|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
30-386 |
7.63e-102 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 313.40 E-value: 7.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKV 109
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 110 REEFKELKARNTKKegdllaaqarlkdleallnskeaalstaLSEKRTLEGELHDLRgqvakleaalgeakKQLQDEMLR 189
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 190 RVDAENRLQTLKEELDFQKNIYSEELRETKRRH--ETRLVEIDNGKQREfesrLADALQELRAQHEDQVEQYKKELEKTY 267
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 268 SAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAE 347
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 568921945 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 |
2.61e-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: 89.40 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 434 ARTSGRVAVEEVDEEG-----KFVRLRNKSNEDQSMGNWQIRRQNGDdplmTYRFPPKFTLKAGQVVTIWASG----AGA 504
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 568921945 505 THSPPTDLVWKaqntwgcGSSLRTALINSTGEEVAMR 541
Cdd:pfam00932 77 GYWGPSNAVWN-------NGGDAVALYDANGELVDSV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-368 |
1.33e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 32 KEDLQELNDRLAVYIDRVRSLET--ENAGLRLRITESEEVVSREVSGIK--------AAYEAELGDARKTLDSVAKERAR 101
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERqaEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 102 LQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 182 QLQDEMLRRVDAENRLQTLKeeldfqkniysEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKK 261
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAE-----------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 262 ELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEK 341
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340
....*....|....*....|....*..
gi 568921945 342 EREmAEMRARMQQQLDEYQELLDIKLA 368
Cdd:COG1196 494 LLL-LEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-362 |
6.18e-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: 78.95 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 10 TRSGAQASSTPLSPTR-ITRLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREvsgikaayEA 83
Cdd:TIGR02168 662 TGGSAKTNSSILERRReIEELEEKieeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--------RK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 84 ELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELH 163
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 164 DLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEEL-DFQKNIysEELRETKRRHETRLVEIDNGKQREFEsrla 242
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeSLAAEI--EELEELIEELESELEALLNERASLEE---- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 243 dALQELRAQHEDQVEQykkelEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQK---QLAAKEAK 319
Cdd:TIGR02168 888 -ALALLRSELEELSEE-----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALEN 961
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568921945 320 LRDLEDSLARERdtsrrlLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:TIGR02168 962 KIEDDEEEARRR------LKRLENKIKELGPVNLAAIEEYEEL 998
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-361 |
8.86e-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: 78.17 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 32 KEDLQELNDRLAVYIDRVRSLET--ENAGLRLRITESEEVVSREVSGIKA-AYEAELGDARKTLDSVAKERARLQLELSK 108
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERqaEKAERYKELKAELRELELALLVLRLeELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 109 VREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEaalstalSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 188
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-------QQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 189 RRVDAENRLQTLKEELDFQKNIYsEELRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKELEktyS 268
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELE--EQLETLRSKVAQLELQIASLNNEIERLEARLE---R 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 269 AKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARerdtSRRLLAEKEREMAEM 348
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALDAAERELAQL 487
|
330
....*....|....*....
gi 568921945 349 RAR------MQQQLDEYQE 361
Cdd:TIGR02168 488 QARldslerLQENLEGFSE 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-381 |
1.29e-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: 71.25 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 73 EVSGIkAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEgdllaaqaRLKDLEALLnsKEAALSTAL 152
Cdd:TIGR02169 161 EIAGV-AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--------RYQALLKEK--REYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 153 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELdfqKNIYSEELRETKRRHETRLVEIDN- 231
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 232 -GKQREFESRLADAlQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 310
Cdd:TIGR02169 307 eRSIAEKERELEDA-EERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568921945 311 KQLAAKEAKLRDLE---DSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLE 381
Cdd:TIGR02169 385 DELKDYREKLEKLKreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-387 |
1.40e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 110 REEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLR 189
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 190 RVDAENRLQTLKEELdfqkNIYSEELRETKRRHETRLVEIDNGKQREFESRlaDALQELRAQHEDQveqykkelektySA 269
Cdd:TIGR02168 756 LTELEAEIEELEERL----EEAEEELAEAEAEIEELEAQIEQLKEELKALR--EALDELRAELTLL------------NE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 270 KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMA 346
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELE 897
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568921945 347 EMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-401 |
3.19e-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: 65.56 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 129 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQK 208
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 209 NIYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysakldnarqsaernsnlvga 287
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 288 aheelqqsriridslsaQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 367
Cdd:COG4942 161 -----------------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|....
gi 568921945 368 ALDMEIhayRKLLEGEEERLRLSPSPTSQRSRGR 401
Cdd:COG4942 224 ELEALI---ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-390 |
4.33e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 28 RLQEKEDLQELNDRLAVYIDR---VRSLETENAGLRLRITESE---EVVSREVSGIKAAYEaELGDARKTL--------- 92
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETErerEELAEEVRDLRERLE-ELEEERDDLlaeagldda 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 93 --DSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA 170
Cdd:PRK02224 308 daEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 171 KLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSeELRETKRRHETRLVE----IDNGKQREFESRLADA-- 244
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-ELEATLRTARERVEEaealLEAGKCPECGQPVEGSph 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 245 -------------LQELRAQHEDQVEQYKKELEKTYSAK-----LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQL 306
Cdd:PRK02224 467 vetieedrerveeLEAELEDLEEEVEEVEERLERAEDLVeaedrIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 307 SQLQKQLAAKEAKLRDLEDSLARERDTsrrlLAEKEREMAEMRARMqQQLDEYQELLDIKLALDMEIHAYRKLLEG---- 382
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREAlael 621
|
....*....
gi 568921945 383 -EEERLRLS 390
Cdd:PRK02224 622 nDERRERLA 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-352 |
4.44e-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: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 96 AKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA 175
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 176 LGEAKKQLQdEMLRRVDAENRLQTLKEELDfqkniySEELRETKRRhetrlveidngkqrefesrlADALQELRAQHEDQ 255
Cdd:COG4942 99 LEAQKEELA-ELLRALYRLGRQPPLALLLS------PEDFLDAVRR--------------------LQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 256 VEQYKKELEktysaKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSR 335
Cdd:COG4942 152 AEELRADLA-----ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*..
gi 568921945 336 RLLAEKEREMAEMRARM 352
Cdd:COG4942 227 ALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-362 |
6.84e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKV 109
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 110 REEFKELKAR--NTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLE-------------GELHDLRGQVAKLEA 174
Cdd:COG4717 219 QEELEELEEEleQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlGLLALLFLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 175 ALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRA---- 250
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllae 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 251 ----------QHEDQVEQYKKELEK--TYSAKLDNARQSAERNSNLVGAA--HEELQQSRIRIDSLSAQLSQLQKQLAAK 316
Cdd:COG4717 379 agvedeeelrAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAEL 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568921945 317 EAKLRDLEDSlarerdtsrRLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:COG4717 459 EAELEQLEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-351 |
8.05e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 124 EGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEgelhDLRGQVAKLEAALGEA-KKQLQDEMLRRVDAENRLQTLKE 202
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLE----PIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 203 ELdfqkniysEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNS 282
Cdd:COG4913 296 EL--------EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLEREIERL-ERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568921945 283 NLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 351
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-280 |
2.10e-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: 60.84 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 6 QRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSRevsgikaaYEAEL 85
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES--------LERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 86 GDARKTLDSVAKERARLQLELSKVREEFKELKARNTKkegdllaAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDL 165
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 166 RGQVAKLEAALGEAKKQLqdemlrrVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNG--KQREFESRLAD 243
Cdd:TIGR02168 907 ESKRSELRRELEELREKL-------AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDeeEARRRLKRLEN 979
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568921945 244 ALQELRAQHEDQVEQYKKELE-----KTYSAKLDNARQSAER 280
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKErydflTAQKEDLTEAKETLEE 1021
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
111-355 |
1.10e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 111 EEFKELKARNTKKEGDLLaaQARLKDLEALLNSKEAALSTALSEKRTLegelhDLRGQVAKLEAALGEAKKQLQDEMLRR 190
Cdd:COG3206 163 EQNLELRREEARKALEFL--EEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 191 VDAENRLQTLKEELDFQKNIYSEELR-ETKRRHETRLVEIdngkqrefESRLADALQELRAQHEDqVEQYKKELEKTysa 269
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAEL--------EAELAELSARYTPNHPD-VIALRAQIAAL--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 270 kldnARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ---LAAKEAKLRDLEdslaRERDTSRRLLAEKEREMA 346
Cdd:COG3206 304 ----RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLE----REVEVARELYESLLQRLE 375
|
....*....
gi 568921945 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 ... |
27-363 |
2.14e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.49 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 27 TRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGikaayEAELGDARKTLDSvakERARLQLEL 106
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-----RQELEKAKRKLEG---ESTDLQEQI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 107 SKVREEFKELKARNTKKEGDLLAAQARLKDleallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQlqde 186
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEE-------ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ---- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 187 mlrRVDAENRLQTLKEELD--FQKNIYSEELReTKRRHETRLVEidngKQREFESRLADA-LQELRAQHEDQVEQYKKEL 263
Cdd:pfam01576 294 ---RRDLGEELEALKTELEdtLDTTAAQQELR-SKREQEVTELK----KALEEETRSHEAqLQEMRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 264 EKTYSAK--LDNARQSAERNSNLVGAAHEELQQSRI----RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTS 334
Cdd:pfam01576 366 EQAKRNKanLEKAKQALESENAELQAELRTLQQAKQdsehKRKKLEGQLQELQARLSESERQRAELAEKLSKlqsELESV 445
|
330 340 350
....*....|....*....|....*....|..
gi 568921945 335 RRLLAEKERE---MAEMRARMQQQLDEYQELL 363
Cdd:pfam01576 446 SSLLNEAEGKnikLSKDVSSLESQLQDTQELL 477
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-389 |
2.41e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 59 LRLRITESEEVVSRE--VSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVR----------EEFKELKARNTKKEGD 126
Cdd:PRK03918 174 IKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkeleelkEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 127 LLAAQARLKDLEALLNSKEAALSTaLSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDf 206
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 207 QKNIYSEELRETKRrhetRLVEIDNgKQREFESRlADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERnsnlvg 286
Cdd:PRK03918 332 ELEEKEERLEELKK----KLKELEK-RLEELEER-HELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEK------ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 287 aAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEdSLARERDTSRRLLAEKERE--MAEMRARMQQQLDEYQELLD 364
Cdd:PRK03918 399 -AKEEIEE---EISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEE 473
|
330 340
....*....|....*....|....*
gi 568921945 365 IKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKL 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-388 |
4.52e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 25 RITRLqeKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV---SREVSGIKAAYEAELGDARKTLDSVAKERAR 101
Cdd:COG4913 339 RLEQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFaalRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 102 LQLELSKVREEFKELKARNTKKEGDLLAAQARlkdLEALLNSKEAALSTA--LSEKRT--------LEGELHDLR----- 166
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELPFVgeLIEVRPeeerwrgaIERVLGGFAltllv 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 167 -----GQVA------KLEAAL--GEAKKQLQDEMLRRVDAenrlQTLKEELDFQKNIYS-------------------EE 214
Cdd:COG4913 494 ppehyAAALrwvnrlHLRGRLvyERVRTGLPDPERPRLDP----DSLAGKLDFKPHPFRawleaelgrrfdyvcvdspEE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 215 LRETKR--------RHETRLVEID--------------NGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYSAKLD 272
Cdd:COG4913 570 LRRHPRaitragqvKGNGTRHEKDdrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 273 NARQSAERNSNL--VGAAHEELQQSRIRIDSL---SAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEReMAE 347
Cdd:COG4913 649 ALQRLAEYSWDEidVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-AEE 727
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568921945 348 MRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
72-364 |
6.07e-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: 55.67 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 72 REVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELK---ARNTKKEGDLLAAQARLKDLEALLNSKEAAL 148
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 149 STALSEK----RTLEGELHDLRGQVAKLEAALGEAKK-------QLQDEMLRRVDAENRLQTLKEEL-----DFQKNIYS 212
Cdd:pfam07888 121 LAQRAAHeariRELEEDIKTLTQRVLERETELERMKErakkagaQRKEEEAERKQLQAKLQQTEEELrslskEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 213 EELRETK----RRHETRLVEIDNGKQR---EFESRLAD--ALQELRAQHEDQVEQYKKELEKTYS------AKLDNAR-Q 276
Cdd:pfam07888 201 LAQRDTQvlqlQDTITTLTQKLTTAHRkeaENEALLEElrSLQERLNASERKVEGLGEELSSMAAqrdrtqAELHQARlQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 277 SAERNSNLVGAA-------------HEELQQS----RIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA 339
Cdd:pfam07888 281 AAQLTLQLADASlalregrarwaqeRETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|..
gi 568921945 340 EKEREMAEMRARMQ-------QQLDEYQELLD 364
Cdd:pfam07888 361 ESRRELQELKASLRvaqkekeQLQAEKQELLE 392
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-388 |
6.13e-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: 56.22 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 101 RLQLELSKVrEEFKELKARNTKKEGDLLAAQarlkdlealLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALgeak 180
Cdd:TIGR02168 204 SLERQAEKA-ERYKELKAELRELELALLVLR---------LEELREELEELQEELKEAEEELEELTAELQELEEKL---- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 181 kqlqdemlrrvdaeNRLQTLKEELDFQKNIYSEELRETK---RRHETRLVEID-------------NGKQREFESRLaDA 244
Cdd:TIGR02168 270 --------------EELRLEVSELEEEIEELQKELYALAneiSRLEQQKQILRerlanlerqleelEAQLEELESKL-DE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 245 LQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLE 324
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESL-EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568921945 325 DSlaRERDTSRRLLAEKEREMAEMRArMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:TIGR02168 414 DR--RERLQQEIEELLKKLEEAELKE-LQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-355 |
8.19e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 24 TRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESE------EVVSREVSGIKAAYEAELGDARKTLDSVAK 97
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELEseleeaREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 98 ERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNS----------KEAALSTALSEKR----TLEGELH 163
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRerveELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 164 DLRGQVAKLEA------ALGEAKKQLQDEMLRRVDAENRLQTLKEELDfQKNIYSEELRETKRRHETRLVEID------- 230
Cdd:PRK02224 486 DLEEEVEEVEErleraeDLVEAEDRIERLEERREDLEELIAERRETIE-EKRERAEELRERAAELEAEAEEKReaaaeae 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 231 -------------NGKQREFESRL----------------ADALQELRAQHEDQVE---------QYKKELEKTYSAKLD 272
Cdd:PRK02224 565 eeaeeareevaelNSKLAELKERIeslerirtllaaiadaEDEIERLREKREALAElnderrerlAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 273 NARQSAERNSNlvGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA---------EKER 343
Cdd:PRK02224 645 EARIEEAREDK--ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAlealydeaeELES 722
|
410
....*....|..
gi 568921945 344 EMAEMRARMQQQ 355
Cdd:PRK02224 723 MYGDLRAELRQR 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-362 |
1.92e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 162 LHDLRGQVAKLEAALGEAKKQLqDEMLRRVDAENRLQTLKEEL-DFQKNIYSEELRE-TKRRHETRLVEIDNGKQREFES 239
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQL-KSLERQAEKAERYKELKAELrELELALLVLRLEElREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 240 RLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ---LAAK 316
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKldeLAEE 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568921945 317 EAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
82-267 |
2.32e-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: 52.23 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSkeaalstALSEKrtlegE 161
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-------VRNNK-----E 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 162 LHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKniysEELRETKRRHETRLVEIDngkqrefesrl 241
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE----AELEEKKAELDEELAELE----------- 155
|
170 180
....*....|....*....|....*.
gi 568921945 242 aDALQELRAQHEDQVEQYKKELEKTY 267
Cdd:COG1579 156 -AELEELEAEREELAAKIPPELLALY 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-388 |
2.83e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 96 AKERARLQLE--LSKVREEF-KELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKL 172
Cdd:pfam01576 710 ATEDAKLRLEvnMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 173 EAALGEAKKQL--------------------QDEMLRRV-DAENRLQTLKEE-LDFQKNIYSEE---------------- 214
Cdd:pfam01576 790 NKGREEAVKQLkklqaqmkdlqreleearasRDEILAQSkESEKKLKNLEAElLQLQEDLAASErarrqaqqerdelade 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 215 ----------LRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKEL--EKTYSAKLDNARQSAERNS 282
Cdd:pfam01576 870 iasgasgksaLQDEKRRLEARIAQLE--EELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQN 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 283 NLVGAAHEELQqsriridslSAQLSQLQKQLAAKEAKLRDLEDSL---ARERDTSRRLLAEKEREMAEMRARMQ---QQL 356
Cdd:pfam01576 948 KELKAKLQEME---------GTVKSKFKSSIAALEAKIAQLEEQLeqeSRERQAANKLVRRTEKKLKEVLLQVEderRHA 1018
|
330 340 350
....*....|....*....|....*....|..
gi 568921945 357 DEYQELLDiKLALDMEiHAYRKLLEGEEERLR 388
Cdd:pfam01576 1019 DQYKDQAE-KGNSRMK-QLKRQLEEAEEEASR 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-448 |
3.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 31 EKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVR 110
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 111 EEFKELKARN---TKKEGDLLAAQARLKDLEALLnSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEM 187
Cdd:COG1196 387 ELLEALRAAAelaAQLEELEEAEEALLERLERLE-EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 188 LRRVDAENRLQTLKEELDfqkniysEELRETKRRHETRLVEIDNGKQREFESRLADALQELR--AQHEDQVEQYKKELEK 265
Cdd:COG1196 466 AELLEEAALLEAALAELL-------EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 266 TYSAKLDNARQSAERNSNLVGAAHEELQQSR-------IRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLL 338
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 339 AE-----------KEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSS 407
Cdd:COG1196 619 GDtllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568921945 408 QSQGGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEE 448
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-362 |
3.37e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 29 LQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESE---EVVSREVSGIKAAYEA-----------------ELGDA 88
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKEIEQLEQEEEKlkerleeleedlssleqEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 89 RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQ------------ARLKDLEALLNSKEAALSTALSEKR 156
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskleeevsrieARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 157 TLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELdfqkniysEELRETKRRHETRLVEIDNGKqre 236
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELERKI--- 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 237 fesrladalQELRAQHEDqveqyKKELEKTYSAKLDNArqsAERNSNLvgaahEELQQSRIRIDSLSAQLSQLQKQLAAK 316
Cdd:TIGR02169 906 ---------EELEAQIEK-----KRKRLSELKAKLEAL---EEELSEI-----EDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568921945 317 EAKLRDLED--SLARE--RDTSRRL--LAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:TIGR02169 964 EEEIRALEPvnMLAIQeyEEVLKRLdeLKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
104-265 |
7.61e-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: 50.69 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 104 LELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ- 182
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 183 ----LQDEM----LRRVDAENRLQTLKEELDFQKniysEELRETKRRHETRLVEIDNgKQREFESRLADaLQELRAQHED 254
Cdd:COG1579 90 eyeaLQKEIeslkRRISDLEDEILELMERIEELE----EELAELEAELAELEAELEE-KKAELDEELAE-LEAELEELEA 163
|
170
....*....|.
gi 568921945 255 QVEQYKKELEK 265
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
24-178 |
9.14e-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: 50.31 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 24 TRITRLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVsREVSGIKAAYEAELGDAR--KTLDSVA 96
Cdd:COG1579 17 SELDRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-EEVEARIKKYEEQLGNVRnnKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 97 KERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEkrtLEGELHDLRGQVAKLEAAL 176
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI 172
|
..
gi 568921945 177 GE 178
Cdd:COG1579 173 PP 174
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-350 |
9.35e-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: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 24 TRITRLQEKEDL--QELNdRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAeLGDARKTLDSVAKERAR 101
Cdd:pfam15921 517 AEITKLRSRVDLklQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQ 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 102 LQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 182 QLqdEMLRR--VDAENRLQTLKEELDFQKNIYSEELRETKRRHET------RLVEIDNGKQREFESRLA--DALQELRAQ 251
Cdd:pfam15921 675 DY--EVLKRnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdgHAMKVAMGMQKQITAKRGqiDALQSKIQF 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 252 HEDQVEQYKKE--LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRidsLSAQLSQLQKQLAAKEAKLRDLEDSLAR 329
Cdd:pfam15921 753 LEEAMTNANKEkhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR---LKEKVANMEVALDKASLQFAECQDIIQR 829
|
330 340
....*....|....*....|.
gi 568921945 330 ERDTSRRLLAEKEREMAEMRA 350
Cdd:pfam15921 830 QEQESVRLKLQHTLDVKELQG 850
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
32-357 |
9.36e-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: 51.61 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIkAAYEAELGDARKTLDSVAKERARLQLELSKVRE 111
Cdd:pfam19220 68 RRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIEL-RDKTAQAEALERQLAAETEQNRALEEENKALRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 112 EFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRV 191
Cdd:pfam19220 147 EAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 192 DAENRLQTLKEELDFQKNIYSEELRETKRRHET----------RLVEIDNGkQREFESRLADA----------LQELRAQ 251
Cdd:pfam19220 227 RAEAQLEEAVEAHRAERASLRMKLEALTARAAAteqllaearnQLRDRDEA-IRAAERRLKEAsierdtlerrLAGLEAD 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 252 HEDQVEQYKKelektysakLDNARQSAERNSNLVG---AAHE-ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDledsl 327
Cdd:pfam19220 306 LERRTQQFQE---------MQRARAELEERAEMLTkalAAKDaALERAEERIASLSDRIAELTKRFEVERAALEQ----- 371
|
330 340 350
....*....|....*....|....*....|
gi 568921945 328 arerdTSRRLLAEKEREMAEmRARMQQQLD 357
Cdd:pfam19220 372 -----ANRRLKEELQRERAE-RALAQGALE 395
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-342 |
1.15e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 138 EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRE 217
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 218 TKR--RHETRLVEIDNGKQ-REFESRLaDALQELRAQHEDQVEQYKKELEKtysakLDNARQSAERNSNLVGAAHEELQQ 294
Cdd:COG3883 95 LYRsgGSVSYLDVLLGSESfSDFLDRL-SALSKIADADADLLEELKADKAE-----LEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568921945 295 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKE 342
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-351 |
1.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 26 ITRLQEKED-LQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIK-AAYEAELGDARKTLDSVAK---ERA 100
Cdd:COG4913 609 RAKLAALEAeLAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 101 RLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAK 180
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 181 KQLQDemlRRVDAENRLQTLKEELdfqkniySEELRETKRRHETRLVEIDNGKQ--REFESRLADALQELRAQHEDQVEQ 258
Cdd:COG4913 769 ENLEE---RIDALRARLNRAEEEL-------ERAMRAFNREWPAETADLDADLEslPEYLALLDRLEEDGLPEYEERFKE 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 259 YKKELEKT----YSAKLDNARQSAERNSNLVGAAHEEL---QQSRIRID---SLSAQLSQLQKQL--AAKEAKLRDLEDS 326
Cdd:COG4913 839 LLNENSIEfvadLLSKLRRAIREIKERIDPLNDSLKRIpfgPGRYLRLEarpRPDPEVREFRQELraVTSGASLFDEELS 918
|
330 340
....*....|....*....|....*...
gi 568921945 327 LARERDTSR---RLLAEKEREMAEMRAR 351
Cdd:COG4913 919 EARFAALKRlieRLRSEEEESDRRWRAR 946
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
114-205 |
1.70e-06 |
|
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: 50.50 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 114 KELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKL-EAALGEAKKQLQdemlrrvD 192
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALA-------N 329
|
90
....*....|...
gi 568921945 193 AENRLQTLKEELD 205
Cdd:TIGR04320 330 AEARLAKAKEALA 342
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-388 |
1.71e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 189 RRVDAENRL----------------------------------QTLKEELD-FQKNIYSEELRETKRRHETRLVEIDNGK 233
Cdd:COG1196 173 RKEEAERKLeateenlerledilgelerqleplerqaekaeryRELKEELKeLEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 234 QREfesrlaDALQELRAQHEDQVEQYKKELE------KTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS 307
Cdd:COG1196 253 AEL------EELEAELAELEAELEELRLELEelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 308 QLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEE 384
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
....
gi 568921945 385 ERLR 388
Cdd:COG1196 407 EAEE 410
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
90-387 |
2.83e-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: 50.56 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 90 KTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLE----------ALLNSKEAALSTALSEkrtLE 159
Cdd:pfam01576 377 KAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNE---AE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 160 GELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEElrETKRRHETRLVEIDNGKQREFES 239
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE--EEAKRNVERQLSTLQAQLSDMKK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 240 RLADALQELraqheDQVEQYKKELEKtysaKLDNARQSAERNSnlvgAAHEELQQSRIR----IDSLSAQLSQLQKQLAA 315
Cdd:pfam01576 532 KLEEDAGTL-----EALEEGKKRLQR----ELEALTQQLEEKA----AAYDKLEKTKNRlqqeLDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921945 316 KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDmEIHAYRKLLEGEEERL 387
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
185-390 |
5.35e-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: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 185 DEMLRRVDAENRLQTLKEELDFQKNIYSEELRE---TKRRHETRLVEID-NGKQREFESRLADALQE--LRAQHEDQVEQ 258
Cdd:COG3206 93 RPVLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGSNVIEISyTSPDPELAAAVANALAEayLEQNLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 259 YKKELE------KTYSAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 330
Cdd:COG3206 173 ARKALEfleeqlPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568921945 331 RDTSRRLLAekEREMAEMRARMQQQLDEYQELL--------DIKlALDMEIHAYRKLLEGEEERLRLS 390
Cdd:COG3206 253 PDALPELLQ--SPVIQQLRAQLAELEAELAELSarytpnhpDVI-ALRAQIAALRAQLQQEAQRILAS 317
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-387 |
5.81e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 25 RITRLQEKEDL-QELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSrEVSGIKAAYEAELGDARKTLDSVA--KERAR 101
Cdd:PRK03918 284 ELKELKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEelEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 102 LQLELSKVREEFKELKARNTKKEgdllaaqarLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLT---------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 182 QLQDEML--RRVDAENRLQTLKEELDFQKNIYSE--ELRETKRRHETRLVEIDNGKQREfesrladalQELRAQHE--DQ 255
Cdd:PRK03918 434 AKGKCPVcgRELTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELRELEKVLKKE---------SELIKLKElaEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 256 VEQYKKELEKTYSAKLdnarqsaERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERD 332
Cdd:PRK03918 505 LKELEEKLKKYNLEEL-------EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLK 577
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568921945 333 TSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKlaldMEIHAYRKLLEGEEERL 387
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEYLELKDAE----KELEREEKELKKLEEEL 628
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-228 |
7.35e-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: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 25 RITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVsrevsgikAAYEAELGDARKTLDSVAKERA--RL 102
Cdd:COG3206 197 ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL--------AALRAQLGSGPDALPELLQSPViqQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 103 QLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNS-KEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568921945 182 QlqdemlrrvdaENRLQTLKEELDFQKNIYSEELretKRRHETRLVE 228
Cdd:COG3206 349 L-----------EAELRRLEREVEVARELYESLL---QRLEEARLAE 381
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
139-348 |
7.73e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 139 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQdeMLRRV----------DAENRLQTLKEELDFqk 208
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ--LLNKLlpqanlladeTLADRLEELREELDA-- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 209 niySEELRETKRRHETRLVEIDngkqrefesRLADALQELRAQHEDQVEQYK--KELEKTYSAKLDNARQSAERNSNLVG 286
Cdd:COG3096 905 ---AQEAQAFIQQHGKALAQLE---------PLVAVLQSDPEQFEQLQADYLqaKEQQRRLKQQIFALSEVVQRRPHFSY 972
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921945 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 |
1.05e-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: 49.07 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 34 DLQELNDRLAVYIDRVRSLETENAGLRLRITESE----EVVSREVSGIKAAYEAELGDARKTLDSVAKE-RARLQLELSK 108
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 109 VREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAaLSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 188
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 189 RRVDAENRLQTLKEELDFQKNIYSEELREtkrrhetrlveiDNGKQREFESRLADALQELRAQ-HEDQVEQYKKELEKTY 267
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTLLHFLRK------------EAPDWEQSIGKVISPELLHRTDlDPEVWDGSVGGELNLY 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 268 SAKLDNAR-------QSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:pfam12128 582 GVKLDLKRidvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE 661
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568921945 341 KERE---MAEMRARMQQQLDEYQELLDIKL-ALDMEIHAYRKLLEGEEERLR 388
Cdd:pfam12128 662 KQSEkdkKNKALAERKDSANERLNSLEAQLkQLDKKHQAWLEEQKEQKREAR 713
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
82-352 |
1.72e-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: 48.30 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTAL-SEKRTLEG 160
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLR-RVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFES 239
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 240 RLADalqelraqhEDQVEQYKKELeKTYSAKLDNARQ-SAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAA 315
Cdd:pfam12128 763 LGVD---------PDVIAKLKREI-RTLERKIERIAVrRQEVLRYFDWYQETWLQRRprlATQLSNIERAISELQQQLAR 832
|
250 260 270
....*....|....*....|....*....|....*..
gi 568921945 316 KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARM 352
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-387 |
1.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 32 KEDLQELNDRLAVYIDRVRSLETENAGLRlRITESEEVVSREVSGIKAaYEAELGDARKTLDSVAKERARLQ-LELSKVR 110
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTgLTPEKLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 111 EEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRT-------------------LEGELHDLRGQVAK 171
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelleeYTAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 172 LEAALGEAKKQLQdEMLRRVDAENRLQTLKEELDFQKniyseELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQ 251
Cdd:PRK03918 471 IEEKERKLRKELR-ELEKVLKKESELIKLKELAEQLK-----ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 252 HED--QVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSA------QLSQLQKQLAAKEAKLRDL 323
Cdd:PRK03918 545 KKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKL 624
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568921945 324 EDSLarerDTSRRLLAEKEREMAEMRARMQQQL-----DEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:PRK03918 625 EEEL----DKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
25-362 |
2.26e-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: 47.51 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 25 RITRLQEK-EDLQE-LNDR---LAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDsvaker 99
Cdd:pfam10174 395 KINVLQKKiENLQEqLRDKdkqLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE------ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 100 arlqlELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALgea 179
Cdd:pfam10174 469 -----ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL--- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 180 KKQLQDEMLRRVDAE--NRLQTLKEELDFqkniYSEELRETKRRHEtRLVEIdngkQREFESRLADALQELRAQHEDQVE 257
Cdd:pfam10174 541 KKAHNAEEAVRTNPEinDRIRLLEQEVAR----YKEESGKAQAEVE-RLLGI----LREVENEKNDKDKKIAELESLTLR 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 258 QYKKELEKTYSAKLdnaRQSAERNSNLvgaahEELQQSRIRIDSL--SAQLSQLQKQLAAKEAKLRDLEDSLARERDTsR 335
Cdd:pfam10174 612 QMKEQNKKVANIKH---GQQEMKKKGA-----QLLEEARRREDNLadNSQQLQLEELMGALEKTRQELDATKARLSST-Q 682
|
330 340
....*....|....*....|....*..
gi 568921945 336 RLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:pfam10174 683 QSLAEKDGHLTNLRAERRKQLEEILEM 709
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-362 |
2.51e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 96 AKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKE-----------------AALSTALSEKRTL 158
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreeletleaeiedlrETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 159 EGELHDLRGQVAKLEAALGEAKKQLQDE-------MLRRVDAENRLQTLKEELDFQK------NIYSEELRETKRRHETR 225
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREELEDRDEELRDRLEECRvaaqahNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 226 LVEIDN----------------GKQREFESRLADALQELRAQHED------QVEQYKKEL----------EKTYSAKLDN 273
Cdd:PRK02224 358 AEELREeaaeleseleeareavEDRREEIEELEEEIEELRERFGDapvdlgNAEDFLEELreerdelrerEAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 274 ARQSAERNSNLV-------------GAAH-EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED---------SLARE 330
Cdd:PRK02224 438 ARERVEEAEALLeagkcpecgqpveGSPHvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedrieRLEER 517
|
330 340 350
....*....|....*....|....*....|..
gi 568921945 331 RDTSRRLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-174 |
2.61e-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: 47.76 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 5 SQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRlritesEEVVSREVSgiKAAYEAE 84
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR------DELKDYREK--LEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 85 LGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRT------- 157
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDlkeeydr 480
|
170
....*....|....*..
gi 568921945 158 LEGELHDLRGQVAKLEA 174
Cdd:TIGR02169 481 VEKELSKLQRELAEAEA 497
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
131-366 |
2.79e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 131 QARLKDL--EALLNSKEAALSTALSEkrTLegelhDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTLKEELDFQK 208
Cdd:PRK11281 42 QAQLDALnkQKLLEAEDKLVQQDLEQ--TL-----ALLDKIDRQKEETEQLKQQLAQ-------APAKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 209 NIYSEELRETkrrhetrlveIDNGKQREFESRLADALQELraqhedqvEQYKKELEkTYSAKLDNARQSAERNSNLVGAA 288
Cdd:PRK11281 108 DDNDEETRET----------LSTLSLRQLESRLAQTLDQL--------QNAQNDLA-EYNSQLVSLQTQPERAQAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 289 HEELQQSRIRIDSLSA--------QLSQLQKQLAAKEAKLrDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ 360
Cdd:PRK11281 169 SQRLQQIRNLLKGGKVggkalrpsQRVLLQAEQALLNAQN-DLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQ 247
|
....*.
gi 568921945 361 ELLDIK 366
Cdd:PRK11281 248 EAINSK 253
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
28-308 |
3.31e-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: 47.25 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 28 RLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEvvsrEVSGIKAayeaELGDARKTLDSV------- 95
Cdd:COG3096 344 RQQEKieryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEE----EVDSLKS----QLADYQQALDVQqtraiqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 96 -----AKERARLQLELSK-----VREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAAL------------STALS 153
Cdd:COG3096 416 qqavqALEKARALCGLPDltpenAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYelvckiageverSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 154 EKRTLEGELHDLR---GQVAKLEAALGEAKK---------QLQDEMLRR----VDAENRLQTLKEELDFQKNIYSEELRE 217
Cdd:COG3096 496 TARELLRRYRSQQalaQRLQQLRAQLAELEQrlrqqqnaeRLLEEFCQRigqqLDAAEELEELLAELEAQLEELEEQAAE 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 218 -TKRRHETR--LVEIdNGKQREFESR------LADALQELRAQHEDQVEQykkelektySAKLDNARQSAERNSNLVGAA 288
Cdd:COG3096 576 aVEQRSELRqqLEQL-RARIKELAARapawlaAQDALERLREQSGEALAD---------SQEVTAAMQQLLEREREATVE 645
|
330 340
....*....|....*....|
gi 568921945 289 HEELQQSRIRIDSLSAQLSQ 308
Cdd:COG3096 646 RDELAARKQALESQIERLSQ 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-387 |
3.40e-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: 47.37 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 153 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAEnRLQTLKEELdfQKNIYSEELREtKRRHETRLVEIDNg 232
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK--REYEGYELLKE-KEALERQKEAIER- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 233 kqrefesRLADALQELraqheDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGaahEELQQSRIRIDSLSAQLSQL--- 309
Cdd:TIGR02169 245 -------QLASLEEEL-----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLers 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 310 -------QKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 382
Cdd:TIGR02169 310 iaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
....*
gi 568921945 383 EEERL 387
Cdd:TIGR02169 390 YREKL 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-325 |
3.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 20 PLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAE-LGDARKTLDSVAKE 98
Cdd:PRK03918 439 PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqLKELEEKLKKYNLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 99 rarlqlELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEA---ALSTALSEKRTLEGELHDLR-GQVAKLEA 174
Cdd:PRK03918 519 ------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekKLDELEEELAELLKELEELGfESVEELEE 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 175 ALGEAKKqLQDEMLRRVDAENRLQTLKEELDFQKNiyseelretkrrhetrlvEIDngKQREFESRLADALQELRAQHEd 254
Cdd:PRK03918 593 RLKELEP-FYNEYLELKDAEKELEREEKELKKLEE------------------ELD--KAFEELAETEKRLEELRKELE- 650
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921945 255 qveqykkELEKTYSA-KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 325
Cdd:PRK03918 651 -------ELEKKYSEeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
161-362 |
5.44e-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: 44.92 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESR 240
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL--------EDLEKEIKRLELEIEEVEA-RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 241 LAdalqelRAQHEDQVEQYKKELEKtysakLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL 320
Cdd:COG1579 82 LG------NVRNNKEYEALQKEIES-----LKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568921945 321 RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQL-DEYQEL 362
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIPPELlALYERI 183
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-319 |
6.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 99 RARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALge 178
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 179 akkQLQDEMLRRVDAENRLQTLKEELdfqkniysEELRETKRRHETRLVEIDNGKQ--REFESRLADALQELRAQHEDQV 256
Cdd:COG4717 126 ---QLLPLYQELEALEAELAELPERL--------EELEERLEELRELEEELEELEAelAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921945 257 EQYKKELEktysaKLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:COG4717 195 QDLAEELE-----ELQQRLAELE----------EELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
33-307 |
6.82e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 33 EDLQELNdrlAVYIDrvrSLETENAGLRLR-ITESEEVVSREVSGIKAAYEAELGD----ARKTLDSVAKERARLQLELS 107
Cdd:PRK05771 23 EALHELG---VVHIE---DLKEELSNERLRkLRSLLTKLSEALDKLRSYLPKLNPLreekKKVSVKSLEELIKDVEEELE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 108 KVREEFKELKARNTKkegdllaAQARLKDLEALLNskeaalstALSEKRTLEGELHDLRGQvAKLEAALGEAKKQLQDEM 187
Cdd:PRK05771 97 KIEKEIKELEEEISE-------LENEIKELEQEIE--------RLEPWGNFDLDLSLLLGF-KYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 188 LRRVDAENrLQTLKEELD------FQKNIYSEELRETKRRHETRLVEIDNGKqrefesrladALQELRAQHEDQVEQYKK 261
Cdd:PRK05771 161 KLESDVEN-VEYISTDKGyvyvvvVVLKELSDEVEEELKKLGFERLELEEEG----------TPSELIREIKEELEEIEK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568921945 262 ELEKTysakLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS 307
Cdd:PRK05771 230 ERESL----LEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
80-351 |
6.99e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 80 AYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLE 159
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 160 GELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDA-ENRLQTLKEELDFQKNIYsEELRETKRRHETRLVEIDNGKQRE 236
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSidKLRKEIERlEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 237 FESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKqlaak 316
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAQE-LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK----- 237
|
250 260 270
....*....|....*....|....*....|....*
gi 568921945 317 eaKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 351
Cdd:COG1340 238 --ELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-362 |
7.01e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 28 RLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREvsgikaayEAELGDARKTLDSVAKERARLQLELS 107
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--------EEALEEAAEEEAELEEEEEALLELLA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 108 KVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTA-----LSEKRTLEGELHDLRGQVAKLEAALGEA--- 179
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaallLAGLRGLAGAVAVLIGVEAAYEAALEAAlaa 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 180 ----------------------------------------------KKQLQDEMLRRVDAENR---------LQTLKEEL 204
Cdd:COG1196 547 alqnivveddevaaaaieylkaakagratflpldkiraraalaaalARGAIGAAVDLVASDLReadaryyvlGDTLLGRT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 205 DFQKNIYSEELRETKRRHETRLVEID-------NGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQS 277
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEgeggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 278 AERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDtsrrlLAEKEREMAEMRARMQQ--- 354
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELERLEREIEAlgp 781
|
410
....*....|..
gi 568921945 355 ----QLDEYQEL 362
Cdd:COG1196 782 vnllAIEEYEEL 793
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
82-250 |
9.83e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKarntkKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRtlegE 161
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALEAELAELPERLEELEERLE----E 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 162 LHDLRGQVAKLEAALGEAKKQLQDEMLR-RVDAENRLQTLKEELDF---QKNIYSEELRETKRRHETRLVEIDNGKQREF 237
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170
....*....|...
gi 568921945 238 ESRLADALQELRA 250
Cdd:COG4717 238 AAALEERLKEARL 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
82-388 |
1.06e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARN-------TKKEGDLLAAQARLKDLEALLNSKEAALST--AL 152
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKeelenelNLLEKEKLNIQKNIDKIKNKLLKLELLLSNlkKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 153 SEK-RTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELREtkrrhetrlVEIDN 231
Cdd:TIGR04523 210 IQKnKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---------LEQNN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 232 GKQREFEsrlaDALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNlvgaaheELQQSRIRIDSLSAQLSQLQK 311
Cdd:TIGR04523 281 KKIKELE----KQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN-------QISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921945 312 QLAAKEAklrdledslarERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:TIGR04523 350 ELTNSES-----------ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6-377 |
1.11e-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: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 6 QRRATRSGAQASSTPLsptritRLQEKEDLQELNDRLAVYIDRvrsLETENAGLRLRITESEEVVSREVSgikaayEAEL 85
Cdd:pfam12128 409 QLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLKSR---LGELKLRLNQATATPELLLQLENF------DERI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 86 GDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALstalsekrtlegeLHDL 165
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL-------------LHFL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 166 RGQVAKLEAALGeakKQLQDEMLRRVD--AENRLQTLKEELdfqkNIYSEELRETKRRHETRLVEIDNGKQR--EFESRL 241
Cdd:pfam12128 541 RKEAPDWEQSIG---KVISPELLHRTDldPEVWDGSVGGEL----NLYGVKLDLKRIDVPEWAASEEELRERldKAEEAL 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 242 ADAlQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNSNLVGAAHEELQQSRIRID-SLSAQLSQLQKQLAAKEAKL 320
Cdd:pfam12128 614 QSA-REKQAAAEEQLVQANGELEKA-SREETFARTALKNARLDLRRLFDEKQSEKDKKNkALAERKDSANERLNSLEAQL 691
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568921945 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 |
1.13e-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: 45.73 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 25 RITRLQEKEDLQELNDRLAVYIDRVRSLETENAGL--RLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARL 102
Cdd:TIGR00618 278 VLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 103 QLElSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:TIGR00618 358 RDA-HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 183 LQDEMLRRVDAENRLQTLK----------------EELDFQKNIYSEELRETKRRHETRLVEIdNGKQREFESRLADALQ 246
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKlekihlqesaqslkerEQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNP 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 247 ELRA------------QHEDQVEQYKKELEKT-------------YSAKLDNARQS------------------------ 277
Cdd:TIGR00618 516 ARQDidnpgpltrrmqRGEQTYAQLETSEEDVyhqltserkqrasLKEQMQEIQQSfsiltqcdnrskedipnlqnitvr 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 278 --------AERNSNLVGAAHEELQQSRIRID--SLSAQLSQLQKQLAAKEAKLRDLEDSLA--RERDTSRRLLAEKEREM 345
Cdd:TIGR00618 596 lqdlteklSEAEDMLACEQHALLRKLQPEQDlqDVRLHLQQCSQELALKLTALHALQLTLTqeRVREHALSIRVLPKELL 675
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568921945 346 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-341 |
1.24e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 29 LQEKED-LQELNDRLAVYIDRVRSLETENAGLRLRITESEEVvsrevsgikaayeaelgdaRKTLDSVAKErarLQLELS 107
Cdd:TIGR04523 365 LEEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL-------------------NQQKDEQIKK---LQQEKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 108 KVREEFKELKARNTKkegdllaAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD-- 185
Cdd:TIGR04523 423 LLEKEIERLKETIIK-------NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSke 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 186 ---EMLRRV--DAENRLQTLKEELDFQKNiYSEELRETKRRHETRLVEIDNgKQREFESRLAdalqelRAQHEDQVEQYK 260
Cdd:TIGR04523 496 kelKKLNEEkkELEEKVKDLTKKISSLKE-KIEKLESEKKEKESKISDLED-ELNKDDFELK------KENLEKEIDEKN 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 261 KELEktysakldnarQSAERNSNLVgAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:TIGR04523 568 KEIE-----------ELKQTQKSLK-KKQEEKQE---LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
.
gi 568921945 341 K 341
Cdd:TIGR04523 633 I 633
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
52-402 |
1.25e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 52 LETENAGLRLRITESEEVVSR--EVSGIKAAYEAELGDARKTLdsvaKERARLQLELSKVREEFKELKARNTKKEGDLLA 129
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSEleEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 130 AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA----ALGEAKKQLQDEMLRRVDAENRLQTL----K 201
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdkLLLENKELTQEASDMTLELKKHQEDIinckK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 202 EELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELeKTYSAKLDNARQSAERN 281
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM-KILENKCNNLKKQIENK 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 282 SNLVGAAHEELQQSRIRIDSLSAQL-------SQLQKQLAAKEAKLRDLEDSLARE----RDTSRRLL--AEKEREMAEM 348
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENKQLnayeikvNKLELELASAKQKFEEIIDNYQKEiedkKISEEKLLeeVEKAKAIADE 686
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921945 349 RARMQQQLDE--YQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRA 402
Cdd:pfam05483 687 AVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA 742
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
79-185 |
1.40e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.65 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 79 AAYEAELGDARKTLDSVAKERARLQLELskvrEEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTL 158
Cdd:COG1566 106 LGAEAEIAAAEAQLAAAQAQLDLAQREL----ERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREE 181
|
90 100
....*....|....*....|....*..
gi 568921945 159 EgELHDLRGQVAKLEAALGEAKKQLQD 185
Cdd:COG1566 182 E-ELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
296-388 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 296 RIRIDSLSAQLSQLQKQLAA----KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALD- 370
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEq 482
|
90 100
....*....|....*....|
gi 568921945 371 --MEIHAYRKLLEGEEERLR 388
Cdd:COG0542 483 ryGKIPELEKELAELEEELA 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
155-388 |
1.77e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 155 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTLKEeldfQKNIYSeeLRETKRRHETRLVEIdngkq 234
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALEEFRQ----KNGLVD--LSEEAKLLLQQLSEL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 235 refESRLADAlQELRAQHEDQVEQYKKELEKTYSAkldnarQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS------- 307
Cdd:COG3206 225 ---ESQLAEA-RAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvi 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 308 QLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
.
gi 568921945 388 R 388
Cdd:COG3206 375 E 375
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
21-387 |
2.35e-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: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 21 LSPTRITRLQEKE-DLQELNDRLavyidrvRSLETENAGLRLRITESEEVVSREVSGIKAAyeaelgdarKTLDSVAKER 99
Cdd:TIGR00606 731 LAPGRQSIIDLKEkEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESA---------KVCLTDVTIM 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 100 ARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEA 179
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE-----KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 180 KK---QLQDEMLRRVDAENRLQTLKEELDF------QKNIYSEELRETKRRHETRLVEIDNGKQREfESRLADALQELRa 250
Cdd:TIGR00606 870 KSeklQIGTNLQRRQQFEEQLVELSTEVQSlireikDAKEQDSPLETFLEKDQQEKEELISSKETS-NKKAQDKVNDIK- 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 251 QHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSlsaQLSQLQKQLAAKEAKLRDLEDSLAR- 329
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE---DMRLMRQDIDTQKIQERWLQDNLTLr 1024
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921945 330 ----ERDTSRRLLAEKEREMAEMraRMQQQLDEYQELLD-IKLALDMEIHAYRKLLEGEEERL 387
Cdd:TIGR00606 1025 krenELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEEnIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
51-319 |
2.50e-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: 44.38 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 51 SLETENAGLRLRITESEEVVSREVSGIKAAYEA-------ELGDARKTLDSVAKERARLQLELSKVREEfkelKARNTKK 123
Cdd:pfam18971 571 SLQEANKLIKDFLSSNKELAGKALNFNKAVAEAkstgnydEVKKAQKDLEKSLRKREHLEKEVEKKLES----KSGNKNK 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 124 EGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLqDEMLRRVD-----AENRLQ 198
Cdd:pfam18971 647 MEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSF-DEFKNGKNkdfskAEETLK 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 199 TLKEELDfQKNIYSEELRETKRRHETrLVEIDNGKQREFeSRLADALQELRAQHEDQVeqykkeLEKTYSAKLDNARQSA 278
Cdd:pfam18971 726 ALKGSVK-DLGINPEWISKVENLNAA-LNEFKNGKNKDF-SKVTQAKSDLENSVKDVI------INQKVTDKVDNLNQAV 796
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568921945 279 ErnsnlVGAAHEELQqsriRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:pfam18971 797 S-----VAKAMGDFS----RVEQVLADLKNFSKEQLAQQAQ 828
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
78-291 |
2.69e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRT 157
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 158 -----------LEGE-LHDLRGQVAKLEAALGEAKKQLQDemlrRVDAENRLQTLKEELDFQKniysEELRETKRRHETR 225
Cdd:COG3883 98 sggsvsyldvlLGSEsFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKL----AELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568921945 226 LVEIDngKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEE 291
Cdd:COG3883 170 KAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
79-383 |
2.79e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 79 AAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTL 158
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 159 EGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELdfqkniysEELRETKRRHETRLVEIDNGKQREFE 238
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL--------KELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 239 SRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA 318
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921945 319 KLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGE 383
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-341 |
3.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 78 KAAYEAELGDARKTLDSVAK-ERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKR 156
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 157 TLEGE---------LHDLRGQVAKLEAALGEAKKQLqdEMLRRVDAENRLQtlKEELDFQKNIYSEELRETKRRHETRLV 227
Cdd:PTZ00121 1614 KAEEAkikaeelkkAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 228 EIDNGKQREFESRLADALQELRAQHEDQVEQYKKElEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRiridslsaQLS 307
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--------KIA 1760
|
250 260 270
....*....|....*....|....*....|....*...
gi 568921945 308 QLQKQLAAKEAKLRDLEDSLARE----RDTSRRLLAEK 341
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEeldeEDEKRRMEVDK 1798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-325 |
3.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 132 ARLKDLEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVDAENRLQTLKEELdfqkN 209
Cdd:COG4717 71 KELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAEL----A 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 210 IYSEELRETKRRHEtrlveidngkqrefesRLADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAH 289
Cdd:COG4717 143 ELPERLEELEERLE----------------ELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 568921945 290 EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 325
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-205 |
3.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 8 RATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGD 87
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 88 A-------RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEG 160
Cdd:COG1196 653 GeggsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568921945 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELD 205
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
47-363 |
4.77e-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: 43.57 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 47 DRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKegd 126
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 127 llaaqarLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL-----QDEMLRRVDAENRLQT-- 199
Cdd:pfam15921 344 -------IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeQNKRLWDRDTGNSITIdh 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 200 LKEELDfQKNIYSEELR--------ETKRRHETRLVEIdNGKQREFESrladaLQELRAQHEDQVEQYKKELEKTYSAKL 271
Cdd:pfam15921 417 LRRELD-DRNMEVQRLEallkamksECQGQMERQMAAI-QGKNESLEK-----VSSLTAQLESTKEMLRKVVEELTAKKM 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 272 dnARQSAERNSNLVGAAheeLQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED------SLARERDTSRRLLAEKEREM 345
Cdd:pfam15921 490 --TLESSERTVSDLTAS---LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdhlrNVQTECEALKLQMAEKDKVI 564
|
330
....*....|....*...
gi 568921945 346 AEMRarmqQQLDEYQELL 363
Cdd:pfam15921 565 EILR----QQIENMTQLV 578
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
53-472 |
5.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 53 ETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKEL-----------KARNT 121
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeakkadeakkKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 122 KKEGDLLA----------------AQARLKDLEALLNSKEAALSTALSEKRTLEgELHDLRGQVAKLEAA--LGEAKKQL 183
Cdd:PTZ00121 1328 KKKADAAKkkaeeakkaaeaakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAkkKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 184 QDEMLRRVDAENRLQTLKEELDFQKNI-----YSEELRET----KRRHETRLVEidNGKQREFESRLADALQElRAQHED 254
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEEKKKAdeakkKAEEAKKAdeakKKAEEAKKAE--EAKKKAEEAKKADEAKK-KAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 255 QVEQYKKELEKTySAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA-KLRDLEDSLARE- 330
Cdd:PTZ00121 1484 KADEAKKKAEEA-KKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEe 1562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 331 -RDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQS 409
Cdd:PTZ00121 1563 kKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921945 410 QGGGSVTKKRKLESSESRSSFSQHARTSgrvaveevDEEGKFVRLRNKSNEDQSMGNWQIRRQ 472
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKA--------EEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
79-204 |
5.23e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 79 AAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQArLKDLEALLNSKE-AALSTALSEKRT 157
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEIEsLKRRISDLEDEI 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568921945 158 LE--GELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEEL 204
Cdd:COG1579 113 LElmERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
57-198 |
5.38e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 57 AGLRLRITESEEVVSREVSGIKAAYEAELGDARktlDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKD 136
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAK---ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921945 137 LEALLNSKEAALSTALSEkrtLEGELHDLRgqvAKLEAALGEAKKQLQDEMLRRVDAENRLQ 198
Cdd:PRK12705 103 LENQLEEREKALSARELE---LEELEKQLD---NELYRVAGLTPEQARKLLLKLLDAELEEE 158
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
86-348 |
6.45e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 86 GDARKTLDSVAKERARLQlelsKVREEFKELK--ARNTKKEGDLLAAQarLKDLEAL---------LNSKEAALSTALSE 154
Cdd:COG0497 151 AGLEELLEEYREAYRAWR----ALKKELEELRadEAERARELDLLRFQ--LEELEAAalqpgeeeeLEEERRRLSNAEKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 155 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemLRRVDAEnrLQTLKEELDfqkNIYsEELRETKR--RHETRLVEIDNG 232
Cdd:COG0497 225 REALQEALEALSGGEGGALDLLGQALRALER--LAEYDPS--LAELAERLE---SAL-IELEEAASelRRYLDSLEFDPE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 233 KQREFESRLaDALQELRAQHEDQVEQykkelektysakldnarqsaernsnlVGAAHEELQQSRIRIDSLSAQLSQLQKQ 312
Cdd:COG0497 297 RLEEVEERL-ALLRRLARKYGVTVEE--------------------------LLAYAEELRAELAELENSDERLEELEAE 349
|
250 260 270
....*....|....*....|....*....|....*..
gi 568921945 313 LAAKEAKLRDLEDSLARER-DTSRRLLAEKEREMAEM 348
Cdd:COG0497 350 LAEAEAELLEAAEKLSAARkKAAKKLEKAVTAELADL 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-339 |
7.65e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 77 IKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKR 156
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 157 TLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQRE 236
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 237 FESRLADALQELRAQHEDQVEQykkELEKtysaKLDNARQSAER--NSNLvgAAHEELQQSRIRIDSLSAQLSQLQKqla 314
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLE---ELER----ELERLEREIEAlgPVNL--LAIEEYEELEERYDFLSEQREDLEE--- 809
|
250 260
....*....|....*....|....*
gi 568921945 315 AKEaKLRDLEDSLarERDTSRRLLA 339
Cdd:COG1196 810 ARE-TLEEAIEEI--DRETRERFLE 831
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
129-361 |
8.72e-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: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 129 AAQARLKDLEALLNSKEAALSTALSEKRTLEGElhdlrgQVAKLEAALGEAKKQLQDEMLRRVDAENRL-QTLKEELDFQ 207
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQAVKA------HTDSLKEASDTAEISREKATDSALQKAEALaEKLKEVINLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 208 KNIYSEELRETK-RRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVE----QYKKELEKTY-----SAKLDNARQS 277
Cdd:pfam09731 203 KQSEEEAAPPLLdAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVAseriVFQQELVSIFpdiipVLKEDNLLSN 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 278 AERNSnLVGAAHEELQQSRIRIDSLSAQLSQ-LQKQLAAKEAKLRDLEDSLARE-----RDTSRRLLAEKEREMAEMRAR 351
Cdd:pfam09731 283 DDLNS-LIAHAHREIDQLSKKLAELKKREEKhIERALEKQKEELDKLAEELSARleevrAADEAQLRLEFEREREEIRES 361
|
250
....*....|
gi 568921945 352 MQQQLDEYQE 361
Cdd:pfam09731 362 YEEKLRTELE 371
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
145-363 |
9.52e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 145 EAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVD--AENRLQTLKEELDFQkniySEELRETKR 220
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLLPRLNllADETLADRVEEIREQ----LDEAEEAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 221 ---RHETRLVEIDngkqrefesRLADALQELRAQHE---DQVEQYKKELEKTYSAKLD--------------NARQSAER 280
Cdd:PRK04863 912 fvqQHGNALAQLE---------PIVSVLQSDPEQFEqlkQDYQQAQQTQRDAKQQAFAltevvqrrahfsyeDAAEMLAK 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 281 NSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSlareRDTSRRLLAEKEREM----------AEMRA 350
Cdd:PRK04863 983 NSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS----YDAKRQMLQELKQELqdlgvpadsgAEERA 1058
|
250
....*....|...
gi 568921945 351 RMQQqlDEYQELL 363
Cdd:PRK04863 1059 RARR--DELHARL 1069
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
63-385 |
9.90e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 63 ITESEEVVSREVSGIKAAYEAE-LGDARKTLDS---------VAKERARLQLELSKVREEFKElkarNTKKEGDLLAAQA 132
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEkLKNIELTAHCdklllenkeLTQEASDMTLELKKHQEDIIN----CKKQEERMLKQIE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 133 RLKDLEALLNSKEAALSTALSEKRTlegelhDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDfQKNIYS 212
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQKGD------EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE-NKNKNI 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 213 EELRE------TKRRHETRLVEIDNGKQREFESRLADALQELraqhEDQVEQYKKELEKTYSAKlDNARQSAERNSNLVG 286
Cdd:pfam05483 611 EELHQenkalkKKGSAENKQLNAYEIKVNKLELELASAKQKF----EEIIDNYQKEIEDKKISE-EKLLEEVEKAKAIAD 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 287 AAHEELQQSRIRIDSLSAQLSQLQKqlaakeaKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ-ELLDI 365
Cdd:pfam05483 686 EAVKLQKEIDKRCQHKIAEMVALME-------KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLSL 758
|
330 340
....*....|....*....|
gi 568921945 366 KLALDMEIHAYRKLLEGEEE 385
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
253-371 |
9.99e-04 |
|
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: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 253 EDQVEQYKKELEKTYsAKLDNARQsaernsnlvgaAHEELQQSRIRID------SLSAQLSQLQKQLAAKEAKLRDLEDS 326
Cdd:COG3524 176 EDAVRFAEEEVERAE-ERLRDARE-----------ALLAFRNRNGILDpeataeALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568921945 327 L---ARERDTSRRLLAEKEREMAEMRARM---------QQQLDEYQEL-LDIKLALDM 371
Cdd:COG3524 244 LspnSPQVRQLRRRIAALEKQIAAERARLtgasggdslASLLAEYERLeLEREFAEKA 301
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
69-199 |
1.04e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 69 VVSREVSGIKAAYE------AELGDA----RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLE 138
Cdd:PRK09039 43 FLSREISGKDSALDrlnsqiAELADLlsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568921945 139 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQT 199
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-398 |
1.46e-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: 41.98 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRItESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVRE 111
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAEL-EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 112 EFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL-QDEMLRR 190
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaEAEAQAR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 191 VDAENRLQTLKEELDFQKNIYS-----EELRETKRRHETRL------------VEIDNGKQREFE--------------- 238
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKASIQGvhgtvAQLGSVGERYATAIevaagnrlnnvvVEDDAVAKEAIEllkrrkagratflpl 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 239 SRLADALQELRAQHEDQVEQYKKEL---EKTYSA-------------KLDNARQ-------------------------S 277
Cdd:TIGR02169 581 NKMRDERRDLSILSEDGVIGFAVDLvefDPKYEPafkyvfgdtlvveDIEAARRlmgkyrmvtlegelfeksgamtggsR 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 278 AERNSNLVGAAHEE------------------LQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA 339
Cdd:TIGR02169 661 APRGGILFSRSEPAelqrlrerleglkrelssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568921945 340 EKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRS 398
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
114-349 |
1.78e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 114 KELKARNTKKEGDLLaaQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRG--------------QVAKLEAALGEA 179
Cdd:pfam10174 336 KEQRAAILQTEVDAL--RLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerkinvlqkKIENLQEQLRDK 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 180 KKQLqDEMLRRV-----DAENR---LQTLKEELDFQKNIYsEELRETKRRHE-TRLVEIDNGKQrefesRLADALQELRA 250
Cdd:pfam10174 414 DKQL-AGLKERVkslqtDSSNTdtaLTTLEEALSEKERII-ERLKEQREREDrERLEELESLKK-----ENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 251 QHEDQVEQYKKELEKTYSAKldNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA------KLRDLE 324
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHAS--SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeindRIRLLE 564
|
250 260
....*....|....*....|....*
gi 568921945 325 DSLARERDTSRRLLAEKEREMAEMR 349
Cdd:pfam10174 565 QEVARYKEESGKAQAEVERLLGILR 589
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
241-349 |
1.88e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 241 LADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKE 317
Cdd:PRK09039 79 LQDSVANLRAS-LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALE 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 568921945 318 AKLRDLE----DSLARERDTSRRL---LAEKEREMAEMR 349
Cdd:PRK09039 158 AALDASEkrdrESQAKIADLGRRLnvaLAQRVQELNRYR 196
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-251 |
2.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 96 AKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLE-ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA 174
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 175 ALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRET-------KRRHETRLVEIDNGKQRefESRLADALQE 247
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeaalrdlRRELRELEAEIASLERR--KSNIPARLLA 444
|
....
gi 568921945 248 LRAQ 251
Cdd:COG4913 445 LRDA 448
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-448 |
2.17e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 49 VRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERarlQLELSKVREEFKELK--ARNTKKEGD 126
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEH---EVEITGLTEKASSARsqANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 127 LLAAQAR---------LKDLEALLNSKEAALSTAlseKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL 197
Cdd:pfam15921 303 IIQEQARnqnsmymrqLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 198 QTLKEELDFQKNIYSEELRETKR---RHETRLVEIDNGKqREFESRLADaLQELRAQHEDQVEQYKKELEKTYSAkLDNA 274
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDHLR-RELDDRNME-VQRLEALLKAMKSECQGQMERQMAA-IQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 275 RQSAERNSNLVGAAHEELQQSRIRIDSLSAQlsqlQKQLAAKEAKLRDLEDSLARERdtsrRLLAEKEREMAEMRARMQQ 354
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAK----KMTLESSERTVSDLTASLQEKE----RAIEATNAEITKLRSRVDL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 355 QLDEYQELldiklaldmeihayrkllEGEEERLRlspsptsqRSRGRASSHSSQSQGGGSVTKKRKLESSESRSSFSQHA 434
Cdd:pfam15921 529 KLQELQHL------------------KNEGDHLR--------NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582
|
410
....*....|....
gi 568921945 435 RTSGRVAVEEVDEE 448
Cdd:pfam15921 583 RTAGAMQVEKAQLE 596
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
28-387 |
2.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 28 RLQEK-----EDLQELNDRLavyidrvrsletenaglrlritESEEVVSREVSGIKAAYEAELGDARKTLDsvakeraRL 102
Cdd:PRK04863 345 RQQEKieryqADLEELEERL----------------------EEQNEVVEEADEQQEENEARAEAAEEEVD-------EL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 103 QLELSKVREEFKELKARNtkkeGDLLAAQARLKDLEALLNSKEAALSTAlsekrtlEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:PRK04863 396 KSQLADYQQALDVQQTRA----IQYQQAVQALERAKQLCGLPDLTADNA-------EDWLEEFQAKEQEATEELLSLEQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 183 LQ--DEMLRRVD-AENRLQTLKEELDfqKNIYSEELRETKRRHETRLVEIDNGKQREfeSRLADALQELRAQHedQVEQY 259
Cdd:PRK04863 465 LSvaQAAHSQFEqAYQLVRKIAGEVS--RSEAWDVARELLRRLREQRHLAEQLQQLR--MRLSELEQRLRQQQ--RAERL 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 260 KKELEKTYSAKLDNA---RQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERDT 333
Cdd:PRK04863 539 LAEFCKRLGKNLDDEdelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQariQRLAARAPAWLAAQDALARLREQ 618
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568921945 334 SRRLLAEKEREMAEmrarMQQQLDEYQELldiKLALDmEIHAYRKLLEGEEERL 387
Cdd:PRK04863 619 SGEEFEDSQDVTEY----MQQLLEREREL---TVERD-ELAARKQALDEEIERL 664
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
26-198 |
2.84e-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: 40.81 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 26 ITRLQEKEDLqELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSrEVSGIKAAYEAELGDARKTLDSVAKERARLQLE 105
Cdd:pfam05911 79 KTKEWEKIKA-ELEAKLVETEQELLRAAAENDALSRSLQERENLLM-KLSEEKSQAEAEIEALKSRLESCEKEINSLKYE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 106 LSKVReefKELKARNTKKEGDLLAAQARLKdlEALLNSKEAAlstalsekrTLEGELHDLRGQVAKL---EAALgeAKKQ 182
Cdd:pfam05911 157 LHVLS---KELEIRNEEKNMSRRSADAAHK--QHLESVKKIA---------KLEAECQRLRGLVRKKlpgPAAL--AQMK 220
|
170
....*....|....*.
gi 568921945 183 LQDEMLRRVDAENRLQ 198
Cdd:pfam05911 221 LEVEMLGRDSGETRLR 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
25-182 |
2.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 25 RITRLQEKedLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGI-----------------------KAAY 81
Cdd:COG4942 63 RIAALARR--IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlgrqpplalllspedfldavrRLQY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 82 EAELGDARK----TLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEkrt 157
Cdd:COG4942 141 LKYLAPARReqaeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE--- 217
|
170 180
....*....|....*....|....*
gi 568921945 158 LEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
164-386 |
3.01e-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: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 164 DLRGQVAKLEAALGE-AKKQLQDEMLrrVDAENRLQTLKEELDFQKNIYSEElretkrrhetrlVEIDNGKQREFESRLA 242
Cdd:COG0610 648 DYRGIFENLKKALALySEEDGKEDVL--TDPEEALEELKEALDELRALFPEG------------VDFSAFDPTEKLEALD 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 243 DALQELRAQHEDQVEQYK--KELEKTYSAkldnARQSAErnsnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK--EA 318
Cdd:COG0610 714 EAVERFLGDEEARKEFKKlfKELSRLYNL----LSPDDE----FGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKeyEE 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568921945 319 KLRDL-EDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:COG0610 786 KIRQLlDEAIDLERKEIKPRIKQNPVQYRKFSELLEEIIEEYNNGALDADEVLEELEELAKEVKEEEER 854
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-363 |
3.20e-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: 3.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921945 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDT-SRRLLAEKEREMAEMRARMQQQLDEYQELL 363
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQDL 85
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
166-399 |
3.28e-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: 40.49 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 166 RGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKE----ELDFQKNIYSEELR---ETKR-----RHETRLVEIDNGK 233
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERmamEREReleriRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 234 QREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYSAKLdnarQSAERnsnlvgaaHEELQQSRIRIDSLSAQlsqlqk 311
Cdd:pfam17380 367 QEEIAMEISRmrELERLQMERQQKNERVRQELEAARKVKI----LEEER--------QRKIQQQKVEMEQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 312 QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRarmQQQLDEYQElldiKLALDMEihaYRKLLEGEEERLRLSP 391
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLR---QQEEERKRK----KLELEKE---KRDRKRAEEQRRKILE 498
|
....*...
gi 568921945 392 SPTSQRSR 399
Cdd:pfam17380 499 KELEERKQ 506
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
103-372 |
3.29e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 103 QLELSKVREEF-----KELKARNTKKEGDLLAAQARlkdLEALLNS-----------KEaalSTALSEKR--TLEGELHD 164
Cdd:pfam10174 276 QMEVYKSHSKFmknkiDQLKQELSKKESELLALQTK---LETLTNQnsdckqhievlKE---SLTAKEQRaaILQTEVDA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 165 LRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELD--------FQKNIysEELRETKRRHETRLVEI-DNGKQR 235
Cdd:pfam10174 350 LRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDvkerkinvLQKKI--ENLQEQLRDKDKQLAGLkERVKSL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 236 EFESRLADA----LQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNL---VGAAHEELQQSRIRIDSLSAQLSQ 308
Cdd:pfam10174 428 QTDSSNTDTalttLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLkekVSALQPELTEKESSLIDLKEHASS 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921945 309 LQKQLAAKEAKLRDLEDSLARERDTSRRLLAE-KEREMAEMRARMQQQLDEYQELLDIKLALDME 372
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQKKEECSKLENQlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKE 572
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-363 |
3.40e-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: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921945 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELL 363
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
298-364 |
3.44e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 3.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921945 298 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER------EMAEMRARMQQQLDEYQELLD 364
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaELAGAGAAAEGRAGELAQELD 126
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
29-372 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 29 LQEKEDL----QELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKaayeaELGDARKTLDSVAKERARLQ- 103
Cdd:pfam05622 6 QEEKDELaqrcHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGK-----KYLLLQKQLEQLQEENFRLEt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 104 ------LELSKVREEFKELKARNtkKEGDLLAAQAR-LKD-LEALLNSKEAAL---STALSEKRTLEgELHDLRGQVAKL 172
Cdd:pfam05622 81 arddyrIKCEELEKEVLELQHRN--EELTSLAEEAQaLKDeMDILRESSDKVKkleATVETYKKKLE-DLGDLRRQVKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 173 E---AALGEAKKQLQDEMLRRVDAENRLQTLKEEL-DFQKNIYSEELRETKRRHE-TRLVEIDNGKQREFESRLA--DAL 245
Cdd:pfam05622 158 EernAEYMQRTLQLEEELKKANALRGQLETYKRQVqELHGKLSEESKKADKLEFEyKKLEEKLEALQKEKERLIIerDTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 246 QE---------------------------------------------LRAQHEDQV-----EQYKKELEKTYSAKLDNAR 275
Cdd:pfam05622 238 REtneelrcaqlqqaelsqadallspssdpgdnlaaeimpaeireklIRLQHENKMlrlgqEGSYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 276 QsaeRNSNLvgaaHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKlrdLEDSLARERDTSRRLlaEKEREMAEMRARMQQQ 355
Cdd:pfam05622 318 R---RKNEL----ETQNRLANQRILELQQQVEELQKALQEQGSK---AEDSSLLKQKLEEHL--EKLHEAQSELQKKKEQ 385
|
410
....*....|....*..
gi 568921945 356 LDEYQELLDIKLALDME 372
Cdd:pfam05622 386 IEELEPKQDSNLAQKID 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-390 |
3.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 245 LQELRAQHEDQVEQYKKELEKTYSAK---LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLR 321
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921945 322 DLEDSLARERDTSRRllAEKEREMAEMRARMQ---QQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLS 390
Cdd:COG4717 120 KLEKLLQLLPLYQEL--EALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
82-364 |
3.85e-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: 40.54 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGE 161
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 162 LHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQtlKEELDFQkniyseELRETKRRHETRLVEIdngkqREFESRL 241
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--KEEKGRQ------ELEKAKRKLEGESTDL-----QEQIAEL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 242 ADALQELRAQ---HEDQVEQYKKELEKTYSAKlDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA 318
Cdd:pfam01576 228 QAQIAELRAQlakKEEELQAALARLEEETAQK-NNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 319 KLRDLEDSLA--------RERDTS--RRLLAEK----EREMAEMRARMQQQLDEYQELLD 364
Cdd:pfam01576 307 ELEDTLDTTAaqqelrskREQEVTelKKALEEEtrshEAQLQEMRQKHTQALEELTEQLE 366
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-324 |
4.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 112 EFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRG------------------------ 167
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDklkknkdkinklnsdlskinseik 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 168 ----QVAKLEAALGEAKKQLQ--DEMLRRVDAE---------------NRLQTLKEELDFQKNIYSEE----------LR 216
Cdd:TIGR04523 114 ndkeQKNKLEVELNKLEKQKKenKKNIDKFLTEikkkekeleklnnkyNDLKKQKEELENELNLLEKEklniqknidkIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 217 ETKRRHETRLVEID--NGKQREFESRLADaLQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNSNLVGAAHEELQQ 294
Cdd:TIGR04523 194 NKLLKLELLLSNLKkkIQKNKSLESQISE-LKKQNNQLKDNIEKKQQEINEK-TTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270
....*....|....*....|....*....|
gi 568921945 295 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLE 324
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
31-146 |
4.55e-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: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 31 EKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSRevsgikaaYEAELGDARKTLDSVAKER----------A 100
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--------LERELSEARSEERREIRKDreisrldreiE 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568921945 101 RLQLELSKVREEFKELKARntkkegdllaaQARLKDLEALLNSKEA 146
Cdd:COG2433 476 RLERELEEERERIEELKRK-----------LERLKELWKLEHSGEL 510
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
33-225 |
5.62e-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: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 33 EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEevvsrevsgIKAAY---EAELgDARKTldsVAKERARLQLELSKV 109
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENLELDEAEEALEEIEER---------IDQLYdllEKEV-DAKKY---VEKNLPEIEDYLEHA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 110 REEFKELKA--RNTKK-----EGDLlaaqARLKDLEALLNSKEAALstALSEKRTLEGEL--HDLRGQVAKLEAALGEAK 180
Cdd:pfam06160 304 EEQNKELKEelERVQQsytlnENEL----ERVRGLEKQLEELEKRY--DEIVERLEEKEVaySELQEELEEILEQLEEIE 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568921945 181 KQlQDEMlrrvdaENRLQTL-KEELDFQKNI--YSEELRETKRRHETR 225
Cdd:pfam06160 378 EE-QEEF------KESLQSLrKDELEAREKLdeFKLELREIKRLVEKS 418
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
27-357 |
6.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 27 TRLQEKEDLQELNDRlavyidrvRSLETENAGLRLRITESEEVVSRevsgiKAAYEAELGDARKTLDSVAKErarlqleL 106
Cdd:PRK11281 37 TEADVQAQLDALNKQ--------KLLEAEDKLVQQDLEQTLALLDK-----IDRQKEETEQLKQQLAQAPAK-------L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 107 SKVREEFKELKARNTKKEGDLLAAQArLKDLEALLNSKEAALSTAlsekrtlegelhdlrgqvaklEAALGEAKKQLQDe 186
Cdd:PRK11281 97 RQAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQLQNA---------------------QNDLAEYNSQLVS- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 187 mlrrvdaenrLQTLKEELdfQKNIYSeelretkrrHETRLVEIDNgkqrefesRLADALQELRAQHEDQVEQYKKELeKT 266
Cdd:PRK11281 154 ----------LQTQPERA--QAALYA---------NSQRLQQIRN--------LLKGGKVGGKALRPSQRVLLQAEQ-AL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 267 YSAKLDNARQSAERNSNLvgaahEELQQSriRIDSLSAQLSQLQKQLA-----------------AKEAKLRD------- 322
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQL-----QDLLQK--QRDYLTARIQRLEHQLQllqeainskrltlsektVQEAQSQDeaariqa 276
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568921945 323 ---LEDSLARERDTSRRLLAEKER--EMAEMRARMQQQLD 357
Cdd:PRK11281 277 nplVAQELEINLQLSQRLLKATEKlnTLTQQNLRVKNWLD 316
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
81-386 |
7.47e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 81 YEAELGDARKTLDSVAKErarlqlELSKVREEFkelkarnTKKEGDLlaaQARLKDLEALLNSKEAALSTALSEKRTLEG 160
Cdd:pfam15921 57 YEVELDSPRKIIAYPGKE------HIERVLEEY-------SHQVKDL---QRRLNESNELHEKQKFYLRQSVIDLQTKLQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEI---------DN 231
Cdd:pfam15921 121 EMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIrsilvdfeeAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 232 GKQ-----------------------REFESRLA----------DALQELRA-----------QHEDQVEQYKKELEKTY 267
Cdd:pfam15921 201 GKKiyehdsmstmhfrslgsaiskilRELDTEISylkgrifpveDQLEALKSesqnkielllqQHQDRIEQLISEHEVEI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 268 SAKLDNArQSAERNSNLVGAAHEELQ-QSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMA 346
Cdd:pfam15921 281 TGLTEKA-SSARSQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELT 359
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568921945 347 EMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
170-263 |
8.06e-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: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 170 AKLEAALGEAKKQLQDEmlrrvdaENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELR 249
Cdd:smart00935 21 KQLEKEFKKRQAELEKL-------EKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEEL 93
|
90
....*....|....
gi 568921945 250 AQHEDQVEQYKKEL 263
Cdd:smart00935 94 QKILDKINKAIKEV 107
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
212-388 |
9.75e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 212 SEELRETKRRHETRLVEIDNGKQREfesRLADALQELRAqHEDQVEQYKKELEKTYS------------------AKLDN 273
Cdd:COG2433 312 KEDLSVEEKLHLAREYGYDNDHERD---ALAAALKAYDA-YKNKFERVEKKVPPDVDrdevkarvirglsieealEELIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921945 274 ARQSAERNSNLVGAAHEElqqsrIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLlaekEREMAEMRARMQ 353
Cdd:COG2433 388 KELPEEEPEAEREKEHEE-----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL----ERELSEARSEER 458
|
170 180 190
....*....|....*....|....*....|....*
gi 568921945 354 QQLDEYQELldikLALDMEIHAYRKLLEGEEERLR 388
Cdd:COG2433 459 REIRKDREI----SRLDREIERLERELEEERERIE 489
|
|
| |
