|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
30-386 |
3.07e-99 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 303.77 E-value: 3.07e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKV 109
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 110 REEFKELKARNTKKegdliaaqarlkdleallnskeaalstaLSEKRTLEGELHDLRgqvakleaalgeakKQLQDEMLR 189
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 190 RVDAENRLQTMKEELDFQKNIYSEELRETKRRH--ETRLVEIDNGKQREfesrLADALQELRAQHEDQVEQYKKELEKTY 267
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 268 SAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAE 347
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 5031875 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 |
2.84e-21 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 89.02 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 434 ARTSGRVAVEEVDEEG-----KFVRLRNKSNEDQSMGNWQIKRQNGDdpllTYRFPPKFTLKAGQVVTIWAAG----AGA 504
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 5031875 505 THSPPTDLVWKAQNTWgcgnslrTALINSTGEEVAMR 541
Cdd:pfam00932 77 GYWGPSNAVWNNGGDA-------VALYDANGELVDSV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-368 |
3.77e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 32 KEDLQELNDRLAVYIDRVRSLET--ENAGLRLRITESEEVVSREVSGIK--------AAYEAELGDARKTLDSVAKERAR 101
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERqaEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 102 LQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 182 QLQdemlrrvDAENRLQTMKEELDFQKniysEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKK 261
Cdd:COG1196 345 ELE-------EAEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 262 ELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEK 341
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340
....*....|....*....|....*..
gi 5031875 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 |
4.55e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 10 TRSGAQASSTPLSPTR-ITRLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREvsgikaayEA 83
Cdd:TIGR02168 662 TGGSAKTNSSILERRReIEELEEKieeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--------RK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 84 ELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELH 163
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 164 DLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEEL-DFQKNIysEELRETKRRHETRLVEIDNGKQREFEsrla 242
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIeSLAAEI--EELEELIEELESELEALLNERASLEE---- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 243 dALQELRAQHEDQVEQykkelEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQK---QLAAKEAK 319
Cdd:TIGR02168 888 -ALALLRSELEELSEE-----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALEN 961
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 5031875 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 |
6.00e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 32 KEDLQELNDRLAVYIDRVRSLET--ENAGLRLRITESEEVVSREVSGIKA-AYEAELGDARKTLDSVAKERARLQLELSK 108
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERqaEKAERYKELKAELRELELALLVLRLeELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 109 VREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEaalstalSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 188
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-------QQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 189 RRVDAENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKELEktyS 268
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELE--EQLETLRSKVAQLELQIASLNNEIERLEARLE---R 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 269 AKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARerdtSRRLLAEKEREMAEM 348
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALDAAERELAQL 487
|
330
....*....|....*....
gi 5031875 349 RAR------MQQQLDEYQE 361
Cdd:TIGR02168 488 QARldslerLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-387 |
7.12e-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: 68.54 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 110 REEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLR 189
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 190 RVDAENRlqtmKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRlaDALQELRAQHEDQveqykkelektySA 269
Cdd:TIGR02168 756 LTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR--EALDELRAELTLL------------NE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 270 KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMA 346
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELE 897
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 5031875 347 EMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-381 |
2.63e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 73 EVSGIkAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEgdliaaqaRLKDLEALLnsKEAALSTAL 152
Cdd:TIGR02169 161 EIAGV-AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--------RYQALLKEK--REYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 153 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqKNIYSEELRETKRRHETRLVEIDN- 231
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 232 -GKQREFESRLADAlQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 310
Cdd:TIGR02169 307 eRSIAEKERELEDA-EERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031875 311 KQLAAKEAKLRDLE---DSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLE 381
Cdd:TIGR02169 385 DELKDYREKLEKLKreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-352 |
2.49e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 96 AKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA 175
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 176 LGEAKKQLQdEMLRRVDAENRLQTMKEELDfqkniySEELRETKRRhetrlveidngkqrefesrlADALQELRAQHEDQ 255
Cdd:COG4942 99 LEAQKEELA-ELLRALYRLGRQPPLALLLS------PEDFLDAVRR--------------------LQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 256 VEQYKKELEktysaKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSR 335
Cdd:COG4942 152 AEELRADLA-----ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*..
gi 5031875 336 RLLAEKEREMAEMRARM 352
Cdd:COG4942 227 ALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-401 |
4.77e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 129 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQK 208
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 209 NIYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysakldnarqsaernsnlvga 287
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 288 aheelqqsriridslsaQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 367
Cdd:COG4942 161 -----------------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|....
gi 5031875 368 ALDMEIhayRKLLEGEEERLRLSPSPTSQRSRGR 401
Cdd:COG4942 224 ELEALI---ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-386 |
9.47e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 28 RLQEKEDLQELNDRLAVYIDR---VRSLETENAGLRLRITESE---EVVSREVSGIKAAYEaELGDARKTL--------- 92
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETErerEELAEEVRDLRERLE-ELEEERDDLlaeagldda 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 93 --DSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA 170
Cdd:PRK02224 308 daEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 171 KLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSeELRETKRRHETRLVE----IDNGKQREFESRLADA-- 244
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-ELEATLRTARERVEEaealLEAGKCPECGQPVEGSph 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 245 -------------LQELRAQHEDQVEQYKKELEKTYSAK-----LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQL 306
Cdd:PRK02224 467 vetieedrerveeLEAELEDLEEEVEEVEERLERAEDLVeaedrIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 307 SQLQKQLAAKEAKLRDLEDSLARERDTsrrlLAEKEREMAEMRARMqQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-264 |
1.82e-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: 57.37 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 6 QRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSRevsgikaaYEAEL 85
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES--------LERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 86 GDARKTLDSVAKERARLQLELSKVREEFKELKARNTKkegdliaAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDL 165
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELREL 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 166 RGQVAKLEAALGEAKKQLqdemlrrVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNG--KQREFESRLAD 243
Cdd:TIGR02168 907 ESKRSELRRELEELREKL-------AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDeeEARRRLKRLEN 979
|
250 260
....*....|....*....|.
gi 5031875 244 ALQELRAQHEDQVEQYKKELE 264
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKE 1000
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-351 |
1.84e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 124 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEgelhDLRGQVAKLEAALGEA-KKQLQDEMLRRVDAENRLQTMKE 202
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLE----PIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 203 ELdfqkniysEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNS 282
Cdd:COG4913 296 EL--------EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLEREIERL-ERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031875 283 NLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 351
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-362 |
2.73e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 30 QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKV 109
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 110 REEFKELKAR--NTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLE-------------GELHDLRGQVAKLEA 174
Cdd:COG4717 219 QEELEELEEEleQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlGLLALLFLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 175 ALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRA---- 250
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllae 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 251 ----------QHEDQVEQYKKELEK--TYSAKLDNARQSAERNSNLVGAA--HEELQQSRIRIDSLSAQLSQLQKQLAAK 316
Cdd:COG4717 379 agvedeeelrAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAEL 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 5031875 317 EAKLRDLEDSlarerdtsrRLLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:COG4717 459 EAELEQLEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-355 |
1.19e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 131 QARLKDLEALLNSKEAALSTALSEKRTLegelhDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNI 210
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 211 YSEELR-ETKRRHETRLVEIdngkqrefESRLADALQELRAQHEDqVEQYKKELEKTysakldnARQSAERNSNLVGAAH 289
Cdd:COG3206 256 LPELLQsPVIQQLRAQLAEL--------EAELAELSARYTPNHPD-VIALRAQIAAL-------RAQLQQEAQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031875 290 EELQQSRIRIDSLSAQLSQLQKQ---LAAKEAKLRDLEdslaRERDTSRRLLAEKEREMAEMRARMQQQ 355
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARlaeLPELEAELRRLE----REVEVARELYESLLQRLEEARLAEALT 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-448 |
1.99e-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: 54.29 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 162 LHDLRGQVAKLEAALGEAKKQLqDEMLRRVDAENRLQTMKEEL-DFQKNIYSEELRE-TKRRHETRLVEIDNGKQREFES 239
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQL-KSLERQAEKAERYKELKAELrELELALLVLRLEElREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 240 RLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 320 LRDLE----------DSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:TIGR02168 339 LAELEekleelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5031875 390 SPSPTSQRSRgRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEE 448
Cdd:TIGR02168 419 LQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-355 |
5.32e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 24 TRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESE------EVVSREVSGIKAAYEAELGDARKTLDSVAK 97
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELEseleeaREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 98 ERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNS----------KEAALSTALSEKR----TLEGELH 163
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRerveELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 164 DLRGQVAKLEA------ALGEAKKQLQDEMLRRVDAENRLQTMKEELDfQKNIYSEELRETKRRHETRLVEID------- 230
Cdd:PRK02224 486 DLEEEVEEVEErleraeDLVEAEDRIERLEERREDLEELIAERRETIE-EKRERAEELRERAAELEAEAEEKReaaaeae 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 231 -------------NGKQREFESRL----------------ADALQELRAQHEDQVE---------QYKKELEKTYSAKLD 272
Cdd:PRK02224 565 eeaeeareevaelNSKLAELKERIeslerirtllaaiadaEDEIERLREKREALAElnderrerlAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 273 NARQSAERNSNlvGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA---------EKER 343
Cdd:PRK02224 645 EARIEEAREDK--ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAlealydeaeELES 722
|
410
....*....|..
gi 5031875 344 EMAEMRARMQQQ 355
Cdd:PRK02224 723 MYGDLRAELRQR 734
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-388 |
7.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 25 RITRLqeKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV---SREVSGIKAAYEAELGDARKTLDSVAKERAR 101
Cdd:COG4913 339 RLEQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFaalRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 102 LQLELSKVREEFKELKARNTKKEGDLIAAQARlkdLEALLNSKEAALSTAlsekrtleGELHDLRGQVAK----LEAALG 177
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELPFV--------GELIEVRPEEERwrgaIERVLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 178 EAK-------KQLQD--EMLRRVDAENRLQTMK-------------------EELDFQKNIYS----------------- 212
Cdd:COG4913 486 GFAltllvppEHYAAalRWVNRLHLRGRLVYERvrtglpdperprldpdslaGKLDFKPHPFRawleaelgrrfdyvcvd 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 213 --EELRETKR--------RHETRLVEID--------------NGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYS 268
Cdd:COG4913 566 spEELRRHPRaitragqvKGNGTRHEKDdrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQ 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 269 AKLDNARQSAERNSNL--VGAAHEELQQSRIRIDSL---SAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER 343
Cdd:COG4913 645 ERREALQRLAEYSWDEidVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 5031875 344 eMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:COG4913 725 -AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-389 |
8.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 59 LRLRITESEEVVSRE--VSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVR----------EEFKELKARNTKKEGD 126
Cdd:PRK03918 174 IKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkeleelkEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 127 LIAAQARLKDLEALLNSKEAALSTaLSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDf 206
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 207 QKNIYSEELRETKRrhetRLVEIDNgKQREFESRlADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERnsnlvg 286
Cdd:PRK03918 332 ELEEKEERLEELKK----KLKELEK-RLEELEER-HELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEK------ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 287 aAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEdSLARERDTSRRLLAEKERE--MAEMRARMQQQLDEYQELLD 364
Cdd:PRK03918 399 -AKEEIEE---EISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEE 473
|
330 340
....*....|....*....|....*
gi 5031875 365 IKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKL 498
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
72-364 |
8.53e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 72 REVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELK---ARNTKKEGDLIAAQARLKDLEALLNSKEAAL 148
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 149 STALSEK----RTLEGELHDLRGQVAKLEAALGEAKK-------QLQDEMLRRVDAENRLQTMKEEL-----DFQKNIYS 212
Cdd:pfam07888 121 LAQRAAHeariRELEEDIKTLTQRVLERETELERMKErakkagaQRKEEEAERKQLQAKLQQTEEELrslskEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 213 EELRETK----RRHETRLVEIDNGKQR---EFESRLAD--ALQELRAQHEDQVEQYKKELEKTYS------AKLDNAR-Q 276
Cdd:pfam07888 201 LAQRDTQvlqlQDTITTLTQKLTTAHRkeaENEALLEElrSLQERLNASERKVEGLGEELSSMAAqrdrtqAELHQARlQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 277 SAERNSNLVGAA-------------HEELQQS----RIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLA 339
Cdd:pfam07888 281 AAQLTLQLADASlalregrarwaqeRETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|..
gi 5031875 340 EKEREMAEMRARMQ-------QQLDEYQELLD 364
Cdd:pfam07888 361 ESRRELQELKASLRvaqkekeQLQAEKQELLE 392
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-363 |
1.39e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 27 TRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGikaayEAELGDARKTLDSvakERARLQLEL 106
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-----RQELEKAKRKLEG---ESTDLQEQI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 107 SKVREEFKELKARNTKKEGDLIAAQARLKDleallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQlqde 186
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEE-------ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ---- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 187 mlrRVDAENRLQTMKEELD--FQKNIYSEELReTKRRHETRLVEidngKQREFESRLADA-LQELRAQHEDQVEQYKKEL 263
Cdd:pfam01576 294 ---RRDLGEELEALKTELEdtLDTTAAQQELR-SKREQEVTELK----KALEEETRSHEAqLQEMRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 264 EKTYSAK--LDNARQSAERNSNLVGAAHEELQQSRI----RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTS 334
Cdd:pfam01576 366 EQAKRNKanLEKAKQALESENAELQAELRTLQQAKQdsehKRKKLEGQLQELQARLSESERQRAELAEKLSKlqsELESV 445
|
330 340 350
....*....|....*....|....*....|..
gi 5031875 335 RRLLAEKERE---MAEMRARMQQQLDEYQELL 363
Cdd:pfam01576 446 SSLLNEAEGKnikLSKDVSSLESQLQDTQELL 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-388 |
1.46e-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: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 189 RRVDAENRLQTMKEELDfqkniyseelretkrRHETRLVEIDN-----GKQ-------REFESRLADALQELRAQHEDQV 256
Cdd:COG1196 173 RKEEAERKLEATEENLE---------------RLEDILGELERqleplERQaekaeryRELKEELKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 257 EQYKKELEktysAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRR 336
Cdd:COG1196 238 EAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5031875 337 LLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 388
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
82-267 |
2.42e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSkeaalstALSEKrtlegE 161
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-------VRNNK-----E 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 162 LHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKniysEELRETKRRHETRLVEIDngkqrefesrl 241
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE----AELEEKKAELDEELAELE----------- 155
|
170 180
....*....|....*....|....*.
gi 5031875 242 aDALQELRAQHEDQVEQYKKELEKTY 267
Cdd:COG1579 156 -AELEELEAEREELAAKIPPELLALY 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-389 |
4.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 31 EKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVR 110
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 111 EEFKELKARN---TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRgqvaklEAALGEAKKQLQDEM 187
Cdd:COG1196 387 ELLEALRAAAelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE------EAAEEEAELEEEEEA 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 188 LRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTY 267
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 268 SAKLDNARQSAERNSNLVGAAHEELQQSR-------IRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 341 -----------KEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:COG1196 621 tllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-310 |
4.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 26 ITRLQEKE-DLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIK-AAYEAELGDARKTLDSVAK---ERA 100
Cdd:COG4913 609 RAKLAALEaELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 101 RLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLegelhdlrgqvakLEAALgeak 180
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-------------LRALL---- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 181 kqlqDEMLRRVDAENRLQTMKEELdfQKNIysEELRETKRRHETRLVEIDNGKQREFESRLAD------ALQELRAQHED 254
Cdd:COG4913 752 ----EERFAAALGDAVERELRENL--EERI--DALRARLNRAEEELERAMRAFNREWPAETADldadleSLPEYLALLDR 823
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5031875 255 QVEQykkELEKtYSAKLDNARQSAERN--SNLVGAAHEELQQSRIRIDSLSAQLSQLQ 310
Cdd:COG4913 824 LEED---GLPE-YEERFKELLNENSIEfvADLLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-350 |
5.04e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 24 TRITRLQEKEDL--QELNdRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAeLGDARKTLDSVAKERAR 101
Cdd:pfam15921 517 AEITKLRSRVDLklQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQ 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 102 LQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 182 QLqdEMLRR--VDAENRLQTMKEELDFQKNIYSEELRETKRRHET------RLVEIDNGKQREFESRLA--DALQELRAQ 251
Cdd:pfam15921 675 DY--EVLKRnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdgHAMKVAMGMQKQITAKRGqiDALQSKIQF 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 252 HEDQVEQYKKE--LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRidsLSAQLSQLQKQLAAKEAKLRDLEDSLAR 329
Cdd:pfam15921 753 LEEAMTNANKEkhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR---LKEKVANMEVALDKASLQFAECQDIIQR 829
|
330 340
....*....|....*....|.
gi 5031875 330 ERDTSRRLLAEKEREMAEMRA 350
Cdd:pfam15921 830 QEQESVRLKLQHTLDVKELQG 850
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-362 |
5.14e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 29 LQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV---SREVSGIKAAYEA-----------------ELGDA 88
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKlkerleeleedlssleqEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 89 RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQ------------ARLKDLEALLNSKEAALSTALSEKR 156
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskleeevsrieARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 157 TLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKqre 236
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELERKI--- 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 237 fesrladalQELRAQHEDqveqyKKELEKTYSAKLDNArqsAERNSNLvgaahEELQQSRIRIDSLSAQLSQLQKQLAAK 316
Cdd:TIGR02169 906 ---------EELEAQIEK-----KRKRLSELKAKLEAL---EEELSEI-----EDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 5031875 317 EAKLRDLED--SLARE--RDTSRRL--LAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:TIGR02169 964 EEEIRALEPvnMLAIQeyEEVLKRLdeLKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-388 |
6.79e-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: 49.02 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 96 AKERARLQLE--LSKVREEF-KELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKL 172
Cdd:pfam01576 710 ATEDAKLRLEvnMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 173 EAALGEAKKQL--------------------QDEMLRRV-DAENRLQTMKEE-LDFQKNIYSEE---------------- 214
Cdd:pfam01576 790 NKGREEAVKQLkklqaqmkdlqreleearasRDEILAQSkESEKKLKNLEAElLQLQEDLAASErarrqaqqerdelade 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 215 ----------LRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKEL--EKTYSAKLDNARQSAERNS 282
Cdd:pfam01576 870 iasgasgksaLQDEKRRLEARIAQLE--EELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQN 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 283 NLVGAAHEELQqsriridslSAQLSQLQKQLAAKEAKLRDLEDSL---ARERDTSRRLLAEKEREMAEMRARMQ---QQL 356
Cdd:pfam01576 948 KELKAKLQEME---------GTVKSKFKSSIAALEAKIAQLEEQLeqeSRERQAANKLVRRTEKKLKEVLLQVEderRHA 1018
|
330 340 350
....*....|....*....|....*....|..
gi 5031875 357 DEYQELLDiKLALDMEiHAYRKLLEGEEERLR 388
Cdd:pfam01576 1019 DQYKDQAE-KGNSRMK-QLKRQLEEAEEEASR 1048
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
24-178 |
6.96e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 24 TRITRLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVsREVSGIKAAYEAELGDAR--KTLDSVA 96
Cdd:COG1579 17 SELDRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-EEVEARIKKYEEQLGNVRnnKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 97 KERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEkrtLEGELHDLRGQVAKLEAAL 176
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI 172
|
..
gi 5031875 177 GE 178
Cdd:COG1579 173 PP 174
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
32-357 |
8.99e-06 |
|
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: 48.14 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIkAAYEAELGDARKTLDSVAKERARLQLELSKVRE 111
Cdd:pfam19220 68 RRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIEL-RDKTAQAEALERQLAAETEQNRALEEENKALRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 112 EFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRV 191
Cdd:pfam19220 147 EAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 192 DAENRLQTMKEELDFQKNIYSEELRETKRRHET----------RLVEIDNGkQREFESRLADALQElRAQHEDQVEQYKK 261
Cdd:pfam19220 227 RAEAQLEEAVEAHRAERASLRMKLEALTARAAAteqllaearnQLRDRDEA-IRAAERRLKEASIE-RDTLERRLAGLEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 262 ELEK--TYSAKLDNARQSAERNSNLVG---AAHE-ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDledslarerdTSR 335
Cdd:pfam19220 305 DLERrtQQFQEMQRARAELEERAEMLTkalAAKDaALERAEERIASLSDRIAELTKRFEVERAALEQ----------ANR 374
|
330 340
....*....|....*....|..
gi 5031875 336 RLLAEKEREMAEmRARMQQQLD 357
Cdd:pfam19220 375 RLKEELQRERAE-RALAQGALE 395
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
131-366 |
1.13e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 131 QARLKDL--EALLNSKEAALSTALSEkrTLegelhDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEELDFQK 208
Cdd:PRK11281 42 QAQLDALnkQKLLEAEDKLVQQDLEQ--TL-----ALLDKIDRQKEETEQLKQQLAQ-------APAKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 209 NIYSEELRETkrrhetrlveIDNGKQREFESRLADALQELraqhedqvEQYKKELeKTYSAKLDNARQSAERNSNLVGAA 288
Cdd:PRK11281 108 DDNDEETRET----------LSTLSLRQLESRLAQTLDQL--------QNAQNDL-AEYNSQLVSLQTQPERAQAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 289 HEELQQSRIRIDSLSA--------QLSQLQKQLAAKEAKLrDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ 360
Cdd:PRK11281 169 SQRLQQIRNLLKGGKVggkalrpsQRVLLQAEQALLNAQN-DLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQ 247
|
....*.
gi 5031875 361 ELLDIK 366
Cdd:PRK11281 248 EAINSK 253
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
185-390 |
1.40e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 185 DEMLRRVDAENRLQTMKEELDFQKNIYSEELRE---TKRRHETRLVEID-NGKQREFESRLADALQE--LRAQHEDQVEQ 258
Cdd:COG3206 93 RPVLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGSNVIEISyTSPDPELAAAVANALAEayLEQNLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 259 YKKELE------KTYSAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 330
Cdd:COG3206 173 ARKALEfleeqlPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031875 331 RDTSRRLLAekEREMAEMRARMQQQLDEYQELL--------DIKlALDMEIHAYRKLLEGEEERLRLS 390
Cdd:COG3206 253 PDALPELLQ--SPVIQQLRAQLAELEAELAELSarytpnhpDVI-ALRAQIAALRAQLQQEAQRILAS 317
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
104-265 |
1.49e-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: 46.46 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 104 LELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ- 182
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 183 ----LQDEM----LRRVDAENRLQTMKEELDFQKniysEELRETKRRHETRLVEIDNgKQREFESRLADaLQELRAQHED 254
Cdd:COG1579 90 eyeaLQKEIeslkRRISDLEDEILELMERIEELE----EELAELEAELAELEAELEE-KKAELDEELAE-LEAELEELEA 163
|
170
....*....|.
gi 5031875 255 QVEQYKKELEK 265
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-416 |
1.92e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 138 EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRE 217
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 218 TKR--RHETRLVEIDNGKQ-REFESRLaDALQELRAQHEDQVEQYKKELEKtysakLDNARQSAERNSNLVGAAHEELQQ 294
Cdd:COG3883 95 LYRsgGSVSYLDVLLGSESfSDFLDRL-SALSKIADADADLLEELKADKAE-----LEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 295 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIH 374
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 5031875 375 AYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVT 416
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAG 290
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-228 |
2.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 25 RITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVsrevsgikAAYEAELGDARKTLDSVAKERA--RL 102
Cdd:COG3206 197 ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL--------AALRAQLGSGPDALPELLQSPViqQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 103 QLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNS-KEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5031875 182 QlqdemlrrvdaENRLQTMKEELDFQKNIYSEELretKRRHETRLVE 228
Cdd:COG3206 349 L-----------EAELRRLEREVEVARELYESLL---QRLEEARLAE 381
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
90-387 |
3.83e-05 |
|
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: 46.71 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 90 KTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLE----------ALLNSKEAALSTALSEkrtLE 159
Cdd:pfam01576 377 KAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNE---AE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 160 GELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEElrETKRRHETRLVEIDNGKQREFES 239
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE--EEAKRNVERQLSTLQAQLSDMKK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 240 RLADALQELraqheDQVEQYKKELEKtysaKLDNARQSAERNSnlvgAAHEELQQSRIR----IDSLSAQLSQLQKQLAA 315
Cdd:pfam01576 532 KLEEDAGTL-----EALEEGKKRLQR----ELEALTQQLEEKA----AAYDKLEKTKNRlqqeLDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031875 316 KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDmEIHAYRKLLEGEEERL 387
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-387 |
4.73e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 25 RITRLQEKEDL-QELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSrEVSGIKAAYEAELGDARKTLDSVA--KERAR 101
Cdd:PRK03918 284 ELKELKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEelEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 102 LQLELSKVREEFKELKARNTKKEgdliaaqarLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKK 181
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLT---------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 182 QLQDEML--RRVDAENRLQTMKEELDFQKNIYSE--ELRETKRRHETRLVEIDNGKQREfesrladalQELRAQHE--DQ 255
Cdd:PRK03918 434 AKGKCPVcgRELTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELRELEKVLKKE---------SELIKLKElaEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 256 VEQYKKELEKTYSAKLdnarqsaERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERD 332
Cdd:PRK03918 505 LKELEEKLKKYNLEEL-------EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLK 577
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 5031875 333 TSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKlaldMEIHAYRKLLEGEEERL 387
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEYLELKDAE----KELEREEKELKKLEEEL 628
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
139-348 |
4.98e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 139 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQdeMLRRV----------DAENRLQTMKEELDFqk 208
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ--LLNKLlpqanlladeTLADRLEELREELDA-- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 209 niySEELRETKRRHETRLVEIDngkqrefesRLADALQELRAQHEDQVEQYK--KELEKTYSAKLDNARQSAERNSNLVG 286
Cdd:COG3096 905 ---AQEAQAFIQQHGKALAQLE---------PLVAVLQSDPEQFEQLQADYLqaKEQQRRLKQQIFALSEVVQRRPHFSY 972
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031875 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. ... |
82-352 |
8.13e-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: 45.60 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTAL-SEKRTLEG 160
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLR-RVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFES 239
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 240 RLADalqelraqhEDQVEQYKKELeKTYSAKLDNARQ-SAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAA 315
Cdd:pfam12128 763 LGVD---------PDVIAKLKREI-RTLERKIERIAVrRQEVLRYFDWYQETWLQRRprlATQLSNIERAISELQQQLAR 832
|
250 260 270
....*....|....*....|....*....|....*..
gi 5031875 316 KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARM 352
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-388 |
8.20e-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: 45.60 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 34 DLQELNDRLAVYIDRVRSLETENAGLRLRITESE----EVVSREVSGIKAAYEAELGDARKTLDSVAKE-RARLQLELSK 108
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 109 VREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAaLSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 188
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 189 RRVDAENRLQTMKEELDFQKNIYSEELREtkrrhetrlveiDNGKQREFESRLADALQELRAQ-HEDQVEQYKKELEKTY 267
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTLLHFLRK------------EAPDWEQSIGKVISPELLHRTDlDPEVWDGSVGGELNLY 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 268 SAKLDNAR-------QSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 340
Cdd:pfam12128 582 GVKLDLKRidvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE 661
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 5031875 341 KERE---MAEMRARMQQQLDEYQELLDIKL-ALDMEIHAYRKLLEGEEERLR 388
Cdd:pfam12128 662 KQSEkdkKNKALAERKDSANERLNSLEAQLkQLDKKHQAWLEEQKEQKREAR 713
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
33-307 |
8.22e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 33 EDLQELNdrlAVYIDrvrSLETENAGLRLR-ITESEEVVSREVSGIKAAYEAELGD----ARKTLDSVAKERARLQLELS 107
Cdd:PRK05771 23 EALHELG---VVHIE---DLKEELSNERLRkLRSLLTKLSEALDKLRSYLPKLNPLreekKKVSVKSLEELIKDVEEELE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 108 KVREEFKELKARntkkegdLIAAQARLKDLEALLNskeaalstALSEKRTLEGELHDLRGQvAKLEAALGEAKKQLQDEM 187
Cdd:PRK05771 97 KIEKEIKELEEE-------ISELENEIKELEQEIE--------RLEPWGNFDLDLSLLLGF-KYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 188 LRRVDAENrLQTMKEELD------FQKNIYSEELRETKRRHETRLVEIDNGKqrefesrladALQELRAQHEDQVEQYKK 261
Cdd:PRK05771 161 KLESDVEN-VEYISTDKGyvyvvvVVLKELSDEVEEELKKLGFERLELEEEG----------TPSELIREIKEELEEIEK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5031875 262 ELEKTysakLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS 307
Cdd:PRK05771 230 ERESL----LEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-340 |
1.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 96 AKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKE-----------------AALSTALSEKRTL 158
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreeletleaeiedlrETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 159 EGELHDLRGQVAKLEAALGEAkkqLQDEMLRRVDAEnRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDN--GKQRE 236
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDL---LAEAGLDDADAE-AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESlrEDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 237 FESRlADALQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK 316
Cdd:PRK02224 354 LEER-AEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
250 260
....*....|....*....|....
gi 5031875 317 EAKLRDLEDSLARerdtSRRLLAE 340
Cdd:PRK02224 432 EATLRTARERVEE----AEALLEA 451
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
80-351 |
1.11e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 80 AYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLE 159
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 160 GELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDA-ENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEIDNGKQRE 236
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSidKLRKEIERlEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 237 FESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKqlaak 316
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAQE-LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK----- 237
|
250 260 270
....*....|....*....|....*....|....*
gi 5031875 317 eaKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 351
Cdd:COG1340 238 --ELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-174 |
1.60e-04 |
|
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: 44.67 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRItESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVRE 111
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAEL-EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031875 112 EFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTAL--------------SEKRTLEGELHDLRGQVAKLEA 174
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlskyeqelydlkEEYDRVEKELSKLQRELAEAEA 497
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
296-388 |
1.87e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 296 RIRIDSLSAQLSQLQKQLAA----KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALD- 370
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEq 482
|
90 100
....*....|....*....|
gi 5031875 371 --MEIHAYRKLLEGEEERLR 388
Cdd:COG0542 483 ryGKIPELEKELAELEEELA 502
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
57-212 |
3.86e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 57 AGLRLRITESEEVVSREVSGIKAAYEAELGDARktlDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKD 136
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAK---ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 137 LEALLNSKEAALSTALSEkrtLEGELHDLRgqvAKLEAALGEAKKQLQDEMLRRVDAENRLQ------TMKEELDFQKNI 210
Cdd:PRK12705 103 LENQLEEREKALSARELE---LEELEKQLD---NELYRVAGLTPEQARKLLLKLLDAELEEEkaqrvkKIEEEADLEAER 176
|
..
gi 5031875 211 YS 212
Cdd:PRK12705 177 KA 178
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-325 |
4.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 20 PLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAE-LGDARKTLDSVAKE 98
Cdd:PRK03918 439 PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqLKELEEKLKKYNLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 99 rarlqlELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNskeaalstalsEKRTLEGELHDLRGQVAKLEAALGE 178
Cdd:PRK03918 519 ------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK-----------KLAELEKKLDELEEELAELLKELEE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 179 AKKQLQDEMLRRVdaeNRLQTMKEELDFQKNIYSeELRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEdqveq 258
Cdd:PRK03918 582 LGFESVEELEERL---KELEPFYNEYLELKDAEK-ELEREEKELKKLEEELD--KAFEELAETEKRLEELRKELE----- 650
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031875 259 ykkELEKTYSA-KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 325
Cdd:PRK03918 651 ---ELEKKYSEeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-319 |
4.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 99 RARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALge 178
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 179 akkQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKQ--REFESRLADALQELRAQHEDQV 256
Cdd:COG4717 126 ---QLLPLYQELEALEAELAELPERL--------EELEERLEELRELEEELEELEAelAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031875 257 EQYKKELEktysaKLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:COG4717 195 QDLAEELE-----ELQQRLAELE----------EELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-387 |
5.43e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 153 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAEnRLQTMKEELdfQKNIYSEELREtKRRHETRLVEIDNg 232
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK--REYEGYELLKE-KEALERQKEAIER- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 233 kqrefesRLADALQELraqheDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGaahEELQQSRIRIDSLSAQLSQL--- 309
Cdd:TIGR02169 245 -------QLASLEEEL-----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLers 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 310 -------QKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 382
Cdd:TIGR02169 310 iaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
....*
gi 5031875 383 EEERL 387
Cdd:TIGR02169 390 YREKL 394
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
73-403 |
5.89e-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: 42.79 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 73 EVSGIKAAYEAELGDARKTLdsvaKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTAL 152
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 153 SEKRTLEGELHDLRGQVAKLEA----ALGEAKKQLQDEMLRRVDAENRLQTM----KEELDFQKNIYSEELRETKRRHET 224
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAhcdkLLLENKELTQEASDMTLELKKHQEDIinckKQEERMLKQIENLEEKEMNLRDEL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 225 RLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELeKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSA 304
Cdd:pfam05483 551 ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM-KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 305 QL-------SQLQKQLAAKEAKLRDLEDSLARE----RDTSRRLL--AEKEREMAEMRARMQQQLDE--YQELLDIKLAL 369
Cdd:pfam05483 630 QLnayeikvNKLELELASAKQKFEEIIDNYQKEiedkKISEEKLLeeVEKAKAIADEAVKLQKEIDKrcQHKIAEMVALM 709
|
330 340 350
....*....|....*....|....*....|....
gi 5031875 370 DMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRAS 403
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAA 743
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-341 |
6.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 78 KAAYEAELGDARKTLDSVAK-ERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKR 156
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 157 TLEGE---------LHDLRGQVAKLEAALGEAKKQLqdEMLRRVDAENRLQtmKEELDFQKNIYSEELRETKRRHETRLV 227
Cdd:PTZ00121 1614 KAEEAkikaeelkkAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 228 EIDNGKQREFESRLADALQELRAQHEDQVEQYKKElEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRiridslsaQLS 307
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--------KIA 1760
|
250 260 270
....*....|....*....|....*....|....*...
gi 5031875 308 QLQKQLAAKEAKLRDLEDSLARE----RDTSRRLLAEK 341
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEeldeEDEKRRMEVDK 1798
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
28-308 |
6.39e-04 |
|
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: 43.02 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 28 RLQEK-----EDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEvvsrEVSGIKAayeaELGDARKTLDSV------- 95
Cdd:COG3096 344 RQQEKieryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEE----EVDSLKS----QLADYQQALDVQqtraiqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 96 -----AKERARLQLELSK-----VREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAAL------------STALS 153
Cdd:COG3096 416 qqavqALEKARALCGLPDltpenAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYelvckiageverSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 154 EKRTLEGELHDLR---GQVAKLEAALGEAKK---------QLQDEMLRR----VDAENRLQTMKEELDFQKNIYSEELRE 217
Cdd:COG3096 496 TARELLRRYRSQQalaQRLQQLRAQLAELEQrlrqqqnaeRLLEEFCQRigqqLDAAEELEELLAELEAQLEELEEQAAE 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 218 -TKRRHETR--LVEIdNGKQREFESR------LADALQELRAQHEDQVEQykkelektySAKLDNARQSAERNSNLVGAA 288
Cdd:COG3096 576 aVEQRSELRqqLEQL-RARIKELAARapawlaAQDALERLREQSGEALAD---------SQEVTAAMQQLLEREREATVE 645
|
330 340
....*....|....*....|
gi 5031875 289 HEELQQSRIRIDSLSAQLSQ 308
Cdd:COG3096 646 RDELAARKQALESQIERLSQ 665
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
79-185 |
6.91e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 79 AAYEAELGDARKTLDSVAKERARLQLELskvrEEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTL 158
Cdd:COG1566 106 LGAEAEIAAAEAQLAAAQAQLDLAQREL----ERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREE 181
|
90 100
....*....|....*....|....*..
gi 5031875 159 EgELHDLRGQVAKLEAALGEAKKQLQD 185
Cdd:COG1566 182 E-ELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
25-362 |
7.07e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 25 RITRLQEK-EDLQE-LNDR---LAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDsvaker 99
Cdd:pfam10174 395 KINVLQKKiENLQEqLRDKdkqLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE------ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 100 arlqlELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALgea 179
Cdd:pfam10174 469 -----ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL--- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 180 KKQLQDEMLRRVDAE--NRLQTMKEELDFqkniYSEELRETKRRHEtRLVEIdngkQREFESRLADALQELRAQHEDQVE 257
Cdd:pfam10174 541 KKAHNAEEAVRTNPEinDRIRLLEQEVAR----YKEESGKAQAEVE-RLLGI----LREVENEKNDKDKKIAELESLTLR 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 258 QYKKELEKTYSAKLdnaRQSAERNSNLvgaahEELQQSRIRIDSLSAQLSQLQ-KQLAAKEAKLRDLEDSLARERDTSRR 336
Cdd:pfam10174 612 QMKEQNKKVANIKH---GQQEMKKKGA-----QLLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLSSTQQ 683
|
330 340
....*....|....*....|....*.
gi 5031875 337 LLAEKEREMAEMRARMQQQLDEYQEL 362
Cdd:pfam10174 684 SLAEKDGHLTNLRAERRKQLEEILEM 709
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
161-362 |
7.34e-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: 41.45 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 161 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESR 240
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL--------EDLEKEIKRLELEIEEVEA-RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 241 LAdalqelRAQHEDQVEQYKKELEKtysakLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL 320
Cdd:COG1579 82 LG------NVRNNKEYEALQKEIES-----LKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5031875 321 RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQL-DEYQEL 362
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIPPELlALYERI 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-362 |
8.85e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 28 RLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELS 107
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 108 KVREEFKE--LKARNTKKEGDLIAAQARLKDLE---ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:COG1196 538 AALEAALAaaLQNIVVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 183 LQDEMLRRVDAENRLQTMKEELDfqkniySEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE 262
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAV------TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 263 LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDtsrrlLAEKE 342
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELE 766
|
330 340
....*....|....*....|....*..
gi 5031875 343 REMAEMRARMQQ-------QLDEYQEL 362
Cdd:COG1196 767 RELERLEREIEAlgpvnllAIEEYEEL 793
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
155-388 |
9.37e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 155 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQtmkeelDFQKNIYSEELRETKRRHETRLVEIdngkq 234
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALE------EFRQKNGLVDLSEEAKLLLQQLSEL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 235 refESRLADAlQELRAQHEDQVEQYKKELEKTYSAkldnarQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS------- 307
Cdd:COG3206 225 ---ESQLAEA-RAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvi 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 308 QLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 387
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
.
gi 5031875 388 R 388
Cdd:COG3206 375 E 375
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
51-319 |
1.16e-03 |
|
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: 42.07 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 51 SLETENAGLRLRITESEEVVSREVSGIKAAYEA-------ELGDARKTLDSVAKERARLQLELSKVREEfkelKARNTKK 123
Cdd:pfam18971 571 SLQEANKLIKDFLSSNKELAGKALNFNKAVAEAkstgnydEVKKAQKDLEKSLRKREHLEKEVEKKLES----KSGNKNK 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 124 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLqDEMLRRVD-----AENRLQ 198
Cdd:pfam18971 647 MEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSF-DEFKNGKNkdfskAEETLK 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 199 TMKEELDfQKNIYSEELRETKRRHETrLVEIDNGKQREFeSRLADALQELRAQHEDQVeqykkeLEKTYSAKLDNARQSA 278
Cdd:pfam18971 726 ALKGSVK-DLGINPEWISKVENLNAA-LNEFKNGKNKDF-SKVTQAKSDLENSVKDVI------INQKVTDKVDNLNQAV 796
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 5031875 279 ErnsnlVGAAHEELQqsriRIDSLSAQLSQLQKQLAAKEAK 319
Cdd:pfam18971 797 S-----VAKAMGDFS----RVEQVLADLKNFSKEQLAQQAQ 828
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
82-250 |
1.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 82 EAELGDARKTLDSVAKERARLQLELSKVREEFKELKarntkKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRtlegE 161
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALEAELAELPERLEELEERLE----E 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 162 LHDLRGQVAKLEAALGEAKKQLQDEMLR-RVDAENRLQTMKEELDF---QKNIYSEELRETKRRHETRLVEIDNGKQREF 237
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170
....*....|...
gi 5031875 238 ESRLADALQELRA 250
Cdd:COG4717 238 AAALEERLKEARL 250
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
69-199 |
1.34e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 69 VVSREVSGIKAAYE------AELGDA----RKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLE 138
Cdd:PRK09039 43 FLSREISGKDSALDrlnsqiAELADLlsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031875 139 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQT 199
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
124-205 |
1.58e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 124 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA-ALGEAKKQLQDEMLRRVDAENRLQTMKE 202
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAqALQTAQNNLATAQAALANAEARLAKAKE 339
|
...
gi 5031875 203 ELD 205
Cdd:TIGR04320 340 ALA 342
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
253-371 |
1.65e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.99 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 253 EDQVEQYKKELEKTYsAKLDNARQsaernsnlvgaAHEELQQSRIRID------SLSAQLSQLQKQLAAKEAKLRDLEDS 326
Cdd:COG3524 176 EDAVRFAEEEVERAE-ERLRDARE-----------ALLAFRNRNGILDpeataeALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 5031875 327 L---ARERDTSRRLLAEKEREMAEMRARM---------QQQLDEYQEL-LDIKLALDM 371
Cdd:COG3524 244 LspnSPQVRQLRRRIAALEKQIAAERARLtgasggdslASLLAEYERLeLEREFAEKA 301
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
114-325 |
2.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 114 KELKARNTKKEGDLIAAQARLKDLEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLqdEMLRRVDA 193
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREEL--EKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 194 ENRLQTMKEELDFQKNIYSEELRETKRRHETRLveidngkqrefesrladALQELRAQHEDQVEQYKKELEKTYSAKLDN 273
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELR-----------------ELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5031875 274 ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 325
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
21-387 |
2.69e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 21 LSPTRITRLQEKE-DLQELNDRLavyidrvRSLETENAGLRLRITESEEVVSREVSGIKAAyeaelgdarKTLDSVAKER 99
Cdd:TIGR00606 731 LAPGRQSIIDLKEkEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESA---------KVCLTDVTIM 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 100 ARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEA 179
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE-----KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 180 KK---QLQDEMLRRVDAENRLQTMKEELDF------QKNIYSEELRETKRRHETRLVEIDNGKqrEFESRLADALQELRA 250
Cdd:TIGR00606 870 KSeklQIGTNLQRRQQFEEQLVELSTEVQSlireikDAKEQDSPLETFLEKDQQEKEELISSK--ETSNKKAQDKVNDIK 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 251 QHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSlsaQLSQLQKQLAAKEAKLRDLEDSLAR- 329
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE---DMRLMRQDIDTQKIQERWLQDNLTLr 1024
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031875 330 ----ERDTSRRLLAEKEREMAEMraRMQQQLDEYQELLD-IKLALDMEIHAYRKLLEGEEERL 387
Cdd:TIGR00606 1025 krenELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEEnIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
78-404 |
2.70e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKArntkkegdLIAAQARLkdleALLNSKEAALSTALSEKRT 157
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSR--------FIGSHLAV----AFEADPEAELRQLNRRRVE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 158 LEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVD--AENRLQTMKEELDFQkniySEELRETKR---RHETRLVEID 230
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSalNRLLPRLNllADETLADRVEEIREQ----LDEAEEAKRfvqQHGNALAQLE 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 231 ngkqrefesRLADALQELRAQHeDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 310
Cdd:PRK04863 925 ---------PIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRL 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 311 KQLAAKEAKLRD-LEDSLARERDTSRRLLAEKERemaemRARMQQQLDEY-QELLDIKLALDmeihayrkllEGEEERLR 388
Cdd:PRK04863 995 EQAEQERTRAREqLRQAQAQLAQYNQVLASLKSS-----YDAKRQMLQELkQELQDLGVPAD----------SGAEERAR 1059
|
330
....*....|....*....
gi 5031875 389 LSPSPTSQR---SRGRASS 404
Cdd:PRK04863 1060 ARRDELHARlsaNRSRRNQ 1078
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
241-349 |
2.78e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 241 LADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKE 317
Cdd:PRK09039 79 LQDSVANLRAS-LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALE 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 5031875 318 AKLRDLE----DSLARERDTSRRL---LAEKEREMAEMR 349
Cdd:PRK09039 158 AALDASEkrdrESQAKIADLGRRLnvaLAQRVQELNRYR 196
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-462 |
3.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVR-------EEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALST 150
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 151 ALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ-----DEMLRRVDAENRLQTMKEELDFQKNiYSEELR----ETKRR 221
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKK-KADEAKkaaeAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 222 HETRLVE----IDNGKQREfESRLADALQelRAQHEDQVEQYKK--ELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS 295
Cdd:PTZ00121 1513 DEAKKAEeakkADEAKKAE-EAKKADEAK--KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 296 RIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE--RDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEi 373
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 374 hayrkllEGEEERLRLSPSPTSQRSRGRASSHSSQTQgggsvTKKRKLEstESRSSFSQHARTSGRVAVEEVDEEGKFVR 453
Cdd:PTZ00121 1669 -------KAEEDKKKAEEAKKAEEDEKKAAEALKKEA-----EEAKKAE--ELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
....*....
gi 5031875 454 LRNKSNEDQ 462
Cdd:PTZ00121 1735 AKKEAEEDK 1743
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-448 |
3.71e-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: 40.49 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 49 VRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERarlQLELSKVREEFKELK--ARNTKKEGD 126
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEH---EVEITGLTEKASSARsqANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 127 LIAAQAR---------LKDLEALLNSKEAALSTAlseKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL 197
Cdd:pfam15921 303 IIQEQARnqnsmymrqLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 198 QTMKEELDFQKNIYSEELRETKR---RHETRLVEIDNgKQREFESRLADaLQELRAQHEDQVEQYKKELEKTYSAkLDNA 274
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDH-LRRELDDRNME-VQRLEALLKAMKSECQGQMERQMAA-IQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 275 RQSAERNSNLVGaaheELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERdtsrRLLAEKEREMAEMRARMQQ 354
Cdd:pfam15921 457 NESLEKVSSLTA----QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE----RAIEATNAEITKLRSRVDL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 355 QLDEYQELldiklaldmeihayrkllEGEEERLRlspsptsqRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHA 434
Cdd:pfam15921 529 KLQELQHL------------------KNEGDHLR--------NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582
|
410
....*....|....
gi 5031875 435 RTSGRVAVEEVDEE 448
Cdd:pfam15921 583 RTAGAMQVEKAQLE 596
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
298-364 |
4.43e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 4.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031875 298 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER------EMAEMRARMQQQLDEYQELLD 364
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaELAGAGAAAEGRAGELAQELD 126
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
79-383 |
4.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 79 AAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTL 158
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 159 EGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKQREFE 238
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL--------KELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 239 SRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA 318
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031875 319 KLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGE 383
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
25-389 |
4.83e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 25 RITRLQEKEDLQELNDRLAVYIDRVRSLE--TENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARL 102
Cdd:TIGR00618 278 VLEETQERINRARKAAPLAAHIKAVTQIEqqAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 103 QLElSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:TIGR00618 358 RDA-HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 183 LQDEMLRRVDAENRLQTMK----------------EELDFQKNIYSEELRETKRRHETRLVEIdNGKQREFESRLADALQ 246
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKlekihlqesaqslkerEQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNP 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 247 ELRA------------QHEDQVEQYKKELEKT-------------YSAKLDNARQS------------------------ 277
Cdd:TIGR00618 516 ARQDidnpgpltrrmqRGEQTYAQLETSEEDVyhqltserkqrasLKEQMQEIQQSfsiltqcdnrskedipnlqnitvr 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 278 --------AERNSNLVGAAHEELQQSRIRID--SLSAQLSQLQKQLAAKEAKLRDLEDSLA--RERDTSRRLLAEKEREM 345
Cdd:TIGR00618 596 lqdlteklSEAEDMLACEQHALLRKLQPEQDlqDVRLHLQQCSQELALKLTALHALQLTLTqeRVREHALSIRVLPKELL 675
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 5031875 346 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 389
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
47-363 |
5.00e-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: 40.10 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 47 DRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKegd 126
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 127 liaaqarLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL-----QDEMLRRVDAENRLQT-- 199
Cdd:pfam15921 344 -------IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeQNKRLWDRDTGNSITIdh 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 200 MKEELDfQKNIYSEELR--------ETKRRHETRLVEIdNGKQREFESrladaLQELRAQHEDQVEQYKKELEKTYSAKL 271
Cdd:pfam15921 417 LRRELD-DRNMEVQRLEallkamksECQGQMERQMAAI-QGKNESLEK-----VSSLTAQLESTKEMLRKVVEELTAKKM 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 272 dnARQSAERNSNLVGAAheeLQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED------SLARERDTSRRLLAEKEREM 345
Cdd:pfam15921 490 --TLESSERTVSDLTAS---LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdhlrNVQTECEALKLQMAEKDKVI 564
|
330
....*....|....*...
gi 5031875 346 AEMRarmqQQLDEYQELL 363
Cdd:pfam15921 565 EILR----QQIENMTQLV 578
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
129-361 |
5.07e-03 |
|
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: 39.74 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 129 AAQARLKDLEALLNSKEAALSTALSEKRTLEGElhdlrgQVAKLEAALGEAKKQLQDEMLRRVDAENRL-QTMKEELDFQ 207
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQAVKA------HTDSLKEASDTAEISREKATDSALQKAEALaEKLKEVINLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 208 KNIYSEELRETK-RRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVE----QYKKELEKTY-----SAKLDNARQS 277
Cdd:pfam09731 203 KQSEEEAAPPLLdAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVAseriVFQQELVSIFpdiipVLKEDNLLSN 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 278 AERNSnLVGAAHEELQQSRIRIDSLSAQLSQ-LQKQLAAKEAKLRDLEDSLARE-----RDTSRRLLAEKEREMAEMRAR 351
Cdd:pfam09731 283 DDLNS-LIAHAHREIDQLSKKLAELKKREEKhIERALEKQKEELDKLAEELSARleevrAADEAQLRLEFEREREEIRES 361
|
250
....*....|
gi 5031875 352 MQQQLDEYQE 361
Cdd:pfam09731 362 YEEKLRTELE 371
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
164-386 |
5.74e-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: 39.85 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 164 DLRGQVAKLEAALGE-AKKQLQDEMLrrVDAENRLQTMKEELDFQKNIYSEElretkrrhetrlVEIDNGKQREFESRLA 242
Cdd:COG0610 648 DYRGIFENLKKALALySEEDGKEDVL--TDPEEALEELKEALDELRALFPEG------------VDFSAFDPTEKLEALD 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 243 DALQELRAQHEDQVEQYK--KELEKTYSAkldnARQSAErnsnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK--EA 318
Cdd:COG0610 714 EAVERFLGDEEARKEFKKlfKELSRLYNL----LSPDDE----FGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKeyEE 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031875 319 KLRDL-EDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 386
Cdd:COG0610 786 KIRQLlDEAIDLERKEIKPRIKQNPVQYRKFSELLEEIIEEYNNGALDADEVLEELEELAKEVKEEEER 854
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-341 |
6.26e-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: 39.62 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 29 LQEKED-LQELNDRLAVYIDRVRSLETENAGLRLRITESEEVvsrevsgiKAAYEAELGDARKTLDSVAKERARLQLELS 107
Cdd:TIGR04523 365 LEEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL--------NQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 108 KVREEFKELKARNTKKEgdliaaqARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDem 187
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKE-------LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE-- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 188 lrrvdAENRLQTMKEELDFQKNiYSEELRETKRRHETRLVEIDNgKQREFESRLAdalqelRAQHEDQVEQYKKELEkty 267
Cdd:TIGR04523 508 -----LEEKVKDLTKKISSLKE-KIEKLESEKKEKESKISDLED-ELNKDDFELK------KENLEKEIDEKNKEIE--- 571
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031875 268 sakldnarQSAERNSNLVgAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEK 341
Cdd:TIGR04523 572 --------ELKQTQKSLK-KKQEEKQE---LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
78-291 |
6.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 78 KAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRT 157
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 158 -----------LEGE-LHDLRGQVAKLEAALGEAKKQLQDemlrRVDAENRLQTMKEELDFQKniysEELRETKRRHETR 225
Cdd:COG3883 98 sggsvsyldvlLGSEsFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKL----AELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031875 226 LVEIDngKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEE 291
Cdd:COG3883 170 KAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
26-198 |
7.02e-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: 39.27 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 26 ITRLQEKEDLqELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSrEVSGIKAAYEAELGDARKTLDSVAKERARLQLE 105
Cdd:pfam05911 79 KTKEWEKIKA-ELEAKLVETEQELLRAAAENDALSRSLQERENLLM-KLSEEKSQAEAEIEALKSRLESCEKEINSLKYE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 106 LSKVReefKELKARNTKKEGDLIAAQARLKdlEALLNSKEAAlstalsekrTLEGELHDLRGQVAKL---EAALgeAKKQ 182
Cdd:pfam05911 157 LHVLS---KELEIRNEEKNMSRRSADAAHK--QHLESVKKIA---------KLEAECQRLRGLVRKKlpgPAAL--AQMK 220
|
170
....*....|....*.
gi 5031875 183 LQDEMLRRVDAENRLQ 198
Cdd:pfam05911 221 LEVEMLGRDSGETRLR 236
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-363 |
7.88e-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: 37.17 E-value: 7.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031875 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELL 363
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
114-349 |
8.08e-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: 39.03 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 114 KELKARNTKKEGDliAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRG--------------QVAKLEAALGEA 179
Cdd:pfam10174 336 KEQRAAILQTEVD--ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerkinvlqkKIENLQEQLRDK 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 180 KKQLqDEMLRRVDA--------ENRLQTMKEELDFQKNIYsEELRETKRRHE-TRLVEIDNGKQrefesRLADALQELRA 250
Cdd:pfam10174 414 DKQL-AGLKERVKSlqtdssntDTALTTLEEALSEKERII-ERLKEQREREDrERLEELESLKK-----ENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 251 QHEDQVEQYKKELEKTYSAKldNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA------KLRDLE 324
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHAS--SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeindRIRLLE 564
|
250 260
....*....|....*....|....*
gi 5031875 325 DSLARERDTSRRLLAEKEREMAEMR 349
Cdd:pfam10174 565 QEVARYKEESGKAQAEVERLLGILR 589
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
79-204 |
8.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 79 AAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEG---------DLIAAQARLKDLEALLNSKEAALS 149
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 5031875 150 TALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEEL 204
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-363 |
8.14e-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: 8.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031875 302 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDT-SRRLLAEKEREMAEMRARMQQQLDEYQELL 363
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQDL 85
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-251 |
8.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 96 AKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLE-ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA 174
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 175 ALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRET-------KRRHETRLVEIDNGKQRefESRLADALQE 247
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeaalrdlRRELRELEAEIASLERR--KSNIPARLLA 444
|
....
gi 5031875 248 LRAQ 251
Cdd:COG4913 445 LRDA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-339 |
8.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 77 IKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKR 156
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 157 TLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQRE 236
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 237 FESRLADALQELRAQHEDQVEQykkELEKtysaKLDNARQSAER--NSNLvgAAHEELQQSRIRIDSLSAQLSQLQKqla 314
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLE---ELER----ELERLEREIEAlgPVNL--LAIEEYEELEERYDFLSEQREDLEE--- 809
|
250 260
....*....|....*....|....*
gi 5031875 315 AKEaKLRDLEDSLarERDTSRRLLA 339
Cdd:COG1196 810 ARE-TLEEAIEEI--DRETRERFLE 831
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
31-146 |
8.96e-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: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 31 EKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSRevsgikaaYEAELGDARKTLDSVAKER----------A 100
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--------LERELSEARSEERREIRKDreisrldreiE 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 5031875 101 RLQLELSKVREEFKELKARntkkegdliaaQARLKDLEALLNSKEA 146
Cdd:COG2433 476 RLERELEEERERIEELKRK-----------LERLKELWKLEHSGEL 510
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
83-377 |
9.50e-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: 39.00 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 83 AELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGEL 162
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDER 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 163 HDLRGQ--------------VAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDF------QKNIYSEELRETKRRH 222
Cdd:pfam01576 499 NSLQEQleeeeeakrnverqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAltqqleEKAAAYDKLEKTKNRL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 223 ETRL--VEIDNGKQREFESRLadalqELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRID 300
Cdd:pfam01576 579 QQELddLLVDLDHQRQLVSNL-----EKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE 653
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031875 301 SLSAQLSQLQKQLAAKEAKLRDLEDSlARERDTSRRLLaekEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYR 377
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKN-VHELERSKRAL---EQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALK 726
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
257-425 |
9.60e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.88 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 257 EQYKKELEKTYSAKLDN------ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 330
Cdd:PRK10929 26 KQITQELEQAKAAKTPAqaeiveALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 331 R------DTSRRLLaEKEREmaemrarMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSqrSRGRASS 404
Cdd:PRK10929 106 AleqeilQVSSQLL-EKSRQ-------AQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT--PLAQAQL 175
|
170 180
....*....|....*....|.
gi 5031875 405 HSSQTQgggSVTKKRKLESTE 425
Cdd:PRK10929 176 TALQAE---SAALKALVDELE 193
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|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
32-358 |
9.92e-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: 39.03 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 32 KEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVS------REVSGIKAAYEAELGDARKTLDSVAKERARLQLE 105
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNkktkqlQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 106 LSKVREEFKElkarntkKEGDLIAAQARLKDLEALLNSKEAALST---ALSEKrtlEGELHDLRGQVAKLEAALGEAKKQ 182
Cdd:pfam10174 403 IENLQEQLRD-------KDKQLAGLKERVKSLQTDSSNTDTALTTleeALSEK---ERIIERLKEQREREDRERLEELES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 183 LQDEMLRRVDAENRLQTMKEE-----LDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQelRAQHEDQVE 257
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEkesslIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK--KAHNAEEAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031875 258 QYKKElektYSAKLDNARQSAERNSnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRL 337
Cdd:pfam10174 551 RTNPE----INDRIRLLEQEVARYK-------EESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKK 619
|
330 340
....*....|....*....|.
gi 5031875 338 LAEKEREMAEMRARMQQQLDE 358
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQLLEE 640
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