|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-330 |
5.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 59 EVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTL 138
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 139 ESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNH 218
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 219 ISDcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIF 298
Cdd:COG1196 402 LEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270
....*....|....*....|....*....|..
gi 568937085 299 TVEREKRKDELLDIAKSKQDRTNSELQNLRQK 330
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-331 |
1.18e-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: 53.52 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168 381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568937085 292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKV 331
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-330 |
4.59e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 212 IIEAVNHISDCSGKFKLLEHALRDAKMaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQeksc 291
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSE-------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA---- 462
|
250 260 270
....*....|....*....|....*....|....*....
gi 568937085 292 lhdeliftvEREKRKDELLDIaKSKQDRTNSELQNLRQK 330
Cdd:TIGR02169 463 ---------DLSKYEQELYDL-KEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-288 |
1.18e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 65 IEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVL----TLEERCSKLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 141 NQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHIS 220
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937085 221 DCSGKFKLLEHALRDAKMAETcvvREKQDYKQKLKALRIEVNKLKEDL----NEKTTENNEQREEIIRLKQE 288
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAealeNKIEDDEEEARRRLKRLENK 980
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-316 |
3.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 62 TSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 142 QAECQTALQKTQQQLQEMAQKATHSTLLS----EDLEARNENLSSTLVDLSAQVGQLQAREQALTTmiklkdkdiieavn 217
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA-------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 218 hisdcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4942 165 -----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....*....
gi 568937085 298 FTVEREKRKDELLDIAKSK 316
Cdd:COG4942 234 AEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-330 |
6.12e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 96 QLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKAthsTLLSEDLEA 175
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 176 RNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDcsgkFKLLEHALRDAkmaetcvVREKQDYKQKLK 255
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQ-------AEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937085 256 ALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDELLDIAKSKQDRTNSELQNLRQK 330
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-333 |
1.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 125 TDIIKSLMKKVKTLEsNQAEcqTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTM 204
Cdd:COG1196 192 EDILGELERQLEPLE-RQAE--KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIR 284
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568937085 285 LKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKVLR 333
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-217 |
5.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 64 TIEKQRKELQLLIGELKDRDKELNDmVAVHQRQLLSWEEDRQKVL-------TLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDassddlaALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 137 TLESNQAECQTALQKTQQQLQEMAQKAthSTLLSEDLEARNENLSSTLVdLSAQVGQLQAREQALTTMIKLKDKDIIEAV 216
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAM 793
|
.
gi 568937085 217 N 217
Cdd:COG4913 794 R 794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-334 |
6.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 125 TDIIKSLMKKVKTLESnQAECQTALQKTQQQLqemaqKATHSTLLSEDLEARNENLSStlvdLSAQVGQLQAREQALTTM 204
Cdd:TIGR02168 192 EDILNELERQLKSLER-QAEKAERYKELKAEL-----RELELALLVLRLEELREELEE----LQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEV--------------NKLKEDLNE 270
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLeeleaqleelesklDELAEELAE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937085 271 KTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKVLRN 334
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-324 |
7.18e-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: 41.59 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEAR------------NENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDI 212
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 213 IEAVNHISDCSGKFKLLEHALRDAKMaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKscl 292
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI--- 905
|
250 260 270
....*....|....*....|....*....|..
gi 568937085 293 hDELIFTVEREKRKDELLDIAKSKQDRTNSEL 324
Cdd:TIGR02169 906 -EELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-333 |
9.97e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 95 RQLLSWEEDRQKVLTLEERcSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEmaqkathstlLSEDLE 174
Cdd:COG1196 216 RELKEELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE----------LELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 175 ARNENLSSTLVDLSAQVGQ----------LQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVV 244
Cdd:COG1196 285 EAQAEEYELLAELARLEQDiarleerrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 245 REKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSEL 324
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
....*....
gi 568937085 325 QNLRQKVLR 333
Cdd:COG1196 445 EEAAEEEAE 453
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-328 |
1.55e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 143 AECQTALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIieavnhiSDC 222
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKEL-------KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 223 SGKFKLLEHALRDAKMAEtcVVREKQ----DYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIF 298
Cdd:TIGR04523 544 EDELNKDDFELKKENLEK--EIDEKNkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
250 260 270
....*....|....*....|....*....|
gi 568937085 299 TVEREKRKDELLDIAKSKQDRTNSELQNLR 328
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-332 |
1.89e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 106 KVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLV 185
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 186 DLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLK 265
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937085 266 EDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKVL 332
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-297 |
2.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 64 TIEKQRKELQLLIGELKDRDKELND-MVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELhkrtdiikslmkkvKTLESNQ 142
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERlAELEYLRAALRLWFAQRRLELLEAELEELRAEL--------------ARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 143 AECQTALQKTQQQLQEM-AQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAreqaLTTMIKLKDKDIIEAvnhisd 221
Cdd:COG4913 312 ERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA----LLAALGLPLPASAEE------ 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937085 222 csgkFKLLEHALRDAKmaetcvvrekQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4913 382 ----FAALRAEAAALL----------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-288 |
3.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQtALQKTQQQLQEMAQkaT 164
Cdd:COG4913 591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS--A 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 165 HSTLlsEDLEARNENLSSTLVDLSA---QVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAkmAET 241
Cdd:COG4913 667 EREI--AELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568937085 242 CVVREKQDYKQKLKALRIE--VNKLKEDLNEK----TTENNEQREEIIRLKQE 288
Cdd:COG4913 743 ARLELRALLEERFAAALGDavERELRENLEERidalRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-217 |
4.13e-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: 38.95 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 71 ELQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLESnqaECQTALQ 150
Cdd:pfam15921 378 QLQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS---ECQGQME 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 151 KTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKdIIEAVN 217
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKER-AIEATN 516
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
65-200 |
5.66e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 65 IEKQRKELQlliGELKDRDKELNDMvavhQRQLLsweedrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:PRK12704 66 IHKLRNEFE---KELRERRNELQKL----EKRLL------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937085 145 CQTALQKTQQQLQEMAQkathstlLSEDlEARNENLSSTLVDLSAQVGQL------QAREQA 200
Cdd:PRK12704 133 LEELIEEQLQELERISG-------LTAE-EAKEILLEKVEEEARHEAAVLikeieeEAKEEA 186
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
59-333 |
6.64e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 38.16 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 59 EVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQrQLLSWEEDRQKVLTLEercsklegeLHKRTDIIKSLMKKVKTL 138
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITME---------LQKKSSELEEMTKFKNNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 139 ESNQAECQTALQKTQQQLQEMAQKAThstlLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAvnh 218
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEK----IAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL--- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 219 isdcsgKFKLLEHALRDAKMAETC--VVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDEL 296
Cdd:pfam05483 477 ------KTELEKEKLKNIELTAHCdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
250 260 270
....*....|....*....|....*....|....*..
gi 568937085 297 IFTVEREKRKDellDIAKSKQDRTNSELQNLRQKVLR 333
Cdd:pfam05483 551 ESVREEFIQKG---DEVKCKLDKSEENARSIEYEVLK 584
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
65-334 |
8.00e-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: 38.08 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 65 IEKQRKELQLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKI----KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTtmiKLKDKDIIEAVN-HISDCS 223
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---NQKEQDWNKELKsELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937085 224 GKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTT-------ENNEQREEIIRLKQEKSCLHDEL 296
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeieklkkENQSYKQEIKNLESQINDLESKI 400
|
250 260 270
....*....|....*....|....*....|....*...
gi 568937085 297 IFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKVLRN 334
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
|
| |
