|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
55-366 |
6.89e-138 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 396.60 E-value: 6.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 55 SEKETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLLCPSYQSYFKTIEELQQKILCTKSENARLVVQIDNA 134
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 135 KLAADDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLRCQLGD-RLNVEV 213
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 214 DAAPTVDLNRVLNETRSQYEALVETNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLR 293
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14917115 294 DSLENTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCN 366
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-362 |
2.01e-11 |
|
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: 66.23 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 110 IEELQQKILCTKSENARLVVQIDNAKLAADDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLC 189
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 190 LKSNHEqEVNTLRCQLGDRLnvEVDAAPTVDLNRVLNETRSQYEALVETNRREVEQWF---------TTQTEELNKQVVS 260
Cdd:TIGR02168 314 LERQLE-ELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAELEelesrleelEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 261 SSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESE-ARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEY 339
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260
....*....|....*....|...
gi 14917115 340 QVLLDVRARLECEINTYRSLLES 362
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-350 |
4.40e-11 |
|
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: 65.08 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 54 GSEKETMQFLNDRlasylEKVRQLERDNAELENLIRERSQQQEPLLcpsyqsyfKTIEELQQKILCTKSENARLVVQIDN 133
Cdd:TIGR02168 664 GSAKTNSSILERR-----REIEELEEKIEELEEKIAELEKALAELR--------KELEELEEELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 134 AKLAADDFRTKYQTELSLRQLVESD-------INGLRRILDELTLCKSDLEAQVESLKEELLclksNHEQEVNTLRCQLg 206
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKElteleaeIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREAL- 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 207 DRLNVEVDaaptvDLNRVLNETRSQYEALvETNRREVEQwfttQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIEL 286
Cdd:TIGR02168 806 DELRAELT-----LLNEEAANLRERLESL-ERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14917115 287 QAQHNLRDSLENTLTESEARYSSQLSQVQslitNVESQLAEIRSDLERQNQEyqvLLDVRARLE 350
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELR----ELESKRSELRRELEELREK---LAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-363 |
5.25e-11 |
|
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: 64.69 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 63 LNDRLASYLEKVRQLERDNAELENLIRERSQQQEpLLCPSYQSYFKTIEELQQKILCTKSENARLVVQIDNAKLAADDFR 142
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 143 TKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNtlrcqlgdrlnvevDAAPTVDLN 222
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER--------------RIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 223 RVLNETRSQYEALVETNRREVEQwFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQaqhnlrdSLENTLTE 302
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEALLNERASLEEALALLRSELEELSEELR-------ELESKRSE 912
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14917115 303 SEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESE 363
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
130-350 |
1.95e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 130 QIDNAKLAADDFRTKYQtelslrqLVESDiNGLRRILDELtlckSDLEAQVESLKEELlclksnheQEVNTLRCQLGDRL 209
Cdd:COG3206 190 ELEEAEAALEEFRQKNG-------LVDLS-EEAKLLLQQL----SELESQLAEARAEL--------AEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 210 NVEVDAAPTVDLNRVLNETRSQYEALvETNRREVEQWFTtqteELNKQVVSSSEQLQSYQAEI-IELRRTVNALEIELQA 288
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYT----PNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14917115 289 QHNLRDSLENTLTESEARYSSqlsqvqslITNVESQLAEIRSDLERQNQEYQVLLdvrARLE 350
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLL---QRLE 375
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-362 |
3.79e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 176 LEAQVESLKEELlclkSNHEQEVNTLRCQ-----LGDRLNVEVDAapTVDLNRVLNETRSQYEALvETNRREVEQWFTTQ 250
Cdd:COG3206 180 LEEQLPELRKEL----EEAEAALEEFRQKnglvdLSEEAKLLLQQ--LSELESQLAEARAELAEA-EARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 251 TEELNKqvVSSSEQLQSYQAEIIELRRTVNALEIELQAQH----NLRDSLENTLTESEARYSSQLSQVQSLITNVESQLA 326
Cdd:COG3206 253 PDALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREA 330
|
170 180 190
....*....|....*....|....*....|....*....
gi 14917115 327 EIRSDLERQNQEYQVLLDVRA---RLECEINTYRSLLES 362
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAelrRLEREVEVARELYES 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-350 |
8.88e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 66 RLASYLEKVRQLERDNAELENLIRERSQQQEpllcpsyqsyfkTIEELQQKILCTKSENARLVVQIDNAKLAADDFRTKY 145
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEA------------ELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 146 QTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLRCQLGDRLNVEVDAAptvDLNRVL 225
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL---EAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 226 NETRSQYEALVETNRREveqwfTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEA 305
Cdd:COG1196 375 AEAEEELEELAEELLEA-----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 14917115 306 RYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLE 350
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-353 |
3.70e-08 |
|
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: 54.77 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 98 LLCPSYQSYFKTIEELQQKIlctksenARLVVQIDNAKLAADDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLE 177
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 178 AQVESLKEELLCLksnhEQEVNTLRCQLGDRLNVEVDAAPTVDLNRVLNEtrsqyEALVETNRREveQWFTTQTEELNKQ 257
Cdd:COG4942 83 AELAELEKEIAEL----RAELEAQKEELAELLRALYRLGRQPPLALLLSP-----EDFLDAVRRL--QYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 258 VvsssEQLQSYQAEIIELRRtvnaleiELQAQHNLRDSLENTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQ 337
Cdd:COG4942 152 A----EELRADLAELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....*.
gi 14917115 338 EYQVLLDVRARLECEI 353
Cdd:COG4942 221 EAEELEALIARLEAEA 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-363 |
7.13e-08 |
|
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: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 223 RVLNETRSQY-EALVETNRREVEQ---WFTTQTEELNKQV----------------VSSSEQLQSYQAEIIELRRTVNAL 282
Cdd:COG3206 152 AVANALAEAYlEQNLELRREEARKaleFLEEQLPELRKELeeaeaaleefrqknglVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 283 EIELQAQHNLRDSLENTL-----TESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLL----DVRARLECEI 353
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRaqiaALRAQLQQEA 311
|
170
....*....|
gi 14917115 354 NTYRSLLESE 363
Cdd:COG3206 312 QRILASLEAE 321
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-328 |
8.82e-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: 54.68 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 63 LNDRLASYLEKVRQLERDNAELENLIRErsQQQEpllcpsYQSYFKTIEELQQKILCTKSENARLVVQIDNAKLAADDF- 141
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEE--LQKE------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 142 --RTKYQTELSLRQ----LVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSN---HEQEVNTLRCQLGdRLNVE 212
Cdd:TIGR02168 330 skLDELAEELAELEekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIE-RLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 213 VDAApTVDLNRVLNETRSQYEALVETNRREVEQWFTTQTEELNK---QVVSSSEQLQSYQAEIIELRRTVNALEIELQAQ 289
Cdd:TIGR02168 409 LERL-EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 14917115 290 HNLRDSLENTLT--ESEARYSSQLSQVQSLITNVESQLAEI 328
Cdd:TIGR02168 488 QARLDSLERLQEnlEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
144-350 |
1.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 144 KYQTELSLRQLVES--DINGLRRILDELTLCKSDLEAQVESLKEELlclkSNHEQEVNTLRCQLgDRLNVEVDAAptvdl 221
Cdd:COG1196 217 ELKEELKELEAELLllKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLEL-EELELELEEA----- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 222 NRVLNETRSQYEALVETNRREVEQW--FTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENT 299
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14917115 300 LTESEARYSSQLSQVQSL---ITNVESQLAEIRSDLERQNQEYQVLLDVRARLE 350
Cdd:COG1196 367 LLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-315 |
2.24e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 57 KETMQFLNDRLASYLEKVRQLErdnAELENLirersQQQEPLLCPS--YQSYFKTIEELQQKILCTKSENARLVVQIDNA 134
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAE---AALEEF-----RQKNGLVDLSeeAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 135 KLAADdfrtkyQTELSLRQLVESDIngLRRILDELtlckSDLEAQVESLKEELlclKSNH------EQEVNTLRCQLGDR 208
Cdd:COG3206 246 RAQLG------SGPDALPELLQSPV--IQQLRAQL----AELEAELAELSARY---TPNHpdvialRAQIAALRAQLQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 209 LNvevdaaptvdlnRVLNETRSQYEALvetnrREVEQWFTTQTEELNKQVvsssEQLQSYQAEIIELRRtvnaleiELQA 288
Cdd:COG3206 311 AQ------------RILASLEAELEAL-----QAREASLQAQLAQLEARL----AELPELEAELRRLER-------EVEV 362
|
250 260
....*....|....*....|....*..
gi 14917115 289 QHNLRDSLENTLTESEARYSSQLSQVQ 315
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-358 |
3.27e-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: 52.75 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 143 TKYQT--ELSLRQLVESDINgLRRILDELtlckSDLEAQVESLK------EELLCLKsnhEQEVNTLRCQLGDRLNVEVD 214
Cdd:TIGR02168 168 SKYKErrKETERKLERTREN-LDRLEDIL----NELERQLKSLErqaekaERYKELK---AELRELELALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 215 AAPTvdLNRVLNETRSQYEALvETNRREVEqwftTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRD 294
Cdd:TIGR02168 240 ELEE--LQEELKEAEEELEEL-TAELQELE----EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14917115 295 SLENTLTESEAR----------YSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS 358
Cdd:TIGR02168 313 NLERQLEELEAQleeleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-361 |
3.57e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 68 ASYLEKVRQLERDNAELENLIRErsqqqepllcpSYQSYFKTIEELQQKILCTKSENARLVVQIDN------------AK 135
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELRE-----------AKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesgnlddqlQK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 136 LAADdfRTKYQTELSL-----RQLVESD------INGLRRILDELTLCKSDLEAQVESLKEEllClKSNHEQEVNTLRcq 204
Cdd:pfam15921 382 LLAD--LHKREKELSLekeqnKRLWDRDtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSE--C-QGQMERQMAAIQ-- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 205 lGDRLNVEVDAAPTVDLNRVLNETRSQYEAL------VETNRREVEQwFTTQTEELNKQVvssseqlQSYQAEIIELRRT 278
Cdd:pfam15921 455 -GKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtLESSERTVSD-LTASLQEKERAI-------EATNAEITKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 279 VNALEIELQAQHNLRDSLENTLTESEArYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS 358
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL 604
|
...
gi 14917115 359 LLE 361
Cdd:pfam15921 605 ELQ 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-360 |
8.92e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 65 DRLASYLEKVRQLERDNAELENLIRERSQQQEPL--------LCPSYQSYFKTIEELQQKIlctksenARLVVQIDNAKL 136
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqRLAEYSWDEIDVASAEREI-------AELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 137 AADDFRtkyQTELSLRQLvESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEqevntlrcqlgdrlnvEVDAA 216
Cdd:COG4913 683 SSDDLA---ALEEQLEEL-EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----------------AAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 217 PTVDLNRVLNETRSQyeALVETNRREVEQWFTTQTEELNKQVVSSSEQL--------QSYQAEIIELRRTVNALEiELQA 288
Cdd:COG4913 743 ARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELeramrafnREWPAETADLDADLESLP-EYLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 289 qhnLRDSLENT-LTESEARYSSQLSQ-----VQSLITNVESQLAEIRSDLERQNQE-----------YQvlLDVRARLEC 351
Cdd:COG4913 820 ---LLDRLEEDgLPEYEERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSlkripfgpgryLR--LEARPRPDP 894
|
....*....
gi 14917115 352 EINTYRSLL 360
Cdd:COG4913 895 EVREFRQEL 903
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
153-338 |
2.66e-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: 48.38 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 153 QLVESDINGLRRILDELTLCKSDLEAQVESLKEELlclkSNHEQEVNTLRcqlgdrlnvevdaaptvdlnrvlnETRSQY 232
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLE------------------------KEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 233 EALVETNRREVEQWfttqTEELNKqvVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLS 312
Cdd:COG1579 65 ELEIEEVEARIKKY----EEQLGN--VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*.
gi 14917115 313 QVQSLITNVESQLAEIRSDLERQNQE 338
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-359 |
2.99e-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: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 56 EKETMQFLNDRL--ASYLEKVRQLERDNAELENLIRERSQQQEpllcpsyqsyfkTIEELQQKIlctkSENARLVVQIdN 133
Cdd:TIGR02169 209 KAERYQALLKEKreYEGYELLKEKEALERQKEAIERQLASLEE------------ELEKLTEEI----SELEKRLEEI-E 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 134 AKLAADDFRTKYQTELSLRQL------VESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHE------QEVNTL 201
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVkekigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereiEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 202 RCQLGDRLNvevdaaptvDLNRVLNETRSQYEALVETNRReveqWFttqteelnkqvvsssEQLQSYQAEIIELRRTVNA 281
Cdd:TIGR02169 352 RDKLTEEYA---------ELKEELEDLRAELEEVDKEFAE----TR---------------DELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14917115 282 LEIELQAQHNLRDSLENTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSL 359
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-338 |
3.52e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 138 ADDFRTKYQTELS----LRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSN---HEQEVNTLRCQLGDRLN 210
Cdd:COG3883 14 ADPQIQAKQKELSelqaELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 211 VE-VDAAPTVDLNRVLNeTRSQYEALvetNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQ 289
Cdd:COG3883 94 ALyRSGGSVSYLDVLLG-SESFSDFL---DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14917115 290 hnlRDSLENTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQE 338
Cdd:COG3883 170 ---KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-350 |
4.65e-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: 48.91 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 71 LEKVRQLERDNAELENLIRERSQQQEPLL-----CPSYQSYFKTIEELQQKILctksenarlvvqidnaklaaddFRTKY 145
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRrerekAERYQALLKEKREYEGYEL----------------------LKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 146 QTELSLRQlVESDINGLRRILDELTLCKSDLEAQVESLKEEL----LCLKSNHEQEVNTLRCQLGDrlnVEVDAAPTVDL 221
Cdd:TIGR02169 234 ALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnKKIKDLGEEEQLRVKEKIGE---LEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 222 NRVLN-------ETRSQYEALVETNRREVEQwFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAqhnLRD 294
Cdd:TIGR02169 310 IAEKEreledaeERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE---TRD 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14917115 295 SLENTLTESEA----RYSSQ--LSQVQSLITNVESQLAEIRSDLER----QNQEYQVLLDVRARLE 350
Cdd:TIGR02169 386 ELKDYREKLEKlkreINELKreLDRLQEELQRLSEELADLNAAIAGieakINELEEEKEDKALEIK 451
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
56-361 |
4.89e-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: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 56 EKETMQFLNDRLASYLEKVRQLERDNAELEN----LIRERSQQQEPLlcPSYQSYFKTIEELQQKILCTKSEnARLVVQI 131
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKkhqqLCEEKNALQEQL--QAETELCAEAEEMRARLAARKQE-LEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 132 DNAKLAADDFRTkyQTELSLRQLVESDINGLRRILDE-------LTLCKSDLEAQVESLKEELLCLKsNHEQEVNTLRCQ 204
Cdd:pfam01576 80 LESRLEEEEERS--QQLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 205 LGDRLN-VEVDAAPTVDLNRVLNETRSQYEALV----------ETNRREVEQWfttqTEELNKQVVSSSEQLQSYQAEII 273
Cdd:pfam01576 157 LEERISeFTSNLAEEEEKAKSLSKLKNKHEAMIsdleerlkkeEKGRQELEKA----KRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 274 ELRRTVNALEIELQAqhnlrdsLENTLTESEARYSSQLSQVQSLitnvESQLAEIRSDLERQNQEYQVLLDVRARLECEI 353
Cdd:pfam01576 233 ELRAQLAKKEEELQA-------ALARLEEETAQKNNALKKIREL----EAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
....*...
gi 14917115 354 NTYRSLLE 361
Cdd:pfam01576 302 EALKTELE 309
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
67-350 |
5.91e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 67 LASYLEKVRQLERDNAELENLIRERSQQQEPL--LCPSYQSYFKTIEELQQKILCTKSENARLVVQIDNAKLAADDFRTK 144
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLdeLEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 145 YQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTL-RCQLGDRLNVEVDAAPTVDLNR 223
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAaAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 224 VLNETRSQYEALVETNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTES 303
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 14917115 304 EARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLE 350
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEA 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-377 |
7.49e-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: 48.51 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 72 EKVRQLERDNAEL---ENLIRERSQQQEPL-----LCPSYQSYFKTIEELQQKILCTKSEnaRLVVQIDNAKLAADDFRT 143
Cdd:TIGR02168 176 ETERKLERTRENLdrlEDILNELERQLKSLerqaeKAERYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 144 KYQTELSLRQLVESDINGLRRILDELtlcksdlEAQVESLKEELLclksNHEQEVNTLRCQLgdrlnvevdaaptvdlnR 223
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSEL-------EEEIEELQKELY----ALANEISRLEQQK-----------------Q 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 224 VLNETRSQyealVETNRREVEqwftTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTES 303
Cdd:TIGR02168 306 ILRERLAN----LERQLEELE----AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14917115 304 EAryssQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCNLPSNPCATTNA 377
Cdd:TIGR02168 378 EE----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-358 |
1.58e-05 |
|
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: 47.42 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 63 LNDRLASYLEKVRQLERDNAELENLiRERS--QQQEPLLCPSYQSYFKTIEELQQKILCTKSENARLV----VQIDN-AK 135
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKL-RSRVdlKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENmTQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 136 LAADDFRTKYQTELSLRQLvESDINGLRRILDELTLCKSDLEAQVESLKEELlclkSNHEQEVNTLRCQLGDRLNVEVDA 215
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLELEKVKLVNAGSERLRAVKDI 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 216 APTVDlnRVLNE---TRSQYEALVEtNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNL 292
Cdd:pfam15921 652 KQERD--QLLNEvktSRNELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14917115 293 RDSLENTLTESEARYSSQLSQVQSL---ITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS 358
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLeeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
58-338 |
2.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 58 ETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLLcpsyqsyfKTIEELQqkilcTKSENARLVVQidNAKLA 137
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR--------ERAAELE-----AEAEEKREAAA--EAEEE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 138 ADDFRTKYQTELSLRQLVESDINGLRRILDELTLcKSDLEAQVESLKEellclKSNHEQEVNTLRcqlGDRLnvevdaap 217
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLRE-----KREALAELNDER---RERL-------- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 218 tvdlnRVLNETRSQYEALVETNRREVEQWFTTQTEELNKQVvssSEQLQSYQAEIIELRRTVNALEIELQAQHNLRD--- 294
Cdd:PRK02224 630 -----AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEIGAVENELEELEELRErre 701
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 14917115 295 SLENTLTESEARYssqlSQVQSLitnvESQLAEIRSDLERQNQE 338
Cdd:PRK02224 702 ALENRVEALEALY----DEAEEL----ESMYGDLRAELRQRNVE 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
258-364 |
2.25e-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: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 258 VVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEAR----------YSSQLSQVQSLITNVESQLAE 327
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraLEQELAALEAELAELEKEIAE 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 14917115 328 IRSDLERQNQEYQVLLDVRARLEcEINTYRSLLESED 364
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLG-RQPPLALLLSPED 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
146-358 |
4.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 146 QTELSLRQLVES--DINGLRRILDeltlcksDLEAQVESLkEELLCLKSNHEQ---EVNTLRcQLGDRLNVEVDAAPTVD 220
Cdd:COG4913 222 DTFEAADALVEHfdDLERAHEALE-------DAREQIELL-EPIRELAERYAAareRLAELE-YLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 221 LNRVLNETRSQYEALvETNRREVEQwfttQTEELNKQVVSSSEQLQSYQAEIIE-LRRTVNALEIELQAQHNLRDSLENT 299
Cdd:COG4913 293 LEAELEELRAELARL-EAELERLEA----RLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14917115 300 LT-------ESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS 358
Cdd:COG4913 368 LAalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
74-298 |
4.34e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.01 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 74 VRQLERDNAELENLIRERSQQ---QEPLLcpsYQSYFKTIEELQQ----KILCTKSeNARLvvqidNAKLAADDFRTKYQ 146
Cdd:smart00787 72 CKELKKYISEGRDLFKEIEEEtliNNPPL---FKEYFSASPDVKLlmdkQFQLVKT-FARL-----EAKKMWYEWRMKLL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 147 TelSLRQLVESDINGLRRILDELTlcksDLEAQVESLKEELLCLKSNHEQEVNTLRcqlgdRLNVEVDAAPTVDLNRVLN 226
Cdd:smart00787 143 E--GLKEGLDENLEGLKEDYKLLM----KELELLNSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14917115 227 ETRSQYEALVEtNRREVEQwFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVN------ALEIE-LQAQHNLRDSLEN 298
Cdd:smart00787 212 KLKKLLQEIMI-KVKKLEE-LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEqcrgftFKEIEkLKEQLKLLQSLTG 288
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-362 |
7.87e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 227 ETRSQYEALvETNRREVEQW--------FTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELqAQHNLRdslEN 298
Cdd:TIGR02169 208 EKAERYQAL-LKEKREYEGYellkekeaLERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL-EELNKK---IK 282
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14917115 299 TLTESEARyssqlsQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLES 362
Cdd:TIGR02169 283 DLGEEEQL------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-342 |
8.09e-05 |
|
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: 45.11 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 70 YLEKVRQLERD----NAELENLIRERSQ--QQEPLLCPSYQSYFKTIEELQQKILCTKSENARL-------VVQIDNAKL 136
Cdd:pfam15921 340 YEDKIEELEKQlvlaNSELTEARTERDQfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnSITIDHLRR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 137 AADDFRTKYQTELSLRQLVESD-----------INGLRRILDELTLCKSDLEAQVESLK---EELLCLK---SNHEQEVN 199
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSEcqgqmerqmaaIQGKNESLEKVSSLTAQLESTKEMLRkvvEELTAKKmtlESSERTVS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 200 TLRCQLGDR------LNVEVDAAPT-VDLN-----------RVLNETRSQYEAL--VETNRREVEQWFTTQTEELNKQVV 259
Cdd:pfam15921 500 DLTASLQEKeraieaTNAEITKLRSrVDLKlqelqhlknegDHLRNVQTECEALklQMAEKDKVIEILRQQIENMTQLVG 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 260 SSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEARY--------------SSQLSQVQSLITNVESQL 325
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVsdlelekvklvnagSERLRAVKDIKQERDQLL 659
|
330 340
....*....|....*....|
gi 14917115 326 AEI---RSDLERQNQEYQVL 342
Cdd:pfam15921 660 NEVktsRNELNSLSEDYEVL 679
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-348 |
8.64e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 195 EQEVNTLRCQLgDRLNVEVDAaptvdLNRVLNETRSQYEALVEtnrrEVEQWfTTQTEELNKQVVSSSEQLQSYQAEIIE 274
Cdd:COG4372 44 QEELEQLREEL-EQAREELEQ-----LEEELEQARSELEQLEE----ELEEL-NEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14917115 275 LRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQSLitnvESQLAEIRSDLERQNQEYQVLLDVRAR 348
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL----EEQLESLQEELAALEQELQALSEAEAE 182
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
76-363 |
9.11e-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: 44.78 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 76 QLERDNAELENLIRERSQQQEPL--LCPSYQSYFKTIEELQQKILCTKSENARLVVQI-DNAKLAADDFRTKYQTELSLR 152
Cdd:pfam01576 413 QLQELQARLSESERQRAELAEKLskLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqDTQELLQEETRQKLNLSTRLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 153 QLvESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLRCQLGDRLNVEVDAAptvDLNRVLNETRSQY 232
Cdd:pfam01576 493 QL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELE---ALTQQLEEKAAAY 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 233 EALVETNRReVEQWFTTQTEEL--NKQVVSSSEQLQS----------------------YQAEIIELRRTVNALEIELQA 288
Cdd:pfam01576 569 DKLEKTKNR-LQQELDDLLVDLdhQRQLVSNLEKKQKkfdqmlaeekaisaryaeerdrAEAEAREKETRALSLARALEE 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 289 QHNLRDSLENTLTESEARYSSQLSQVQSLITNV----------ESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS 358
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhelerskralEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKA 727
|
....*
gi 14917115 359 LLESE 363
Cdd:pfam01576 728 QFERD 732
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
61-360 |
1.15e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 61 QFLNDRLASYLEkvRQLERDNAELENLIRERSQQQEPLLCPSYQSYFKTIEELQQKILCTK-SENARLVVQID-NAKLAA 138
Cdd:COG5185 211 ETGNLGSESTLL--EKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKlGENAESSKRLNeNANNLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 139 DDFRtkyQTELSLRQLVES-DINGLRRILDELtLCKSDLEAQVESLKEE----LLCLKSNHEQEVNTLRCQLgDRLNVEV 213
Cdd:COG5185 289 KQFE---NTKEKIAEYTKSiDIKKATESLEEQ-LAAAEAEQELEESKREtetgIQNLTAEIEQGQESLTENL-EAIKEEI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 214 DAAPTVDLNRVLNETRSQYEALVETNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLR 293
Cdd:COG5185 364 ENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14917115 294 DSLENTLTESEARYSSQLSQVQS-----LITNVESQLAEIRSDLERQNQEYQVLLD----VRARLECEINTYRSLL 360
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEeaydeINRSVRSKKEDLNEELTQIESRVSTLKAtlekLRAKLERQLEGVRSKL 519
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
166-333 |
1.41e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.25 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 166 LDELTLCKSDLEAQVESLKEELlclKSNHEQEVNTLRCQLGDRLN-VEVDAAPTVD-LNRVLNETRSQYEALVETNRREV 243
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQEL---VDRLEKETEALRERLQKDLEeVRAKLEPYLEeLQAKLGQNVEELRQRLEPYTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 244 EQWFTTQTEELNKQVVSSSEQLQSYQAEIIE-LRRTVNALEIELQA---QH--NLRDSLENTLTESEARYSSQLSQVQsl 317
Cdd:pfam01442 83 RKRLNADAEELQEKLAPYGEELRERLEQNVDaLRARLAPYAEELRQklaERleELKESLAPYAEEVQAQLSQRLQELR-- 160
|
170
....*....|....*.
gi 14917115 318 iTNVESQLAEIRSDLE 333
Cdd:pfam01442 161 -EKLEPQAEDLREKLD 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
71-363 |
2.48e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 71 LEKV-RQLERDNAELENLIRERSQQQEPLLcpsyQSYFKTIEELQQKILCTKSENARlvvqidnaklaaddfrtKYQTEL 149
Cdd:pfam01576 206 LEKAkRKLEGESTDLQEQIAELQAQIAELR----AQLAKKEEELQAALARLEEETAQ-----------------KNNALK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 150 SLRQLvESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLRCQLGDRLNVEVDAAptvDLNRVLNETR 229
Cdd:pfam01576 265 KIREL-EAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVT---ELKKALEEET 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 230 SQYEALVETNRREVEQWFTTQTEEL-----NKQVVSSSEQ---------------LQSYQAEIIELRRTVNALEIELQAQ 289
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLeqakrNKANLEKAKQalesenaelqaelrtLQQAKQDSEHKRKKLEGQLQELQAR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 290 HNLRDSLENTLTESEARYSSQLSQVQSLITNVESQ---LAEIRSDLERQNQEYQVLLDVRAR-----------LECEINT 355
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKnikLSKDVSSLESQLQDTQELLQEETRqklnlstrlrqLEDERNS 500
|
....*...
gi 14917115 356 YRSLLESE 363
Cdd:pfam01576 501 LQEQLEEE 508
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-364 |
2.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 263 EQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESE---ARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEY 339
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100
....*....|....*....|....*
gi 14917115 340 QVLLDVRARLECEINTYRSLLESED 364
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAERE 149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
51-339 |
3.72e-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: 42.75 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 51 SFNGSEKETMQFLNDR-------LASYLEKVRQLERDNAEL-------ENLIRERSQQQEPLLcpSYQSYFKT------- 109
Cdd:TIGR02169 667 LFSRSEPAELQRLRERleglkreLSSLQSELRRIENRLDELsqelsdaSRKIGEIEKEIEQLE--QEEEKLKErleelee 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 110 -IEELQQKILCTKSENARLVVQIDNAKLAAddfrTKYQTELS--LRQLVESDINGLRRILDELTLCKSDLEAQVESLKEE 186
Cdd:TIGR02169 745 dLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 187 L---LCLKSNHEQEVNTLRcqlgdrlnvevdaaptvdlnrvlnetrsQYEALVETNRREVEQwfttQTEELNKQVVSSSE 263
Cdd:TIGR02169 821 LnrlTLEKEYLEKEIQELQ----------------------------EQRIDLKEQIKSIEK----EIENLNGKKEELEE 868
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14917115 264 QLQSYQAEIIELRRTVNALEIElqaqhnlRDSLENTLTESEARYSSQLSQVQSLITNVeSQLAEIRSDLERQNQEY 339
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKE-------RDELEAQLRELERKIEELEAQIEKKRKRL-SELKAKLEALEEELSEI 936
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-363 |
7.10e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 55 SEKETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLLcpsyqsyfKTIEELQQKILCTKS--ENARLVVQId 132
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK--------KEIEELEEKVKELKElkEKAEEYIKL- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 133 nAKLAADDFRTKYQTELSLRQLvESDINGLRRILDELTLCKS---DLEAQVESLKEELLCLKSNHE--QEVNTLRCQLgD 207
Cdd:PRK03918 299 -SEFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAKKEEL-E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 208 RLNVEVDAAPTVDLNRVLNETRSQYEAL------VETNRREVEQwfttQTEELNKQVVS-------------------SS 262
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIeeeiskITARIGELKK----EIKELKKAIEElkkakgkcpvcgrelteehRK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 263 EQLQSYQAEIIELRRTVNAL-EIELQAQHNLRDsLENTLteSEARYSSQLSQVQSLITNVESQLAEIR-SDLERQNQEYQ 340
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIeEKERKLRKELRE-LEKVL--KKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYE 528
|
330 340
....*....|....*....|...
gi 14917115 341 VLLDVRARLECEINTYRSLLESE 363
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKL 551
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
221-332 |
8.47e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 221 LNRVLNETRSQYEALvETNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAE---IIELRRTvnaleiELQAQHNLRDSLE 297
Cdd:pfam15921 76 IERVLEEYSHQVKDL-QRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR------ESQSQEDLRNQLQ 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 14917115 298 NTLTESEA----------RYSSQLSQVQSLITNVESQLAEIRSDL 332
Cdd:pfam15921 149 NTVHELEAakclkedmleDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-358 |
8.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 61 QFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPL----------LCPSYQSYFKTIEELQQKILCTKSENARLVVQ 130
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 131 ID---NAKLAADDFRTKYQTE---------LSLRQLVESDINGLRRILDELTLC--------------KSDLEAQVESLk 184
Cdd:COG4717 229 LEqleNELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVlgllallflllareKASLGKEAEEL- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 185 EELLCLKSNHEQEVNTLRCQLGdrLNVEVDAAPTVDLNRVLNETRSQYEALVETNRR-EVEQWFTTQTEELNKQVVSSSE 263
Cdd:COG4717 308 QALPALEELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 264 QLQS---YQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEaryssqlsqvqslitnVESQLAEIRSDLERQNQEYQ 340
Cdd:COG4717 386 ELRAaleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE----------------LEEELEELEEELEELEEELE 449
|
330
....*....|....*...
gi 14917115 341 VLLDVRARLECEINTYRS 358
Cdd:COG4717 450 ELREELAELEAELEQLEE 467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-361 |
9.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 177 EAQVESLKEELLCLksnhEQEVNTLRCQLgDRLNVEVDAaptvdlnrvLNETRSQYEALVETNRREVEqWFTTQTE--EL 254
Cdd:COG4913 609 RAKLAALEAELAEL----EEELAEAEERL-EALEAELDA---------LQERREALQRLAEYSWDEID-VASAEREiaEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 255 NKQVvsssEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEarysSQLSQVQSLITNVESQLAEI------ 328
Cdd:COG4913 674 EAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAedlarl 745
|
170 180 190
....*....|....*....|....*....|....*...
gi 14917115 329 --RSDLE---RQNQEYQVLLDVRARLECEINTYRSLLE 361
Cdd:COG4913 746 elRALLEerfAAALGDAVERELRENLEERIDALRARLN 783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-335 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 104 QSYFKTIEELQQKIlctksENARLvvQID---NAKLAADDFRTKYQTELSLRQLVE-SDINGLRRILDELTLCKSDLEAQ 179
Cdd:COG4913 231 VEHFDDLERAHEAL-----EDARE--QIEllePIRELAERYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 180 VESLKEELLCLKS---NHEQEVNTLRCQL----GDRLNV---EVDAApTVDLNRVlNETRSQYEALVetnrREVEQWFTT 249
Cdd:COG4913 304 LARLEAELERLEArldALREELDELEAQIrgngGDRLEQlerEIERL-ERELEER-ERRRARLEALL----AALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 250 QTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEARyssqlsqvqslITNVESQLAEIR 329
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR-----------KSNIPARLLALR 446
|
....*.
gi 14917115 330 SDLERQ 335
Cdd:COG4913 447 DALAEA 452
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
128-279 |
1.77e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.10 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 128 VVQIDNAKLAADDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLrcqlgd 207
Cdd:pfam00529 60 LDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 208 rlnvEVDAAP---TVDLNRVLNETRSQYEALV---ETNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEII----ELRR 277
Cdd:pfam00529 134 ----PIGGISresLVTAGALVAQAQANLLATVaqlDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKlaklDLER 209
|
..
gi 14917115 278 TV 279
Cdd:pfam00529 210 TE 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-361 |
3.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 136 LAADDFRTKYQTELslrQLVESDINGLRRILDELTLCKSDLEAQVESLKEELlclkSNHEQEVNTLRCQLGDrlnvevda 215
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAA-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 216 aptvdLNRVLNETRSQYEALvetnRREVEQwfttQTEELNKQVVSSSEQLQSYQAEII-------ELRRTVNALEIELQA 288
Cdd:COG4942 81 -----LEAELAELEKEIAEL----RAELEA----QKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14917115 289 QHNLRDSLENTLTESEARYSSQLSQVQSLiTNVESQLAEIRSDLERQNQEYQVLLdvrARLECEINTYRSLLE 361
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAEL-EALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
57-291 |
3.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 57 KETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLLcpsyqsyfKTIEELQQKIlctKSENARLVVQIDN-AK 135
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEI---AELRAELEAQKEElAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 136 LAADDFRTKYQTELSLRqLVESDINGLRRILDELTLCKSDLEAQVESLKEELlclksnheQEVNTLRCQLGDRLNvevda 215
Cdd:COG4942 109 LLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARREQAEELRADL--------AELAALRAELEAERA----- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14917115 216 aptvDLNRVLNETRSQYEALvETNRREVEQwfttQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHN 291
Cdd:COG4942 175 ----ELEALLAELEEERAAL-EALKAERQK----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
56-366 |
3.13e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 56 EKETMQFLNDRLASYLEKVRQLERDNAELENLIRERsqqQEPLLCPSYQS--YFKTIEELQQKILcTKSENARlvVQIDN 133
Cdd:COG5185 227 EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQN---TDLRLEKLGENaeSSKRLNENANNLI-KQFENTK--EKIAE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 134 AKLAADDFRTKYQTELSLRQLVESD--INGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLRCQLGDR--- 208
Cdd:COG5185 301 YTKSIDIKKATESLEEQLAAAEAEQelEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEeld 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 209 -LNVEVDAAPTVDLNRVLNETRSQYEAL--VETNRREVEQwfttQTEELNKQVVSSSEQLQSYQAEIIEL-----RRTVN 280
Cdd:COG5185 381 sFKDTIESTKESLDEIPQNQRGYAQEILatLEDTLKAADR----QIEELQRQIEQATSSNEEVSKLLNELiselnKVMRE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 281 ALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS-- 358
Cdd:COG5185 457 ADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGya 536
|
....*....
gi 14917115 359 -LLESEDCN 366
Cdd:COG5185 537 hILALENLI 545
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
78-362 |
3.54e-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: 39.77 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 78 ERDNAELENLIRERSQQQEPLLCPSYQSYFKTIEELQQkilctksenarlvvQIDNAKlaaddfRTKYQTELSlRQLVES 157
Cdd:pfam01576 326 EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTE--------------QLEQAK------RNKANLEKA-KQALES 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 158 DINGLRRILDELTLCKSDLEAQVESLKEELlclksnheQEVNtLRCQLGDRLNVEvdaaptvdLNRVLNETRSQYEAlVE 237
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQL--------QELQ-ARLSESERQRAE--------LAEKLSKLQSELES-VS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 238 TNRREVEqwftTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQSL 317
Cdd:pfam01576 447 SLLNEAE----GKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 14917115 318 itnvESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLES 362
Cdd:pfam01576 523 ----QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
58-242 |
4.26e-03 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 39.26 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 58 ETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQ----------QEPLLcPSYQSyfKTIEELQQKIlctksenARL 127
Cdd:TIGR03007 190 ENGGILPDQEGDYYSEISEAQEELEAARLELNEAIAQrdalkrqlggEEPVL-LAGSS--VANSELDGRI-------EAL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 128 VVQIDNAKLAADD-----FRTKYQTElSLRQLVESDI------NGLRRILD----ELTLCKSDLEAQVESLKEELLCLKS 192
Cdd:TIGR03007 260 EKQLDALRLRYTDkhpdvIATKREIA-QLEEQKEEEGsaknggPERGEIANpvyqQLQIELAEAEAEIASLEARVAELTA 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14917115 193 NHEQEVNTLRcqlgdrlNVEVDAAPTVDLNRVLNETRSQYEALVEtnRRE 242
Cdd:TIGR03007 339 RIERLESLLR-------TIPEVEAELTQLNRDYEVNKSNYEQLLT--RRE 379
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
55-338 |
5.40e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.35 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 55 SEKETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLlcpsyqsyFKTIEELQQKILCTKSENARLVVQIDNA 134
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDEL--------NAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 135 KLAADDFRTKyqtelsLRQLVEsDINGLRRILDELTLCKSDLEA---QVESLKEELLC--LKSNHEQE-VNTLRcQLGDR 208
Cdd:COG1340 77 KEERDELNEK------LNELRE-ELDELRKELAELNKAGGSIDKlrkEIERLEWRQQTevLSPEEEKElVEKIK-ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 209 LNvevDAAPTVDLNRVLNETRSQYEALVEtnrreveqwfttQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQA 288
Cdd:COG1340 149 LE---KAKKALEKNEKLKELRAELKELRK------------EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 14917115 289 QHNLRDSLE---NTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQE 338
Cdd:COG1340 214 LHKEIVEAQekaDELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
113-360 |
6.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 113 LQQKILCTKSENARLVVQIDNAKlaaDDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCL-- 190
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ---QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLvm 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 191 ----KSNHEQEVNTLRCQLG---DRLNVEV------DAAPTVdlnrvlNETRSQYEALVETNRREVEQwFTTQTEELNKQ 257
Cdd:PHA02562 249 diedPSAALNKLNTAAAKIKskiEQFQKVIkmyekgGVCPTC------TQQISEGPDRITKIKDKLKE-LQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 258 VvsssEQLQSYQAEIIELRRTVNALEIELqaqhnlrdsleNTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQ 337
Cdd:PHA02562 322 I----DELEEIMDEFNEQSKKLLELKNKI-----------STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
250 260
....*....|....*....|....*.
gi 14917115 338 EYQVLLDVRARLECEINTY---RSLL 360
Cdd:PHA02562 387 ELDKIVKTKSELVKEKYHRgivTDLL 412
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
257-381 |
6.97e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 38.63 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 257 QVVSSSEQLQSYQAEIIELRRTVNAL-EIELQ----------AQHNLRDSLENTLTESEARYSSQ----------LSQVQ 315
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNALpAITLTltadevaaalAQHAEQRPLRQRLVALHGQIVPQqkrlaqlqvaIQNVT 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14917115 316 SLITNVESQLAEIRSDLERQNQEYqvlLDVRARLECE-----INTYRSLLEsedcnlPSNPCATTNACSKP 381
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQL---ADVKTICEQEarikdLEAQRAQLQ------AGQPCPLCGSTSHP 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
63-217 |
8.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 63 LNDRLASYLEKVRQLERDNAELENLIRERSQQQEpllcpsyQSYFKTIEELQQKI------LCTKSEN-ARLVVQIDNAK 135
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIR-------GNGGDRLEQLEREIerlereLEERERRrARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 136 LA----ADDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCL---KSNHEQEVNTLRCQLGDR 208
Cdd:COG4913 373 LPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLerrKSNIPARLLALRDALAEA 452
|
....*....
gi 14917115 209 LNVEVDAAP 217
Cdd:COG4913 453 LGLDEAELP 461
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
108-365 |
9.66e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 38.30 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 108 KTIEELQQKIlcTKSENARLVVQIDNAKLAADDFRTK----Y---QTELSLRQLVESDINGLRRILDELtlcksdlEAQV 180
Cdd:pfam06160 237 KEIQQLEEQL--EENLALLENLELDEAEEALEEIEERidqlYdllEKEVDAKKYVEKNLPEIEDYLEHA-------EEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 181 ESLKEELLCLKSN---HEQEVNTLRcQLGDRLNvEVDAAPTVDLNRVLNE--TRSQYEALVETNRREVEQwFTTQTEELN 255
Cdd:pfam06160 308 KELKEELERVQQSytlNENELERVR-GLEKQLE-ELEKRYDEIVERLEEKevAYSELQEELEEILEQLEE-IEEEQEEFK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14917115 256 KQVVSSS-------EQLQSYQAEIIELRRTVnaleielqAQHNL---RDSLENTLTESEARYSS---QLSQVQSLITNVE 322
Cdd:pfam06160 385 ESLQSLRkdelearEKLDEFKLELREIKRLV--------EKSNLpglPESYLDYFFDVSDEIEDladELNEVPLNMDEVN 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 14917115 323 SQLAEIRSDLERQNQEYQVLLDVrARL-ECEI---NTYRS--------LLESEDC 365
Cdd:pfam06160 457 RLLDEAQDDVDTLYEKTEELIDN-ATLaEQLIqyaNRYRSsnpevaeaLTEAELL 510
|
|
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