNALAVISLIDIETNR--SRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksireiENEANNLNN 633
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622908228 886 TRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKEK 921
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDL 669
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
487-924 |
2.04e-04 |
|
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: 45.58 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 487 EMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRL----NSSETADL---LKEKDEQI-- 557
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNqlqpDPAKTKALqtvIEMKDTKIss 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 558 -----RGLMEEGEKLSKQQLHNSNI----IKKL---RAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRE 625
Cdd:pfam10174 245 lerniRDLEDEVQMLKTNGLLHTEDreeeIKQMevyKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 626 NIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhkaNAAKDSEAQEAALSREM-KAKEELSAALEK 704
Cdd:pfam10174 325 HIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDL---TEEKSTLAGEIRDLKDMlDVKERKINVLQK 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 705 AQEEARQQQETLAIQVGDLR--------------LALQRTEQAAARKE---DYLRHEIS-ELQQRLQEAEN---RNQELS 763
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKervkslqtdssntdTALTTLEEALSEKEriiERLKEQRErEDRERLEELESlkkENKDLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 764 QSVSSTTRPLLRQ---IENLQATLGSQTSSWEK-----------LEKNLSDRLGESQTLLAAAVERERAATEELLANKIQ 829
Cdd:pfam10174 482 EKVSALQPELTEKessLIDLKEHASSLASSGLKkdsklksleiaVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIR 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 830 msSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERK 909
Cdd:pfam10174 562 --LLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLE 639
|
490
....*....|....*
gi 1622908228 910 KAIFTQEAIKEKERK 924
Cdd:pfam10174 640 EARRREDNLADNSQQ 654
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
491-755 |
2.65e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 491 VKEEsssISSLKDEFTQRIAEAEKKVQLACkERDAAKKEIKNIKEELATRLNSsetadlLKEKDEQIRGLMEEGEKlskq 570
Cdd:pfam05701 143 VKEE---LESLRKEYASLVSERDIAIKRAE-EAVSASKEIEKTVEELTIELIA------TKESLESAHAAHLEAEE---- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 571 qlhnsniiKKLRAKDKENENMVaKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNS----VVERQEKDLGRLQV 646
Cdd:pfam05701 209 --------HRIGAALAREQDKL-NWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDlkaeLAAYMESKLKEEAD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 647 DMDELEEKNRSIQAALDSAYKELTDLhKANAAKdsEAQEAALSRemKAKEELSAALEKAQEE--ARQQQETLA-IQVGDL 723
Cdd:pfam05701 280 GEGNEKKTSTSIQAALASAKKELEEV-KANIEK--AKDEVNCLR--VAAASLRSELEKEKAElaSLRQREGMAsIAVSSL 354
|
250 260 270
....*....|....*....|....*....|....*
gi 1622908228 724 RLALQRTEQ---AAARKEDYLRHEISELQQRLQEA 755
Cdd:pfam05701 355 EAELNRTKSeiaLVQAKEKEAREKMVELPKQLQQA 389
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
723-915 |
2.93e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 723 LRLALQRTEQAAARKEDYLRHEISELQQRLQEAEN-----RNQELSQSVSSTTRPLLRQIENL-------QATLGSQTSS 790
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefRQKNGLVDLSEEAKLLLQQLSELesqlaeaRAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 791 WEKLEKNLSDRLGESQTLLAAAVERERAATE-ELLANKIQMSSMESQNS----LLRQENSRFQAQLESEKNRLckLEDEN 865
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLaELEAELAELSARYTPNHpdviALRAQIAALRAQLQQEAQRI--LASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622908228 866 NRYQVeLENLKDEYVRTLEETRKE-KTLLNSQLEMERMKVEQERKKAIFTQ 915
Cdd:COG3206 320 AELEA-LQAREASLQAQLAQLEARlAELPELEAELRRLEREVEVARELYES 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
521-670 |
3.08e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 521 KERDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENEN--MVAKLNKK 598
Cdd:COG1579 17 SELDRLEHRLKELPAELA------ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622908228 599 VKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELT 670
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
456-1052 |
3.26e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTqriaeAEKKVQlacKERDAAKKEIKNIKE 535
Cdd:TIGR00606 222 IRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK-----ALKSRK---KQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ELATRlNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQ-------- 607
Cdd:TIGR00606 294 KVFQG-TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRardsliqs 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 608 -HLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEA 686
Cdd:TIGR00606 373 lATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 687 AlsREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKED-YLRHEISELQQRLQEAENRNQELSQS 765
Cdd:TIGR00606 453 Q--EELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 766 VSSttrplLRQIENLQAtlgSQTSSWEKLEKNLSDRLGESQTLLAAavereraateelLANKIQMSSMESQnslLRQENS 845
Cdd:TIGR00606 531 TTT-----RTQMEMLTK---DKMDKDEQIRKIKSRHSDELTSLLGY------------FPNKKQLEDWLHS---KSKEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 846 RFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKaiftqeaikeKERKP 925
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSS----------KQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 926 FSVSSTptmsrsssisgvdmagLQTSFLSQDESHDHSFGPMSVSangsnlyDAVRMGAGSSIIENLQSQLKLREGEITHL 1005
Cdd:TIGR00606 658 LAGATA----------------VYSQFITQLTDENQSCCPVCQR-------VFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1622908228 1006 QLEIGNLEKTRSIMaeeLVKLTNQNDELEEKVKEIPKLRTQLRDLDQ 1052
Cdd:TIGR00606 715 ESELKKKEKRRDEM---LGLAPGRQSIIDLKEKEIPELRNKLQKVNR 758
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
555-804 |
3.53e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 555 EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGK----EEVEKQHRENIKKL 630
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEAleklEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 631 NSVVERQEKDlgrlqvdmdelEEKNRSIQAALDSAykeltdlhkANAAKDSEAQEAALSREMKakeELSAALEKAQEEAR 710
Cdd:pfam00261 81 KVLENRALKD-----------EEKMEILEAQLKEA---------KEIAEEADRKYEEVARKLV---VVEGDLERAEERAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 711 QQQETLAIQVGDLRLA------LQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSsttrPLLRQIENLQATL 784
Cdd:pfam00261 138 LAESKIVELEEELKVVgnnlksLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQ----KLEKEVDRLEDEL 213
|
250 260
....*....|....*....|
gi 1622908228 785 GSQTSSWEKLEKNLSDRLGE 804
Cdd:pfam00261 214 EAEKEKYKAISEELDQTLAE 233
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
695-1092 |
3.87e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 695 KEELSAALEKAQEEARQQQETLAIQvGDLRLALQRTEQAAARKEDylrheISELQQRLQEAEnrnQELSQSvssttrplL 774
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQ-QDLEQTLALLDKIDRQKEE-----TEQLKQQLAQAP---AKLRQA--------Q 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 775 RQIENLQATLGSQTS------SWEKLEKNLSDRLGESQTLlaaavereraaTEELLANKIQMSSMESQ----NSLLRQEN 844
Cdd:PRK11281 101 AELEALKDDNDEETRetlstlSLRQLESRLAQTLDQLQNA-----------QNDLAEYNSQLVSLQTQperaQAALYANS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 845 SRFQ---AQLESEK-NRLCKLEDENNRYQVELE--NLKDEYVRT-LEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEA 917
Cdd:PRK11281 170 QRLQqirNLLKGGKvGGKALRPSQRVLLQAEQAllNAQNDLQRKsLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 918 IKEKERKpfsvSSTPTMSRSSSISgvDMAGLQTSFLSQDES---HDHSFGPMSVSANGSNLY-DAVRMgagSSIIENL-Q 992
Cdd:PRK11281 250 INSKRLT----LSEKTVQEAQSQD--EAARIQANPLVAQELeinLQLSQRLLKATEKLNTLTqQNLRV---KNWLDRLtQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 993 SQLKLREgEITHLQleiGNLEKTRsIMAEELVKLTnQNDELEEKVKEIPKLR------TQLRD----LDQRYNTILQmyG 1062
Cdd:PRK11281 321 SERNIKE-QISVLK---GSLLLSR-ILYQQQQALP-SADLIEGLADRIADLRleqfeiNQQRDalfqPDAYIDKLEA--G 392
|
410 420 430
....*....|....*....|....*....|
gi 1622908228 1063 EKAEEAEELRLDLEDVKNMYKTQIDELLRQ 1092
Cdd:PRK11281 393 HKSEVTDEVRDALLQLLDERRELLDQLNKQ 422
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
458-714 |
4.96e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 458 EKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEEL 537
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 538 atrlnsSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNK------KVKELEEELQHLKQ 611
Cdd:COG1340 81 ------DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelveKIKELEKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 612 VLDGKEEVE------KQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhKANAAKDSEAQE 685
Cdd:COG1340 155 ALEKNEKLKelraelKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA-QEKADELHEEII 233
|
250 260
....*....|....*....|....*....
gi 1622908228 686 AALSREMKAKEELSAALEKAQEEARQQQE 714
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
438-786 |
5.46e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 438 EALSEKEDV--CKVTLTVEflNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKE-------ESSSISSLkDEFTQR 508
Cdd:PRK04863 287 EALELRRELytSRRQLAAE--QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTalrqqekIERYQADL-EELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 509 IAEAEKKVQLACKERD-------AAKKEIKNIKEELAtrlNSSETADLLKEKDEQIRGlmeegeklSKQQLHNSNIIKKL 581
Cdd:PRK04863 364 LEEQNEVVEEADEQQEenearaeAAEEEVDELKSQLA---DYQQALDVQQTRAIQYQQ--------AVQALERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 582 RAKDKEN-ENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHR---ENIKKLNSVVERQE------------------- 638
Cdd:PRK04863 433 PDLTADNaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayQLVRKIAGEVSRSEawdvarellrrlreqrhla 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 639 KDLGRLQVDMDELE---EKNRSIQAALDSAYKeltdlhKANAAKDSEAQEAALSREMKAK-EELSAALEKAQE---EARQ 711
Cdd:PRK04863 513 EQLQQLRMRLSELEqrlRQQQRAERLLAEFCK------RLGKNLDDEDELEQLQEELEARlESLSESVSEARErrmALRQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 712 QQETLAIQVGDLR------LALQRT-----EQAAARKEDylRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENL 780
Cdd:PRK04863 587 QLEQLQARIQRLAarapawLAAQDAlarlrEQSGEEFED--SQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
....*.
gi 1622908228 781 QATLGS 786
Cdd:PRK04863 665 SQPGGS 670
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
459-629 |
6.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 459 KLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQlackerdAAKKEIKNIKEELA 538
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 539 TRLNSSETADLLKEKDEQIRglmeEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEE 618
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|.
gi 1622908228 619 VEKQHRENIKK 629
Cdd:COG1579 160 ELEAEREELAA 170
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
571-935 |
6.45e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 571 QLHNSNIIKKLRAKDKENENMVAKLnKKVKELEEELQHLKQVLDGKEEVEKQ-----------HRENIKKLNSVVERQEK 639
Cdd:COG5185 211 ETGNLGSESTLLEKAKEIINIEEAL-KGFQDPESELEDLAQTSDKLEKLVEQntdlrleklgeNAESSKRLNENANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 640 DLGRLQVDMDELEEKNrSIQAALDSAYKELTDLH-KANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAI 718
Cdd:COG5185 290 QFENTKEKIAEYTKSI-DIKKATESLEEQLAAAEaEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 719 QVgdlrlALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNL 798
Cdd:COG5185 369 EV-----ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 799 SDRLGESQTLLAAAVERERAATEEllANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDE 878
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEE--AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ 521
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622908228 879 YVRTLEETRKEKTLLNSQLEmermkvEQERKKAIFTQEAIKEKERKPFSVSSTPTMS 935
Cdd:COG5185 522 VAESLKDFMRARGYAHILAL------ENLIPASELIQASNAKTDGQAANLRTAVIDE 572
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
437-570 |
6.65e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 437 PEALSEKEDvckvtlTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLK---------DEFTQ 507
Cdd:COG1579 30 PAELAELED------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622908228 508 RIAEAEKKVQLACKERDAAKKEIKNIKEELATRlnSSETADLLKEKDEQIRGLMEEGEKLSKQ 570
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAE 164
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
393-951 |
6.82e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 393 EESGRSATPVNCEQPDILVSSTPINEGHTVLDRVAEQCEPAESQPEA-LSEKEDVCKVTLTVEFLNEKLEKREAQLLSLS 471
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAqINDLEDVADKAISNDDPEEIEKKIENIVTKID 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 472 KEKALLEEAyDNLKDEMFRVKEESSSISSLKD-----------EFTQRIAEAEKKVQLACKERDAAKKEIKNIKE----- 535
Cdd:TIGR01612 1184 KKKNIYDEI-KKLLNEIAEIEKDKTSLEEVKGinlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEkspei 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ------------ELATrLNSSETAD-----LLKEKDEQIRGLMEEGEKLSKQQLHNSNI--IKK-LRAKDKENENMVAKL 595
Cdd:TIGR01612 1263 enemgiemdikaEMET-FNISHDDDkdhhiISKKHDENISDIREKSLKIIEDFSEESDIndIKKeLQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 596 NKKVKELEE-----ELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDeLEEKNRSIQAALDSayKELT 670
Cdd:TIGR01612 1342 NLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKSKIESTLDD--KDID 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 671 DLHKanaaKDSEAQEAALSREMKAKEELsaalekaqEEARQQQETLAIQVGDLRLALQRTEQAAARKEDY----LRHEIS 746
Cdd:TIGR01612 1419 ECIK----KIKELKNHILSEESNIDTYF--------KNADENNENVLLLFKNIEMADNKSQHILKIKKDNatndHDFNIN 1486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 747 ELQQRLQEAENRNQELSQSVSST--TRPLLRQIENLQATLGSQTSSWE--------------------KLEKNLSDRLGE 804
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIekNKELFEQYKKDVTELLNKYSALAiknkfaktkkdseiiikeikDAHKKFILEAEK 1566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 805 SQTLLAAAVERERAATEELLANK--------IQMSSMESQNSLLRQENSRFQAQ-----------------LESEKNRLC 859
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIEDDAAKNDksnkaaidIQLSLENFENKFLKISDIKKKINdclketesiekkissfsIDSQDTELK 1646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 860 KLEDENNRYQVELENLKDEYvRTLEETRKEKTLLNSQLEMERMKVEQERKK-AIFTQEAIKE------KERKPFSVSSTP 932
Cdd:TIGR01612 1647 ENGDNLNSLQEFLESLKDQK-KNIEDKKKELDELDSEIEKIEIDVDQHKKNyEIGIIEKIKEiaiankEEIESIKELIEP 1725
|
650 660
....*....|....*....|
gi 1622908228 933 TMSR-SSSISGVDMAGLQTS 951
Cdd:TIGR01612 1726 TIENlISSFNTNDLEGIDPN 1745
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
509-791 |
8.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 509 IAEAEKKVQLACKERDAAKKEIKNIKEElatrlnssetadlLKEKDEQIRGLMEEgeklskqqlhnsniikklrakdken 588
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAE-------------LDALQAELEELNEE------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 589 enmVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQV-----DMDELEEKNRSIQAALD 663
Cdd:COG3883 53 ---YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 664 SAYKELTDLHKANAAKdsEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRH 743
Cdd:COG3883 130 ADADLLEELKADKAEL--EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622908228 744 EISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSW 791
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
601-872 |
8.78e-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: 43.19 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 601 ELEEELQHLKQVLDGKEEVEKQHRENIKKLnsvverqEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKD 680
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 681 SEAQeaALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKedylRHEISELQQRLQEAENRNQ 760
Cdd:pfam05557 76 ELNR--LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQST----NSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 761 ELSQ------SVSSTTRPLLRQIENLQATLGSQTsSWEKLEKNLSDRLGESQTLLAAAvereraatEELLANKIQMSSME 834
Cdd:pfam05557 150 EAEQlrqnleKQQSSLAEAEQRIKELEFEIQSQE-QDSEIVKNSKSELARIPELEKEL--------ERLREHNKHLNENI 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622908228 835 SQNSLLRQENSRFQAQLESE---KNRLCKLEDENNRYQVEL 872
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKLEREekyREEAATLELEKEKLEQEL 261
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
488-701 |
9.75e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 488 MFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDA-AKKEIKNIKEELATRLNSSEtadllKEKDEQIRGLMEEGEK 566
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERR-----NELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 567 LSKQQlhnsniiKKLRAKDKENENMVAKLNKKVKELEEelqhLKQVLDGKEEVEKQHRENIKKLNSVVERQEKdlgrlqv 646
Cdd:PRK12704 98 LDRKL-------ELLEKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELERISGLTAEEAKEIL------- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622908228 647 dMDELEEKNRSIQAALDSAYKEltdlhkanaakdsEAQEAAlsrEMKAKEELSAA 701
Cdd:PRK12704 160 -LEKVEEEARHEAAVLIKEIEE-------------EAKEEA---DKKAKEILAQA 197
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
649-761 |
1.06e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 649 DELEEKNRSIQaaldsaykELTD---LHKANAAkDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRL 725
Cdd:PRK09039 53 SALDRLNSQIA--------ELADllsLERQGNQ-DLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622908228 726 AL----QRTEQAAARKEDY------LRHEISELQQRLQEAENRNQE 761
Cdd:PRK09039 124 ELdsekQVSARALAQVELLnqqiaaLRRQLAALEAALDASEKRDRE 169
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
456-673 |
1.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLsKEKAllEEAyDNLKDEMFRVKEE-SSSISSLKDEFTQRIAEAEKKVQlacKERDAAKKEIKNIK 534
Cdd:PRK00409 518 LNELIASLEELEREL-EQKA--EEA-EALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQ---QAIKEAKKEADEII 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 535 EELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDK---ENENMVAKLNKKVKELEEELQ---- 607
Cdd:PRK00409 591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkyLSLGQKGEVLSIPDDKEAIVQagim 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622908228 608 ----HLKQV-LDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDmDELEEKNRSIQAALDSAYKELTDLH 673
Cdd:PRK00409 671 kmkvPLSDLeKIQKPKKKKKKKPKTVKPKPRTVSLELDLRGMRYE-EALERLDKYLDDALLAGYGEVLIIH 740
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
626-717 |
1.23e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.41 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 626 NIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKA-NAAKDSEAQEAAlsremKAKEELSAALEK 704
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKElANAQAQALQTAQ-----NNLATAQAALAN 329
|
90
....*....|...
gi 1622908228 705 AQEEARQQQETLA 717
Cdd:TIGR04320 330 AEARLAKAKEALA 342
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
354-710 |
1.24e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 354 LVPITVNSSTPKSKTVESAEGKSEEVNETlvIPTEEAEMEESGRSATPVNCEQPDILVSSTPIneghTVLDRVAEQCEPA 433
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRD--IQRLKNDIEEQETLLGTIMPEEESAKVCLTDV----TIMERFQMELKDV 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 434 ESQPEALSEKEDVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKeesSSISSLKDEFTQrIAEAE 513
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK---SKTNELKSEKLQ-IGTNL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 514 KKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQirglmeegeklskqqlHNSNIIKKLRAKDKENENMVA 593
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ----------------EKEELISSKETSNKKAQDKVN 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 594 KLNKKVKELEEELQHL-KQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL 672
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIeNKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1024
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622908228 673 HKANAAKDSEAQEAALSREMKAKE--ELSAALEKAQEEAR 710
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQvlQMKQEHQKLEENID 1064
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
540-662 |
1.31e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 540 RLNSSETADLLKEKDEQIRGLMEEGEKLSKQQlhnsniikklrakDKENENMVAKLNKKVKELEEELQHLKQvldgKEEV 619
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQLEIEKEALKKEQ-------------DEASFERLAELRDELAELEEELEALKA----RWEA 465
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622908228 620 EKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAAL 662
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
421-637 |
1.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 421 TVLDRVAEQCEPAESQPEALsEKEDVCKVTLTVEFLNEKLEKREAQLLS----------LSKEKALLEEAYDNLKDEMFR 490
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKY-NLEELEKKAEEYEKLKEKLIKLKGEIKSlkkelekleeLKKKLAELEKKLDELEEELAE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 491 VKEESSSIS-SLKDEFTQRIAEAEK------KVQLACKERDAAKKEIKNIKEEL-ATRLNSSETADLLKEKDEQIRGLM- 561
Cdd:PRK03918 575 LLKELEELGfESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELdKAFEELAETEKRLEELRKELEELEk 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 562 ----EEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVldgKEEVEK---------QHRENIK 628
Cdd:PRK03918 655 kyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA---KKELEKlekalerveELREKVK 731
|
....*....
gi 1622908228 629 KLNSVVERQ 637
Cdd:PRK03918 732 KYKALLKER 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
463-756 |
1.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 463 REAQLLSLSKEKALLEEAYDNLKdemFRVKEESSSISSLKD-------------------EFTQRIAEAEKKVQLACKER 523
Cdd:PRK04863 784 REKRIEQLRAEREELAERYATLS---FDVQKLQRLHQAFSRfigshlavafeadpeaelrQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 524 DAAKKEIKNIKEEL---------ATRLNSSETADLLKEKDEQIRGLmEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAK 594
Cdd:PRK04863 861 QQQRSQLEQAKEGLsalnrllprLNLLADETLADRVEEIREQLDEA-EEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQ 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 595 LNKKVKELEEELQHLKQVLDGKEEVeKQHRENIKKLNSV---------VERQEKDLGRLQVDMDELEEKNRSIQAALDSA 665
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFALTEV-VQRRAHFSYEDAAemlaknsdlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 666 YKELTDLHKANAAKDSEAQEaalsremkAKEELSA----ALEKAQEEARQQQETLAIQvgdLRLALQRTEQaAARKEDYL 741
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQE--------LKQELQDlgvpADSGAEERARARRDELHAR---LSANRSRRNQ-LEKQLTFC 1086
|
330
....*....|....*
gi 1622908228 742 RHEISELQQRLQEAE 756
Cdd:PRK04863 1087 EAEMDNLTKKLRKLE 1101
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
464-910 |
1.91e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 464 EAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAA------KKEIKNIKEEL 537
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEEsdlerlKEEIEKSSKQR 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 538 ATRLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGK 616
Cdd:TIGR00606 656 AMLAGATAVYSqFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 617 EEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL----HKANAAKDSEAQEAALSREM 692
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimeRFQMELKDVERKIAQQAAKL 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 693 KAKeELSAALEKAQEEARQQQETLAIQVGDLRLaLQRTEQAAARKEDYLRHEISELQ-QRLQEAENRNQelSQSVSSTTR 771
Cdd:TIGR00606 816 QGS-DLDRTVQQVNQEKQEKQHELDTVVSKIEL-NRKLIQDQQEQIQHLKSKTNELKsEKLQIGTNLQR--RQQFEEQLV 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 772 PLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSS----MESQNSLLRQENSRF 847
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgyMKDIENKIQDGKDDY 971
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622908228 848 QAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLemERMKVEQERKK 910
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL--TLRKRENELKE 1032
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
457-852 |
1.95e-03 |
|
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: 42.41 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 457 NEKLEKREAQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLkdefTQRIAEAEKKVQlackerdAAKKEIKNIKEE 536
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL----TASLQEKERAIE-------ATNAEITKLRSR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 537 LATRLNSSETadlLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMV--------------AKLNKKVKEL 602
Cdd:pfam15921 526 VDLKLQELQH---LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 603 EEELQHLKQVLDGKE--------EVEKQHRENIKKLNSVVERQeKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhK 674
Cdd:pfam15921 603 RLELQEFKILKDKKDakireleaRVSDLELEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL-K 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 675 ANAAKDSEAQEAALSRemkakeeLSAALEKAQEEARQQQETLAIQVGD----LRLALQRTEQAAARkedylRHEISELQQ 750
Cdd:pfam15921 681 RNFRNKSEEMETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSdghaMKVAMGMQKQITAK-----RGQIDALQS 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 751 RLQEAENrnqelSQSVSSTTRPLLRQIENLQatlgSQTSSWEKLEKNlsDRLGESQTLLAAAVERERAATE-ELLANKIQ 829
Cdd:pfam15921 749 KIQFLEE-----AMTNANKEKHFLKEEKNKL----SQELSTVATEKN--KMAGELEVLRSQERRLKEKVANmEVALDKAS 817
|
410 420
....*....|....*....|...
gi 1622908228 830 MSSMESQNSLLRQENSRFQAQLE 852
Cdd:pfam15921 818 LQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
674-802 |
1.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 674 KANAAKDSEAQEAALSR----EMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEISELQ 749
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622908228 750 QRLQEAENRNQELSQsvssttrpLLRQIENLQATLgsqtsswEKLEKNLSDRL 802
Cdd:PRK12704 107 KREEELEKKEKELEQ--------KQQELEKKEEEL-------EELIEEQLQEL 144
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
479-786 |
2.05e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 479 EAYDNLKDEMFRVKEESSSISSLK-DEFTQRIAEAEKKVQLACKERDAAKKEIKNI---KEELATRLNSSETAdlLKEKD 554
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAEKNILLLNQARLQALEDLEKIlteKEALQGKINILEMR--LSETD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 555 EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLdgkeEVEKQHRENIKKLNSVV 634
Cdd:PLN02939 184 ARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDI----QFLKAELIEVAETEERV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 635 ERQEKDLGRLQVDMDELEEKNRSIQAaldsaykeltdlhkaNAAKDSEAQEAALsreMKAKEELSAALEKAQEEARQQQE 714
Cdd:PLN02939 260 FKLEKERSLLDASLRELESKFIVAQE---------------DVSKLSPLQYDCW---WEKVENLQDLLDRATNQVEKAAL 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622908228 715 TLAiQVGDLRLALQRTEQ--AAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGS 786
Cdd:PLN02939 322 VLD-QNQDLRDKVDKLEAslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSK 394
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
508-762 |
2.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 508 RIAEAEKKVQLACKERDAAKKEIKNIKEEL---ATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAK 584
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 585 DKENENMVAklnkkvkELEEELQHLKQVLDGKEEVEKQHREnikklnSVVERQEKDLGRLQVDMDELEEKNRSIQAALDS 664
Cdd:COG1196 621 TLLGRTLVA-------ARLEAALRRAVTLAGRLREVTLEGE------GGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 665 AYKELTDLHKAnaakdsEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHE 744
Cdd:COG1196 688 LAEEELELEEA------LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
250
....*....|....*...
gi 1622908228 745 ISELQQRLQEAENRNQEL 762
Cdd:COG1196 762 LEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
589-1091 |
2.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 589 ENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERqekdlgrlqvdMDELEEKNRSIQAALDSAYKE 668
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE-----------INEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 669 LTDLHK-ANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLrlalqrtEQAAARKEDY--LRHEI 745
Cdd:PRK03918 230 VKELEElKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-------KELKEKAEEYikLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 746 SELQQRLQEAENRNQELSQSVSSTTRpLLRQIENLQATLGSQTSSWEKLEKNLSdRLGESQTLLAAAVERERAAtEELLA 825
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEE-RIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEEL-ERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 826 NKIQMSSMESQNSLLRQENSRFQAQLESEK--NRLCKLEDENNRYQVELENLKDEYV------RTLEETRKEKTLLNSQL 897
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKitARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 898 EMERmkVEQERKKAIFTQEAIKEKERKPFSV-SSTPTMSRSSSISgvdmaglqtSFLSQDESHDHSFGPMSVSANgSNLY 976
Cdd:PRK03918 460 ELKR--IEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELA---------EQLKELEEKLKKYNLEELEKK-AEEY 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 977 DAVR-----MGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRSIMAEELVKLTNQN-DELEEKVKEIPKLRTQ---L 1047
Cdd:PRK03918 528 EKLKeklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEyleL 607
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1622908228 1048 RDLDQRYNTILQMYGEKAEEAEELRLDLEDVKN---MYKTQIDELLR 1091
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKrleELRKELEELEK 654
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
486-809 |
2.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 486 DEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLnsSETADLLKEKDEQIRGLMEEGE 565
Cdd:pfam07888 20 TDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR--RELESRVAELKEELRQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 566 KLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQ 645
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 646 VDMDELEEKNRSIQAALDSAYKEL---------------TDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQE--- 707
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLaqrdtqvlqlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 708 ------------------EARQQQETLAIQVGDLRLA--------------LQRTEQAAARKEDYLRHEISELQQRLQEA 755
Cdd:pfam07888 258 eelssmaaqrdrtqaelhQARLQAAQLTLQLADASLAlregrarwaqeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1622908228 756 ENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLL 809
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
598-716 |
2.20e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 598 KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQvdmDELEEKNRSIQaaldsAYKEltdlhKANA 677
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE---AELEEKDERIE-----RLER-----ELSE 452
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622908228 678 AKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETL 716
Cdd:COG2433 453 ARSEERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
429-800 |
2.45e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 429 QCEPAESQPEALSEKedVCKVTLTVEFLNEKLEKREAQLLSLSKEKALLE----EAYDNLKDEMFRVKEESSSISSLKDE 504
Cdd:pfam01576 420 RLSESERQRAELAEK--LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLEsqlqDTQELLQEETRQKLNLSTRLRQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 505 FTQRIAEAEKKVQlackERDAAKKEIKNIKEELATrlnssetadlLKEKDEQIRGLMEEGEKLSKQQLHNsniIKKLRAK 584
Cdd:pfam01576 498 RNSLQEQLEEEEE----AKRNVERQLSTLQAQLSD----------MKKKLEEDAGTLEALEEGKKRLQRE---LEALTQQ 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 585 DKENENMVAKLNKKVKELEEEL-------QHLKQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKNRS 657
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELddllvdlDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 658 IQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEelSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARK 737
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN--VHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 718
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622908228 738 EDYLRHEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSD 800
Cdd:pfam01576 719 EVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKE 781
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
700-986 |
2.63e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 700 AALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEISELQQRLQEAENRNQELSQSVSSTTRPLLRQIEN 779
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA----ELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 780 LQATlGSQTSSWEKL--EKNLSDRLGESQTLlaaavereraateellaNKIqmssMESQNSLLRQENSRfQAQLESEKNR 857
Cdd:COG3883 95 LYRS-GGSVSYLDVLlgSESFSDFLDRLSAL-----------------SKI----ADADADLLEELKAD-KAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 858 LCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQEAIKEKERKPFSVSSTPTMSRS 937
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622908228 938 SSISGVDMAGLQTSFLSQDESHDHSFGPMSVSANGSNLYDAVRMGAGSS 986
Cdd:COG3883 232 AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
535-910 |
2.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 535 EELATRLNSSETADLLKEKDEQIRGLMEEGEklskQQLHNSNIIKKLRAKDK-ENENMVAKLNKKVKELEEELQHLKQVL 613
Cdd:PRK04863 331 QAASDHLNLVQTALRQQEKIERYQADLEELE----ERLEEQNEVVEEADEQQeENEARAEAAEEEVDELKSQLADYQQAL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 614 DGKEEVEKQHRENIKKLnsvvERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL-HK---ANAAKDSEAQEAALS 689
Cdd:PRK04863 407 DVQQTRAIQYQQAVQAL----ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLeQKlsvAQAAHSQFEQAYQLV 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 690 REMKAKEELSAALEKAQEEARQQQEtlaiqvgdLRLALQRTEQaaarkedyLRHEISELQQRLQEaeNRNQElsqsvsst 769
Cdd:PRK04863 483 RKIAGEVSRSEAWDVARELLRRLRE--------QRHLAEQLQQ--------LRMRLSELEQRLRQ--QQRAE-------- 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 770 trpllRQIENLQATLGSQTSSWEKLEKNLSDRlgesqtllaaavereraaTEELLANKIQMSSMESQNSLLRQEnsrfQA 849
Cdd:PRK04863 537 -----RLLAEFCKRLGKNLDDEDELEQLQEEL------------------EARLESLSESVSEARERRMALRQQ----LE 589
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622908228 850 QLESEKNRLCKLEDENNRYQVELENLK-------------DEYVRTLEETRKEKTLLNSQLEMERMKVEQERKK 910
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLReqsgeefedsqdvTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
456-801 |
2.95e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 456 LNEKLEKREAQLLSLSKEKalLEEAYDNLKDEMFRVKEEsssisslkdeftqrIAEAEKKVQlackerdAAKKEIKNIKE 535
Cdd:NF033838 104 LNVLKEKSEAELTSKTKKE--LDAAFEQFKKDTLEPGKK--------------VAEATKKVE-------EAEKKAKDQKE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 536 ELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQlhnsniikklrAKDKENENMVAKLNKKVKELEEELQHLKQVLDG 615
Cdd:NF033838 161 EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEE-----------AKEPRDEEKIKQAKAKVESKKAEATRLEKIKTD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 616 KEEVEKQHREnikklnsVVERQEKDLGRLQVDMDELEE-KNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKA 694
Cdd:NF033838 230 REKAEEEAKR-------RADAKLKEAVEKNVATSEQDKpKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKP 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 695 KEELSAAlEKAQEEARQQQEtlaiqvgDLRLALQRTEQAAARKEdyLRHEISELQQRLQEAEnrnQELSQSVSSTTRPlL 774
Cdd:NF033838 303 EKKVAEA-EKKVEEAKKKAK-------DQKEEDRRNYPTNTYKT--LELEIAESDVKVKEAE---LELVKEEAKEPRN-E 368
|
330 340
....*....|....*....|....*..
gi 1622908228 775 RQIENLQATLGSQTSSWEKLEKNLSDR 801
Cdd:NF033838 369 EKIKQAKAKVESKKAEATRLEKIKTDR 395
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
616-906 |
3.00e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 616 KEEVEKQHREnikkLNSVVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEaaLSREMKAK 695
Cdd:pfam07888 68 REQWERQRRE----LESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRE--LEEDIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 696 EELSAALEKAQEEARQQQETLAIQVGDL---RLALQRTEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTTR- 771
Cdd:pfam07888 142 TQRVLERETELERMKERAKKAGAQRKEEeaeRKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQk 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 772 ------------PLLRQIENLQATLGSQTSSWEKLEKNLSDRLGE---SQTLLAAAVERERAATEELLANKIQMSSMESQ 836
Cdd:pfam07888 222 lttahrkeaeneALLEELRSLQERLNASERKVEGLGEELSSMAAQrdrTQAELHQARLQAAQLTLQLADASLALREGRAR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 837 NSllrQENSRFQAQLESEKNRLCKLEDE--------------NNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERM 902
Cdd:pfam07888 302 WA---QERETLQQSAEADKDRIEKLSAElqrleerlqeermeREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQK 378
|
....
gi 1622908228 903 KVEQ 906
Cdd:pfam07888 379 EKEQ 382
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
502-922 |
3.34e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 502 KDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEgekLSKQQLHNSNIIKKL 581
Cdd:pfam05622 9 KDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ---LQEENFRLETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 582 RAKDKENENMVAKLNKKVKELE---EELQHLKQVLDgkeeVEKQHRENIKKLNSVVERQEK---DLGRLQVDMDELEEKN 655
Cdd:pfam05622 86 RIKCEELEKEVLELQHRNEELTslaEEAQALKDEMD----ILRESSDKVKKLEATVETYKKkleDLGDLRRQVKLLEERN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 656 RS-IQAALDsaYKEltDLHKANAAKdseAQEAALSREM-----KAKEELSAAlEKAQEEARQQQETLAiqvgdlrlALQR 729
Cdd:pfam05622 162 AEyMQRTLQ--LEE--ELKKANALR---GQLETYKRQVqelhgKLSEESKKA-DKLEFEYKKLEEKLE--------ALQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 730 TEQAAARKEDYLRHEISEL------QQRLQEAENRNQELSQSVSSTTRPLL-----RQIENLQAtlgSQTSSWEKLEKNL 798
Cdd:pfam05622 226 EKERLIIERDTLRETNEELrcaqlqQAELSQADALLSPSSDPGDNLAAEIMpaeirEKLIRLQH---ENKMLRLGQEGSY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 799 SDRLGESQTLLAAavereraateellANKiQMSSMESQNSLLRQENSRFQAQLEsEKNRLCKLEDENNRYQVELENLKDE 878
Cdd:pfam05622 303 RERLTELQQLLED-------------ANR-RKNELETQNRLANQRILELQQQVE-ELQKALQEQGSKAEDSSLLKQKLEE 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1622908228 879 YVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFT-QEAIKEKE 922
Cdd:pfam05622 368 HLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDElQEALRKKD 412
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
477-708 |
4.07e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 477 LEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIaEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETadlLKEKDEQ 556
Cdd:PTZ00440 455 LKKSINQLKTLISIMKSFYDLIISEKDSMDSKE-KKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKN---IEDYYIT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 557 IRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQhrenIKKLNSVVER 636
Cdd:PTZ00440 531 IEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNI----IQQIEELINE 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622908228 637 QEKDLGRLQVDMDELEEKNRSIqaaLDSAYKELTDLHKANAAKDSEAQEaALSREMKAKEELSAALEKAQEE 708
Cdd:PTZ00440 607 ALFNKEKFINEKNDLQEKVKYI---LNKFYKGDLQELLDELSHFLDDHK-YLYHEAKSKEDLQTLLNTSKNE 674
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
533-614 |
4.73e-03 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 37.95 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 533 IKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVA---KLNKKVKELEEELQHL 609
Cdd:pfam02403 14 VKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAevkELKDELKALEAELKEL 93
|
....*
gi 1622908228 610 KQVLD 614
Cdd:pfam02403 94 EAELD 98
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
462-598 |
5.36e-03 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 40.78 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 462 KREAQLLSLSKEKALLEEAYDNLKDEM-----FRV--KEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIK 534
Cdd:PTZ00399 501 KAEMKLISLDKKKKQLLQLCDKLRDEWlpnlgIRIedKPDGPSVWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKK 580
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622908228 535 EELAT-RLNSSETADLLKEK-------DEQIRGLM-EEGEKLSKQQLhnSNIIKKLRAKDKENENMVAKLNKK 598
Cdd:PTZ00399 581 KELEKlEKAKIPPAEFFKRQedkysafDETGLPTHdADGEEISKKER--KKLSKEYDKQAKLHEEYLAKGGKS 651
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
489-714 |
5.60e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.78 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 489 FRVKEESSSISSLKDEFTQRIAEA-----------EKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEkdeQI 557
Cdd:pfam05667 268 SGASRSAQDLAELLSSFSGSSTTDtgltkgsrfthTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQE---QL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 558 RGLMEEGEKLSKQqlhnsniIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEkqhrENIKKLNSVVERQ 637
Cdd:pfam05667 345 EDLESSIQELEKE-------IKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAE----ENIAKLQALVDAS 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622908228 638 EKDLgrlqvdmDELEEKNRSIQAALDSAYKELTDlhkANAAKDSEAQeaalsREMKAKEELSAALEKAQEEARQQQE 714
Cdd:pfam05667 414 AQRL-------VELAGQWEKHRVPLIEEYRALKE---AKSNKEDESQ-----RKLEEIKELREKIKEVAEEAKQKEE 475
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
648-754 |
6.04e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 38.75 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 648 MDELEEKNRSIQAALDSAYKELTDLhkANAAKDSEAQEAalsremKAKEELSAALEKAQEEARQQQETLAIQVGdlRLAL 727
Cdd:PRK14473 34 LNLLNERTRRIEESLRDAEKVREQL--ANAKRDYEAELA------KARQEAAKIVAQAQERARAQEAEIIAQAR--REAE 103
|
90 100
....*....|....*....|....*..
gi 1622908228 728 QRTEQAAARKEDYLRHEISELQQRLQE 754
Cdd:PRK14473 104 KIKEEARAQAEQERQRMLSELKSQIAD 130
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
988-1074 |
8.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 988 IENLQSQLKLREGEIthlqleIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEE 1067
Cdd:COG3206 300 IAALRAQLQQEAQRI------LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
....*..
gi 1622908228 1068 AEELRLD 1074
Cdd:COG3206 374 LEEARLA 380
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
492-899 |
9.49e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 492 KEESSSISSLKDEFTQRIAEAEKKVQLACKE----RDAAKKEIKNIKEELATRLNSSETA----DLLKEKDEQIRGLMEE 563
Cdd:COG5022 798 KLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGRSLKAkkrfSLLKKETIYLQSAQRV 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 564 GE---KLSKQQLHNSNIiKKLRAKDKENENMVAKLNKKVKE--------LEEELQHLKQVLDGKEEVEKQHREnikklns 632
Cdd:COG5022 878 ELaerQLQELKIDVKSI-SSLKLVNLELESEIIELKKSLSSdlienlefKTELIARLKKLLNNIDLEEGPSIE------- 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 633 vvERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAAL-----------SREMKAKEELSAA 701
Cdd:COG5022 950 --YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElskqygalqesTKQLKELPVEVAE 1027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 702 LEKAQE------EARQQQETLAIQVGDLRLALQRTE----QAAARKEDYLRHEISELQQRLQEAENRNQELSQsVSSTTR 771
Cdd:COG5022 1028 LQSASKiissesTELSILKPLQKLKGLLLLENNQLQarykALKLRRENSLLDDKQLYQLESTENLLKTINVKD-LEVTNR 1106
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 772 PLLRQIENLQATLGSQTSSweKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMEsqnsllRQENSRFQAQL 851
Cdd:COG5022 1107 NLVKPANVLQFIVAQMIKL--NLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEA------LPSPPPFAALS 1178
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622908228 852 ESEKNRLCKLEDENNRYQVELENLKDEyvrTLEETRKEKTLLNSQLEM 899
Cdd:COG5022 1179 EKRLYQSALYDEKSKLSSSEVNDLKNE---LIALFSKIFSGWPRGDKL 1223
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
490-623 |
9.79e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 490 RVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKE-IKNIKEELatrlnssetADLLKEKDEqirglMEEGEKLS 568
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFErLAELRDEL---------AELEEELEA-----LKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622908228 569 KQQLHNsniIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLdgKEEVEKQH 623
Cdd:COG0542 467 KELIEE---IQELKEELEQRYGKIPELEKELAELEEELAELAPLL--REEVTEED 516
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
510-713 |
9.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 510 AEAEKKVQLACKERDAAKKEIKNIKEEL-----ATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHN--SNIIKKLR 582
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiAALLAEAG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622908228 583 AKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKlnsvvERQEKDLGRLQVDMDELEEKNRSIQAAL 662
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREEL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622908228 663 DSAYKELTDLHKANAAKDSEAQEAALSREMKAKEE-------LSAALEKAQEEARQQQ 713
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELEELKAELRELAEewaalklALELLEEAREEYREER 513
|
|
| |
