|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-329 |
4.24e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 51 YRRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKS 130
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 131 LMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDK 210
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 211 DIIEAVNHISDcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKS 290
Cdd:COG1196 394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270
....*....|....*....|....*....|....*....
gi 568937075 291 CLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-334 |
8.74e-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: 53.91 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168 381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568937075 292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQVCPSC 334
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-329 |
4.30e-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: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 212 IIEAVNHISDCSGKFKLLEHALRDAKMaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQeksc 291
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSE-------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA---- 462
|
250 260 270
....*....|....*....|....*....|....*...
gi 568937075 292 lhdeliftvEREKRKDELLDIaKSKQDRTNSELQNLRQ 329
Cdd:TIGR02169 463 ---------DLSKYEQELYDL-KEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-288 |
6.57e-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: 51.21 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 65 IEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVL----TLEERCSKLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 141 NQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHIS 220
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937075 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 |
1.42e-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: 46.30 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 62 TSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 142 QAECQTALQKTQQQLQEMAQKATHSTLLS----EDLEARNENLSSTLVDLSAQVGQLQAREQALTTmiklkdkdiieavn 217
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA-------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 218 hisdcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4942 165 -----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....*....
gi 568937075 298 FTVEREKRKDELLDIAKSK 316
Cdd:COG4942 234 AEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-329 |
2.80e-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: 45.53 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 96 QLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKAthsTLLSEDLEA 175
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 176 RNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDcsgkFKLLEHALRDAkmaetcvVREKQDYKQKLK 255
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQ-------AEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937075 256 ALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-217 |
3.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 64 TIEKQRKELQLLIGELKDRDKELNDmVAVHQRQLLSWEEDRQKVL-------TLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDassddlaALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 137 TLESNQAECQTALQKTQQQLQEMAQKAthSTLLSEDLEARNENLSSTLVdLSAQVGQLQAREQALTTMIKLKDKDIIEAV 216
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAM 793
|
.
gi 568937075 217 N 217
Cdd:COG4913 794 R 794
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-329 |
4.02e-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: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 187 LSAQVGQL--QAR--EQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVN 262
Cdd:COG1196 198 LERQLEPLerQAEkaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937075 263 KLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-324 |
4.30e-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: 42.36 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEARN------------ENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDI 212
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 213 IEAVNHISDCSGKFKLLEHALRDAKMaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKscl 292
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI--- 905
|
250 260 270
....*....|....*....|....*....|..
gi 568937075 293 hDELIFTVEREKRKDELLDIAKSKQDRTNSEL 324
Cdd:TIGR02169 906 -EELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-328 |
4.83e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 143 AECQTALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIieavnhiSDC 222
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKEL-------KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 223 SGKFKLLEHALRDAKMAEtcVVREKQ----DYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIF 298
Cdd:TIGR04523 544 EDELNKDDFELKKENLEK--EIDEKNkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
250 260 270
....*....|....*....|....*....|
gi 568937075 299 TVEREKRKDELLDIAKSKQDRTNSELQNLR 328
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-329 |
1.05e-03 |
|
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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 95 RQLLSWEEDRQKVLTLEERcSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEmaqkathstlLSEDLE 174
Cdd:COG1196 216 RELKEELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE----------LELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 175 ARNENLSS-----------------TLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAK 237
Cdd:COG1196 285 EAQAEEYEllaelarleqdiarleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 238 MAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQ 317
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250
....*....|..
gi 568937075 318 DRTNSELQNLRQ 329
Cdd:COG1196 445 EEAAEEEAELEE 456
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-323 |
1.17e-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: 40.77 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 63 STIEKQRKELQLLIGELK-----DRDKELNDMVAVHQRQLLsweedrqkvlTLEERCSKLEGELHKRTDIIKSLMKKVKT 137
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLE----------EIQNQISQNNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 138 LESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVN 217
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 218 HISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELi 297
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV- 512
|
250 260
....*....|....*....|....*.
gi 568937075 298 ftVEREKRKDELldiaKSKQDRTNSE 323
Cdd:TIGR04523 513 --KDLTKKISSL----KEKIEKLESE 532
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-297 |
1.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 64 TIEKQRKELQLLIGELKDRDKELND-MVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELhkrtdiikslmkkvKTLESNQ 142
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERlAELEYLRAALRLWFAQRRLELLEAELEELRAEL--------------ARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 143 AECQTALQKTQQQLQEM-AQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAreqaLTTMIKLKDKDIIEAvnhisd 221
Cdd:COG4913 312 ERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA----LLAALGLPLPASAEE------ 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937075 222 csgkFKLLEHALRDAKmaetcvvrekQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4913 382 ----FAALRAEAAALL----------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-288 |
2.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQtALQKTQQQLQEMAQkaT 164
Cdd:COG4913 591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS--A 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 165 HSTLlsEDLEARNENLSSTLVDLSA---QVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAkmAET 241
Cdd:COG4913 667 EREI--AELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568937075 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 |
3.11e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 71 ELQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLESnqaECQTALQ 150
Cdd:pfam15921 378 QLQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS---ECQGQME 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 151 KTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKdIIEAVN 217
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKER-AIEATN 516
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
65-200 |
4.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 65 IEKQRKELQlliGELKDRDKELNDMvavhQRQLLsweedrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:PRK12704 66 IHKLRNEFE---KELRERRNELQKL----EKRLL------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937075 145 CQTALQKTQQQLQEMAQkathstlLSEDlEARNENLSSTLVDLSAQVGQL------QAREQA 200
Cdd:PRK12704 133 LEELIEEQLQELERISG-------LTAE-EAKEILLEKVEEEARHEAAVLikeieeEAKEEA 186
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
110-344 |
7.03e-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: 38.23 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 110 LEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSA 189
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 190 QVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRI---------- 259
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTeledtldtta 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 260 -----------EVNKLKEDLNEKTTENNEQREEiirLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQN-L 327
Cdd:pfam01576 317 aqqelrskreqEVTELKKALEEETRSHEAQLQE---MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAeL 393
|
250
....*....|....*..
gi 568937075 328 RQVCPSCLRCEHREKKV 344
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKL 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
65-329 |
7.42e-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: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 65 IEKQRKELQLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKI----KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTtmiKLKDKDIIEAVN-HISDCS 223
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---NQKEQDWNKELKsELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 224 GKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTT-------ENNEQREEIIRLKQEKSCLHDEL 296
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeieklkkENQSYKQEIKNLESQINDLESKI 400
|
250 260 270
....*....|....*....|....*....|...
gi 568937075 297 IFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
59-342 |
9.36e-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: 37.78 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 59 EVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQrQLLSWEEDRQKVLTLEercsklegeLHKRTDIIKSLMKKVKTL 138
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITME---------LQKKSSELEEMTKFKNNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 139 ESNQAECQTALQKTQQQLQEMAQKAThstlLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAvnh 218
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEK----IAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL--- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937075 219 isdcsgKFKLLEHALRDAKMAETC--VVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDEL 296
Cdd:pfam05483 477 ------KTELEKEKLKNIELTAHCdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568937075 297 IFTVEREKRKDellDIAKSKQDRTNselQNLRQVCPSCLRCEHREK 342
Cdd:pfam05483 551 ESVREEFIQKG---DEVKCKLDKSE---ENARSIEYEVLKKEKQMK 590
|
|
| |
