|
Name |
Accession |
Description |
Interval |
E-value |
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
14-182 |
4.03e-26 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 107.56 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 14 KACTELSLDSSLHAINLHCNNISKITSIDHIWNLRHLDLSSNQISQIEGLNTLTKLCTLNLSCNLITRVEGLEALVN--- 90
Cdd:cd21340 15 TKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLTNlee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 91 ---------------------------LTRLNLSYNHISDLSGLIPLHglkyKLRYIDLHSNYIDSIHHLLQCTVGLHFL 143
Cdd:cd21340 95 lhienqrlppgekltfdprslaalsnsLRVLNISGNNIDSLEPLAPLR----NLEQLDASNNQISDLEELLDLLSSWPSL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958749331 144 TNLILEkdgeGNPICLVPGYRAIILQTLPQLRILDCKNI 182
Cdd:cd21340 171 RELDLT----GNPVCKKPKYRDKIILASKSLEVLDGKEI 205
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
17-181 |
5.00e-12 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 69.19 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 17 TELSLDSSLHAINLHCNNISKITSIDHIWNLRHLDLSSNQISQI-EGLNTLTKLCTLNLSCNLITRV-EGLEALVNLTRL 94
Cdd:COG4886 85 LLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 95 NLSYNHISDLSGliPLHGLKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLVPGyraiILQTLPQL 174
Cdd:COG4886 165 DLSNNQLTDLPE--ELGNLT-NLKELDLSNNQITDLPEPLG---NLTNLEELDL----SGNQLTDLPE----PLANLTNL 230
|
....*..
gi 1958749331 175 RILDCKN 181
Cdd:COG4886 231 ETLDLSN 237
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
528-897 |
1.01e-09 |
|
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: 62.77 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 528 ELKASAADREINLlrtslRQEKEQVQqlHDLLALKEQEHRQEIETREffndaefqdALTKRLSKEERKHEQEVKEYQEKI 607
Cdd:TIGR02168 206 ERQAEKAERYKEL-----KAELRELE--LALLVLRLEELREELEELQ---------EELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 608 NILNQQYLDLENEFRIAltvearrfkdvqdgfedvatelakskhaliwaQRKENESSSLIKDLTSMVKEQKTKLSEVCKL 687
Cdd:TIGR02168 270 EELRLEVSELEEEIEEL--------------------------------QKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 688 KQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTERkvwgHELAYQGTSLSQSRGKLEA 767
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL----EELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 768 QIESLCRENESLRKThesdcdalrikckiIEDQTETIRKLKdglQEKDGQIKMLQEQITiieKCSQEQLNEKTSQLDSIV 847
Cdd:TIGR02168 394 QIASLNNEIERLEAR--------------LERLEDRRERLQ---QEIEELLKKLEEAEL---KELQAELEELEEELEELQ 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958749331 848 EKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLET 897
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
405-999 |
3.99e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 405 VEQLDQERE-----MRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEvivhRLQNEIK 479
Cdd:COG1196 202 LEPLERQAEkaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 480 KLTIELmkaRDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSLRQEKEQVQQLHDLL 559
Cdd:COG1196 278 ELELEL---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 560 ALKEQEHRQEIETREFFNDAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKDVQDGF 639
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 640 EDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDKQKSIQIELL 719
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 720 KHEKNQLISELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRGKLEAQIESLCRENESlRKThesdcdalrikckiied 799
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-RAT----------------- 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 800 qTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQL-------DSIVEKLERHNERKEKLKQQLKAKELELE 872
Cdd:COG1196 576 -FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtllgrTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 873 EIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKKLRAERDRSLELQKDAVEKLQNMDDAFKRQVDAIVEAHQTE 952
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1958749331 953 ITQLANEKQRYIECANLKVQQIEDEMRgllEETCKNK-KLMEEKIKQL 999
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPD---LEELERElERLEREIEAL 779
|
|
| LRR_9 |
pfam14580 |
Leucine-rich repeat; |
50-182 |
1.49e-08 |
|
Leucine-rich repeat;
Pssm-ID: 405295 [Multi-domain] Cd Length: 175 Bit Score: 55.15 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 50 LDLSSNQISQIEGLNTLTKLCTLNLSCNLITRV-EGL-EALVNLTRLNLSYNHISDLSGLIPLHGLKyKLRYIDLHSNyi 127
Cdd:pfam14580 47 IDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLK-KLTFLSLLRN-- 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958749331 128 dsihhllqctvglhfltnlilekdgegnPICLVPGYRAIILQTLPQLRILDCKNI 182
Cdd:pfam14580 124 ----------------------------PVTNKPHYRLYVIYKVPQLRLLDFRKV 150
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
491-876 |
2.60e-07 |
|
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: 54.52 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 491 QQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSLRQEKEQVQQLhdllalkEQEHRQEI 570
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------EEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 571 ETREFFndAEFQDALtkrlSKEERKHEQEVKEYQEKINILNQQYLDLENEF-RIALTVE--ARRFKDVQDGFEDVATELa 647
Cdd:pfam07888 108 ASSEEL--SEEKDAL----LAQRAAHEARIRELEEDIKTLTQRVLERETELeRMKERAKkaGAQRKEEEAERKQLQAKL- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 648 kskhaliwaQRKENESSSLIKDLTSMVKEQKTKLSEVCKlkqeaaanLQNQINTLEILIEDDKQKSIQIELLKHEKNQLI 727
Cdd:pfam07888 181 ---------QQTEEELRSLSKEFQELRNSLAQRDTQVLQ--------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 728 SELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRgkLEAQIESL----------------CRENESLRKTHESDCDAlr 791
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR--LQAAQLTLqladaslalregrarwAQERETLQQSAEADKDR-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 792 ikckiIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERhnERKEKLKQQLKAKELeL 871
Cdd:pfam07888 320 -----IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV--AQKEKEQLQAEKQEL-L 391
|
....*
gi 1958749331 872 EEIRK 876
Cdd:pfam07888 392 EYIRQ 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
356-898 |
5.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 356 RKMRQPYLRDLYVRSSLVNCNNLREVDEQKNGMIKVDKSASNDNTYRSLVEQLDQEREMRWKAEQTEKKLMDY---IDEL 432
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 433 HKQANEKKDV----HSQAIITTDRLKDAIFKERHCKAQLEViVHRLQNEIKKLTIELMKA----RDQQEDHIRHLRTLER 504
Cdd:PTZ00121 1335 KKKAEEAKKAaeaaKAEAEAAADEAEAAEEKAEAAEKKKEE-AKKKADAAKKKAEEKKKAdeakKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 505 ALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSlrQEKEQVQQLHDllalKEQEHRQEIETREFFNDAEFQDA 584
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKK----KAEEAKKADEAKKKAEEAKKADE 1487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 585 LTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKDVQDGFEDV--ATELAKSKHALIWAQRKENE 662
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAE 1567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 663 SSSLIKDLTSMVKEQktklSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRT 742
Cdd:PTZ00121 1568 EAKKAEEDKNMALRK----AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 743 ERKVWGHELAYQGTSLSQSRGKLEAQIESLCRENESLRKTHESDCDALRIKCKIIED--QTETIRKLKDGLQEKDGQIKM 820
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakKAEELKKKEAEEKKKAEELKK 1723
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749331 821 LQEqitiIEKCSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQ 898
Cdd:PTZ00121 1724 AEE----ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
815-1009 |
1.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 815 DGQIKMLQEQITIIekcsQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLsn 894
Cdd:COG3883 15 DPQIQAKQKELSEL----QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 895 letqvkevkekfenkekklrAERDRSLELQKDAVEKL------QNMDDAFKRQ--VDAIVEAHQTEITQLANEKQRyIEC 966
Cdd:COG3883 89 --------------------GERARALYRSGGSVSYLdvllgsESFSDFLDRLsaLSKIADADADLLEELKADKAE-LEA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749331 967 ANLKVQQIEDEMRGLLEETCKNKKLMEEKIKQLACAISDIQKE 1009
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
392-624 |
7.85e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 392 DKSASNDNTYRSLVEQLDQEREmrwKAEQTEKKLMDYidelhKQANEKKDVHSQAIITTDRLKDaifkerhckaqleviv 471
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRK---ELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSE---------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 472 hrLQNEIKKLTIELMKARDQqedhirhLRTLERALEKMEKQKAQQQQAqmRLIQEVELKASAADREINLLRTSLRQEKEQ 551
Cdd:COG3206 224 --LESQLAEARAELAEAEAR-------LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749331 552 VQQLHDLLALKEQEHRQEIETREFFNDAEFQdaltkRLSKEERKHEQEVKEYQEKINILN---QQYLDLENEFRIA 624
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELE-----ALQAREASLQAQLAQLEARLAELPeleAELRRLEREVEVA 363
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
46-110 |
9.37e-04 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 43.30 E-value: 9.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749331 46 NLRHLDLSSNQISQI--EGLNTLTKLCTLNLSCNLITRV--EGLEALVNLTRLNLSYNhisDLSGLIPL 110
Cdd:PLN00113 476 RLENLDLSRNQFSGAvpRKLGSLSELMQLKLSENKLSGEipDELSSCKKLVSLDLSHN---QLSGQIPA 541
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
788-1010 |
1.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 788 DALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERHnerKEKLKQQLKAK 867
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 868 ELELEEIRKAYSTLNKKWHDKGEllsNLETQVKEVKEKFENKEKKLRAERDRSLELQKDAVEKLQNmDDAFKRQVDAIVE 947
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIE 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749331 948 AHQTEITQLANEKQRYIEcanlKVQQIEDEMRGL---LEETCKNKKLMEEKIKQLACAISDIQKEM 1010
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTE----EYAELKEELEDLraeLEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
401-647 |
3.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 401 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQAnekKDVHSQAIITTDRLKDA-IFKERHCKA-QLeviVHRLQNEI 478
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLSLEQKLSVAqAAHSQFEQAyQL---VRKIAGEV 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 479 -----KKLTIELM------KARDQQEDHIR-HLRTLERALEKMEKQKAQQQQAQMRLIQ----EVELKASAADREINL-- 540
Cdd:PRK04863 490 srseaWDVARELLrrlreqRHLAEQLQQLRmRLSELEQRLRQQQRAERLLAEFCKRLGKnlddEDELEQLQEELEARLes 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 541 ----------LRTSLRQEKEQVQQLHDLLALKEQEHR--QEIETR------EFFNDAEFQDALTKRLSKEERKHEQEVKE 602
Cdd:PRK04863 570 lsesvseareRRMALRQQLEQLQARIQRLAARAPAWLaaQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTVERDE 649
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958749331 603 YQEKINILNQQYLDL---ENEFRIALTVEARRFKDV--QDGFEDVATELA 647
Cdd:PRK04863 650 LAARKQALDEEIERLsqpGGSEDPRLNALAERFGGVllSEIYDDVSLEDA 699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-622 |
4.33e-03 |
|
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: 41.20 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 392 DKSASNDNTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTD-------RLKDAIFKERHCK 464
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 465 AQLEVIVHRLQNEIKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAAD------REI 538
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelseelREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 539 NLLRTSLRQEKEQVQQLHDLLALKEQEHRQEIET-----REFFND-AEFQDALTKRLSKEERKHEQEVKEYQEKINILNQ 612
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
250
....*....|
gi 1958749331 613 QYLDLENEFR 622
Cdd:TIGR02168 987 VNLAAIEEYE 996
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
14-182 |
4.03e-26 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 107.56 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 14 KACTELSLDSSLHAINLHCNNISKITSIDHIWNLRHLDLSSNQISQIEGLNTLTKLCTLNLSCNLITRVEGLEALVN--- 90
Cdd:cd21340 15 TKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLTNlee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 91 ---------------------------LTRLNLSYNHISDLSGLIPLHglkyKLRYIDLHSNYIDSIHHLLQCTVGLHFL 143
Cdd:cd21340 95 lhienqrlppgekltfdprslaalsnsLRVLNISGNNIDSLEPLAPLR----NLEQLDASNNQISDLEELLDLLSSWPSL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958749331 144 TNLILEkdgeGNPICLVPGYRAIILQTLPQLRILDCKNI 182
Cdd:cd21340 171 RELDLT----GNPVCKKPKYRDKIILASKSLEVLDGKEI 205
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
17-181 |
5.00e-12 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 69.19 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 17 TELSLDSSLHAINLHCNNISKITSIDHIWNLRHLDLSSNQISQI-EGLNTLTKLCTLNLSCNLITRV-EGLEALVNLTRL 94
Cdd:COG4886 85 LLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 95 NLSYNHISDLSGliPLHGLKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLVPGyraiILQTLPQL 174
Cdd:COG4886 165 DLSNNQLTDLPE--ELGNLT-NLKELDLSNNQITDLPEPLG---NLTNLEELDL----SGNQLTDLPE----PLANLTNL 230
|
....*..
gi 1958749331 175 RILDCKN 181
Cdd:COG4886 231 ETLDLSN 237
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
23-207 |
1.73e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 67.27 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 23 SSLHAINLHCNNISKI-TSIDHIWNLRHLDLSSNQISQIEGLNTLTKLCTLNLSCNLITRVEGLEALVNLTRLNLSYNHI 101
Cdd:COG4886 205 TNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 102 SDLS-GLIPLHGLKYKLRYIDLHSNYIDSIHHLLQCTVGLHFLTNLILEKDGEGNPICLVPGYRAIILQTLPQLRILDCK 180
Cdd:COG4886 285 TDLKlKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLT 364
|
170 180
....*....|....*....|....*..
gi 1958749331 181 NIFGEPVSLEEMNSSHLQCFEGLLDNL 207
Cdd:COG4886 365 LLLTLGLLGLLEATLLTLALLLLTLLL 391
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
528-897 |
1.01e-09 |
|
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: 62.77 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 528 ELKASAADREINLlrtslRQEKEQVQqlHDLLALKEQEHRQEIETREffndaefqdALTKRLSKEERKHEQEVKEYQEKI 607
Cdd:TIGR02168 206 ERQAEKAERYKEL-----KAELRELE--LALLVLRLEELREELEELQ---------EELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 608 NILNQQYLDLENEFRIAltvearrfkdvqdgfedvatelakskhaliwaQRKENESSSLIKDLTSMVKEQKTKLSEVCKL 687
Cdd:TIGR02168 270 EELRLEVSELEEEIEEL--------------------------------QKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 688 KQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTERkvwgHELAYQGTSLSQSRGKLEA 767
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL----EELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 768 QIESLCRENESLRKThesdcdalrikckiIEDQTETIRKLKdglQEKDGQIKMLQEQITiieKCSQEQLNEKTSQLDSIV 847
Cdd:TIGR02168 394 QIASLNNEIERLEAR--------------LERLEDRRERLQ---QEIEELLKKLEEAEL---KELQAELEELEEELEELQ 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958749331 848 EKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLET 897
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
405-999 |
3.99e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 405 VEQLDQERE-----MRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEvivhRLQNEIK 479
Cdd:COG1196 202 LEPLERQAEkaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 480 KLTIELmkaRDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSLRQEKEQVQQLHDLL 559
Cdd:COG1196 278 ELELEL---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 560 ALKEQEHRQEIETREFFNDAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKDVQDGF 639
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 640 EDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDKQKSIQIELL 719
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 720 KHEKNQLISELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRGKLEAQIESLCRENESlRKThesdcdalrikckiied 799
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-RAT----------------- 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 800 qTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQL-------DSIVEKLERHNERKEKLKQQLKAKELELE 872
Cdd:COG1196 576 -FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtllgrTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 873 EIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKKLRAERDRSLELQKDAVEKLQNMDDAFKRQVDAIVEAHQTE 952
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1958749331 953 ITQLANEKQRYIECANLKVQQIEDEMRgllEETCKNK-KLMEEKIKQL 999
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPD---LEELERElERLEREIEAL 779
|
|
| LRR_9 |
pfam14580 |
Leucine-rich repeat; |
50-182 |
1.49e-08 |
|
Leucine-rich repeat;
Pssm-ID: 405295 [Multi-domain] Cd Length: 175 Bit Score: 55.15 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 50 LDLSSNQISQIEGLNTLTKLCTLNLSCNLITRV-EGL-EALVNLTRLNLSYNHISDLSGLIPLHGLKyKLRYIDLHSNyi 127
Cdd:pfam14580 47 IDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLK-KLTFLSLLRN-- 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958749331 128 dsihhllqctvglhfltnlilekdgegnPICLVPGYRAIILQTLPQLRILDCKNI 182
Cdd:pfam14580 124 ----------------------------PVTNKPHYRLYVIYKVPQLRLLDFRKV 150
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-1010 |
2.50e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 401 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEVIVHRLQNEIKK 480
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 481 LTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAqmrlIQEVELKASAADREINLLRTSLRQEKEQVQQLHDLLA 560
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 561 LKEQE------HRQEIETREFFNDAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRialtvearrfkD 634
Cdd:TIGR02168 390 QLELQiaslnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-----------R 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 635 VQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDK--QK 712
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEgyEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 713 SIQIELLKHEKNQLISELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRGKLEAQIESLcRENESLRKTHESDCDALRI 792
Cdd:TIGR02168 538 AIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 793 -------KCKIIEDQTETIRKLKDGLQE-----KDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERHNERKEKL 860
Cdd:TIGR02168 617 alsyllgGVLVVDDLDNALELAKKLRPGyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 861 KQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKKLRAERDRSLELQKDAVEKLQNMDDAF-- 938
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEee 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 939 -----------KRQVDAIVEAHQTEITQLANEKQRY----IECANL--KVQQIEDEMRGL---LEETCKNKKLMEEKIKQ 998
Cdd:TIGR02168 777 laeaeaeieelEAQIEQLKEELKALREALDELRAELtllnEEAANLreRLESLERRIAATerrLEDLEEQIEELSEDIES 856
|
650
....*....|..
gi 1958749331 999 LACAISDIQKEM 1010
Cdd:TIGR02168 857 LAAEIEELEELI 868
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
740-1000 |
1.20e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 740 LRTERKVWGHEL-AYQGTSLSQSRGKLEAQIESLCRENESLRKTHESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQI 818
Cdd:COG1196 218 LKEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 819 KMLQEQITIiekcSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQ 898
Cdd:COG1196 298 ARLEQDIAR----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 899 VKEVKEKFENKEKKLRAERDRSLELQKDAVEKLQNMDDAFKRQvDAIVEAHQTEITQLANEKQRYIEcANLKVQQIEDEM 978
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEE-EEEALEEAAEEE 451
|
250 260
....*....|....*....|..
gi 1958749331 979 RGLLEETCKNKKLMEEKIKQLA 1000
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAA 473
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
491-876 |
2.60e-07 |
|
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: 54.52 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 491 QQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSLRQEKEQVQQLhdllalkEQEHRQEI 570
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------EEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 571 ETREFFndAEFQDALtkrlSKEERKHEQEVKEYQEKINILNQQYLDLENEF-RIALTVE--ARRFKDVQDGFEDVATELa 647
Cdd:pfam07888 108 ASSEEL--SEEKDAL----LAQRAAHEARIRELEEDIKTLTQRVLERETELeRMKERAKkaGAQRKEEEAERKQLQAKL- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 648 kskhaliwaQRKENESSSLIKDLTSMVKEQKTKLSEVCKlkqeaaanLQNQINTLEILIEDDKQKSIQIELLKHEKNQLI 727
Cdd:pfam07888 181 ---------QQTEEELRSLSKEFQELRNSLAQRDTQVLQ--------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 728 SELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRgkLEAQIESL----------------CRENESLRKTHESDCDAlr 791
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR--LQAAQLTLqladaslalregrarwAQERETLQQSAEADKDR-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 792 ikckiIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERhnERKEKLKQQLKAKELeL 871
Cdd:pfam07888 320 -----IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV--AQKEKEQLQAEKQEL-L 391
|
....*
gi 1958749331 872 EEIRK 876
Cdd:pfam07888 392 EYIRQ 396
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
403-1010 |
4.43e-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: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 403 SLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITT--------DRLKDAIfkeRHCKAQLEvivhRL 474
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSI---AEKERELE----DA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 475 QNEIKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAAD-----------------RE 537
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkdyrekleklkRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 538 INLLRTSLRQEKEQVQQLHDLLAlkeqEHRQEIETREFfNDAEFQDALtKRLSKEERKHEQEVKEYQEKINILNQQYLDL 617
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELA----DLNAAIAGIEA-KINELEEEK-EDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 618 ENEFRialtvearrfkDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAANLQ- 696
Cdd:TIGR02169 475 KEEYD-----------RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEv 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 697 ---NQINTleILIEDDKQKSIQIELLKHEK---------NQLISEL---------------------------------- 730
Cdd:TIGR02169 544 aagNRLNN--VVVEDDAVAKEAIELLKRRKagratflplNKMRDERrdlsilsedgvigfavdlvefdpkyepafkyvfg 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 731 ---------AAKESLIY-------------------GLRTERKVWGHELAYQGTSLSQSR--GKLEAQIESLCRENESLr 780
Cdd:TIGR02169 622 dtlvvedieAARRLMGKyrmvtlegelfeksgamtgGSRAPRGGILFSRSEPAELQRLRErlEGLKRELSSLQSELRRI- 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 781 kthESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQI-TIIEKCSQEQLNEKtsqldsivEKLERHNERKEK 859
Cdd:TIGR02169 701 ---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeEDLSSLEQEIENVK--------SELKELEARIEE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 860 LKQQLKAKELELEEIRKAYStlNKKWHDKGELLSNLETQVKEVKEKFENKEKKLRaERDRSLELQKDAVEKLQNMDDAFK 939
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLN-RLTLEKEYLEKEIQELQEQRIDLK 846
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749331 940 RQVDAIVEAHQTEITQLAnEKQRYIECANLKVQQIEDEMRGL---LEETCKNKKLMEEKIKQLACAISDIQKEM 1010
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLkkeRDELEAQLRELERKIEELEAQIEKKRKRL 919
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
464-1009 |
4.95e-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: 53.97 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 464 KAQLEVIVHRLQNEIKKLTIELMKARDQQEDHIRHLRT----LERALEKMEKQKAQQQQAQMRLIQEVELKASAADREIN 539
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 540 LLRTS-------LRQEKEQVQQLHDLLaLKEQEHRQEIETREffndAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQ 612
Cdd:pfam15921 153 ELEAAkclkedmLEDSNTQIEQLRKMM-LSHEGVLQEIRSIL----VDFEEASGKKIYEHDSMSTMHFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 613 QyLDLENEFrialtVEARRFKdVQDGFEDVATElAKSKHALIWAQRKENessslIKDLTSMVKEQKTKLSEVCKLKQEAA 692
Cdd:pfam15921 228 E-LDTEISY-----LKGRIFP-VEDQLEALKSE-SQNKIELLLQQHQDR-----IEQLISEHEVEITGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 693 ANLQNQintLEILIEDDKQKSI----QIELLKHEKNQLISEL-AAK---ESLIYGLRTERKVWGHELAYQGT---SLSQS 761
Cdd:pfam15921 295 NSIQSQ---LEIIQEQARNQNSmymrQLSDLESTVSQLRSELrEAKrmyEDKIEELEKQLVLANSELTEARTerdQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 762 RGKLEAQIESLC-----RENE-SLRKTHES---DCDAlrikckiieDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCS 832
Cdd:pfam15921 372 SGNLDDQLQKLLadlhkREKElSLEKEQNKrlwDRDT---------GNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 833 QEQL----------NEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVkev 902
Cdd:pfam15921 443 QGQMerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI--- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 903 keKFENKEKKLRAERDRSLELQKDAVEKLQNMDDAFKRQV---DAIVEAHQTEI---TQLANEKQRYIECANLKVQQIED 976
Cdd:pfam15921 520 --TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMaekDKVIEILRQQIenmTQLVGQHGRTAGAMQVEKAQLEK 597
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958749331 977 EM---RGLLEETCKNKKLMEEKIKQLACAISDIQKE 1009
Cdd:pfam15921 598 EIndrRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
640-995 |
5.43e-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: 53.92 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 640 EDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELL 719
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 720 KHEKNQLISELAAKESLIyglrterkvwghelayqgtslsqsrGKLEAQIESLcreneslrKTHESDcDALRIKCKIIED 799
Cdd:TIGR02169 757 KSELKELEARIEELEEDL-------------------------HKLEEALNDL--------EARLSH-SRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 800 QTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQE---QLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRK 876
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 877 AYSTLNKKwhdkgelLSNLETQVKEVKEKFENKEKKLRAERDRSLELQ---KDAVEKLQNMDDAFKRQV-----DAIVEA 948
Cdd:TIGR02169 883 RLGDLKKE-------RDELEAQLRELERKIEELEAQIEKKRKRLSELKaklEALEEELSEIEDPKGEDEeipeeELSLED 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958749331 949 HQTEITQLANEKQRYIECANLKVQQIEDEMRGLLEETCKNKKLMEEK 995
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
587-998 |
7.25e-07 |
|
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: 53.49 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 587 KRLSKEERKHEQEVKEYQEKINILNQQYLDLENEfriaLTVEARRFKDVQDGFEDVATELAKSKHALIwaqRKENESSSL 666
Cdd:TIGR04523 57 KNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDK----LKKNKDKINKLNSDLSKINSEIKNDKEQKN---KLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 667 IKDLTSMVKEQKTKLSEVCKLKQEaAANLQNQINTLEILIEDdkqksiqielLKHEKNQLISELAAKESLIYGLRTERKV 746
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEE----------LENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 747 WGHELAYQGTsLSQSRGKLEAQIESLCRENESLRKTHESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQIT 826
Cdd:TIGR04523 199 LELLLSNLKK-KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 827 IIEKcsqeQLNEKTSQLDSIVEKLERHNERKE-----KLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKE 901
Cdd:TIGR04523 278 QNNK----KIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 902 VKEKFENKEKKLRAERDRSLELQKDAVEKLQNMDDAFKRQVDaiVEAHQTEITQLANEKQRYIECANLKVQQIEDEMRGL 981
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND--LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
410
....*....|....*..
gi 1958749331 982 LEETCKNKKLMEEKIKQ 998
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQ 448
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
402-965 |
7.41e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 402 RSLVEQLDQEREMRWKAEQTEKKLM--DYIDELHKQANEKKdvhsQAIITTDRLKDAI--FKERHCKAQLEVIVHRLQNE 477
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAAR----ERLAELEYLRAALrlWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 478 IKKLTIELMKARDQQEDHIRHLRTLERALEKmekqkaqqqqAQMRLIQEVELKASAADREINLLRTSLRQEKEQVQQLH- 556
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRG----------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGl 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 557 -------DLLALKEQ--EHRQEIETREFFNDAEFQDALTKR--LSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIAL 625
Cdd:COG4913 374 plpasaeEFAALRAEaaALLEALEEELEALEEALAEAEAALrdLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 626 TVEARRFK------DVQDGFED--VATELAKSKHALiwaqrkenessSLIkdltsmVKEqktklsevcklKQEAAA---- 693
Cdd:COG4913 454 GLDEAELPfvgeliEVRPEEERwrGAIERVLGGFAL-----------TLL------VPP-----------EHYAAAlrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 694 ---NLQNQINTLEILIEDDKQKSIQIEllkheKNQLISELAAKESLIYG-LRTE-RKVWGH-------ELAYQGTSL--- 758
Cdd:COG4913 506 nrlHLRGRLVYERVRTGLPDPERPRLD-----PDSLAGKLDFKPHPFRAwLEAElGRRFDYvcvdspeELRRHPRAItra 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 759 ---SQSRGKLEAQIESLCRE-------NESLRKTHESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQI-TI 827
Cdd:COG4913 581 gqvKGNGTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 828 IEKCS-QEQLNEKTSQLDSIVE---KLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVkEVK 903
Cdd:COG4913 661 IDVASaEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAA 739
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958749331 904 EKFENKEKKLRAERDRSLELQKDAVEKLQnmdDAFKRQVDAIVEAHQTEITQLANEKQRYIE 965
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELR---ENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-919 |
1.89e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 401 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEVIVHRLQNEIKK 480
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 481 LTIELMKARDQQEDHIRHLRTLERALEKMEKqkaqqqqaqmRLIQEVELKASAADREINLLRTSLRQEKEQVQQLHDLLA 560
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEE----------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 561 LKEQEHRQEIETREFFNDAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKDVQDGFE 640
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 641 DVA---TELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEV---------------------CKLKQEAAANLQ 696
Cdd:COG1196 464 LLAellEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaalllaglrglagavavligVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 697 NQINTLEILIEDDKQKSIQIELLKHEK--------NQLISELAAKESLIYGLRTERKVWGHE-LAYQGTSLSQSRGKLEA 767
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKagratflpLDKIRARAALAAALARGAIGAAVDLVAsDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 768 QIESLCRENESLRKTHESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIV 847
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749331 848 EKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKKL-RAERDR 919
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELeRLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
475-737 |
2.42e-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: 51.60 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 475 QNEIKKLT--------------IELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAADReINL 540
Cdd:TIGR02168 676 RREIEELEekieeleekiaeleKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ-LSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 541 LRTSLRQEKEQVQQLHDLLALKEQEHRQEIETREffndaEFQDALTKRLSKEERKHEQEVKEYQE-KINILNQQYLDLEN 619
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELE-----AQIEQLKEELKALREALDELRAELTLlNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 620 EFRIALTveARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTsmvkEQKTKLSEVCKLKQEAAANLQNQI 699
Cdd:TIGR02168 830 ERRIAAT--ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL----NERASLEEALALLRSELEELSEEL 903
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958749331 700 NTLEiliEDDKQKSIQIELLKHEKNQLISELAAKESLI 737
Cdd:TIGR02168 904 RELE---SKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
680-952 |
2.68e-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: 51.60 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 680 KLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELaaKESLIYGLRTERKvwgheLAYQGTSLS 759
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEQ-----LEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 760 QSRGKLEAQIESLCR---ENESLRKTHESDCDALRIKCKIIEDQTETIRK-----------LKDGLQEKDGQIKMLQEQI 825
Cdd:TIGR02168 754 KELTELEAEIEELEErleEAEEELAEAEAEIEELEAQIEQLKEELKALREaldelraeltlLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 826 TIIEKC---SQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVkev 902
Cdd:TIGR02168 834 AATERRledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR--- 910
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958749331 903 kekfenkeKKLRAERDRSLELQKDAVEKLQNMDDAFKRQVDAIVEAHQTE 952
Cdd:TIGR02168 911 --------SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
356-898 |
5.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 356 RKMRQPYLRDLYVRSSLVNCNNLREVDEQKNGMIKVDKSASNDNTYRSLVEQLDQEREMRWKAEQTEKKLMDY---IDEL 432
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 433 HKQANEKKDV----HSQAIITTDRLKDAIFKERHCKAQLEViVHRLQNEIKKLTIELMKA----RDQQEDHIRHLRTLER 504
Cdd:PTZ00121 1335 KKKAEEAKKAaeaaKAEAEAAADEAEAAEEKAEAAEKKKEE-AKKKADAAKKKAEEKKKAdeakKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 505 ALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSlrQEKEQVQQLHDllalKEQEHRQEIETREFFNDAEFQDA 584
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKK----KAEEAKKADEAKKKAEEAKKADE 1487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 585 LTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKDVQDGFEDV--ATELAKSKHALIWAQRKENE 662
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAE 1567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 663 SSSLIKDLTSMVKEQktklSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRT 742
Cdd:PTZ00121 1568 EAKKAEEDKNMALRK----AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 743 ERKVWGHELAYQGTSLSQSRGKLEAQIESLCRENESLRKTHESDCDALRIKCKIIED--QTETIRKLKDGLQEKDGQIKM 820
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakKAEELKKKEAEEKKKAEELKK 1723
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749331 821 LQEqitiIEKCSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQ 898
Cdd:PTZ00121 1724 AEE----ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
477-753 |
5.18e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 477 EIKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQ---AQMRLIQEVELKASA-ADREINLLRTSLRQEKEQV 552
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 553 QQLHDLLALKEQEHRQEIETR-----EFFNDAEFQDALTKRLSKEERKHEQ---EVKEYQEKINILNQQYLDLENEFRIA 624
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLakleaEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEEVDKEFAET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 625 LtveaRRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAANLQNQINTLEI 704
Cdd:TIGR02169 384 R----DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958749331 705 LIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTERKVWGHELAY 753
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
476-890 |
5.81e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 476 NEIKKLTIELMKARDQQEDH---IRHLRTLERALEKMEKQKAQQQQAQMRLIQEVEL-----KASAADREINLLRTSLRQ 547
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 548 EKEQVQQLHDL----------LALKEQEHRQEIETREFFNDAEFQDALTK--RLSKEERKHEQEVKEYQEKINILNQQYL 615
Cdd:COG4717 151 LEERLEELRELeeeleeleaeLAELQEELEELLEQLSLATEEELQDLAEEleELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 616 DLENEFRIALTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKlSEVCKLKQEAAANL 695
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR-EKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 696 QNQINTLEiliedDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTERKVWghelayqgtslsqSRGKLEAQIESLCRE 775
Cdd:COG4717 310 LPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA-------------EELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 776 NESL-RKTHESDCDALRIKCKIIEDQ---TETIRKLKDGLQEKDGQIKMLQEQITiiEKCSQEQLNEKTSQLDSIVEKLE 851
Cdd:COG4717 372 IAALlAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958749331 852 RHNERKEKLKQQLKA--KELELEEIRKAYSTLNKKWHDKGE 890
Cdd:COG4717 450 ELREELAELEAELEQleEDGELAELLQELEELKAELRELAE 490
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
67-127 |
8.50e-06 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 44.05 E-value: 8.50e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749331 67 TKLCTLNLSCNLITRVEG--LEALVNLTRLNLSYNHISDLSGlIPLHGLKyKLRYIDLHSNYI 127
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSP-GAFSGLP-SLRYLDLSGNRL 61
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
815-1009 |
1.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 815 DGQIKMLQEQITIIekcsQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLsn 894
Cdd:COG3883 15 DPQIQAKQKELSEL----QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 895 letqvkevkekfenkekklrAERDRSLELQKDAVEKL------QNMDDAFKRQ--VDAIVEAHQTEITQLANEKQRyIEC 966
Cdd:COG3883 89 --------------------GERARALYRSGGSVSYLdvllgsESFSDFLDRLsaLSKIADADADLLEELKADKAE-LEA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749331 967 ANLKVQQIEDEMRGLLEETCKNKKLMEEKIKQLACAISDIQKE 1009
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
390-877 |
2.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 390 KVDKSASNDNTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKdvhsqaiittDRLKDaifkerhckaqLEV 469
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----------KEIEE-----------LEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 470 IVHRLqNEIKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQqaqmRLIQEVELKASAAdREINLLRTSLRQEK 549
Cdd:PRK03918 281 KVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE----ERIKELEEKEERL-EELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 550 EQVQQLHDLL--ALKEQEHRQEIETREFFNDAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQQYLDLE---NEFRIA 624
Cdd:PRK03918 355 EELEERHELYeeAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 625 ----------LTVEARR---------FKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIK--DLTSMVKEQKTKLSE 683
Cdd:PRK03918 435 kgkcpvcgreLTEEHRKelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 684 VCKLKQEAAANLQNQINTLEILIEDDkQKSIQIELlkHEKNQLISELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRG 763
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGE-IKSLKKEL--EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 764 KLEAQIESLCRENESLRKTHesdcDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKC--------SQEQ 835
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAE----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeeLREE 667
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958749331 836 LNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKA 877
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
464-713 |
2.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 464 KAQLEvivhRLQNEIKKLTIELMKARDQQEDHIRHLRTLERALEKMEkqkaqqqqaqmRLIQEVELKASAADREINLLRT 543
Cdd:COG4942 26 EAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----------RRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 544 SLRQEKEQVQQLHDLLA---LKEQEHRQEIETREFFNDAEFQDALT--KRLSKEERKHEQEVKEYQEKINILNQQYLDLE 618
Cdd:COG4942 91 EIAELRAELEAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 619 NEfrialtvearrfkdvQDGFEDVATELAKSKHALiwaQRKENESSSLIKDLTSMVKEQKTKLSEvcklKQEAAANLQNQ 698
Cdd:COG4942 171 AE---------------RAELEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAE----LQQEAEELEAL 228
|
250
....*....|....*
gi 1958749331 699 INTLEILIEDDKQKS 713
Cdd:COG4942 229 IARLEAEAAAAAERT 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
391-896 |
3.84e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 391 VDKSASNDNTY--RSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQ----------ANEKKDVHSQAIITTDRLKDAIF 458
Cdd:pfam15921 304 IQEQARNQNSMymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanselteARTERDQFSQESGNLDDQLQKLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 459 KERHcKAQLEVIVHRLQNeiKKL-------TIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQevelKA 531
Cdd:pfam15921 384 ADLH-KREKELSLEKEQN--KRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ----GK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 532 SAADREINLLRTSLRQEKEQVQQLHDLLALKeqehRQEIETREffndaEFQDALTKRLSKEERKHE---QEVKEYQEKIN 608
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAK----KMTLESSE-----RTVSDLTASLQEKERAIEatnAEITKLRSRVD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 609 ILNQQYLDLENEfrialtveARRFKDVQDGFEDVATELA-KSKHALIWAQRKEN-----------------ESSSLIKDl 670
Cdd:pfam15921 528 LKLQELQHLKNE--------GDHLRNVQTECEALKLQMAeKDKVIEILRQQIENmtqlvgqhgrtagamqvEKAQLEKE- 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 671 tsmVKEQKTKLSEVCKLKQEAAAN---LQNQINTLEI----LIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTE 743
Cdd:pfam15921 599 ---INDRRLELQEFKILKDKKDAKireLEARVSDLELekvkLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 744 RKVWGHELAYQGTSLSQSRGKLEAQIESLCRENESLRKTHESdcdalrikckiIEDQTETIRKLKDGLQE----KDGQIK 819
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS-----------MEGSDGHAMKVAMGMQKqitaKRGQID 744
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749331 820 MLQEQITIIEKCSQEQLNEKtsqldsiveklERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLE 896
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEK-----------HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
46-86 |
4.48e-05 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 41.46 E-value: 4.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958749331 46 NLRHLDLSSNQISQIEGLNTLTKLCTLNLS-CNLITRVEGLE 86
Cdd:pfam12799 2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSgNNKITDLSDLA 43
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
23-101 |
5.33e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.74 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 23 SSLHAINLHCNNIskiTSIDHIW-----NLRHLDLSSNQISQIEGlntltklctlnlscnlitrvEGLEALVNLTRLNLS 97
Cdd:pfam13855 1 PNLRSLDLSNNRL---TSLDDGAfkglsNLKVLDLSNNLLTTLSP--------------------GAFSGLPSLRYLDLS 57
|
....
gi 1958749331 98 YNHI 101
Cdd:pfam13855 58 GNRL 61
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
392-624 |
7.85e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 392 DKSASNDNTYRSLVEQLDQEREmrwKAEQTEKKLMDYidelhKQANEKKDVHSQAIITTDRLKDaifkerhckaqleviv 471
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRK---ELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSE---------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 472 hrLQNEIKKLTIELMKARDQqedhirhLRTLERALEKMEKQKAQQQQAqmRLIQEVELKASAADREINLLRTSLRQEKEQ 551
Cdd:COG3206 224 --LESQLAEARAELAEAEAR-------LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749331 552 VQQLHDLLALKEQEHRQEIETREFFNDAEFQdaltkRLSKEERKHEQEVKEYQEKINILN---QQYLDLENEFRIA 624
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELE-----ALQAREASLQAQLAQLEARLAELPeleAELRRLEREVEVA 363
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
19-185 |
7.97e-05 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 46.32 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 19 LSLDSSLHAINLHCNNISK------ITSIDHIWNLRHLDLSSNQISQ------IEGLNTLTKLCTLNLSCNLITrVEGLE 86
Cdd:COG5238 204 LTQNTTVTTLWLKRNPIGDegaeilAEALKGNKSLTTLDLSNNQIGDegvialAEALKNNTTVETLYLSGNQIG-AEGAI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 87 ALV-------NLTRLNLSYNHISDLSGLIPLHGLK--YKLRYIDLHSNYIDSihhllQCTVGL--HFLTNLILEK-DGEG 154
Cdd:COG5238 283 ALAkalqgntTLTSLDLSVNRIGDEGAIALAEGLQgnKTLHTLNLAYNGIGA-----QGAIALakALQENTTLHSlDLSD 357
|
170 180 190
....*....|....*....|....*....|....
gi 1958749331 155 NPIClVPGYRAII--LQTLPQLRILD-CKNIFGE 185
Cdd:COG5238 358 NQIG-DEGAIALAkyLEGNTTLRELNlGKNNIGK 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
660-884 |
9.74e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 660 ENES--SSLIKDLTSMVKEQ-KTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESL 736
Cdd:COG4717 31 PNEAgkSTLLAFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 737 IYGLRTERKVWGHELAYQgtSLSQSRGKLEAQIESLCRENESLRKTHESdcdalrikckiIEDQTETIRKLKDGLQEKDG 816
Cdd:COG4717 111 LEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERLEE-----------LRELEEELEELEAELAELQE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749331 817 QIKMLQEQITIIEKcsqEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKK 884
Cdd:COG4717 178 ELEELLEQLSLATE---EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
712-984 |
9.90e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 712 KSIQIELLKHEKNQLISELAAKESLIYGLRTERKVWGHELAYQGTSLSQSR---GKLEAQIESLCRENESLRKthesdcd 788
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevSELEEEIEELQKELYALAN------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 789 alrikckIIEDQTETIRKLKDGLQEKDGQIKMLQEQITiiekcsqeqlnEKTSQLDSIVEKLERHNERKEKLKQQLKAKE 868
Cdd:TIGR02168 296 -------EISRLEQQKQILRERLANLERQLEELEAQLE-----------ELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 869 LELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKKLRAERDRsLELQKDAVEKL-QNMDDAFKRQVDAIVE 947
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLqQEIEELLKKLEEAELK 436
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958749331 948 AHQTEITQLANEKQRYIECANLKVQQIEdEMRGLLEE 984
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALE-ELREELEE 472
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
832-1010 |
1.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 832 SQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEK 911
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 912 KLRAERDRsLELQKDAVEKL------------QNMDDAFKRQ--VDAIVEAHQTEITQLANEKQRyIECANLKVQQIEDE 977
Cdd:COG4942 98 ELEAQKEE-LAELLRALYRLgrqpplalllspEDFLDAVRRLqyLKYLAPARREQAEELRADLAE-LAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 1958749331 978 MRGLLEETCKNKKLMEEKIKQLACAISDIQKEM 1010
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
67-107 |
1.53e-04 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 39.92 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958749331 67 TKLCTLNLSCNLITRVEGLEALVNLTRLNLSYN-HISDLSGL 107
Cdd:pfam12799 1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDL 42
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
419-875 |
1.87e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 419 EQTEKKLMDYIDELhkqaNEKKDvhsQAIITTDRLKDAIFKERHCKAQLEVivhrLQNEIKKLTIELMKARDQQEDHIRH 498
Cdd:PRK02224 212 ESELAELDEEIERY----EEQRE---QARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 499 LRTLERALEKMEKQKAQqqqaqmrLIQEVELKaSAADREINLLRTSLRQEKEQVQQLHDLLALKEQEHRQEIET-REFFN 577
Cdd:PRK02224 281 VRDLRERLEELEEERDD-------LLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESlREDAD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 578 DAEfQDALTKR-----LSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTvearRFKDVQDGFEDVATELAK---- 648
Cdd:PRK02224 353 DLE-ERAEELReeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV----DLGNAEDFLEELREERDElrer 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 649 ------------------------------------SKHALIWAQRKEN--ESSSLIKDLTSMVKEQKTKLSEVCKLKQE 690
Cdd:PRK02224 428 eaeleatlrtarerveeaealleagkcpecgqpvegSPHVETIEEDRERveELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 691 AA--ANLQNQINTLEILIEDDK----QKSIQIELLKHEKNQLISELAAKESLIYGLRTERKVWGHELAyqgtSLSQSRGK 764
Cdd:PRK02224 508 EDriERLEERREDLEELIAERRetieEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA----ELNSKLAE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 765 LEAQIESLCRENESL--RKTHESDCDALRIKckiIEDQTETIRKLKDGLQEKDGQIKMLQEQI--TIIEKcSQEQLNEKT 840
Cdd:PRK02224 584 LKERIESLERIRTLLaaIADAEDEIERLREK---REALAELNDERRERLAEKRERKRELEAEFdeARIEE-AREDKERAE 659
|
490 500 510
....*....|....*....|....*....|....*
gi 1958749331 841 SQLDSIVEKLERHNERKEKLKQQLKAKELELEEIR 875
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
476-898 |
1.88e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 476 NEIKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKasaaDREINLLRTSLRQEKEQVQQL 555
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 556 HDLLALKEQEHRQEIETREFFNDAEFQDALT----KRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVearr 631
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE---- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 632 FKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQeaaanlQNQINTLEILIEDDKQ 711
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE------QDWNKELKSELKNQEK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 712 KSIQIELLKHEKNQLISELaakESLIYGLRTERKvwghELAYQGTSLSQSRGKLEAQIESLCRENESLRKTHESdcdaLR 791
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQL---NEQISQLKKELT----NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN----LE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 792 IKCKIIEDQTETIRKLKdglQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVE----------KLERHNERKEKLK 861
Cdd:TIGR04523 391 SQINDLESKIQNQEKLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDltnqdsvkelIIKNLDNTRESLE 467
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958749331 862 QQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQ 898
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
18-127 |
1.92e-04 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 44.65 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 18 ELSLDSSLHAINLHCNNISK--ITSIDHIW----NLRHLDLSSNQISQI------EGLNTLTKLCTLNLSCNLITRVeGL 85
Cdd:cd00116 160 ALRANRDLKELNLANNGIGDagIRALAEGLkancNLEVLDLNNNGLTDEgasalaETLASLKSLEVLNLGDNNLTDA-GA 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958749331 86 EALVN--------LTRLNLSYNHISDLSGLIPLHGLKYK--LRYIDLHSNYI 127
Cdd:cd00116 239 AALASallspnisLLTLSLSCNDITDDGAKDLAEVLAEKesLLELDLRGNKF 290
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
591-905 |
2.50e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 591 KEERKHEQEVKEYQEKINILNQQYLDLENEFrialtvearrfKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDL 670
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKEL-----------TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 671 TSMVKEQKTKLSEVCKLKQEaaanLQNQINTLEiliEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTERKvwghe 750
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQ----KDEQIKKLQ---QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK----- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 751 layqgtSLSQSRGKLEAQIESLCRENESLRKTHESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEK 830
Cdd:TIGR04523 458 ------NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749331 831 csqeQLNEKTSQLDSIVEKLERHNER--KEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEK 905
Cdd:TIGR04523 532 ----EKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
417-896 |
5.19e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 417 KAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTDRLKDAifkerhcKAQLEVIVHrlqnEIKKLTIELMKARDQQEDHI 496
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK-------EKELEEVLR----EINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 497 RHLRTLERALEKMEKQKAQQQQAQMRLiQEVELKASAADREINLLRTSLRQEKEQVQQLHDLLAlKEQEHRQEIETREFF 576
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEKVKELKELKE-KAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 577 NDAEFQ------------DALTKRLSKEERKhEQEVKEYQEKINILNQQYLDLENEFRI-----ALTVEARRFKDVQDGF 639
Cdd:PRK03918 306 LDELREiekrlsrleeeiNGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELyeeakAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 640 --EDVATELAKSKHALIWAQRKENESSSLIKDLTSMVKEQKTKLSE---------VCK--LKQEAAANLQNQInTLEIL- 705
Cdd:PRK03918 385 tpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpVCGreLTEEHRKELLEEY-TAELKr 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 706 IEDDKQKSI-QIELLKHEKNQLISELAAKESLIYGlrterkvwgHELAYQGTSLSQSRGKLEaqIESLCRENESLRKTHE 784
Cdd:PRK03918 464 IEKELKEIEeKERKLRKELRELEKVLKKESELIKL---------KELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 785 sDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQL 864
Cdd:PRK03918 533 -KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510
....*....|....*....|....*....|..
gi 1958749331 865 KAKELELEEIRKAYSTLNKKWHDKGELLSNLE 896
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
664-1009 |
5.47e-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: 44.04 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 664 SSLIKDLTSMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIEL-------LKHEKNQLISELAAKESL 736
Cdd:pfam10174 225 PAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVykshskfMKNKIDQLKQELSKKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 737 IYGLRTerkvwghELAYQGTSLSQSRGKLEAQIESLCREnESLRKTHESDCDALRI-----------KCKIIEDQTE--- 802
Cdd:pfam10174 305 LLALQT-------KLETLTNQNSDCKQHIEVLKESLTAK-EQRAAILQTEVDALRLrleekesflnkKTKQLQDLTEeks 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 803 ----TIRKLKDGLQEKDGQIKMLQEQITIIekcsQEQLNEKTSQLDSIVEK-----------------LERHNERKEKLK 861
Cdd:pfam10174 377 tlagEIRDLKDMLDVKERKINVLQKKIENL----QEQLRDKDKQLAGLKERvkslqtdssntdtalttLEEALSEKERII 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 862 QQLK-AKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKklRAERDRSLELQKDAVEK-----LQNMD 935
Cdd:pfam10174 453 ERLKeQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKE--HASSLASSGLKKDSKLKsleiaVEQKK 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 936 DAFKRQVDAIVEAHQTE------------ITQLANEKQRYIECANlKVQQIEDEMRGLLEETCKNKKLMEEKIKQLACAI 1003
Cdd:pfam10174 531 EECSKLENQLKKAHNAEeavrtnpeindrIRLLEQEVARYKEESG-KAQAEVERLLGILREVENEKNDKDKKIAELESLT 609
|
....*.
gi 1958749331 1004 SDIQKE 1009
Cdd:pfam10174 610 LRQMKE 615
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
675-873 |
5.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 675 KEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESLIYGLRTERKVWGHELAYQ 754
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 755 GTSLSqsrgKLEAQIESlcrenESLrktheSD----CDALRikcKIIEDQTETIRKLKDGLQEKDGQIKMLQEQitiiek 830
Cdd:COG3883 99 GGSVS----YLDVLLGS-----ESF-----SDfldrLSALS---KIADADADLLEELKADKAELEAKKAELEAK------ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958749331 831 csQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEE 873
Cdd:COG3883 156 --LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
524-786 |
6.06e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 524 IQEVELKASAADREINLLRTSLRQEKEQVQQLHDLLalkeQEHRQEIetreffndaefqdaltKRLSKEERKHEQEVKEY 603
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL----AALERRI----------------AALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 604 QEKINILNQQYLDLENEFRIALTVEARRFKDVQD-GFEDVATELAKSKHALIwAQRKENESSSLIKDLTSMVKEQKTKLS 682
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 683 EVCKLKQEaaanLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISELAAKESliyglrterkvwghELAYQGTSLSQSR 762
Cdd:COG4942 161 ELAALRAE----LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA--------------ELAAELAELQQEA 222
|
250 260
....*....|....*....|....
gi 1958749331 763 GKLEAQIESLCRENESLRKTHESD 786
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
526-1009 |
6.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 526 EVELKASAADREINLLRTSLRQEKEQVQQLHDLLALKEqEHRQEIETREffndAEFQDaLTKRLSKEERKHEqevkEYQE 605
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-ERREELETLE----AEIED-LRETIAETERERE----ELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 606 KINILNQQYLDLENEFRIAL-----------TVEARRfKDVQDGFEDVATELAKSKHAliwAQRKENESSSL---IKDLT 671
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLaeaglddadaeAVEARR-EELEDRDEELRDRLEECRVA---AQAHNEEAESLredADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 672 SMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEddkqksiQIELLKHEKNQLISELAAKESLIYGLRTERKvwghel 751
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELREERD------ 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 752 ayqgtSLSQSRGKLEAQIESL---CRENESLRK-----THESDCDALRIKCKIIEDQtETIRKLKDGLQEKDGQIKMLQE 823
Cdd:PRK02224 423 -----ELREREAELEATLRTArerVEEAEALLEagkcpECGQPVEGSPHVETIEEDR-ERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 824 QITiiekcSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVK 903
Cdd:PRK02224 497 RLE-----RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 904 EKFenkekklrAERDRSLELQKDAVEKLQNMDDAFKRQVDAIVEAHQ-----TEITQLANEKQRYIECANLKVQQIEDEM 978
Cdd:PRK02224 572 EEV--------AELNSKLAELKERIESLERIRTLLAAIADAEDEIERlrekrEALAELNDERRERLAEKRERKRELEAEF 643
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958749331 979 RGLLEETCKNKKL--------MEEKIKQLACAISDIQKE 1009
Cdd:PRK02224 644 DEARIEEAREDKEraeeyleqVEEKLDELREERDDLQAE 682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
690-941 |
7.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 690 EAAANLQNQINTLEIL---IEDDKQksiQIELLKH--EKNQLISELAAKESLIYGLRTERKVWGHELAYQgtslsqsrgK 764
Cdd:COG4913 225 EAADALVEHFDDLERAheaLEDARE---QIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLE---------L 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 765 LEAQIEslcrENESLRKTHESDCDALRIKckiIEDQTETIRKLKDGLQEKDGQIKmlqEQItiiekcsQEQLNEKTSQLD 844
Cdd:COG4913 293 LEAELE----ELRAELARLEAELERLEAR---LDALREELDELEAQIRGNGGDRL---EQL-------EREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 845 SIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEKKLRAERdRSLELQ 924
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI-ASLERR 434
|
250
....*....|....*...
gi 1958749331 925 KDAV-EKLQNMDDAFKRQ 941
Cdd:COG4913 435 KSNIpARLLALRDALAEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
499-877 |
8.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 499 LRTLERALEKMEKqkaqqqqaqmrliQ-EV-----ELKASAADREINLLRTSLRQEKEQVQQLHDLLALKEQEHRQEIET 572
Cdd:COG1196 195 LGELERQLEPLER-------------QaEKaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 573 reffndaefQDALTKRLSKEERKH---EQEVKEYQEKINILNQQYLDLENEfriaLTVEARRFKDVQDGFEDVATELAKS 649
Cdd:COG1196 262 ---------LAELEAELEELRLELeelELELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 650 KHALIWAQRKENESSSLIKDLTSMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKNQLISE 729
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 730 LAAKESLIYGLRTERKvwghelayqgtslsqsrgKLEAQIESLCRENESLRkthesdcdalrikckiiEDQTETIRKLKD 809
Cdd:COG1196 409 EEALLERLERLEEELE------------------ELEEALAELEEEEEEEE-----------------EALEEAAEEEAE 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749331 810 GLQEKDGQIKMLQEQitiiekcsQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKA 877
Cdd:COG1196 454 LEEEEEALLELLAEL--------LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
46-110 |
9.37e-04 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 43.30 E-value: 9.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749331 46 NLRHLDLSSNQISQI--EGLNTLTKLCTLNLSCNLITRV--EGLEALVNLTRLNLSYNhisDLSGLIPL 110
Cdd:PLN00113 476 RLENLDLSRNQFSGAvpRKLGSLSELMQLKLSENKLSGEipDELSSCKKLVSLDLSHN---QLSGQIPA 541
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
32-127 |
1.19e-03 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 42.91 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 32 CNNISKITSID---------------HIWNLRHLDLSSNQIS-QIEG--LNTLTKLCTLNLSCNLITRVEGLEALVNLTR 93
Cdd:PLN00113 65 CNNSSRVVSIDlsgknisgkissaifRLPYIQTINLSNNQLSgPIPDdiFTTSSSLRYLNLSNNNFTGSIPRGSIPNLET 144
|
90 100 110
....*....|....*....|....*....|....*
gi 1958749331 94 LNLSYNHisdLSGLIPLH-GLKYKLRYIDLHSNYI 127
Cdd:PLN00113 145 LDLSNNM---LSGEIPNDiGSFSSLKVLDLGGNVL 176
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
19-127 |
1.26e-03 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 42.47 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 19 LSLDSSLHAINLHCNNISK------ITSIDHIWNLRHLDLSSNQISQ------IEGLNTLTKLCTLNLSCNLITrVEGLE 86
Cdd:COG5238 288 LQGNTTLTSLDLSVNRIGDegaialAEGLQGNKTLHTLNLAYNGIGAqgaialAKALQENTTLHSLDLSDNQIG-DEGAI 366
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958749331 87 ALV-------NLTRLNLSYNHISDLSGLIPLHGLKY-KLRYIDLHSNYI 127
Cdd:COG5238 367 ALAkylegntTLRELNLGKNNIGKQGAEALIDALQTnRLHTLILDGNLI 415
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
752-962 |
1.66e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 752 AYQGTSLSQSRGKLEAQIESLCRENESLRKTHESDCDALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKc 831
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 832 SQEQLNEKTSQLDSIVEKLERHNERKEKLKQQlkaKELELEEIRKAYSTLNKKWHDKGELLSNLETQVKEVKEKFENKEK 911
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958749331 912 KLRAERDRsLELQKDAVEKLQNMDDAFKRQVDAIVEAHQTEITQLANEKQR 962
Cdd:COG4942 175 ELEALLAE-LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
90-157 |
1.88e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 37.50 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749331 90 NLTRLNLSYNHISDLSGlIPLHGLKyKLRYIDLHSNYIDSIHhlLQCTVGLHFLTNLILekdgEGNPI 157
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDD-GAFKGLS-NLKVLDLSNNLLTTLS--PGAFSGLPSLRYLDL----SGNRL 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
788-1010 |
1.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 788 DALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERHnerKEKLKQQLKAK 867
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 868 ELELEEIRKAYSTLNKKWHDKGEllsNLETQVKEVKEKFENKEKKLRAERDRSLELQKDAVEKLQNmDDAFKRQVDAIVE 947
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIE 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749331 948 AHQTEITQLANEKQRYIEcanlKVQQIEDEMRGL---LEETCKNKKLMEEKIKQLACAISDIQKEM 1010
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTE----EYAELKEELEDLraeLEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
412-899 |
2.28e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 412 REMRWKAEQTEKKLMDYIDE---LHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEVIVHRLQNEIKKLTIELMKA 488
Cdd:pfam05483 123 QELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 489 RDQQEDhirhlrtlerALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLrtsLRQEKEQVQQLHDLLALKEqehrq 568
Cdd:pfam05483 203 RVQAEN----------ARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLL---LIQITEKENKMKDLTFLLE----- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 569 eiETREFFNDAEFQDALTKRLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKDVQDGFEDVATEL-- 646
Cdd:pfam05483 265 --ESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnk 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 647 AKSKHALIWA-----------------QRKENESSSLiKDLTSMVKEQKTKLSEVCKLKqeaaanlqnqiNTLEILIEDD 709
Cdd:pfam05483 343 AKAAHSFVVTefeattcsleellrteqQRLEKNEDQL-KIITMELQKKSSELEEMTKFK-----------NNKEVELEEL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 710 KQKSIQIELLKHEKNQ---LISELAAKESLIYGLRTERKVWGHELAYQGTSLSQSRGKLEAQIESLCRE--NESLRKTH- 783
Cdd:pfam05483 411 KKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEleKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 784 ESDCDALRIKCKII-----------EDQTETIRKLKDGLQEKDGQIKMLQEQITIIE-----------------KCSQEQ 835
Cdd:pfam05483 491 TAHCDKLLLENKELtqeasdmtlelKKHQEDIINCKKQEERMLKQIENLEEKEMNLRdelesvreefiqkgdevKCKLDK 570
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958749331 836 LNEKTSQLDSIVEKLERHNERKEK----LKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLETQV 899
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENkcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV 638
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
625-896 |
2.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 625 LTVEARRfKDVQDGFE-DVATELAKSKHALIWAQRKENESSSLIKDL-TSMVKEQKTKLSEVCKLKQEAAANLQNQINTL 702
Cdd:PHA02562 147 LSAPARR-KLVEDLLDiSVLSEMDKLNKDKIRELNQQIQTLDMKIDHiQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 703 EILIEDDKQksiQIELLKHEKNQLISELAAKESLIYGLRTERkvwghelayqgtslsqsrGKLEAQIESLCRENESLRKT 782
Cdd:PHA02562 226 VEEAKTIKA---EIEELTDELLNLVMDIEDPSAALNKLNTAA------------------AKIKSKIEQFQKVIKMYEKG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 783 HEsdCDAlrikCK-IIEDQTETIRKLKDGLQEKDGQIKMLQEQItiiekcsqEQLNEKTSQLDSIVEKLERHNERKEKLK 861
Cdd:PHA02562 285 GV--CPT----CTqQISEGPDRITKIKDKLKELQHSLEKLDTAI--------DELEEIMDEFNEQSKKLLELKNKISTNK 350
|
250 260 270
....*....|....*....|....*....|....*
gi 1958749331 862 QQLKAKELELEEIRKAYSTLNKKWHDKGELLSNLE 896
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
404-878 |
2.87e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 404 LVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEVIVHRLQ--NEIKKL 481
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQklQSLCKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 482 TIELMKARDQQEDHIRHLRTLER---ALEKMEKQKAQQQQAQMRLIQEVELKASAADREINLLRTSLRQEKEQVQQLHDL 558
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 559 L-------------ALKEQEHRQEIETREFFNDAEFQDAL---------------TKRLSKEERKHEQEVKEYQEKINIL 610
Cdd:TIGR00618 482 HlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIDnpgpltrrmqrgeqtYAQLETSEEDVYHQLTSERKQRASL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 611 NQQYLDLENEFRI------ALTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKE------------------NESSSL 666
Cdd:TIGR00618 562 KEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklqpeqdlqdvrlhlqQCSQEL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 667 IKDLTSMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSI-QIELLKHEKNQLISELAAKESLIYGLRTERK 745
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKeQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 746 VW-------GHELAYQGTSLSQSRGKLEAQIESLCRENESLrkthesdcDALRIKCKIIEDQTETirKLKDGLQEKDGQI 818
Cdd:TIGR00618 722 EIenassslGSDLAAREDALNQSLKELMHQARTVLKARTEA--------HFNNNEEVTAALQTGA--ELSHLAAEIQFFN 791
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 819 KMLQEQITIIEKCSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAY 878
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
401-647 |
3.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 401 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQAnekKDVHSQAIITTDRLKDA-IFKERHCKA-QLeviVHRLQNEI 478
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLSLEQKLSVAqAAHSQFEQAyQL---VRKIAGEV 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 479 -----KKLTIELM------KARDQQEDHIR-HLRTLERALEKMEKQKAQQQQAQMRLIQ----EVELKASAADREINL-- 540
Cdd:PRK04863 490 srseaWDVARELLrrlreqRHLAEQLQQLRmRLSELEQRLRQQQRAERLLAEFCKRLGKnlddEDELEQLQEELEARLes 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 541 ----------LRTSLRQEKEQVQQLHDLLALKEQEHR--QEIETR------EFFNDAEFQDALTKRLSKEERKHEQEVKE 602
Cdd:PRK04863 570 lsesvseareRRMALRQQLEQLQARIQRLAARAPAWLaaQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTVERDE 649
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958749331 603 YQEKINILNQQYLDL---ENEFRIALTVEARRFKDV--QDGFEDVATELA 647
Cdd:PRK04863 650 LAARKQALDEEIERLsqpGGSEDPRLNALAERFGGVllSEIYDDVSLEDA 699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-622 |
4.33e-03 |
|
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: 41.20 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 392 DKSASNDNTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQANEKKDVHSQAIITTD-------RLKDAIFKERHCK 464
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelraeltLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 465 AQLEVIVHRLQNEIKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQQAQMRLIQEVELKASAAD------REI 538
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelseelREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 539 NLLRTSLRQEKEQVQQLHDLLALKEQEHRQEIET-----REFFND-AEFQDALTKRLSKEERKHEQEVKEYQEKINILNQ 612
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
250
....*....|
gi 1958749331 613 QYLDLENEFR 622
Cdd:TIGR02168 987 VNLAAIEEYE 996
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
668-884 |
5.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 668 KDLTSMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDKQksiQIELLKHEKNQLISELAAKESLIYGLRTERKVW 747
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKA-LLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 748 GHELAYQGTSL----SQSRGKLEAQIESLcreNESLRKTHesdcdALRIKCKIIEDQTETIRKLKDGLQEKDGQIKMLQE 823
Cdd:COG4942 103 KEELAELLRALyrlgRQPPLALLLSPEDF---LDAVRRLQ-----YLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749331 824 QITIIEKCSQEQLNEKTSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKK 884
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
406-715 |
5.34e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 406 EQLDQEREmrwKAEQTEKKLMDYIDELhkqanekkdvhSQAIITTDRLKDAIFKErhcKAQLEVIVHRLQNEIKKLtiel 485
Cdd:TIGR02169 726 EQLEQEEE---KLKERLEELEEDLSSL-----------EQEIENVKSELKELEAR---IEELEEDLHKLEEALNDL---- 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 486 mkardqqEDHIRH--LRTLERALEKMEKQkaqqqqaqmrlIQEVELKASAADREIN---LLRTSLRQEKEQVQQLHDLLA 560
Cdd:TIGR02169 785 -------EARLSHsrIPEIQAELSKLEEE-----------VSRIEARLREIEQKLNrltLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 561 LKEQEHRQEIETreffndaefqdaltkrLSKEERKHEQEVKEYQEKINILNQQYLDLENEFRialtvearrfkdvqdgfe 640
Cdd:TIGR02169 847 EQIKSIEKEIEN----------------LNGKKEELEEELEELEAALRDLESRLGDLKKERD------------------ 892
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749331 641 dvatELAKSKHALiwaQRKENESSSLIKDLTSMVKEQKTKLSEVC-KLKQEAAANLQNQINTLEILIEDDKQKSIQ 715
Cdd:TIGR02169 893 ----ELEAQLREL---ERKIEELEAQIEKKRKRLSELKAKLEALEeELSEIEDPKGEDEEIPEEELSLEDVQAELQ 961
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
430-655 |
6.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 430 DELHKQANEKKDVHSQAIITTDRLKDAIFKERHCKAQLEvivhRLQNEIKKLTIELMKARDQQEDHIRHLRTLERALEKM 509
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 510 EKQKAQQQQAQMRLIQ---------EVELKASAAD-----REINLLRTSLRQEKEQVQQL-HDLLALKEQEHRQEIETRE 574
Cdd:COG4942 96 RAELEAQKEELAELLRalyrlgrqpPLALLLSPEDfldavRRLQYLKYLAPARREQAEELrADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749331 575 FFNDAEFQDALTKRLSKEE-------RKHEQEVKEYQEKINILNQQYLDLENEFRIALTVEARRFKdvqdgfEDVATELA 647
Cdd:COG4942 176 LEALLAELEEERAALEALKaerqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE------RTPAAGFA 249
|
....*...
gi 1958749331 648 KSKHALIW 655
Cdd:COG4942 250 ALKGKLPW 257
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
24-64 |
8.27e-03 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 35.30 E-value: 8.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958749331 24 SLHAINLHCNNISKITSIDHIWNLRHLDLSSN-QISQIEGLN 64
Cdd:pfam12799 2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
|
|
| |
