|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
73-386 |
5.29e-118 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 347.29 E-value: 5.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 73 NEKVTMQNLNDRLASYLENVQALEEANADLEQKIKDWYEKFGPGSCRgldhDYSRYFPIIDDLRTQIISATAHNANIILQ 152
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 153 NDNARLTADDFRMKYENELALHQSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQC-AAGGNV 231
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 232 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSL 311
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106337 312 LAMKHSLECSLTETEGNYCTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIETYCRLIDGDE 386
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-376 |
2.94e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 166 KYENELALHQ--SVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQcaaggnvnvEMNAapgvDL 243
Cdd:COG1196 224 ELEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---------EAQA----EE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 244 TVLLNNMRAEYEALAEQNRRDAEAwfQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLT 323
Cdd:COG1196 291 YELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7106337 324 ETEgnycTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:COG1196 369 EAE----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-377 |
1.76e-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: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 185 RRVLDELTLCRTDLEVQLETLSEELAYLKKNHEE----------------------EMQALQCAAGGNVNVEMNAAPGVD 242
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkeleelsrqisalRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 243 LTVLLNNMRAEYEALAEQNRRDAEAwfQEKSASLQQQISDDAGATT-------SARNELTEMKRTLQTLEIELQSLLAMK 315
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKalrealdELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106337 316 HSLECSLTETEGnyctQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIET 377
Cdd:TIGR02168 834 AATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-365 |
3.12e-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: 46.59 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 132 IDDLRTQIISATAHNANIILQNDNARLTADDFRMKYENELALHQSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAY 211
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 212 L---KKNHEEEMQALQcaagGNVNVEMNAApgVDLTVLLNNMRAEYEAL----------AEQNRRDAEAWFQEKSAsLQQ 278
Cdd:TIGR02168 773 AeeeLAEAEAEIEELE----AQIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAATERRLED-LEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 279 QISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLEC----------SLTETEGNYCTQLAQIQAQISALEEQLH 348
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalallrseleELSEELRELESKRSELRRELEELREKLA 925
|
250
....*....|....*..
gi 7106337 349 QVRTETEGQKLEYEQLL 365
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQ 942
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
196-366 |
1.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 196 TDLEVQLETLSEELAylkknheeEMQALQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALaEQNRRDAEAWFQEKS-- 273
Cdd:COG3206 222 SELESQLAEARAELA--------EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHpd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 274 -ASLQQQISDdagattsARNEL-TEMKRTLQTLEIELQSLLAMKHSLECSLTETEGNYcTQLAQIQAQISALEEQLhQVR 351
Cdd:COG3206 293 vIALRAQIAA-------LRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREV-EVA 363
|
170
....*....|....*
gi 7106337 352 TETegqkleYEQLLN 366
Cdd:COG3206 364 REL------YESLLQ 372
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-378 |
2.38e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 198 LEVQLETLSEELAylkkNHEEEMQALQcAAGGNVNVEMNAAPGVDLTVLLNNMRAEyealAEQNRRDAEAwfqeKSASLQ 277
Cdd:COG3206 180 LEEQLPELRKELE----EAEAALEEFR-QKNGLVDLSEEAKLLLQQLSELESQLAE----ARAELAEAEA----RLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 278 QQISDDAGATTSARN--ELTEMKRTLQTLEIELQSLLAmkhslecslTETEGNycTQLAQIQAQISALEEQLHQ-VRTET 354
Cdd:COG3206 247 AQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSA---------RYTPNH--PDVIALRAQIAALRAQLQQeAQRIL 315
|
170 180
....*....|....*....|....
gi 7106337 355 EGQKLEYEQLLNVKAHLEKEIETY 378
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQL 339
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-358 |
4.87e-04 |
|
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: 42.06 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 175 QSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALqcAAGGNVNVEMNAAPGvdLTVLLNN----- 249
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--AELLRALYRLGRQPP--LALLLSPedfld 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 250 --MRAEY-EALAEQNRRDAEAwFQEKSASLQQQISddagATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETE 326
Cdd:COG4942 134 avRRLQYlKYLAPARREQAEE-LRADLAELAALRA----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|..
gi 7106337 327 GNYCTQLAQIQAQISALEEQLHQVRTETEGQK 358
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
141-386 |
7.23e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 141 SATAHNANIiLQNDNARLTADDFRMKYENELALHQSVDADINglrrvLDELTLCRTDLEVQLETLSEELAYLKKNHEEEM 220
Cdd:pfam05483 151 NATRHLCNL-LKETCARSAEKTKKYEYEREETRQVYMDLNNN-----IEKMILAFEELRVQAENARLEMHFKLKEDHEKI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 221 QALQCAAGGNVNVEMNAAPGV------------DLTVLLNNMRAEYEALAEQNRRDAEAWFQ------------------ 270
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLliqitekenkmkDLTFLLEESRDKANQLEEKTKLQDENLKEliekkdhltkeledikms 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 271 -EKSASLQQQISDDAGATTSARNELTEMKRTlqtlEIELQSLLAMKHSLecSLTETEGNYCTQ---LAQIQAQISALEEQ 346
Cdd:pfam05483 305 lQRSMSTQKALEEDLQIATKTICQLTEEKEA----QMEELNKAKAAHSF--VVTEFEATTCSLeelLRTEQQRLEKNEDQ 378
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 7106337 347 LHQVRTETEGQKLEYEQLLNVKAHLEKEIETYCRLIDGDE 386
Cdd:pfam05483 379 LKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-446 |
9.03e-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: 42.03 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 198 LEVQLETLSEE----LAYLKKNHEEEMQalQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRrdaeawfqEKS 273
Cdd:pfam15921 243 VEDQLEALKSEsqnkIELLLQQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR--------NQN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 274 ASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSlECSLTETE--------GNYCTQLAQIQAQISALEE 345
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS-ELTEARTErdqfsqesGNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 346 QLH---------------------QVRTETEGQKLEYEQ----LLNVKAHLEKEIETYCRLIDGDEGSCVKAKGQGRPGN 400
Cdd:pfam15921 392 ELSlekeqnkrlwdrdtgnsitidHLRRELDDRNMEVQRlealLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 7106337 401 QTKDspktaIVKTVVEELDPRGKVLSSRVHTLEEKSTKVNKTEQRI 446
Cdd:pfam15921 472 STKE-----MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI 512
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
282-374 |
1.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 282 DDAGA-----TTSARNELTEMKRTLQTLEIELQSLLAmkhslecsltETEGNYCTQLAQIQAQISALEEQLHQVRTETEG 356
Cdd:COG0542 396 DEAAArvrmeIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEA 465
|
90
....*....|....*...
gi 7106337 357 QKLEYEQLLNVKAHLEKE 374
Cdd:COG0542 466 EKELIEEIQELKEELEQR 483
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-376 |
1.33e-03 |
|
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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 251 RAEYEALAEQNRR--DAEAWFQEKSASLQQQISDDAGAT-TSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEG 327
Cdd:COG4913 301 RAELARLEAELERleARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 7106337 328 NYCTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
246-364 |
1.84e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 246 LLNNM----RAEYEALAEQNRRDAEAWFQEKSASL-----QQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAmkh 316
Cdd:COG3524 166 LVNQLseraREDAVRFAEEEVERAEERLRDAREALlafrnRNGILDPEATAEALLQLIATLEGQLAELEAELAALRS--- 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 7106337 317 slecslTETEGNycTQLAQIQAQISALEEQLHQVRTE----TEGQKL-----EYEQL 364
Cdd:COG3524 243 ------YLSPNS--PQVRQLRRRIAALEKQIAAERARltgaSGGDSLasllaEYERL 291
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-376 |
2.17e-03 |
|
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: 40.44 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 176 SVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHEEEMQALQcaaggNVNVEMNAapgvdLTVLLNNMRAEYE 255
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-----EERKRRDK-----LTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 256 AL---AEQNRRDAEAWFQEkSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEgnycTQ 332
Cdd:TIGR02169 368 DLraeLEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE----EE 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 7106337 333 LAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-377 |
4.72e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 251 RAEYEALAEQNRRDAEAWFQEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEGN-- 328
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 7106337 329 -YCTQLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIET 377
Cdd:COG1196 306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
270-367 |
4.89e-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: 38.98 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 270 QEKSASLQQQISDdagattsARNELTEMKRTLQTLEIELQSLLAMKHSLECSLTETEG---NYCTQLAQIQAQISALEEQ 346
Cdd:COG4942 19 ADAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKE 91
|
90 100
....*....|....*....|.
gi 7106337 347 LHQVRTETEGQKLEYEQLLNV 367
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-376 |
4.91e-03 |
|
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: 39.28 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 168 ENELAlhqSVDADINGLRRVLDELTLCRTDLEVQLETLSEELAYLKKNHE----------EEMQALQcAAGGNVNVEM-- 235
Cdd:TIGR02169 687 KRELS---SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkerleeleEDLSSLE-QEIENVKSELke 762
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106337 236 NAAPGVDLTVLLNNMRaeyEALAEQNRRDAEAWFQEKSASLQQQisddagattsaRNELTEMKRTLQTLEIELQSLLAMK 315
Cdd:TIGR02169 763 LEARIEELEEDLHKLE---EALNDLEARLSHSRIPEIQAELSKL-----------EEEVSRIEARLREIEQKLNRLTLEK 828
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106337 316 HSLECSLTETEG--NYCT-QLAQIQAQISALEEQLHQVRTETEGQKLEYEQLLNVKAHLEKEIE 376
Cdd:TIGR02169 829 EYLEKEIQELQEqrIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
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