|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
30-386 |
7.57e-103 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 315.71 E-value: 7.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKV 109
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 110 REEFKELKARNTKKegdliaaqarlkdleallnskeaalstaLSEKRTLEGELHDLRgqvakleaalgeakKQLQDEMLR 189
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 190 RVDAENRLQTMKEELDFQKNIYSEELRETKRRH--ETRLVEIDNGKQREfesrLADALQELRAQHEDQVEQYKKELEKTY 267
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 268 SAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAE 347
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 2244986507 348 MRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
434-541 |
3.39e-21 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 89.02 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 434 ARTSGRVAVEEVDEEG-----KFVRLRNKSNEDQSMGNWQIKRQNGDdpllTYRFPPKFTLKAGQVVTIWAAG----AGA 504
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2244986507 505 THSPPTDLVWKAQNTWgcgnslrTALINSTGEEVAMR 541
Cdd:pfam00932 77 GYWGPSNAVWNNGGDA-------VALYDANGELVDSV 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-362 |
2.54e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 10 TRSGAQASSTPLSPTR-ITRLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREvsgikaayEA 83
Cdd:TIGR02168 662 TGGSAKTNSSILERRReIEELEEKieeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--------RK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 84 ELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELH 163
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 164 DLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEEL-DFQKNIysEELRETKRRHETRLVEIDNGKQREFEsrla 242
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeSLAAEI--EELEELIEELESELEALLNERASLEE---- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 243 dALQELRAQHEDQVEQykkelEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQK---QLAAKEAK 319
Cdd:TIGR02168 888 -ALALLRSELEELSEE-----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALEN 961
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2244986507 320 LRDLEDSLARERdtsrrlLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:TIGR02168 962 KIEDDEEEARRR------LKRLENKIKELGPVNLAAIEEYEEL 998
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-368 |
2.90e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 32 KEDLQELNDRLAVYIDRVRSLET--ENAGLRLRITESEEVVSREVSGIK--------AAYEAELGDARKTLDSVAKERAR 101
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERqaEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 102 LQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 182 QLQdemlrrvDAENRLQTMKEELDFQKniysEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKK 261
Cdd:COG1196 345 ELE-------EAEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 262 ELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEK 341
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340
....*....|....*....|....*..
gi 2244986507 342 EREmAEMRARMQQQLDEYQELLDIKLA 368
Cdd:COG1196 494 LLL-LEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-361 |
4.36e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 32 KEDLQELNDRLAVYIDRVRSLET--ENAGLRLRITESEEVVSREVSGIKA-AYEAELGDARKTLDSVAKERARLQLELSK 108
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERqaEKAERYKELKAELRELELALLVLRLeELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 109 VREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEaalstalSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 188
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-------QQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 189 RRVDAENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKELEktyS 268
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELE--EQLETLRSKVAQLELQIASLNNEIERLEARLE---R 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 269 AKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARerdtSRRLLAEKEREMAEM 348
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALDAAERELAQL 487
|
330
....*....|....*....
gi 2244986507 349 RAR------MQQQLDEYQE 361
Cdd:TIGR02168 488 QARldslerLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-387 |
9.63e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 110 REEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLR 189
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 190 RVDAENRlqtmKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRlaDALQELRAQHEDQveqykkelektySA 269
Cdd:TIGR02168 756 LTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR--EALDELRAELTLL------------NE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 270 KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMA 346
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELE 897
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2244986507 347 EMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-381 |
1.86e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 73 EVSGIkAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEgdliaaqaRLKDLEALLnsKEAALSTAL 152
Cdd:TIGR02169 161 EIAGV-AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--------RYQALLKEK--REYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 153 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqKNIYSEELRETKRRHETRLVEIDN- 231
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 232 -GKQREFESRLADAlQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 310
Cdd:TIGR02169 307 eRSIAEKERELEDA-EERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2244986507 311 KQLAAKEAKLRDLEDSLARERDTSRRLLAEKER---EMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLE 381
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-352 |
4.67e-11 |
|
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: 65.17 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 96 AKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA 175
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 176 LGEAKKQLQdEMLRRVDAENRLQTMKEELDfqkniySEELRETKRRhetrlveidngkqrefesrlADALQELRAQHEDQ 255
Cdd:COG4942 99 LEAQKEELA-ELLRALYRLGRQPPLALLLS------PEDFLDAVRR--------------------LQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 256 VEQYKKELEktysaKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSR 335
Cdd:COG4942 152 AEELRADLA-----ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*..
gi 2244986507 336 RLLAEKEREMAEMRARM 352
Cdd:COG4942 227 ALIARLEAEAAAAAERT 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-390 |
5.54e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 28 RLQEKEDLQELNDRLAVYIDR---VRSLETENAGLRLRITESE---EVVSREVSGIKAAYEaELGDARKTL--------- 92
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETErerEELAEEVRDLRERLE-ELEEERDDLlaeagldda 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 93 --DSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA 170
Cdd:PRK02224 308 daEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 171 KLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSeELRETKRRHETRLVE----IDNGKQREFESRLADA-- 244
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-ELEATLRTARERVEEaealLEAGKCPECGQPVEGSph 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 245 -------------LQELRAQHEDQVEQYKKELEKTYSAK-----LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQL 306
Cdd:PRK02224 467 vetieedrerveeLEAELEDLEEEVEEVEERLERAEDLVeaedrIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 307 SQLQKQLAAKEAKLRDLEDSLARERDTsrrlLAEKEREMAEMRARMqQQLDEYQELLDIKLALDMEIHAYRKLLEG---- 382
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREAlael 621
|
....*....
gi 2244986507 383 -EEERLRLS 390
Cdd:PRK02224 622 nDERRERLA 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-401 |
9.03e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 129 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQK 208
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 209 NIYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysakldnarqsaernsnlvga 287
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 288 aheelqqsriridslsaQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 367
Cdd:COG4942 161 -----------------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|....
gi 2244986507 368 ALDMEIhayRKLLEGEEERLRLSPSPTSQRSRGR 401
Cdd:COG4942 224 ELEALI---ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-362 |
6.10e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKV 109
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 110 REEFKELKAR--NTKKEGDLIAAQARLKDLEALLNSkEAALSTALSEKRTLE--------------GELHDLRGQVAKLE 173
Cdd:COG4717 219 QEELEELEEEleQLENELEAAALEERLKEARLLLLI-AAALLALLGLGGSLLsliltiagvlflvlGLLALLFLLLAREK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 174 AALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRA--- 250
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAlla 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 251 -----------QHEDQVEQYKKELEK--TYSAKLDNARQSAERNSNLVGAA--HEELQQSRIRIDSLSAQLSQLQKQLAA 315
Cdd:COG4717 378 eagvedeeelrAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAE 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2244986507 316 KEAKLRDLEDSlarerdtsrRLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:COG4717 458 LEAELEQLEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-280 |
2.64e-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: 60.46 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 6 QRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSRevsgikaaYEAEL 85
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES--------LERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 86 GDARKTLDSVAKERARLQLELSKVREEFKELKARNTKkegdliaAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDL 165
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 166 RGQVAKLEAALGEAKKQLqdemlrrVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNG--KQREFESRLAD 243
Cdd:TIGR02168 907 ESKRSELRRELEELREKL-------AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDeeEARRRLKRLEN 979
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2244986507 244 ALQELRAQHEDQVEQYKKELE-----KTYSAKLDNARQSAER 280
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKErydflTAQKEDLTEAKETLEE 1021
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-351 |
3.41e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 124 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEgelhDLRGQVAKLEAALGEA-KKQLQDEMLRRVDAENRLQTMKE 202
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLE----PIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 203 ELdfqkniysEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNS 282
Cdd:COG4913 296 EL--------EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLEREIERL-ERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244986507 283 NLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 351
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-389 |
1.50e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 59 LRLRITESEEVVSRE--VSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVR----------EEFKELKARNTKKEGD 126
Cdd:PRK03918 174 IKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkeleelkEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 127 LIAAQARLKDLEALLNSKEAALSTaLSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDf 206
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 207 QKNIYSEELRETKRrhetRLVEIDNgKQREFESRlADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERnsnlvg 286
Cdd:PRK03918 332 ELEEKEERLEELKK----KLKELEK-RLEELEER-HELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEK------ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 287 aAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEdSLARERDTSRRLLAEKERE--MAEMRARMQQQLDEYQELLD 364
Cdd:PRK03918 399 -AKEEIEE---EISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEE 473
|
330 340
....*....|....*....|....*
gi 2244986507 365 IKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKL 498
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
72-364 |
2.31e-08 |
|
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: 56.83 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 72 REVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELK---ARNTKKEGDLIAAQARLKDLEALLNSKEAAL 148
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 149 STALSEK----RTLEGELHDLRGQVAKLEAALGEAKK-------QLQDEMLRRVDAENRLQTMKEEL-----DFQKNIYS 212
Cdd:pfam07888 121 LAQRAAHeariRELEEDIKTLTQRVLERETELERMKErakkagaQRKEEEAERKQLQAKLQQTEEELrslskEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 213 EELRETK----RRHETRLVEIDNGKQR---EFESRLAD--ALQELRAQHEDQVEQYKKELEKTYS------AKLDNAR-Q 276
Cdd:pfam07888 201 LAQRDTQvlqlQDTITTLTQKLTTAHRkeaENEALLEElrSLQERLNASERKVEGLGEELSSMAAqrdrtqAELHQARlQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 277 SAERNSNLVGAA-------------HEELQQS----RIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA 339
Cdd:pfam07888 281 AAQLTLQLADASlalregrarwaqeRETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|..
gi 2244986507 340 EKEREMAEMRARMQ-------QQLDEYQELLD 364
Cdd:pfam07888 361 ESRRELQELKASLRvaqkekeQLQAEKQELLE 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-388 |
2.39e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 25 RITRLqeKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV---SREVSGIKAAYEAELGDARKTLDSVAKERAR 101
Cdd:COG4913 339 RLEQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFaalRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 102 LQLELSKVREEFKELKARNTKKEGDLIAAQARlkdLEALLNSKEAALSTAlsekrtleGELHDLRGQVAK----LEAALG 177
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELPFV--------GELIEVRPEEERwrgaIERVLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 178 EAK-------KQLQD--EMLRRVDAENRLQTMK-------------------EELDFQKNIYS----------------- 212
Cdd:COG4913 486 GFAltllvppEHYAAalRWVNRLHLRGRLVYERvrtglpdperprldpdslaGKLDFKPHPFRawleaelgrrfdyvcvd 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 213 --EELRETKR--------RHETRLVEID--------------NGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYS 268
Cdd:COG4913 566 spEELRRHPRaitragqvKGNGTRHEKDdrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQ 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 269 AKLDNARQSAERNSNL--VGAAHEELQQSRIRIDSL---SAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER 343
Cdd:COG4913 645 ERREALQRLAEYSWDEidVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2244986507 344 eMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:COG4913 725 -AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-363 |
2.86e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.11 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 27 TRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGikaayEAELGDARKTLDSvakERARLQLEL 106
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-----RQELEKAKRKLEG---ESTDLQEQI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 107 SKVREEFKELKARNTKKEGDLIAAQARLKDleallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQlqde 186
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEE-------ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ---- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 187 mlrRVDAENRLQTMKEELD--FQKNIYSEELReTKRRHETRLVEidngKQREFESRLADA-LQELRAQHEDQVEQYKKEL 263
Cdd:pfam01576 294 ---RRDLGEELEALKTELEdtLDTTAAQQELR-SKREQEVTELK----KALEEETRSHEAqLQEMRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 264 EKTYSAK--LDNARQSAERNSNLVGAAHEELQQSRI----RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTS 334
Cdd:pfam01576 366 EQAKRNKanLEKAKQALESENAELQAELRTLQQAKQdsehKRKKLEGQLQELQARLSESERQRAELAEKLSKlqsELESV 445
|
330 340 350
....*....|....*....|....*....|..
gi 2244986507 335 RRLLAEKERE---MAEMRARMQQQLDEYQELL 363
Cdd:pfam01576 446 SSLLNEAEGKnikLSKDVSSLESQLQDTQELL 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-448 |
3.01e-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: 56.99 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 162 LHDLRGQVAKLEAALGEAKKQLqDEMLRRVDAENRLQTMKEEL-DFQKNIYSEELRE-TKRRHETRLVEIDNGKQREFES 239
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQL-KSLERQAEKAERYKELKAELrELELALLVLRLEElREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 240 RLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 320 LRDLE----------DSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:TIGR02168 339 LAELEekleelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2244986507 390 SPSPTSQRSRgRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEE 448
Cdd:TIGR02168 419 LQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-355 |
3.16e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 24 TRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESE------EVVSREVSGIKAAYEAELGDARKTLDSVAK 97
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELEseleeaREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 98 ERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNS----------KEAALSTALSEKR----TLEGELH 163
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRerveELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 164 DLRGQVAKLEA------ALGEAKKQLQDEMLRRVDAENRLQTMKEELDfQKNIYSEELRETKRRHETRLVEID------- 230
Cdd:PRK02224 486 DLEEEVEEVEErleraeDLVEAEDRIERLEERREDLEELIAERRETIE-EKRERAEELRERAAELEAEAEEKReaaaeae 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 231 -------------NGKQREFESRL----------------ADALQELRAQHEDQVE---------QYKKELEKTYSAKLD 272
Cdd:PRK02224 565 eeaeeareevaelNSKLAELKERIeslerirtllaaiadaEDEIERLREKREALAElnderrerlAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 273 NARQSAERNSNlvGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA---------EKER 343
Cdd:PRK02224 645 EARIEEAREDK--ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAlealydeaeELES 722
|
410
....*....|..
gi 2244986507 344 EMAEMRARMQQQ 355
Cdd:PRK02224 723 MYGDLRAELRQR 734
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
111-355 |
3.79e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 111 EEFKELKARNTKKEGDLIaaQARLKDLEALLNSKEAALSTALSEKRTLegelhDLRGQVAKLEAALGEAKKQLQDEMLRR 190
Cdd:COG3206 163 EQNLELRREEARKALEFL--EEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 191 VDAENRLQTMKEELDFQKNIYSEELR-ETKRRHETRLVEIdngkqrefESRLADALQELRAQHEDqVEQYKKELEKTysa 269
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAEL--------EAELAELSARYTPNHPD-VIALRAQIAAL--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 270 kldnARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ---LAAKEAKLRDLEdslaRERDTSRRLLAEKEREMA 346
Cdd:COG3206 304 ----RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLE----REVEVARELYESLLQRLE 375
|
....*....
gi 2244986507 347 EMRARMQQQ 355
Cdd:COG3206 376 EARLAEALT 384
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-388 |
8.90e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 96 AKERARLQLE--LSKVREEF-KELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKL 172
Cdd:pfam01576 710 ATEDAKLRLEvnMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 173 EAALGEAKKQL--------------------QDEMLRRV-DAENRLQTMKEE-LDFQKNIYSEE---------------- 214
Cdd:pfam01576 790 NKGREEAVKQLkklqaqmkdlqreleearasRDEILAQSkESEKKLKNLEAElLQLQEDLAASErarrqaqqerdelade 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 215 ----------LRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKEL--EKTYSAKLDNARQSAERNS 282
Cdd:pfam01576 870 iasgasgksaLQDEKRRLEARIAQLE--EELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQN 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 283 NLVGAAHEELQqsriridslSAQLSQLQKQLAAKEAKLRDLEDSL---ARERDTSRRLLAEKEREMAEMRARMQ---QQL 356
Cdd:pfam01576 948 KELKAKLQEME---------GTVKSKFKSSIAALEAKIAQLEEQLeqeSRERQAANKLVRRTEKKLKEVLLQVEderRHA 1018
|
330 340 350
....*....|....*....|....*....|..
gi 2244986507 357 DEYQELLDiKLALDMEiHAYRKLLEGEEERLR 388
Cdd:pfam01576 1019 DQYKDQAE-KGNSRMK-QLKRQLEEAEEEASR 1048
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
82-267 |
1.48e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSkeaalstALSEKrtlegE 161
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-------VRNNK-----E 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 162 LHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKniysEELRETKRRHETRLVEIDngkqrefesrl 241
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE----AELEEKKAELDEELAELE----------- 155
|
170 180
....*....|....*....|....*.
gi 2244986507 242 aDALQELRAQHEDQVEQYKKELEKTY 267
Cdd:COG1579 156 -AELEELEAEREELAAKIPPELLALY 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-388 |
1.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 189 RRVDAENRLQTMKEELD-------------------------FQKniYSEELREtkRRHETRLVEID--NGKQREFESRL 241
Cdd:COG1196 173 RKEEAERKLEATEENLErledilgelerqleplerqaekaerYRE--LKEELKE--LEAELLLLKLRelEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 242 ADALQELR------AQHEDQVEQYKKELE------KTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQL 309
Cdd:COG1196 249 EELEAELEeleaelAELEAELEELRLELEelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 310 QKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:COG1196 329 EEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
..
gi 2244986507 387 LR 388
Cdd:COG1196 409 EE 410
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
32-357 |
2.43e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.53 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIkAAYEAELGDARKTLDSVAKERARLQLELSKVRE 111
Cdd:pfam19220 68 RRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIEL-RDKTAQAEALERQLAAETEQNRALEEENKALRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 112 EFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRV 191
Cdd:pfam19220 147 EAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 192 DAENRLQTMKEELDFQKNIYSEELRETKRRHET----------RLVEIDNGkQREFESRLADA----------LQELRAQ 251
Cdd:pfam19220 227 RAEAQLEEAVEAHRAERASLRMKLEALTARAAAteqllaearnQLRDRDEA-IRAAERRLKEAsierdtlerrLAGLEAD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 252 HEDQVEQYKKelektysakLDNARQSAERNSNLVG---AAHE-ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDledsl 327
Cdd:pfam19220 306 LERRTQQFQE---------MQRARAELEERAEMLTkalAAKDaALERAEERIASLSDRIAELTKRFEVERAALEQ----- 371
|
330 340 350
....*....|....*....|....*....|
gi 2244986507 328 arerdTSRRLLAEKEREMAEmRARMQQQLD 357
Cdd:pfam19220 372 -----ANRRLKEELQRERAE-RALAQGALE 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-362 |
2.43e-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: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 29 LQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV---SREVSGIKAAYEA-----------------ELGDA 88
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKlkerleeleedlssleqEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 89 RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQ------------ARLKDLEALLNSKEAALSTALSEKR 156
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskleeevsrieARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 157 TLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKqre 236
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELERKI--- 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 237 fesrladalQELRAQHEDqveqyKKELEKTYSAKLDNArqsAERNSNLvgaahEELQQSRIRIDSLSAQLSQLQKQLAAK 316
Cdd:TIGR02169 906 ---------EELEAQIEK-----KRKRLSELKAKLEAL---EEELSEI-----EDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 317 EAKLRDLED--SLARE--RDTSRRL--LAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:TIGR02169 964 EEEIRALEPvnMLAIQeyEEVLKRLdeLKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-385 |
3.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 26 ITRLQEKE-DLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIK-AAYEAELGDARKTLDSVAK---ERA 100
Cdd:COG4913 609 RAKLAALEaELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 101 RLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLegelhdlrgqvakLEAALgeak 180
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-------------LRALL---- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 181 kqlqDEMLRRVDAENRLQTMKEELdfQKNIysEELRETKRRHETRLVEIDNGKQREFESRLAD------ALQELRAQHED 254
Cdd:COG4913 752 ----EERFAAALGDAVERELRENL--EERI--DALRARLNRAEEELERAMRAFNREWPAETADldadleSLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 255 QVEQykkELEKtYSAKLDNARQSAERN--SNLVGAAHEELQQSRIRIDSLSAQLSQLQ------KQLAAKEAKL------ 320
Cdd:COG4913 824 LEED---GLPE-YEERFKELLNENSIEfvADLLSKLRRAIREIKERIDPLNDSLKRIPfgpgryLRLEARPRPDpevref 899
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 321 -RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQlDEYQELLDIKLALD----MEIHAYRKLLEGEEE 385
Cdd:COG4913 900 rQELRAVTSGASLFDEELSEARFAALKRLIERLRSE-EEESDRRWRARVLDvrnhLEFDAEEIDREDGEE 968
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
24-178 |
5.71e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 24 TRITRLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVsREVSGIKAAYEAELGDAR--KTLDSVA 96
Cdd:COG1579 17 SELDRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-EEVEARIKKYEEQLGNVRnnKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 97 KERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEkrtLEGELHDLRGQVAKLEAAL 176
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI 172
|
..
gi 2244986507 177 GE 178
Cdd:COG1579 173 PP 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-389 |
7.19e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 31 EKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVR 110
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 111 EEFKELKARN---TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRgqvaklEAALGEAKKQLQDEM 187
Cdd:COG1196 387 ELLEALRAAAelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE------EAAEEEAELEEEEEA 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 188 LRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTY 267
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 268 SAKLDNARQSAERNSNLVGAAHEELQQSR-------IRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 341 -----------KEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:COG1196 621 tllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-350 |
8.28e-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: 52.43 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 24 TRITRLQEKEDL--QELNdRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAeLGDARKTLDSVAKERAR 101
Cdd:pfam15921 517 AEITKLRSRVDLklQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQ 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 102 LQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 182 QLqdEMLRR--VDAENRLQTMKEELDFQKNIYSEELRETKRRHET------RLVEIDNGKQREFESRLA--DALQELRAQ 251
Cdd:pfam15921 675 DY--EVLKRnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdgHAMKVAMGMQKQITAKRGqiDALQSKIQF 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 252 HEDQVEQYKKE--LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRidsLSAQLSQLQKQLAAKEAKLRDLEDSLAR 329
Cdd:pfam15921 753 LEEAMTNANKEkhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR---LKEKVANMEVALDKASLQFAECQDIIQR 829
|
330 340
....*....|....*....|.
gi 2244986507 330 ERDTSRRLLAEKEREMAEMRA 350
Cdd:pfam15921 830 QEQESVRLKLQHTLDVKELQG 850
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
104-265 |
1.02e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 104 LELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ- 182
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 183 ----LQDEM----LRRVDAENRLQTMKEELDFQKniysEELRETKRRHETRLVEIDNgKQREFESRLADaLQELRAQHED 254
Cdd:COG1579 90 eyeaLQKEIeslkRRISDLEDEILELMERIEELE----EELAELEAELAELEAELEE-KKAELDEELAE-LEAELEELEA 163
|
170
....*....|.
gi 2244986507 255 QVEQYKKELEK 265
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-387 |
1.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 25 RITRLQEKEDL-QELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSrEVSGIKAAYEAELGDARKTLDSVA--KERAR 101
Cdd:PRK03918 284 ELKELKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEelEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 102 LQLELSKVREEFKELKARNTKKEgdliaaqarLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLT---------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 182 QLQDEML--RRVDAENRLQTMKEELDFQKNIYSE--ELRETKRRHETRLVEIDNGKQREfesrladalQELRAQHE--DQ 255
Cdd:PRK03918 434 AKGKCPVcgRELTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELRELEKVLKKE---------SELIKLKElaEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 256 VEQYKKELEKTYSAKLdnarqsaERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERD 332
Cdd:PRK03918 505 LKELEEKLKKYNLEEL-------EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLK 577
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2244986507 333 TSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKlaldMEIHAYRKLLEGEEERL 387
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEYLELKDAE----KELEREEKELKKLEEEL 628
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
90-387 |
1.88e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 90 KTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLE----------ALLNSKEAALSTALSEkrtLE 159
Cdd:pfam01576 377 KAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNE---AE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 160 GELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEElrETKRRHETRLVEIDNGKQREFES 239
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE--EEAKRNVERQLSTLQAQLSDMKK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 240 RLADALQELraqheDQVEQYKKELEKtysaKLDNARQSAERNSnlvgAAHEELQQSRIR----IDSLSAQLSQLQKQLAA 315
Cdd:pfam01576 532 KLEEDAGTL-----EALEEGKKRLQR----ELEALTQQLEEKA----AAYDKLEKTKNRlqqeLDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 316 KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDmEIHAYRKLLEGEEERL 387
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
80-351 |
4.48e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 80 AYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLE 159
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 160 GELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDA-ENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEIDNGKQRE 236
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSidKLRKEIERlEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 237 FESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKqlaak 316
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAQE-LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK----- 237
|
250 260 270
....*....|....*....|....*....|....*
gi 2244986507 317 eaKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 351
Cdd:COG1340 238 --ELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
185-390 |
5.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 185 DEMLRRVDAENRLQTMKEELDFQKNIYSEELRE---TKRRHETRLVEID-NGKQREFESRLADALQE--LRAQHEDQVEQ 258
Cdd:COG3206 93 RPVLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGSNVIEISyTSPDPELAAAVANALAEayLEQNLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 259 YKKELE------KTYSAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 330
Cdd:COG3206 173 ARKALEfleeqlPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2244986507 331 RDTSRRLLAekEREMAEMRARMQQQLDEYQELL--------DIKlALDMEIHAYRKLLEGEEERLRLS 390
Cdd:COG3206 253 PDALPELLQ--SPVIQQLRAQLAELEAELAELSarytpnhpDVI-ALRAQIAALRAQLQQEAQRILAS 317
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-228 |
7.85e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 25 RITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVsrevsgikAAYEAELGDARKTLDSVAKERA--RL 102
Cdd:COG3206 197 ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL--------AALRAQLGSGPDALPELLQSPViqQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 103 QLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNS-KEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2244986507 182 QlqdemlrrvdaENRLQTMKEELDFQKNIYSEELretKRRHETRLVE 228
Cdd:COG3206 349 L-----------EAELRRLEREVEVARELYESLL---QRLEEARLAE 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-416 |
9.05e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 138 EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRE 217
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 218 TKR--RHETRLVEIDNGKQ-REFESRLaDALQELRAQHEDQVEQYKKELEKtysakLDNARQSAERNSNLVGAAHEELQQ 294
Cdd:COG3883 95 LYRsgGSVSYLDVLLGSESfSDFLDRL-SALSKIADADADLLEELKADKAE-----LEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 295 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIH 374
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2244986507 375 AYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVT 416
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAG 290
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
131-366 |
9.43e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 131 QARLKDL--EALLNSKEAALSTALSEkrTLegelhDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEELDFQK 208
Cdd:PRK11281 42 QAQLDALnkQKLLEAEDKLVQQDLEQ--TL-----ALLDKIDRQKEETEQLKQQLAQ-------APAKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 209 NIYSEELRETkrrhetrlveIDNGKQREFESRLADALQELraqhedqvEQYKKELEkTYSAKLDNARQSAERNSNLVGAA 288
Cdd:PRK11281 108 DDNDEETRET----------LSTLSLRQLESRLAQTLDQL--------QNAQNDLA-EYNSQLVSLQTQPERAQAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 289 HEELQQSRIRIDSLSA--------QLSQLQKQLAAKEAKLrDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ 360
Cdd:PRK11281 169 SQRLQQIRNLLKGGKVggkalrpsQRVLLQAEQALLNAQN-DLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQ 247
|
....*.
gi 2244986507 361 ELLDIK 366
Cdd:PRK11281 248 EAINSK 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
85-362 |
1.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 85 LGDARKTLDSV-----AKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKE-------------- 145
Cdd:PRK02224 182 LSDQRGSLDQLkaqieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreeletleaeie 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 146 ---AALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDE-------MLRRVDAENRLQTMKEELDFQK------N 209
Cdd:PRK02224 262 dlrETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREELEDRDEELRDRLEECRvaaqahN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 210 IYSEELRETKRRHETRLVEIDN----------------GKQREFESRLADALQELRAQHED------QVEQYKKEL---- 263
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREeaaeleseleeareavEDRREEIEELEEEIEELRERFGDapvdlgNAEDFLEELreer 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 264 ------EKTYSAKLDNARQSAERNSNLV-------------GAAH-EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDL 323
Cdd:PRK02224 422 delrerEAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHvETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2244986507 324 ED---------SLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:PRK02224 502 EDlveaedrieRLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
139-348 |
1.40e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 139 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQdeMLRRV----------DAENRLQTMKEELDFqk 208
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ--LLNKLlpqanlladeTLADRLEELREELDA-- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 209 niySEELRETKRRHETRLVEIDngkqrefesRLADALQELRAQHEDQVEQYK--KELEKTYSAKLDNARQSAERNSNLVG 286
Cdd:COG3096 905 ---AQEAQAFIQQHGKALAQLE---------PLVAVLQSDPEQFEQLQADYLqaKEQQRRLKQQIFALSEVVQRRPHFSY 972
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244986507 287 A-AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED----------SLARERDTSRRLLAEKEREMAEM 348
Cdd:COG3096 973 EdAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAqysqynqvlaSLKSSRDAKQQTLQELEQELEEL 1045
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-388 |
1.42e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 34 DLQELNDRLAVYIDRVRSLETENAGLRLRITESE----EVVSREVSGIKAAYEAELGDARKTLDSVAKE-RARLQLELSK 108
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 109 VREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAaLSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 188
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 189 RRVDAENRLQTMKEELDFQKNIYSEELREtkrrhetrlveiDNGKQREFESRLADALQELRAQ-HEDQVEQYKKELEKTY 267
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTLLHFLRK------------EAPDWEQSIGKVISPELLHRTDlDPEVWDGSVGGELNLY 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 268 SAKLDNAR-------QSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:pfam12128 582 GVKLDLKRidvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE 661
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 341 KERE---MAEMRARMQQQLDEYQELLDIKL-ALDMEIHAYRKLLEGEEERLR 388
Cdd:pfam12128 662 KQSEkdkKNKALAERKDSANERLNSLEAQLkQLDKKHQAWLEEQKEQKREAR 713
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-325 |
1.72e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 32 KEDLQELNDRLAVYIDRVRSLETEnaglrLRITESEEVVSREVSGIKAAYEaELGDARKTLDSVAKErarlqlELSKVRE 111
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKE-----LRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLE------ELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 112 EFKELKARNTKKEGDLIAAQARLKDLEALLNSKEA---ALSTALSEKRTLEGELHDLR-GQVAKLEAALGEAKKqLQDEM 187
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekKLDELEEELAELLKELEELGfESVEELEERLKELEP-FYNEY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 188 LRRVDAENRLQTMKEELDFQKNiyseelretkrrhetrlvEIDngKQREFESRLADALQELRAQHEdqveqykkELEKTY 267
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEE------------------ELD--KAFEELAETEKRLEELRKELE--------ELEKKY 656
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2244986507 268 SA-KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 325
Cdd:PRK03918 657 SEeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
82-352 |
1.93e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTAL-SEKRTLEG 160
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLR-RVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFES 239
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 240 RLADalqelraqhEDQVEQYKKELeKTYSAKLDNARQ-SAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAA 315
Cdd:pfam12128 763 LGVD---------PDVIAKLKREI-RTLERKIERIAVrRQEVLRYFDWYQETWLQRRprlATQLSNIERAISELQQQLAR 832
|
250 260 270
....*....|....*....|....*....|....*..
gi 2244986507 316 KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARM 352
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-319 |
2.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 99 RARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALge 178
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 179 akkQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKQ--REFESRLADALQELRAQHEDQV 256
Cdd:COG4717 126 ---QLLPLYQELEALEAELAELPERL--------EELEERLEELRELEEELEELEAelAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244986507 257 EQYKKELEktysaKLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:COG4717 195 QDLAEELE-----ELQQRLAELE----------EELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
161-362 |
3.91e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESR 240
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL--------EDLEKEIKRLELEIEEVEA-RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 241 LAdalqelRAQHEDQVEQYKKELEKtysakLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL 320
Cdd:COG1579 82 LG------NVRNNKEYEALQKEIES-----LKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2244986507 321 RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQL-DEYQEL 362
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIPPELlALYERI 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-174 |
4.39e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 5 SQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRlritesEEVVSREVSgiKAAYEAE 84
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR------DELKDYREK--LEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 85 LGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRT------- 157
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDlkeeydr 480
|
170
....*....|....*..
gi 2244986507 158 LEGELHDLRGQVAKLEA 174
Cdd:TIGR02169 481 VEKELSKLQRELAEAEA 497
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
25-362 |
4.44e-05 |
|
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: 46.74 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 25 RITRLQEK-EDLQE-LNDR---LAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDsvaker 99
Cdd:pfam10174 395 KINVLQKKiENLQEqLRDKdkqLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE------ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 100 arlqlELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALgea 179
Cdd:pfam10174 469 -----ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL--- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 180 KKQLQDEMLRRVDAE--NRLQTMKEELDFqkniYSEELRETKRRHEtRLVEIdngkQREFESRLADALQELRAQHEDQVE 257
Cdd:pfam10174 541 KKAHNAEEAVRTNPEinDRIRLLEQEVAR----YKEESGKAQAEVE-RLLGI----LREVENEKNDKDKKIAELESLTLR 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 258 QYKKELEKTYSAKLdnaRQSAERNSNLvgaahEELQQSRIRIDSL--SAQLSQLQKQLAAKEAKLRDLEDSLARERDTsR 335
Cdd:pfam10174 612 QMKEQNKKVANIKH---GQQEMKKKGA-----QLLEEARRREDNLadNSQQLQLEELMGALEKTRQELDATKARLSST-Q 682
|
330 340
....*....|....*....|....*..
gi 2244986507 336 RLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:pfam10174 683 QSLAEKDGHLTNLRAERRKQLEEILEM 709
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
52-403 |
4.74e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 52 LETENAGLRLRITESEEVVSR--EVSGIKAAYEAELGDARKTLdsvaKERARLQLELSKVREEFKELKARNTKKEGDLIA 129
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSEleEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 130 AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA----ALGEAKKQLQDEMLRRVDAENRLQTM----K 201
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdkLLLENKELTQEASDMTLELKKHQEDIinckK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 202 EELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELeKTYSAKLDNARQSAERN 281
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM-KILENKCNNLKKQIENK 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 282 SNLVGAAHEELQQSRIRIDSLSAQL-------SQLQKQLAAKEAKLRDLEDSLARE----RDTSRRLL--AEKEREMAEM 348
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENKQLnayeikvNKLELELASAKQKFEEIIDNYQKEiedkKISEEKLLeeVEKAKAIADE 686
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2244986507 349 RARMQQQLDE--YQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRAS 403
Cdd:pfam05483 687 AVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAA 743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-387 |
7.57e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 153 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAEnRLQTMKEELdfQKNIYSEELREtKRRHETRLVEIDNg 232
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK--REYEGYELLKE-KEALERQKEAIER- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 233 kqrefesRLADALQELraqheDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGaahEELQQSRIRIDSLSAQLSQL--- 309
Cdd:TIGR02169 245 -------QLASLEEEL-----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLers 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 310 -------QKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 382
Cdd:TIGR02169 310 iaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
....*
gi 2244986507 383 EEERL 387
Cdd:TIGR02169 390 YREKL 394
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
28-308 |
8.36e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 28 RLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEvvsrEVSGIKAayeaELGDARKTLDSV------- 95
Cdd:COG3096 344 RQQEKieryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEE----EVDSLKS----QLADYQQALDVQqtraiqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 96 -----AKERARLQLELSK-----VREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAAL------------STALS 153
Cdd:COG3096 416 qqavqALEKARALCGLPDltpenAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYelvckiageverSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 154 EKRTLEGELHDLR---GQVAKLEAALGEAKK---------QLQDEMLRR----VDAENRLQTMKEELDFQKNIYSEELRE 217
Cdd:COG3096 496 TARELLRRYRSQQalaQRLQQLRAQLAELEQrlrqqqnaeRLLEEFCQRigqqLDAAEELEELLAELEAQLEELEEQAAE 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 218 -TKRRHETR--LVEIdNGKQREFESR------LADALQELRAQHEDQVEQykkelektySAKLDNARQSAERNSNLVGAA 288
Cdd:COG3096 576 aVEQRSELRqqLEQL-RARIKELAARapawlaAQDALERLREQSGEALAD---------SQEVTAAMQQLLEREREATVE 645
|
330 340
....*....|....*....|
gi 2244986507 289 HEELQQSRIRIDSLSAQLSQ 308
Cdd:COG3096 646 RDELAARKQALESQIERLSQ 665
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
33-307 |
1.01e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 33 EDLQELNdrlAVYIDrvrSLETENAGLRLR-ITESEEVVSREVSGIKAAYEAELGD----ARKTLDSVAKERARLQLELS 107
Cdd:PRK05771 23 EALHELG---VVHIE---DLKEELSNERLRkLRSLLTKLSEALDKLRSYLPKLNPLreekKKVSVKSLEELIKDVEEELE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 108 KVREEFKELKARntkkegdLIAAQARLKDLEALLNskeaalstALSEKRTLEGELHDLRGQvAKLEAALGEAKKQLQDEM 187
Cdd:PRK05771 97 KIEKEIKELEEE-------ISELENEIKELEQEIE--------RLEPWGNFDLDLSLLLGF-KYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 188 LRRVDAENrLQTMKEELD------FQKNIYSEELRETKRRHETRLVEIDNGKqrefesrladALQELRAQHEDQVEQYKK 261
Cdd:PRK05771 161 KLESDVEN-VEYISTDKGyvyvvvVVLKELSDEVEEELKKLGFERLELEEEG----------TPSELIREIKEELEEIEK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2244986507 262 ELEKTysakLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS 307
Cdd:PRK05771 230 ERESL----LEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
82-389 |
1.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKarntkKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRtlegE 161
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALEAELAELPERLEELEERLE----E 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 162 LHDLRGQVAKLEAALGEAKKQLQDEMLR-RVDAENRLQTMKEELDF---QKNIYSEELRETKRRHETRLVEIDNGKQREF 237
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 238 ESRLADALQELR---------------AQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSL 302
Cdd:COG4717 238 AAALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 303 SAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEmrARMQQQLDEYQELLDIKLALDMEihAYRKLLEG 382
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEE--ELRAALEQ 393
|
....*..
gi 2244986507 383 EEERLRL 389
Cdd:COG4717 394 AEEYQEL 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-362 |
1.19e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 28 RLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREvsgikaayEAELGDARKTLDSVAKERARLQLELS 107
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--------EEALEEAAEEEAELEEEEEALLELLA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 108 KVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTA-----LSEKRTLEGELHDLRGQVAKLEAALGEA--- 179
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaallLAGLRGLAGAVAVLIGVEAAYEAALEAAlaa 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 180 ------------------------------------------------------------KKQLQDEMLRRVDAENRLQT 199
Cdd:COG1196 547 alqnivveddevaaaaieylkaakagratflpldkiraraalaaalargaigaavdlvasDLREADARYYVLGDTLLGRT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 200 MKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAE 279
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 280 RNSNlvgAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQ----- 354
Cdd:COG1196 707 RELA---EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvn 783
|
410
....*....|
gi 2244986507 355 --QLDEYQEL 362
Cdd:COG1196 784 llAIEEYEEL 793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-341 |
1.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 78 KAAYEAELGDARKTLDSVAK-ERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKR 156
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 157 TLEGE---------LHDLRGQVAKLEAALGEAKKQLqdEMLRRVDAENRLQtmKEELDFQKNIYSEELRETKRRHETRLV 227
Cdd:PTZ00121 1614 KAEEAkikaeelkkAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 228 EIDNGKQREFESRLADALQELRAQHEDQVEQYKKElEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRiridslsaQLS 307
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--------KIA 1760
|
250 260 270
....*....|....*....|....*....|....*...
gi 2244986507 308 QLQKQLAAKEAKLRDLEDSLARE----RDTSRRLLAEK 341
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEeldeEDEKRRMEVDK 1798
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6-377 |
1.26e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 6 QRRATRSGAQASSTPLsptritRLQEKEDLQELNDRLAVYIDRvrsLETENAGLRLRITESEEVVSREVSgikaayEAEL 85
Cdd:pfam12128 409 QLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLKSR---LGELKLRLNQATATPELLLQLENF------DERI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 86 GDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALstalsekrtlegeLHDL 165
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL-------------LHFL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 166 RGQVAKLEAALGeakKQLQDEMLRRVD--AENRLQTMKEELdfqkNIYSEELRETKRRHETRLVEIDNGKQR--EFESRL 241
Cdd:pfam12128 541 RKEAPDWEQSIG---KVISPELLHRTDldPEVWDGSVGGEL----NLYGVKLDLKRIDVPEWAASEEELRERldKAEEAL 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 242 ADAlQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNSNLVGAAHEELQQSRIRID-SLSAQLSQLQKQLAAKEAKL 320
Cdd:pfam12128 614 QSA-REKQAAAEEQLVQANGELEKA-SREETFARTALKNARLDLRRLFDEKQSEKDKKNkALAERKDSANERLNSLEAQL 691
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2244986507 321 RDLEDSLarerdtsRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLA-LDMEIHAYR 377
Cdd:pfam12128 692 KQLDKKH-------QAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARR 742
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
25-389 |
1.31e-04 |
|
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: 45.34 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 25 RITRLQEKEDLQELNDRLAVYIDRVRSLE--TENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARL 102
Cdd:TIGR00618 278 VLEETQERINRARKAAPLAAHIKAVTQIEqqAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 103 QLElSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:TIGR00618 358 RDA-HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 183 LQDEMLRRVDAENRLQTMK----------------EELDFQKNIYSEELRETKRRHETRLVEIdNGKQREFESRLADALQ 246
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKlekihlqesaqslkerEQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNP 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 247 ELRA------------QHEDQVEQYKKELEKT-------------YSAKLDNARQS------------------------ 277
Cdd:TIGR00618 516 ARQDidnpgpltrrmqRGEQTYAQLETSEEDVyhqltserkqrasLKEQMQEIQQSfsiltqcdnrskedipnlqnitvr 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 278 --------AERNSNLVGAAHEELQQSRIRID--SLSAQLSQLQKQLAAKEAKLRDLEDSLA--RERDTSRRLLAEKEREM 345
Cdd:TIGR00618 596 lqdlteklSEAEDMLACEQHALLRKLQPEQDlqDVRLHLQQCSQELALKLTALHALQLTLTqeRVREHALSIRVLPKELL 675
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2244986507 346 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
296-388 |
1.42e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 296 RIRIDSLSAQLSQLQKQLAA----KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALD- 370
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEq 482
|
90 100
....*....|....*....|
gi 2244986507 371 --MEIHAYRKLLEGEEERLR 388
Cdd:COG0542 483 ryGKIPELEKELAELEEELA 502
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
57-212 |
1.61e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 57 AGLRLRITESEEVVSREVSGIKAAYEAELGDARktlDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKD 136
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAK---ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 137 LEALLNSKEAALSTALSEkrtLEGELHDLRgqvAKLEAALGEAKKQLQDEMLRRVDAENRLQ------TMKEELDFQKNI 210
Cdd:PRK12705 103 LENQLEEREKALSARELE---LEELEKQLD---NELYRVAGLTPEQARKLLLKLLDAELEEEkaqrvkKIEEEADLEAER 176
|
..
gi 2244986507 211 YS 212
Cdd:PRK12705 177 KA 178
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
21-387 |
2.11e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 21 LSPTRITRLQEKE-DLQELNDRLavyidrvRSLETENAGLRLRITESEEVVSREVSGIKAAyeaelgdarKTLDSVAKER 99
Cdd:TIGR00606 731 LAPGRQSIIDLKEkEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESA---------KVCLTDVTIM 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 100 ARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEA 179
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE-----KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 180 KK---QLQDEMLRRVDAENRLQTMKEELDF------QKNIYSEELRETKRRHETRLVEIDNGKQREfESRLADALQELRa 250
Cdd:TIGR00606 870 KSeklQIGTNLQRRQQFEEQLVELSTEVQSlireikDAKEQDSPLETFLEKDQQEKEELISSKETS-NKKAQDKVNDIK- 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 251 QHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSlsaQLSQLQKQLAAKEAKLRDLEDSLAR- 329
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE---DMRLMRQDIDTQKIQERWLQDNLTLr 1024
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244986507 330 ----ERDTSRRLLAEKEREMAEMraRMQQQLDEYQELLD-IKLALDMEIHAYRKLLEGEEERL 387
Cdd:TIGR00606 1025 krenELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEEnIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
114-325 |
2.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 114 KELKARNTKKEGDLIAAQARLKDLEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLqdEMLRRVDA 193
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREEL--EKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 194 ENRLQTMKEELDFQKNIYSEELRETKRRHEtrlveidngkqrefesRLADALQELRAQhEDQVEQYKKELEKTYSAKLDN 273
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLE----------------ELRELEEELEEL-EAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 274 ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 325
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
79-383 |
2.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 79 AAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTL 158
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 159 EGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKQREFE 238
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL--------KELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 239 SRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA 318
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2244986507 319 KLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGE 383
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-341 |
3.02e-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: 43.86 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 29 LQEKED-LQELNDRLAVYIDRVRSLETENAGLRLRITESEEVvsrevsgikaayeaelgdaRKTLDSVAKErarLQLELS 107
Cdd:TIGR04523 365 LEEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL-------------------NQQKDEQIKK---LQQEKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 108 KVREEFKELKARNTKkegdliaAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD-- 185
Cdd:TIGR04523 423 LLEKEIERLKETIIK-------NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSke 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 186 ---EMLRRV--DAENRLQTMKEELDFQKNiYSEELRETKRRHETRLVEIDNgKQREFESRLAdalqelRAQHEDQVEQYK 260
Cdd:TIGR04523 496 kelKKLNEEkkELEEKVKDLTKKISSLKE-KIEKLESEKKEKESKISDLED-ELNKDDFELK------KENLEKEIDEKN 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 261 KELEktysakldnarQSAERNSNLVgAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:TIGR04523 568 KEIE-----------ELKQTQKSLK-KKQEEKQE---LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
.
gi 2244986507 341 K 341
Cdd:TIGR04523 633 I 633
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-462 |
3.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVR-------EEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALST 150
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 151 ALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ-----DEMLRRVDAENRLQTMKEELDFQKNiYSEELR----ETKRR 221
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKK-KADEAKkaaeAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 222 HETRLVE----IDNGKQREfESRLADALQelRAQHEDQVEQYKK--ELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS 295
Cdd:PTZ00121 1513 DEAKKAEeakkADEAKKAE-EAKKADEAK--KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 296 RIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE--RDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEi 373
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 374 hayrkllEGEEERLRLSPSPTSQRSRGRASSHSSQTQgggsvTKKRKLEstESRSSFSQHARTSGRVAVEEVDEEGKFVR 453
Cdd:PTZ00121 1669 -------KAEEDKKKAEEAKKAEEDEKKAAEALKKEA-----EEAKKAE--ELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
....*....
gi 2244986507 454 LRNKSNEDQ 462
Cdd:PTZ00121 1735 AKKEAEEDK 1743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
155-388 |
3.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 155 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEeldfQKNIYSeeLRETKRRHETRLVEIdngkq 234
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALEEFRQ----KNGLVD--LSEEAKLLLQQLSEL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 235 refESRLADAlQELRAQHEDQVEQYKKELEKTYSAkldnarQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS------- 307
Cdd:COG3206 225 ---ESQLAEA-RAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvi 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 308 QLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
.
gi 2244986507 388 R 388
Cdd:COG3206 375 E 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-448 |
3.78e-04 |
|
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: 43.95 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 49 VRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERarlQLELSKVREEFKELK--ARNTKKEGD 126
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEH---EVEITGLTEKASSARsqANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 127 LIAAQAR---------LKDLEALLNSKEAALSTAlseKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL 197
Cdd:pfam15921 303 IIQEQARnqnsmymrqLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 198 QTMKEELDFQKNIYSEELRETKR---RHETRLVEIDNgKQREFESRLADaLQELRAQHEDQVEQYKKELEKTYSAkLDNA 274
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDH-LRRELDDRNME-VQRLEALLKAMKSECQGQMERQMAA-IQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 275 RQSAERNSNLVGaaheELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERdtsrRLLAEKEREMAEMRARMQQ 354
Cdd:pfam15921 457 NESLEKVSSLTA----QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE----RAIEATNAEITKLRSRVDL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 355 QLDEYQELldiklaldmeihayrkllEGEEERLRlspsptsqRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHA 434
Cdd:pfam15921 529 KLQELQHL------------------KNEGDHLR--------NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582
|
410
....*....|....
gi 2244986507 435 RTSGRVAVEEVDEE 448
Cdd:pfam15921 583 RTAGAMQVEKAQLE 596
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
78-404 |
4.57e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKArntkkegdLIAAQARLkdleALLNSKEAALSTALSEKRT 157
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSR--------FIGSHLAV----AFEADPEAELRQLNRRRVE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 158 LEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVD--AENRLQTMKEELDFQkniySEELRETKR---RHETRLVEID 230
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSalNRLLPRLNllADETLADRVEEIREQ----LDEAEEAKRfvqQHGNALAQLE 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 231 ngkqrefesRLADALQELRAQHeDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 310
Cdd:PRK04863 925 ---------PIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRL 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 311 KQLAAKEAKLRD-LEDSLARERDTSRRLLAEKERemaemRARMQQQLDEY-QELLDIKLALDmeihayrkllEGEEERLR 388
Cdd:PRK04863 995 EQAEQERTRAREqLRQAQAQLAQYNQVLASLKSS-----YDAKRQMLQELkQELQDLGVPAD----------SGAEERAR 1059
|
330
....*....|....*....
gi 2244986507 389 LSPSPTSQR---SRGRASS 404
Cdd:PRK04863 1060 ARRDELHARlsaNRSRRNQ 1078
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
79-185 |
4.74e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 79 AAYEAELGDARKTLDSVAKERARLQLELskvrEEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTL 158
Cdd:COG1566 106 LGAEAEIAAAEAQLAAAQAQLDLAQREL----ERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREE 181
|
90 100
....*....|....*....|....*..
gi 2244986507 159 EgELHDLRGQVAKLEAALGEAKKQLQD 185
Cdd:COG1566 182 E-ELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
51-319 |
6.06e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.22 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 51 SLETENAGLRLRITESEEVVSREVSGIKAAYEA-------ELGDARKTLDSVAKERARLQLELSKVREEfkelKARNTKK 123
Cdd:pfam18971 571 SLQEANKLIKDFLSSNKELAGKALNFNKAVAEAkstgnydEVKKAQKDLEKSLRKREHLEKEVEKKLES----KSGNKNK 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 124 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLqDEMLRRVD-----AENRLQ 198
Cdd:pfam18971 647 MEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSF-DEFKNGKNkdfskAEETLK 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 199 TMKEELDfQKNIYSEELRETKRRHETrLVEIDNGKQREFeSRLADALQELRAQHEDQVeqykkeLEKTYSAKLDNARQSA 278
Cdd:pfam18971 726 ALKGSVK-DLGINPEWISKVENLNAA-LNEFKNGKNKDF-SKVTQAKSDLENSVKDVI------INQKVTDKVDNLNQAV 796
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2244986507 279 ErnsnlVGAAHEELQqsriRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:pfam18971 797 S-----VAKAMGDFS----RVEQVLADLKNFSKEQLAQQAQ 828
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
93-388 |
7.36e-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: 42.70 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 93 DSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEAL---LNSKEAA----LSTALSEKRTLEGELHDL 165
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQikdLNDKLKKnkdkINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 166 RGQVAKLEAALGEAKKQLQ--DEMLRRVDAE---------------NRLQTMKEELDFQKNIYSEE----------LRET 218
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKenKKNIDKFLTEikkkekeleklnnkyNDLKKQKEELENELNLLEKEklniqknidkIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 219 KRRHETRLVEID--NGKQREFESRLADaLQELRAQHEDQVEQYKKELEKTYSA------KLDNARQSAERNSNLVGAAHE 290
Cdd:TIGR04523 196 LLKLELLLSNLKkkIQKNKSLESQISE-LKKQNNQLKDNIEKKQQEINEKTTEisntqtQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 291 ELQQSRIRIDSLSAQLSQLQ-------------------KQLAAKEAKLRDLE-----------------DSLARERDTS 334
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKseisdlnnqkeqdwnkelkSELKNQEKKLEEIQnqisqnnkiisqlneqiSQLKKELTNS 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2244986507 335 -------RRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:TIGR04523 355 esensekQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
47-363 |
7.47e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 47 DRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKegd 126
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 127 liaaqarLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL-----QDEMLRRVDAENRLQT-- 199
Cdd:pfam15921 344 -------IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeQNKRLWDRDTGNSITIdh 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 200 MKEELDfQKNIYSEELR--------ETKRRHETRLVEIdNGKQREFESrladaLQELRAQHEDQVEQYKKELEKTYSAKL 271
Cdd:pfam15921 417 LRRELD-DRNMEVQRLEallkamksECQGQMERQMAAI-QGKNESLEK-----VSSLTAQLESTKEMLRKVVEELTAKKM 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 272 dnARQSAERNSNLVGAAheeLQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED------SLARERDTSRRLLAEKEREM 345
Cdd:pfam15921 490 --TLESSERTVSDLTAS---LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdhlrNVQTECEALKLQMAEKDKVI 564
|
330
....*....|....*...
gi 2244986507 346 AEMRarmqQQLDEYQELL 363
Cdd:pfam15921 565 EILR----QQIENMTQLV 578
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
83-422 |
7.68e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 83 AELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGEL 162
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDER 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 163 HDLRGQ--------------VAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDF------QKNIYSEELRETKRRH 222
Cdd:pfam01576 499 NSLQEQleeeeeakrnverqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAltqqleEKAAAYDKLEKTKNRL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 223 ETRL--VEIDNGKQREFESRLadalqELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRID 300
Cdd:pfam01576 579 QQELddLLVDLDHQRQLVSNL-----EKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 301 SLSAQLSQLQKQLAAKEAKLRDLEDSlARERDTSRRLLaekEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLL 380
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKN-VHELERSKRAL---EQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF 729
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2244986507 381 E---------GEEERLRLSpsptSQRSRGRASSHSSQTQGGGSVTKKRKLE 422
Cdd:pfam01576 730 ErdlqardeqGEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLE 776
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
114-349 |
7.87e-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: 42.89 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 114 KELKARNTKKEGDliAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRG--------------QVAKLEAALGEA 179
Cdd:pfam10174 336 KEQRAAILQTEVD--ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerkinvlqkKIENLQEQLRDK 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 180 KKQLqDEMLRRV-----DAENR---LQTMKEELDFQKNIYsEELRETKRRHE-TRLVEIDNGKQrefesRLADALQELRA 250
Cdd:pfam10174 414 DKQL-AGLKERVkslqtDSSNTdtaLTTLEEALSEKERII-ERLKEQREREDrERLEELESLKK-----ENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 251 QHEDQVEQYKKELEKTYSAKldNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA------KLRDLE 324
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHAS--SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeindRIRLLE 564
|
250 260
....*....|....*....|....*
gi 2244986507 325 DSLARERDTSRRLLAEKEREMAEMR 349
Cdd:pfam10174 565 QEVARYKEESGKAQAEVERLLGILR 589
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
32-358 |
9.50e-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: 42.50 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVS------REVSGIKAAYEAELGDARKTLDSVAKERARLQLE 105
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNkktkqlQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 106 LSKVREEFKElkarntkKEGDLIAAQARLKDLEALLNSKEAALST---ALSEK-RTLEgelhDLRGQVAKLEAALGE--- 178
Cdd:pfam10174 403 IENLQEQLRD-------KDKQLAGLKERVKSLQTDSSNTDTALTTleeALSEKeRIIE----RLKEQREREDRERLEele 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 179 -AKKQLQDeMLRRVDAENRLQTMKEE--LDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQelRAQHEDQ 255
Cdd:pfam10174 472 sLKKENKD-LKEKVSALQPELTEKESslIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK--KAHNAEE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 256 VEQYKKElektYSAKLDNARQSAERNSnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSR 335
Cdd:pfam10174 549 AVRTNPE----INDRIRLLEQEVARYK-------EESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQN 617
|
330 340
....*....|....*....|...
gi 2244986507 336 RLLAEKEREMAEMRARMQQQLDE 358
Cdd:pfam10174 618 KKVANIKHGQQEMKKKGAQLLEE 640
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
69-199 |
9.56e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 69 VVSREVSGIKAAYE------AELGDA----RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLE 138
Cdd:PRK09039 43 FLSREISGKDSALDrlnsqiAELADLlsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2244986507 139 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQT 199
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
129-361 |
9.73e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 129 AAQARLKDLEALLNSKEAALSTALSEKRTLEGElhdlrgQVAKLEAALGEAKKQLQDEM-LRRVDAENRLQTMKEELDFQ 207
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQAVKA------HTDSLKEASDTAEISREKATdSALQKAEALAEKLKEVINLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 208 KNIYSEELRETK-RRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVE----QYKKELEKTY-----SAKLDNARQS 277
Cdd:pfam09731 203 KQSEEEAAPPLLdAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVAseriVFQQELVSIFpdiipVLKEDNLLSN 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 278 AERNSnLVGAAHEELQQSRIRIDSLSAQLSQ-LQKQLAAKEAKLRDLEDSLARE-----RDTSRRLLAEKEREMAEMRAR 351
Cdd:pfam09731 283 DDLNS-LIAHAHREIDQLSKKLAELKKREEKhIERALEKQKEELDKLAEELSARleevrAADEAQLRLEFEREREEIRES 361
|
250
....*....|
gi 2244986507 352 MQQQLDEYQE 361
Cdd:pfam09731 362 YEEKLRTELE 371
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
253-371 |
1.05e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 253 EDQVEQYKKELEKTYsAKLDNARQsaernsnlvgaAHEELQQSRIRID------SLSAQLSQLQKQLAAKEAKLRDLEDS 326
Cdd:COG3524 176 EDAVRFAEEEVERAE-ERLRDARE-----------ALLAFRNRNGILDpeataeALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2244986507 327 L---ARERDTSRRLLAEKEREMAEMRARM---------QQQLDEYQEL-LDIKLALDM 371
Cdd:COG3524 244 LspnSPQVRQLRRRIAALEKQIAAERARLtgasggdslASLLAEYERLeLEREFAEKA 301
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
63-385 |
1.17e-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: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 63 ITESEEVVSREVSGIKAAYEAE-LGDARKTLDSvakerARLQLELSKVREEFKELKARNTKKEGDLIAAQAR----LKDL 137
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEkLKNIELTAHC-----DKLLLENKELTQEASDMTLELKKHQEDIINCKKQeermLKQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 138 EALlNSKEAALSTAL-SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDfQKNIYSEELR 216
Cdd:pfam05483 537 ENL-EEKEMNLRDELeSVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE-NKNKNIEELH 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 217 E------TKRRHETRLVEIDNGKQREFESRLADALQELraqhEDQVEQYKKELEKTYSAKlDNARQSAERNSNLVGAAHE 290
Cdd:pfam05483 615 QenkalkKKGSAENKQLNAYEIKVNKLELELASAKQKF----EEIIDNYQKEIEDKKISE-EKLLEEVEKAKAIADEAVK 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 291 ELQQSRIRIDSLSAQLSQLQKqlaakeaKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ-ELLDIKLAL 369
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALME-------KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLSLKKQL 762
|
330
....*....|....*.
gi 2244986507 370 DMEIHAYRKLLEGEEE 385
Cdd:pfam05483 763 EIEKEEKEKLKMEAKE 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
53-472 |
1.26e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 53 ETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKEL-----------KARNT 121
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeakkadeakkKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 122 KKEGDLIA----------------AQARLKDLEALLNSKEAALSTALSEKRTLEgELHDLRGQVAKLEAA--LGEAKKQL 183
Cdd:PTZ00121 1328 KKKADAAKkkaeeakkaaeaakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAkkKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 184 QDEMLRRVDAENRLQTMKEELDFQKNI-----YSEELRET----KRRHETRLVEidNGKQREFESRLADALQElRAQHED 254
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEEKKKAdeakkKAEEAKKAdeakKKAEEAKKAE--EAKKKAEEAKKADEAKK-KAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 255 QVEQYKKELEKTySAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA-KLRDLEDSLARE- 330
Cdd:PTZ00121 1484 KADEAKKKAEEA-KKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEe 1562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 331 -RDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQT 409
Cdd:PTZ00121 1563 kKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244986507 410 QGGGSVTKKRKLESTESRSSFSQHARTSgrvaveevDEEGKFVRLRNKSNEDQSMGNWQIKRQ 472
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKA--------EEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
82-364 |
1.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGE 161
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 162 LHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQtmKEELDFQkniyseELRETKRRHETRLVEIdngkqREFESRL 241
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--KEEKGRQ------ELEKAKRKLEGESTDL-----QEQIAEL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 242 ADALQELRAQ---HEDQVEQYKKELEKTYSAKlDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA 318
Cdd:pfam01576 228 QAQIAELRAQlakKEEELQAALARLEEETAQK-NNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 319 KLRDLEDSLA--------RERDTS--RRLLAEK----EREMAEMRARMQQQLDEYQELLD 364
Cdd:pfam01576 307 ELEDTLDTTAaqqelrskREQEVTelKKALEEEtrshEAQLQEMRQKHTQALEELTEQLE 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-339 |
1.41e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 77 IKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKR 156
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 157 TLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQRE 236
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 237 FESRLADALQELRAQHEDQVEQykkELEKtysaKLDNARQSAER--NSNLvgAAHEELQQSRIRIDSLSAQLSQLQKqla 314
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLE---ELER----ELERLEREIEAlgPVNL--LAIEEYEELEERYDFLSEQREDLEE--- 809
|
250 260
....*....|....*....|....*
gi 2244986507 315 AKEaKLRDLEDSLarERDTSRRLLA 339
Cdd:COG1196 810 ARE-TLEEAIEEI--DRETRERFLE 831
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
124-205 |
1.54e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.25 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 124 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA-ALGEAKKQLQDEMLRRVDAENRLQTMKE 202
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAqALQTAQNNLATAQAALANAEARLAKAKE 339
|
...
gi 2244986507 203 ELD 205
Cdd:TIGR04320 340 ALA 342
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
79-204 |
1.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 79 AAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEG---------DLIAAQARLKDLEALLNSKEAALS 149
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2244986507 150 TALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEEL 204
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-390 |
1.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 245 LQELRAQHEDQVEQYKKELEKTYSAK---LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLR 321
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 322 DLEDSLARERDTSRRllAEKEREMAEMRARMQ---QQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLS 390
Cdd:COG4717 120 KLEKLLQLLPLYQEL--EALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
241-349 |
1.86e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 241 LADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKE 317
Cdd:PRK09039 79 LQDSVANLRAS-LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALE 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 2244986507 318 AKLRDLE----DSLARERDTSRRL---LAEKEREMAEMR 349
Cdd:PRK09039 158 AALDASEkrdrESQAKIADLGRRLnvaLAQRVQELNRYR 196
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
103-372 |
1.91e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 103 QLELSKVREEF-----KELKARNTKKEGDLIAAQARlkdLEALLNS-----------KEaalSTALSEKR--TLEGELHD 164
Cdd:pfam10174 276 QMEVYKSHSKFmknkiDQLKQELSKKESELLALQTK---LETLTNQnsdckqhievlKE---SLTAKEQRaaILQTEVDA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 165 LRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELD--------FQKNIysEELRETKRRHETRLVEI-DNGKQR 235
Cdd:pfam10174 350 LRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDvkerkinvLQKKI--ENLQEQLRDKDKQLAGLkERVKSL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 236 EFESRLADA----LQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNL---VGAAHEELQQSRIRIDSLSAQLSQ 308
Cdd:pfam10174 428 QTDSSNTDTalttLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASS 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2244986507 309 LQKQLAAKEAKLRDLEDSLARERDTSRRLLAE-KEREMAEMRARMQQQLDEYQELLDIKLALDME 372
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQKKEECSKLENQlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKE 572
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
28-387 |
1.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 28 RLQEK-----EDLQELNDRLavyidrvrsletenaglrlritESEEVVSREVSGIKAAYEAELGDARKTLDsvakeraRL 102
Cdd:PRK04863 345 RQQEKieryqADLEELEERL----------------------EEQNEVVEEADEQQEENEARAEAAEEEVD-------EL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 103 QLELSKVREEFKELKARntkkegdliAAQARlkdlEALlnskeaalsTALSEKRTLEGeLHDLrgQVAKLEAALGEAKKQ 182
Cdd:PRK04863 396 KSQLADYQQALDVQQTR---------AIQYQ----QAV---------QALERAKQLCG-LPDL--TADNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 183 LQDEMLRRVDAENRLQTMKEELDFQKNIYS---------------EELRETKRRHETRLVEIDNGKQREfeSRLADALQE 247
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQLQQLR--MRLSELEQR 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 248 LRAQHedQVEQYKKELEKTYSAKLDNA---RQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLR 321
Cdd:PRK04863 529 LRQQQ--RAERLLAEFCKRLGKNLDDEdelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQariQRLAARAPAWL 606
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244986507 322 DLEDSLARERDTSRRLLAEKEREMAEmrarMQQQLDEYQELldiKLALDmEIHAYRKLLEGEEERL 387
Cdd:PRK04863 607 AAQDALARLREQSGEEFEDSQDVTEY----MQQLLEREREL---TVERD-ELAARKQALDEEIERL 664
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-398 |
1.93e-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: 41.59 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRItESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVRE 111
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAEL-EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 112 EFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL-QDEMLRR 190
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaEAEAQAR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 191 VDAENRLQTMKEELDFQKNIYS-----EELRETKRRHETRL------------VEIDNGKQREFE--------------- 238
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKASIQGvhgtvAQLGSVGERYATAIevaagnrlnnvvVEDDAVAKEAIEllkrrkagratflpl 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 239 SRLADALQELRAQHEDQVEQYKKEL---EKTYSA-------------KLDNARQ-------------------------S 277
Cdd:TIGR02169 581 NKMRDERRDLSILSEDGVIGFAVDLvefDPKYEPafkyvfgdtlvveDIEAARRlmgkyrmvtlegelfeksgamtggsR 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 278 AERNSNLVGAAHEE------------------LQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA 339
Cdd:TIGR02169 661 APRGGILFSRSEPAelqrlrerleglkrelssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2244986507 340 EKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRS 398
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
166-453 |
2.14e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 166 RGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKE----ELDFQKNIYSEELR---ETKR-----RHETRLVEIDNGK 233
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERmamEREReleriRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 234 QREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYSAKLdnarQSAERnsnlvgaaHEELQQSRIRIDSLSAQlsqlqk 311
Cdd:pfam17380 367 QEEIAMEISRmrELERLQMERQQKNERVRQELEAARKVKI----LEEER--------QRKIQQQKVEMEQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 312 QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRA----RMQQQLDEYQELLDIKLA-------LDMEIHAYRKLL 380
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2244986507 381 EGEEERLRLSPSPTSQRSRGRASSHSSQTqgggSVTKKRKLESTESRSSFSQHAR--TSGRVAVEEVDEEGKFVR 453
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRRE----AEEERRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMR 579
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
164-386 |
2.60e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.01 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 164 DLRGQVAKLEAALGE-AKKQLQDEMLrrVDAENRLQTMKEELDFQKNIYSEElretkrrhetrlVEIDNGKQREFESRLA 242
Cdd:COG0610 648 DYRGIFENLKKALALySEEDGKEDVL--TDPEEALEELKEALDELRALFPEG------------VDFSAFDPTEKLEALD 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 243 DALQELRAQHEDQVEQYK--KELEKTYSAkldnARQSAErnsnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK--EA 318
Cdd:COG0610 714 EAVERFLGDEEARKEFKKlfKELSRLYNL----LSPDDE----FGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKeyEE 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244986507 319 KLRDL-EDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:COG0610 786 KIRQLlDEAIDLERKEIKPRIKQNPVQYRKFSELLEEIIEEYNNGALDADEVLEELEELAKEVKEEEER 854
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
26-198 |
2.65e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 26 ITRLQEKEDLqELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSrEVSGIKAAYEAELGDARKTLDSVAKERARLQLE 105
Cdd:pfam05911 79 KTKEWEKIKA-ELEAKLVETEQELLRAAAENDALSRSLQERENLLM-KLSEEKSQAEAEIEALKSRLESCEKEINSLKYE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 106 LSKVReefKELKARNTKKEGDLIAAQARLKdlEALLNSKEAAlstalsekrTLEGELHDLRGQVAKL---EAALgeAKKQ 182
Cdd:pfam05911 157 LHVLS---KELEIRNEEKNMSRRSADAAHK--QHLESVKKIA---------KLEAECQRLRGLVRKKlpgPAAL--AQMK 220
|
170
....*....|....*.
gi 2244986507 183 LQDEMLRRVDAENRLQ 198
Cdd:pfam05911 221 LEVEMLGRDSGETRLR 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-251 |
2.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 96 AKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLE-ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA 174
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 175 ALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRET-------KRRHETRLVEIDNGKQRefESRLADALQE 247
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeaalrdlRRELRELEAEIASLERR--KSNIPARLLA 444
|
....
gi 2244986507 248 LRAQ 251
Cdd:COG4913 445 LRDA 448
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
78-291 |
3.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRT 157
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 158 -----------LEGE-LHDLRGQVAKLEAALGEAKKQLQDemlrRVDAENRLQTMKEELDFQKniysEELRETKRRHETR 225
Cdd:COG3883 98 sggsvsyldvlLGSEsFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKL----AELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244986507 226 LVEIDngKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEE 291
Cdd:COG3883 170 KAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
298-364 |
3.40e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 3.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244986507 298 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER------EMAEMRARMQQQLDEYQELLD 364
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaELAGAGAAAEGRAGELAQELD 126
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-363 |
3.48e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 3.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244986507 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDT-SRRLLAEKEREMAEMRARMQQQLDEYQELL 363
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQDL 85
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
29-372 |
3.62e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 29 LQEKEDL----QELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKaayeaELGDARKTLDSVAKERARLQ- 103
Cdd:pfam05622 6 QEEKDELaqrcHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGK-----KYLLLQKQLEQLQEENFRLEt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 104 ------LELSKVREEFKELKARNtkKEGDLIAAQAR-LKD-LEALLNSKEAAL---STALSEKRTLEgELHDLRGQVAKL 172
Cdd:pfam05622 81 arddyrIKCEELEKEVLELQHRN--EELTSLAEEAQaLKDeMDILRESSDKVKkleATVETYKKKLE-DLGDLRRQVKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 173 E---AALGEAKKQLQDEMLRRVDAENRLQTMKEEL-DFQKNIYSEELRETKRRHE-TRLVEIDNGKQREFESRLA--DAL 245
Cdd:pfam05622 158 EernAEYMQRTLQLEEELKKANALRGQLETYKRQVqELHGKLSEESKKADKLEFEyKKLEEKLEALQKEKERLIIerDTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 246 QE---------------------------------------------LRAQHEDQV-----EQYKKELEKTYSAKLDNAR 275
Cdd:pfam05622 238 REtneelrcaqlqqaelsqadallspssdpgdnlaaeimpaeireklIRLQHENKMlrlgqEGSYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 276 QsaeRNSNLvgaaHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKlrdLEDSLARERDTSRRLlaEKEREMAEMRARMQQQ 355
Cdd:pfam05622 318 R---RKNEL----ETQNRLANQRILELQQQVEELQKALQEQGSK---AEDSSLLKQKLEEHL--EKLHEAQSELQKKKEQ 385
|
410
....*....|....*..
gi 2244986507 356 LDEYQELLDIKLALDME 372
Cdd:pfam05622 386 IEELEPKQDSNLAQKID 402
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-363 |
3.81e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 3.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELL 363
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
25-182 |
3.84e-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: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 25 RITRLQEKedLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGI-----------------------KAAY 81
Cdd:COG4942 63 RIAALARR--IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlgrqpplalllspedfldavrRLQY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 82 EAELGDARK----TLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEkrt 157
Cdd:COG4942 141 LKYLAPARReqaeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE--- 217
|
170 180
....*....|....*....|....*
gi 2244986507 158 LEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
31-146 |
4.03e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 31 EKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSRevsgikaaYEAELGDARKTLDSVAKER----------A 100
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--------LERELSEARSEERREIRKDreisrldreiE 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2244986507 101 RLQLELSKVREEFKELKARntkkegdliaaQARLKDLEALLNSKEA 146
Cdd:COG2433 476 RLERELEEERERIEELKRK-----------LERLKELWKLEHSGEL 510
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
86-348 |
4.12e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 86 GDARKTLDSVAKERARLQlelsKVREEFKELK--ARNTKKEGDLIAAQarLKDLEAL---------LNSKEAALSTALSE 154
Cdd:COG0497 151 AGLEELLEEYREAYRAWR----ALKKELEELRadEAERARELDLLRFQ--LEELEAAalqpgeeeeLEEERRRLSNAEKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 155 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemLRRVDAEnrLQTMKEELDfqkNIYsEELRETKR--RHETRLVEIDNG 232
Cdd:COG0497 225 REALQEALEALSGGEGGALDLLGQALRALER--LAEYDPS--LAELAERLE---SAL-IELEEAASelRRYLDSLEFDPE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 233 KQREFESRLaDALQELRAQHEDQVEQykkelektysakldnarqsaernsnlVGAAHEELQQSRIRIDSLSAQLSQLQKQ 312
Cdd:COG0497 297 RLEEVEERL-ALLRRLARKYGVTVEE--------------------------LLAYAEELRAELAELENSDERLEELEAE 349
|
250 260 270
....*....|....*....|....*....|....*..
gi 2244986507 313 LAAKEAKLRDLEDSLARER-DTSRRLLAEKEREMAEM 348
Cdd:COG0497 350 LAEAEAELLEAAEKLSAARkKAAKKLEKAVTAELADL 386
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
136-355 |
5.93e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.55 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 136 DLEALLNSKEAALSTALSEKRTLEGELHD-LRGQVAKLEAALGEAKKQLQDEMLRRVDAE-NRLQTMKEELDFQKNIYSE 213
Cdd:pfam15709 308 NMESEEERSEEDPSKALLEKREQEKASRDrLRAERAEMRRLEVERKRREQEEQRRLQQEQlERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 214 ELRETKRRHETrlveiDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNlvgaaheelq 293
Cdd:pfam15709 388 EIRLRKQRLEE-----ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ---------- 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244986507 294 qsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQ 355
Cdd:pfam15709 453 ----RQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
33-288 |
6.06e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 33 EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEevvsrevsgIKAAY---EAELgDARKTldsVAKERARLQLELSKV 109
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENLELDEAEEALEEIEER---------IDQLYdllEKEV-DAKKY---VEKNLPEIEDYLEHA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 110 REEFKELKA--RNTKK-----EGDLiaaqARLKDLEALLNSKEAALstALSEKRTLEGEL--HDLRGQVAKLEAALGEAK 180
Cdd:pfam06160 304 EEQNKELKEelERVQQsytlnENEL----ERVRGLEKQLEELEKRY--DEIVERLEEKEVaySELQEELEEILEQLEEIE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 181 KQlQDEMlrrvdaENRLQTM-KEELDFQKNI--YSEELRETKRRHETRlveidN--GKQREFESRLADAlqelraqhEDQ 255
Cdd:pfam06160 378 EE-QEEF------KESLQSLrKDELEAREKLdeFKLELREIKRLVEKS-----NlpGLPESYLDYFFDV--------SDE 437
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2244986507 256 VEQYKKELEK------TYSAKLDNARQSAERNS----NLVGAA 288
Cdd:pfam06160 438 IEDLADELNEvplnmdEVNRLLDEAQDDVDTLYekteELIDNA 480
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
30-355 |
6.40e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 39.66 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSG---IKAAYEAELGDARKTLDSVAKE-RARLQ-- 103
Cdd:pfam15070 33 QLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGpseEEQRLQEEAEQLQKELEALAGQlQAQVQdn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 104 LELSKVREEfKELKARNTKKEGDLIAAQA--RLKDLEALLNSKeAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:pfam15070 113 EQLSRLNQE-QEQRLLELERAAERWGEQAedRKQILEDMQSDR-ATISRALSQNRELKEQLAELQNGFVKLTNENMELTS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 182 QLQDEmlrrvdaenrlQTMKEELDFQKNIYSEELRETKrrhetrlveidngKQREFESRLADALQELRAQHEDQVEQY-- 259
Cdd:pfam15070 191 ALQSE-----------QHVKKELAKKLGQLQEELGELK-------------ETLELKSQEAQSLQEQRDQYLAHLQQYva 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 260 --------KKELEKTY--SAKLDNARQSAERNSNL-VGAAHEELQQSRIRIDSLSAQLSQLQKQL--------------- 313
Cdd:pfam15070 247 ayqqlaseKEELHKQYllQTQLMDRLQHEEVQGKVaAEMARQELQETQERLEALTQQNQQLQAQLsllanpgegdglese 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2244986507 314 ----AAKEAKLRDLEDSLARER--DTSRRLLAEKEREMAEMRARMQQQ 355
Cdd:pfam15070 327 eeeeEAPRPSLSIPEDFESREAmvAFFNSALAQAEEERAELRRQLKEQ 374
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
302-428 |
6.62e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 39.61 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARerdtsrrllaEKEREMAEMRArmqqqldEYQELLDIKLALDMEIhayRKLle 381
Cdd:pfam09798 2 LRDKLELLQQEKEKELEKLKNSYEELKS----------SHEEELEKLKQ-------EVQKLEDEKKFLLNEL---RSL-- 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2244986507 382 geeerlrLSPSPTSQRSRGRASSHSSQtqgggSVTKKRKLESTESRS 428
Cdd:pfam09798 60 -------SATSPASSQSHETDTDDSSS-----VSLKKRKIEESTAES 94
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
212-388 |
7.53e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 212 SEELRETKRRHETRLVEIDNGKQREfesRLADALQELRAqHEDQVEQYKKELEKTYS------------------AKLDN 273
Cdd:COG2433 312 KEDLSVEEKLHLAREYGYDNDHERD---ALAAALKAYDA-YKNKFERVEKKVPPDVDrdevkarvirglsieealEELIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 274 ARQSAERNSNLVGAAHEElqqsrIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLlaekEREMAEMRARMQ 353
Cdd:COG2433 388 KELPEEEPEAEREKEHEE-----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL----ERELSEARSEER 458
|
170 180 190
....*....|....*....|....*....|....*
gi 2244986507 354 QQLDEYQELldikLALDMEIHAYRKLLEGEEERLR 388
Cdd:COG2433 459 REIRKDREI----SRLDREIERLERELEEERERIE 489
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
257-425 |
8.51e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.27 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 257 EQYKKELEKTYSAKLDN------ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 330
Cdd:PRK10929 26 KQITQELEQAKAAKTPAqaeiveALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 331 R------DTSRRLLaEKEREmaemrarMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSqrSRGRASS 404
Cdd:PRK10929 106 AleqeilQVSSQLL-EKSRQ-------AQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT--PLAQAQL 175
|
170 180
....*....|....*....|.
gi 2244986507 405 HSSQTQgggSVTKKRKLESTE 425
Cdd:PRK10929 176 TALQAE---SAALKALVDELE 193
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
170-263 |
9.11e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.18 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244986507 170 AKLEAALGEAKKQLQDEmlrrvdaENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELR 249
Cdd:smart00935 21 KQLEKEFKKRQAELEKL-------EKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEEL 93
|
90
....*....|....
gi 2244986507 250 AQHEDQVEQYKKEL 263
Cdd:smart00935 94 QKILDKINKAIKEV 107
|
|
| |
