|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
88-399 |
6.37e-118 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 346.52 E-value: 6.37e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 88 NEKETMQFLNDRLASYLEKVRSLEETNAELESRIQEQCEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRLAVQLDNC 167
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 168 KLATDDFKSKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHEEEVNLLREQLGD-RLSVEL 246
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 247 DTAPTLDLNRVLDEMRCQCETVLANNRREAEEWLAVQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLT 326
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939191766 327 ESLECTVAETEAQYSSQLAQIQCLIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEINTYWGLLDSEDSR 399
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-384 |
1.41e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 110 LEETNAELESRIQEQcEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRLAVQLDNCKLATDDFKSKYESELSLRQLLE 189
Cdd:TIGR02168 682 LEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 190 ADISSLHGILEELTLCKSDLEAHVESLKEDLlclkKNHEEEVNLLREQLgDRLSVELDtaptlDLNRVLDEMRcqceTVL 269
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREAL-DELRAELT-----LLNEEAANLR----ERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 270 ANNRREAEEWlAVQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLECTVAETEAQYSSQLAQIQc 349
Cdd:TIGR02168 827 ESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR- 904
|
250 260 270
....*....|....*....|....*....|....*
gi 1939191766 350 lidNLENQLAEIRCDLERQNQEyqvLLDVKARLEG 384
Cdd:TIGR02168 905 ---ELESKRSELRRELEELREK---LAQLELRLEG 933
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
143-368 |
1.41e-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: 56.31 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 143 IEDLQQKIlctKAENSRLAVQldncklatddfKSKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLC 222
Cdd:COG4942 29 LEQLQQEI---AELEKELAAL-----------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 223 LKKNHEEEVNLLREQLG--------DRLSVELDTAPTLDLNRVLDEMRcqcetVLANNRREAEEWLAVQTEELNQQQLSS 294
Cdd:COG4942 95 LRAELEAQKEELAELLRalyrlgrqPPLALLLSPEDFLDAVRRLQYLK-----YLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939191766 295 AEQLQGCQMEILELKRTASALEIELQAQQSLTESLEctvaETEAQYSSQLAQIQCLIDNLENQLAEIRCDLERQ 368
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-361 |
6.14e-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: 55.06 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 87 SNEKETMQFLNDRLASYLEKVRSLEETNAELESRIQEQcEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRLAVQLDN 166
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL-EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 167 CKLATDDFKSKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHEEevnlLREQLgDRLSVEL 246
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----LESEL-EALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 247 DTAPTlDLNRVLDEMRCQCETV--LANNRREAEEwlavQTEELNQQQLSSAEQLQGCQMEILELKRTASAL-EIELQAQQ 323
Cdd:TIGR02168 883 ASLEE-ALALLRSELEELSEELreLESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAE 957
|
250 260 270
....*....|....*....|....*....|....*...
gi 1939191766 324 SLTESLECTVAETEAQyssqlaqiqclIDNLENQLAEI 361
Cdd:TIGR02168 958 ALENKIEDDEEEARRR-----------LKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-400 |
1.77e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 199 LEELTLCKSDLEAHVESLKEDLLCLKKNHEEevnlLREQLGDRLSVELDtaptldLNRVLDEMRCQCETVLANNRREAEE 278
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEE------LSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 279 W--LAVQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLECTVAETEAQYSSQ---LAQIQCLIDN 353
Cdd:TIGR02168 749 IaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLES 828
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1939191766 354 LENQLAEIRCDLERQNQEYQVLLDVKARLEGEINTYWGLLDSEDSRL 400
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-386 |
1.01e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 177 KYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHEEEVNLLREQLGDRLSVELDTAPTLDLNR 256
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 257 VLDEMRCQCETVLANNRREAEEwLAVQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLectvAET 336
Cdd:COG1196 313 ELEERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL----AEE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1939191766 337 EAQYSSQLAQIQCLIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEI 386
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-385 |
2.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 96 LNDRLASYLEKVRSLEETNAELESRIQEQcEQDIpmvcpdyQRYFNTIEDLQQKILCTKAENSRLAVQLDNCKLATDDFK 175
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEEL-RLEL-------EELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 176 SKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHEEEVNLLREQLGDRLSveldtaptlDLN 255
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE---------LAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 256 RVLDEMRcqcetvLANNRREAEEWLAVQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLEctvaE 335
Cdd:COG1196 387 ELLEALR------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE----E 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1939191766 336 TEAQYSSQLAQIQCLIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGE 385
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-371 |
6.48e-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: 48.53 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 99 RLASYLEKVRSLEETNAELES--RIQEQCEQDIPMVCPDYQRYFNTIEDLQQKIlctKAENSRLAVQldncklatddFKS 176
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASleEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLR----------VKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 177 KYESelslrqlLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHE------EEVNLLREQLGDRLSveldtap 250
Cdd:TIGR02169 295 KIGE-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereiEEERKRRDKLTEEYA------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 251 tlDLNRVLDEMRCQCETVLANNRREAEEWLAVQTE---------ELNQQQLSSAEQLQGCQMEILELKRTASALEIELQA 321
Cdd:TIGR02169 361 --ELKEELEDLRAELEEVDKEFAETRDELKDYREKleklkreinELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1939191766 322 QQSLTESLECTVAETEaqysSQLAQIQCLIDNLENQLAEIRCDLERQNQE 371
Cdd:TIGR02169 439 LEEEKEDKALEIKKQE----WKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
85-383 |
7.32e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 85 FTSNEKETMQFLNDRLA-SYLEkvRSLEETNAELESR---IQEQceqdipmvcpdyqryfntIEDLQQKIlcTKAENsrl 160
Cdd:COG3206 142 YTSPDPELAAAVANALAeAYLE--QNLELRREEARKAlefLEEQ------------------LPELRKEL--EEAEA--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 161 avqldncKLAtdDFKSKYESeLSLRQLLEADISSLhgileeltlckSDLEAHVESLKEDLlclkknheEEVNLLREQLGD 240
Cdd:COG3206 197 -------ALE--EFRQKNGL-VDLSEEAKLLLQQL-----------SELESQLAEARAEL--------AEAEARLAALRA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 241 RLSVELDTAPTLDLNRVLDEMRCQcetvLANNRREAEEWLAVQTE------ELNQQQLSSAEQLQGcqmeilELKRTASA 314
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRAQ----LAELEAELAELSARYTPnhpdviALRAQIAALRAQLQQ------EAQRILAS 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939191766 315 LEIELQAQQSLTESLEctvaETEAQYSSQLAQIQclidNLENQLAEIRCDLERQNQEYQVLLdvkARLE 383
Cdd:COG3206 318 LEAELEALQAREASLQ----AQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLL---QRLE 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-383 |
9.32e-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: 48.14 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 84 VFTSNEKETMQFLNDRLASyLEKVRS-LEETNAELESRIQEqceqdipmvcpdyqrYFNTIEDLQQKILCTKAENSRLAv 162
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEG-LKRELSsLQSELRRIENRLDE---------------LSQELSDASRKIGEIEKEIEQLE- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 163 qldncklatddfksKYESELSLRQL-LEADISSLHGILEELTLCKSDLEAHVESLKEDLlclkKNHEEEVNLLREQLGDR 241
Cdd:TIGR02169 730 --------------QEEEKLKERLEeLEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHS 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 242 LSVELDtaptlDLNRVLDEMRCQCETVLannrREAEEWLavQTEELNQQQLSSAeqLQGCQMEILELKRTASALEIELQA 321
Cdd:TIGR02169 792 RIPEIQ-----AELSKLEEEVSRIEARL----REIEQKL--NRLTLEKEYLEKE--IQELQEQRIDLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939191766 322 QQSLTESLECTVAETEA---QYSSQLAQIQCLIDNLENQLAEIRCDLERQNQEYQ----VLLDVKARLE 383
Cdd:TIGR02169 859 LNGKKEELEEELEELEAalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEkkrkRLSELKAKLE 927
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-385 |
1.55e-05 |
|
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: 47.36 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 110 LEETNAELESrIQEQCEQDIpmvcpDYQRYFNTIEDLQQKILCTKAEnsRLAVQLDNCKLATDDFKSKYESelslrqlLE 189
Cdd:TIGR02168 195 LNELERQLKS-LERQAEKAE-----RYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEE-------LT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 190 ADISSLHGILEELTLCKSDLEAHVESLKEDLLclkkNHEEEVNLLREQLGdRLSVELDtaptlDLNRVLDEMRCQCETvL 269
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQ-ILRERLA-----NLERQLEELEAQLEE-L 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 270 ANNRREAEEWLA---VQTEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLECTVAETEAQYSSQLAQ 346
Cdd:TIGR02168 329 ESKLDELAEELAeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270
....*....|....*....|....*....|....*....
gi 1939191766 347 IQCLIDNLENQLAEIRcDLERQNQEYQvLLDVKARLEGE 385
Cdd:TIGR02168 409 LERLEDRRERLQQEIE-ELLKKLEEAE-LKELQAELEEL 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-362 |
2.05e-05 |
|
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: 46.97 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 93 MQFLNDRLASYLEKVRSLEETNAELESRIQEqCEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRLAVQLDNCKLATD 172
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 173 DFKSKYESelslrqlLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLKKNHEEEVNLLREQLgdRLSVELDTApTL 252
Cdd:TIGR02168 313 NLERQLEE-------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE--SRLEELEEQ-LE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 253 DLNRVLDEMRCQcETVLANNRREAE---EWLAVQTEELNQQQLSSAEQLQ-----GCQMEILELKRTASALEIELQAQQS 324
Cdd:TIGR02168 383 TLRSKVAQLELQ-IASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1939191766 325 LTESLECTVAETEA---QYSSQLAQIQCLIDNLENQLAEIR 362
Cdd:TIGR02168 462 ALEELREELEEAEQaldAAERELAQLQARLDSLERLQENLE 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-398 |
6.07e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 288 NQQQLSSA-EQLQGCQMEILELKRTASALEIELQAQQSLTESLECTVAETEAqyssQLAQIQCLIDNLENQLAEIRCDLE 366
Cdd:COG4942 25 AEAELEQLqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELE 100
|
90 100 110
....*....|....*....|....*....|..
gi 1939191766 367 RQNQEYQVLLDVKARLeGEINTYWGLLDSEDS 398
Cdd:COG4942 101 AQKEELAELLRALYRL-GRQPPLALLLSPEDF 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-386 |
4.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 90 KETMQFLNDRLASYLEKVRSLEETNAELESRIQEQCEQdipmvcpdyqryfntIEDLQQKI-----LCTKAEN-SRLAVQ 163
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE---------------IEELEEKVkelkeLKEKAEEyIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 164 LDNCKLATDDFK---SKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDLLCLkknheEEVNLLREQLgD 240
Cdd:PRK03918 302 YEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-----EEAKAKKEEL-E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 241 RLSVELDTAPTLDLNRVLDEMRCQCETVlannrREAEEWLAVQTEELNQQ--QLSSA-EQLQG-------CQMEI----- 305
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEikELKKAiEELKKakgkcpvCGRELteehr 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 306 --------LELKRTASAL-EIELQAQQSLTESLECTVAETEAQYSSQLAQIQCLIDNLENQLAEIRC-DLERQNQEYQVL 375
Cdd:PRK03918 451 kelleeytAELKRIEKELkEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLeELEKKAEEYEKL 530
|
330
....*....|.
gi 1939191766 376 LDVKARLEGEI 386
Cdd:PRK03918 531 KEKLIKLKGEI 541
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
88-362 |
8.71e-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: 41.54 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 88 NEKET-MQFLNDRLASYLEKVRSLEETNAELESRIQEQ------CEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRL 160
Cdd:TIGR04523 366 EEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 161 AVQLDNCKLATDDFKSKYESELSLRQLLEADISSLHGILE--------------ELTLCKSDLEAHVESLKEDLLCLKKN 226
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkskekelkKLNEEKKELEEKVKDLTKKISSLKEK 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 227 hEEEVNLLREQLGDRLSveldtaptlDLNRVLDEM-----RCQCETVLANNRREAEEWLAVQTE-ELNQQQLSsaEQLQG 300
Cdd:TIGR04523 526 -IEKLESEKKEKESKIS---------DLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSlKKKQEEKQ--ELIDQ 593
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939191766 301 CQMEILELKrtaSALEIELQAQQSLTESLECTVAETEaQYSSQLAQIQCLIDNLENQLAEIR 362
Cdd:TIGR04523 594 KEKEKKDLI---KEIEEKEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
274-386 |
9.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 274 REAEEWLAVQTEELnQQQLSSAEQlqgcqmEILELKRTASALEIELQAQQSLTESlectvaeteAQYSSQLAQIQCLIDN 353
Cdd:COG3206 174 RKALEFLEEQLPEL-RKELEEAEA------ALEEFRQKNGLVDLSEEAKLLLQQL---------SELESQLAEARAELAE 237
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1939191766 354 LENQLAEIRCDLER---------QNQEYQVLLDVKARLEGEI 386
Cdd:COG3206 238 AEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAEL 279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-389 |
1.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 198 ILEEltlckSDLEAHVESLKEDLLCLKKNHE------EEVNLLR---------EQLGDRLSV---ELDTAPTLDLNRVLD 259
Cdd:COG4913 217 MLEE-----PDTFEAADALVEHFDDLERAHEaledarEQIELLEpirelaeryAAARERLAEleyLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 260 EMrcqcETVLANNRREAEEwLAVQTEELNQQQLSSAEQLQGCQMEIL--------ELKRTASALEIEL-------QAQQS 324
Cdd:COG4913 292 LL----EAELEELRAELAR-LEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELeererrrARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939191766 325 LTESLECTVAETEAQYSSQLAQIQ-------CLIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEINTY 389
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAallealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
98-388 |
2.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 98 DRLASYLEKVRSLEETNAELESRIQEQCEQDIPMVCPDYQRYFNTIEDLQQKILCTKAENSRLAVQLDNCKLATDDFKSK 177
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 178 YESELSLRQLLEAD--------------------------------ISSLHGILEELTLCKSDLEAHVESLKEDLLCLKK 225
Cdd:COG4717 236 LEAAALEERLKEARlllliaaallallglggsllsliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 226 NHEEEVNLLREQLGdrLSVELDTAPTLDLNRVLDEMRCQCETVL-ANNRREAEEWLAVQTEELNQQQLSSAEQLQgcqmE 304
Cdd:COG4717 316 LEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEeLEEELQLEELEQEIAALLAEAGVEDEEELR----A 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 305 ILELKRTASALEIEL-QAQQSLTESLECTVAETEAQYSsqlaqiqcliDNLENQLAEIRCDLERQNQEYQVLLDVKARLE 383
Cdd:COG4717 390 ALEQAEEYQELKEELeELEEQLEELLGELEELLEALDE----------EELEEELEELEEELEELEEELEELREELAELE 459
|
....*
gi 1939191766 384 GEINT 388
Cdd:COG4717 460 AELEQ 464
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-284 |
3.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 135 DYQRYFNTIEDLQQKILCTKAENSRLAVqLDNCKLATDD-------FKSKYESELSLRQLLEADISSLHGILEEL--TLC 205
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEelraaleQAEEYQELKEELEELEEQLEELLGELEELleALD 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939191766 206 KSDLEAHVESLKEDLlclkKNHEEEVNLLREQLGdRLSVELDTaptLDLNRVLDEMRCQCETVLANNRREAEEWLAVQT 284
Cdd:COG4717 427 EEELEEELEELEEEL----EELEEELEELREELA-ELEAELEQ---LEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-387 |
3.24e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 253 DLNRVLD---EMRCQCETvLANNRREAEEWLAVQTE-ELNQQQLSSAEqlqgcqmeILELKRTASALEIELQAQQSLTES 328
Cdd:COG1196 187 NLERLEDilgELERQLEP-LERQAEKAERYRELKEElKELEAELLLLK--------LRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939191766 329 LECTVAETEAQyssqlaqiqclIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEIN 387
Cdd:COG1196 258 LEAELAELEAE-----------LEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
254-360 |
3.33e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 37.68 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 254 LNRVLDEMrcqcETVLANNRREAEEWLAvQTEELNQQ---QLSSAEQ-----LQGCQMEILELKRTASAleielQAQQSL 325
Cdd:PRK07353 30 VGKVVEER----EDYIRTNRAEAKERLA-EAEKLEAQyeqQLASARKqaqavIAEAEAEADKLAAEALA-----EAQAEA 99
|
90 100 110
....*....|....*....|....*....|....*
gi 1939191766 326 TESLECTVAETEAQYSSQLAQIQCLIDNLENQLAE 360
Cdd:PRK07353 100 QASKEKARREIEQQKQAALAQLEQQVDALSRQILE 134
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
206-329 |
3.65e-03 |
|
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: 39.23 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 206 KSDLEAHVESLKEDLLCLKKnHEEEVNLLREQLGDR-------------LSVELDTAPTLDLNRVLDEMRCQCETVLANN 272
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMK-ELELLNSIKPKLRDRkdaleeelrqlkqLEDELEDCDPTELDRAKEKLKKLLQEIMIKV 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939191766 273 RREAEewLAVQTEELNQQQLSSAEQLQGCQMEILELKRTA------SALEIE-LQAQQSLTESL 329
Cdd:smart00787 225 KKLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEKKLeqcrgfTFKEIEkLKEQLKLLQSL 286
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
289-362 |
3.79e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.45 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 289 QQQLSSAEQ-LQGCQMEILELKRTASAL--EIELQAQQSLTESLECTVAETEAQY----------SSQLAQIQCLIDNLE 355
Cdd:COG3524 183 EEEVERAEErLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAELEAELaalrsylspnSPQVRQLRRRIAALE 262
|
....*..
gi 1939191766 356 NQLAEIR 362
Cdd:COG3524 263 KQIAAER 269
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
84-389 |
3.83e-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: 39.56 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 84 VFTSNEKE--TMQFLNDRLASYLEKVRSLEET----NAELESRIQEQCEQDIPMvcpdyqryfntIEDLQQKILCTKAEN 157
Cdd:COG5185 237 GFQDPESEleDLAQTSDKLEKLVEQNTDLRLEklgeNAESSKRLNENANNLIKQ-----------FENTKEKIAEYTKSI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 158 SRLAVQLDncklaTDDFKSKYESELSLRQLLEADISSLHGILEELTLCKSDLEAHVESLKEDllclKKNHEEEVNL-LRE 236
Cdd:COG5185 306 DIKKATES-----LEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE----IENIVGEVELsKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 237 QLGDRLSVELDTAPTLDLNRVLDEMRCQCETV--LANNRREAEEwlavQTEELNQQQLSSAEQLQGCQMEILEL-----K 309
Cdd:COG5185 377 EELDSFKDTIESTKESLDEIPQNQRGYAQEILatLEDTLKAADR----QIEELQRQIEQATSSNEEVSKLLNELiselnK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 310 RTASALEIELQAQQSLTESLECTVAETEAQYSSQLAQIQCLIDNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEINTY 389
Cdd:COG5185 453 VMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-330 |
4.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 135 DYQRYFNTIEDLQQKI--------LCTK-AENSRLAVQLDNCKLATDDfkskYESELSLrQLLEADISSLHGILEELTLC 205
Cdd:COG4913 236 DLERAHEALEDAREQIellepireLAERyAAARERLAELEYLRAALRL----WFAQRRL-ELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 206 KSDLEAHVESLKEDLLCLKKNHEE----EVNLLREQLgDRLSVELDtaptlDLNRVLDEMRCQCETVLANNRREAEEWLA 281
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnggdRLEQLEREI-ERLERELE-----ERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1939191766 282 VQtEELNQQQLSSAEQLQGCQMEILELKRTASALEIELQAQQSLTESLE 330
Cdd:COG4913 385 LR-AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
268-386 |
5.12e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 268 VLANNRREAEEWLAVQTEELNQQQLSSAE---QLQGCQMEILELKRTASALEIELQAQQSLTESLECTVAETEAQYSSQL 344
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEEleaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1939191766 345 AQIQclidNLENQLAEIRCDLERQNQEYQVLLDVKARLEGEI 386
Cdd:COG1196 309 ERRR----ELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
228-381 |
5.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 228 EEEVNLLREQLgDRLSVELDtaptlDLNRVLDEMRCQCETvLANNRREAEEwlavQTEELNQQQLSSAEQLQGCQMEILE 307
Cdd:COG4372 44 QEELEQLREEL-EQAREELE-----QLEEELEQARSELEQ-LEEELEELNE----QLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939191766 308 LKRTASALEIELQAQQSLTESLECTVAETEAQYSSQLAQIQclidNLENQLAEIRCDLERQNQEYQVLLDVKAR 381
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK----ELEEQLESLQEELAALEQELQALSEAEAE 182
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|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
89-370 |
8.18e-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: 38.62 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 89 EKETMQFLNDRLASYLEKVRSLEETNAELESRIQEQCEQDIPMVcpdyqryfntiEDLQQKI-LCTKAEN--SRLAVQLD 165
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQ-----------EQLQAETeLCAEAEEmrARLAARKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 166 NCKLATDDFKSKYESE-------LSLRQLLEADISSLHGILEE-------LTLCKSDLEAHVESLKEDLLCLkKNHEEEV 231
Cdd:pfam01576 72 ELEEILHELESRLEEEeersqqlQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDILLL-EDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939191766 232 NLLREQLGDRLSvELDTAPTLDLNRV--LDEMRCQCETVLAN--NRREAEEWLAVQTEELNQQQLSSA----EQLQGCQM 303
Cdd:pfam01576 151 SKERKLLEERIS-EFTSNLAEEEEKAksLSKLKNKHEAMISDleERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939191766 304 EILELKRTASALEIELQAQQSLTEslECTVAETEAQYSsqlaqiqclIDNLENQLAEIRCDLERQNQ 370
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLE--EETAQKNNALKK---------IRELEAQISELQEDLESERA 285
|
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