|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
102-410 |
6.23e-130 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 378.49 E-value: 6.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 102 NEKVELQELNDRFANYIDKVRFLEQQNKIL---LAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLetkISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 179 AEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDV 258
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 259 DVS-KPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTN 337
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14389299 338 ESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESR 410
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
14-101 |
1.60e-17 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 77.05 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 14 MFGGSGTSSRPSSNRSYV-TTSTRTYSLGSALrpstsrslysssPGGAYVTRSSAVRLRSSMPgvRLLQDSVDFSLADAI 92
Cdd:pfam04732 9 MFGDSSSSRPSYSSSSGSrSVSSRSYSRSSSS------------SPSSSSRRSSRSSSRSSYP--SLAADSLDFSLADAL 74
|
....*....
gi 14389299 93 NTEFKNTRT 101
Cdd:pfam04732 75 NQEFKATRT 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-423 |
2.93e-12 |
|
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: 69.32 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 95 EFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLK---------GQGKSRLGDLYEEEMRELRRQVDQLT 165
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrkeLEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 166 NDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIaflkKLHDEEIQEL 245
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 246 QAQIQEQHVQIDvdvskpDLTAALRDVRQQyesvaAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQS 325
Cdd:TIGR02168 823 RERLESLERRIA------ATERRLEDLEEQ-----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 326 LTCEVDALKGTNESLERQMREMEEnfALEAAN-----YQDTIGRLQDEIQNMKEEMArhlREYQDLLNVKMALDIEIATY 400
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRR--ELEELReklaqLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966
|
330 340
....*....|....*....|...
gi 14389299 401 RKLLEGEESRISLPLPNFSSLNL 423
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPVNL 989
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-413 |
7.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 131 LLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDV 210
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 211 DNASLARLDLERKVESLQEEIAFLkklhDEEIQELQAQIQEQHVQID-VDVSKPDLTAALRDVRQQYESVAAKNLQEAEE 289
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEeLEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 290 wykskFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEN---FALEAANYQDTIGRLQ 366
Cdd:COG1196 374 -----LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaeLEEEEEEEEEALEEAA 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 14389299 367 DEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISL 413
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-432 |
3.28e-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: 65.85 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 137 QLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLA 216
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 217 RLDLERKVESLQEEIAFLKKlhdeEIQELQAQIQEQHVQIDVDV-SKPDLTAALRDVRQQYESVAAK--NLQEAEEWYKS 293
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLER----QLEELEAQLEELESKLDELAeELAELEEKLEELKEELESLEAEleELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 294 KFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENfaLEAANYQDTIGRLqDEIQNMK 373
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAEL-EELEEEL 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 14389299 374 EEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLpnfSSLNLRETNLESLP 432
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFS 505
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
132-465 |
1.97e-10 |
|
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: 63.21 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 132 LAELEQLKGQGKSRLGD---LYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEM--LQREEAESTLQSF 206
Cdd:pfam15921 319 LSDLESTVSQLRSELREakrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLadLHKREKELSLEKE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 207 RQ----DVDNASLARLD-LERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQI---DVDVSK-PDLTAALRD----VR 273
Cdd:pfam15921 399 QNkrlwDRDTGNSITIDhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIqgkNESLEKvSSLTAQLEStkemLR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 274 QQYESVAAKNLqeAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEnFAL 353
Cdd:pfam15921 479 KVVEELTAKKM--TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 354 EAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRklLEGEESRIslpLPNFSSLNLRETN------ 427
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR--LELQEFKI---LKDKKDAKIRELEarvsdl 630
|
330 340 350
....*....|....*....|....*....|....*....
gi 14389299 428 -LESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDL 465
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-370 |
4.24e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 106 ELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLY---------EEEMRELRRQVDQLTNDKARVEVERD 176
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarlEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 177 NLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQI 256
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 257 DVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWyKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGT 336
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEE-EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270
....*....|....*....|....*....|....
gi 14389299 337 NESLERQmREMEENFALEAANYQDTIGRLQDEIQ 370
Cdd:COG1196 486 LAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-405 |
3.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 150 YEEEMRELRRQVDQLtndkarveverdnlaEDIMRLREKLQEEMLQREEAESTLQSFRQDVDnaslarldlERKVESLQE 229
Cdd:COG4913 240 AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 230 EIAFLkklhDEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAKNLQEAEewykskfADLSEAanrnNDAL 309
Cdd:COG4913 296 ELEEL----RAELARLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQLE-------REIERL----EREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 310 RQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNV 389
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250
....*....|....*.
gi 14389299 390 KMALDIEIATYRKLLE 405
Cdd:COG4913 435 KSNIPARLLALRDALA 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-388 |
6.62e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 148 DLYEEEMRELRRQVDQLTNDKARVEVERDNLAEdimrlreklqeemlQREEAESTLQSFRQDVDNASlarldLERKVESL 227
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQE--------------RREALQRLAEYSWDEIDVAS-----AEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 228 QEEIAFLKKLHDeEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAKnLQEAEEWYKSKFADLSEAANRNN- 306
Cdd:COG4913 674 EAELERLDASSD-DLAALEEQLEELEAELE------ELEEELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARl 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 307 ------DALRQAKQESNEYRRQVQSLTCEVDALKG----TNESLERQMREMEENFALEAANYQDTIG------RLQDEIQ 370
Cdd:COG4913 746 elrallEERFAAALGDAVERELRENLEERIDALRArlnrAEEELERAMRAFNREWPAETADLDADLEslpeylALLDRLE 825
|
250
....*....|....*...
gi 14389299 371 NmkEEMARHLREYQDLLN 388
Cdd:COG4913 826 E--DGLPEYEERFKELLN 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-416 |
1.51e-06 |
|
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: 50.15 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 179 AEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKK---LHDEEIQELQAQIQEQHVQ 255
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 256 IDV--DVSKPDLTAALRDVRQQYESVAAkNLQEAEEWYKSkFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDAL 333
Cdd:COG4942 99 LEAqkEELAELLRALYRLGRQPPLALLL-SPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 334 KGTNESLERQMREMEEnfalEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEG---EESR 410
Cdd:COG4942 177 EALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAagfAALK 252
|
....*.
gi 14389299 411 ISLPLP 416
Cdd:COG4942 253 GKLPWP 258
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
162-349 |
2.25e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 48.23 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 162 DQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEE 241
Cdd:pfam14988 25 NQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 242 IQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQqyesvaaknlqeaeEWYKSKFADLSEAANRNNDALRQAKQESNEYRR 321
Cdd:pfam14988 105 DREAHLQFLKEKALLEKQLQELRILELGERATR--------------ELKRKAQALKLAAKQALSEFCRSIKRENRQLQK 170
|
170 180
....*....|....*....|....*...
gi 14389299 322 QVQSLTCEVDALKGTNESLERQMREMEE 349
Cdd:pfam14988 171 ELLQLIQETQALEAIKSKLENRKQRLKE 198
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-383 |
2.88e-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: 50.07 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 118 IDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQRE 197
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 198 EAESTLQSFRQDVDnaslarlDLERKVESLQEEIAFLKklhdEEIQELQAQIQEqhvqidVDVSkpdlTAALRDvrqqye 277
Cdd:TIGR02169 333 KLLAEIEELEREIE-------EERKRRDKLTEEYAELK----EELEDLRAELEE------VDKE----FAETRD------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 278 svAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAA- 356
Cdd:TIGR02169 386 --ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAd 463
|
250 260
....*....|....*....|....*....
gi 14389299 357 --NYQDTIGRLQDEIQNMKEEMARHLREY 383
Cdd:TIGR02169 464 lsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-388 |
3.22e-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: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 101 TNEKVELQELNDRFANYIDKVRFLEQQnkilLAELEQLKGQGKSRLGDLYEEEMRElrrQVDQLTNDKARVEVERDNLAE 180
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEAR----IEELEEDLHKLEEALNDLEARLSHS---RIPEIQAELSKLEEEVSRIEA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 181 DIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhDEEIQELQAQIQE---QHVQID 257
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL----EEELEELEAALRDlesRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 258 VDVSkpDLTAALRDVRQQYESVAAKnLQEAEEWYKSKFADLsEAANRNNDALRQAKQESNEYRRQVQSLtcevDALKGTN 337
Cdd:TIGR02169 889 KERD--ELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKL-EALEEELSEIEDPKGEDEEIPEEELSL----EDVQAEL 960
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 14389299 338 ESLERQMREMEENFALEAANYQDTIGRLqDEIQNMKEEMARHLREYQDLLN 388
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-281 |
3.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 100 RTNEKVE-LQELNDRFANYIDKVRFLEQQNkillAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:COG4913 246 DAREQIElLEPIRELAERYAAARERLAELE----YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 179 AEDIMRLREKLQEEMLQR-EEAESTLQSFRQDVDNASLARLDLERKVESLQEEI----AFLKKLHdEEIQELQAQIQEQH 253
Cdd:COG4913 322 REELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALR-AEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*...
gi 14389299 254 VQIDVDVSkpDLTAALRDVRQQYESVAA 281
Cdd:COG4913 401 EALEEALA--EAEAALRDLRRELRELEA 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-359 |
5.91e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 110 LNDRFANYIDKVRFLEQQNKILLAELEQLkgqgksrlgdlyEEEMRELRRQvdqltNDKARVEVERDNLAEDIMRLREKL 189
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA------------EAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 190 QEEMLQREEAESTLQSFRQ--DVDNASLARLDLERKVESLQEEIAFLKKlhdeEIQELQAQIQEQHVQIDvdvskpDLTA 267
Cdd:COG3206 229 AEARAELAEAEARLAALRAqlGSGPDALPELLQSPVIQQLRAQLAELEA----ELAELSARYTPNHPDVI------ALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 268 ALRDVRQQYESVAAKNLQEAE---EWYKSKFADLSEAANRNNDALRQAKQESNEYRRqvqsLTCEVDALKGTNESLERQM 344
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEaelEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRL 374
|
250
....*....|....*
gi 14389299 345 REMEENFALEAANYQ 359
Cdd:COG3206 375 EEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-365 |
1.18e-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: 47.45 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 98 NTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRlgdlyEEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-----ARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 178 LAEDIMRLREKLQEEM--LQREEAESTLQS-FRQDVDNASLARLD-LERKVESLQEEIAFLKKlHDEEIQELQAQIQEQh 253
Cdd:COG4942 95 LRAELEAQKEELAELLraLYRLGRQPPLALlLSPEDFLDAVRRLQyLKYLAPARREQAEELRA-DLAELAALRAELEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 254 vqidvdvskpdltaalrdvRQQYESVAAKNLQEAEEwykskfadLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDAL 333
Cdd:COG4942 173 -------------------RAELEALLAELEEERAA--------LEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|..
gi 14389299 334 KGTNESLERQMREMEENFAleAANYQDTIGRL 365
Cdd:COG4942 226 EALIARLEAEAAAAAERTP--AAGFAALKGKL 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-385 |
3.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 181 DIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKklhdEEIQELQAQIQEQHVQIDvdv 260
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----AEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 261 skpdltaalRDVRQQYES----------VAAKNLQEaeewYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEV 330
Cdd:COG3883 90 ---------ERARALYRSggsvsyldvlLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14389299 331 DALKGTNESLERQMREMEENFAlEAANYQDTIGRLQDEIQNMKEEMARHLREYQD 385
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-341 |
3.84e-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: 46.21 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 90 DAINTEFKNTRTNEKVELQElndRFANYIDKVRFLEQQNKILLAELEQLKGQGKSrlgdlYEEEMRELRRQVDQLTNDKA 169
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRVKE---KIGELEAEIASLERSIAEKERELEDAEERLAK-----LEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 170 RVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFL---KKLHDEEIQELQ 246
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELADLN 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 247 AQIQEQHVQI-DVDVSKPDLTAALRDVRQQYESVAAKnlqeaEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQS 325
Cdd:TIGR02169 427 AAIAGIEAKInELEEEKEDKALEIKKQEWKLEQLAAD-----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
250
....*....|....*.
gi 14389299 326 LTCEVDALKGTNESLE 341
Cdd:TIGR02169 502 SEERVRGGRAVEEVLK 517
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
152-242 |
4.60e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 152 EEMRELRRQVDQLTNDKARVEVERD--------NLAEDIMRLREKLqEEMLQREEAESTL----QSFRQDVDNASLARLD 219
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEEL-EALKARWEAEKELieeiQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|...
gi 14389299 220 LERKVESLQEEIAFLKKLHDEEI 242
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEV 512
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
119-400 |
5.89e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 119 DKVRFLEQQNKILLAELEQLKGQGKsrlgdLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDI----MRLREKLQEEML 194
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 195 QREEAESTLQSFRQdvdnaslARLDLERKVESLQEEIAFLKKlHDEEIQELQaQIQEQhvqidvdvskPDLTAALRDvrq 274
Cdd:PHA02562 249 DIEDPSAALNKLNT-------AAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQ-QISEG----------PDRITKIKD--- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 275 qyesvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKgtneslerqmremeenfALE 354
Cdd:PHA02562 307 -----KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK-----------------KVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 14389299 355 AAnyqdtIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATY 400
Cdd:PHA02562 365 AA-----IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
64-382 |
7.96e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 64 RSSAVRLRSSMPGVRLlQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQnkILLaeLEQLKGQGK 143
Cdd:PLN02939 81 RTVMELPQKSTSSDDD-HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKN--ILL--LNQARLQAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 144 SRLGDLYEEEmRELRRQVDQL------TNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAEstlqsfRQDVDNASLAR 217
Cdd:PLN02939 156 EDLEKILTEK-EALQGKINILemrlseTDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATE------GLCVHSLSKEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 218 LDLERKVESLQEEIAFLKKLHDE--EIQELQAQIQEQHVQIDVDVSKPD--LTAALRDVRQ----QYESVAAK--NLQEA 287
Cdd:PLN02939 229 DVLKEENMLLKDDIQFLKAELIEvaETEERVFKLEKERSLLDASLRELEskFIVAQEDVSKlsplQYDCWWEKveNLQDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 288 EEWYKSKFADLSEAANRNND------ALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALeaanYQDT 361
Cdd:PLN02939 309 LDRATNQVEKAALVLDQNQDlrdkvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL----YQES 384
|
330 340
....*....|....*....|.
gi 14389299 362 IGRLQDEIQNMKEEMARHLRE 382
Cdd:PLN02939 385 IKEFQDTLSKLKEESKKRSLE 405
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
98-378 |
1.01e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 98 NTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKgqgksrlgdlyeEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA------------EKRDELNAQVKELREEAQELREKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 178 LAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLD---LERKVESLQEEI--AFLKKLHD----EEIQELQAQ 248
Cdd:COG1340 69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQqtEVLSPEEEkelvEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 249 IQEQHVQIDVDVSKPDLTAALRDVRQQYESvaaknlqeaeewYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTC 328
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEE------------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 14389299 329 EVDALKGTNESLERQMREMEEnfalEAANYQDTIGRLQDEIQNMKEEMAR 378
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQK----ELRELRKELKKLRKKQRALKREKEK 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-342 |
1.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 104 KVELQELNDRFANY--IDKVRFLEQQNKILLAELEQLKGQgKSRLgDLYEEEMRELRRQVDQLTNDKARVEVERDNLAED 181
Cdd:COG4913 637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAE-LERL-DASSDDLAALEEQLEELEAELEELEEELDELKGE 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 182 IMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLD-----------LERKVESLQEEIAFLKKLHD---EEIQELQA 247
Cdd:COG4913 715 IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavERELRENLEERIDALRARLNraeEELERAMR 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 248 QIQEQHVQIDVDVSkPDLtAALRDVRQQYESVAAKNLQEAEEwyksKFADLSEAANRNN--DALRQAKQESNEYRRQVQS 325
Cdd:COG4913 795 AFNREWPAETADLD-ADL-ESLPEYLALLDRLEEDGLPEYEE----RFKELLNENSIEFvaDLLSKLRRAIREIKERIDP 868
|
250
....*....|....*..
gi 14389299 326 LtcevdalkgtNESLER 342
Cdd:COG4913 869 L----------NDSLKR 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-411 |
1.67e-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: 44.29 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 180 EDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQID-V 258
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAsL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 259 DVSKPDLTAALRDVRQQYESVAAKNLQEAEE----------WYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTC 328
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 329 EVDALKGTNESLERQMRE-------MEENFALEAANYQDTIGRLQD-----------------EIQNMKEEMARHLREYQ 384
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEvdkefaetrdelkdyreKLEKLKREINELKRELD 409
|
250 260
....*....|....*....|....*..
gi 14389299 385 DLLNVKMALDIEIATYRKLLEGEESRI 411
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
90-384 |
1.81e-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: 44.34 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 90 DAINTEFKNTRTNEKVELQELNdRFANYIDKVRFLEqqnkillAELEQLKGQ--GKSRLGDLYEEEMRELRRQVDQLTND 167
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQ-------TECEALKLQmaEKDKVIEILRQQIENMTQLVGQHGRT 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 168 KARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDL----------------ER--------- 222
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagserlravkdikqERdqllnevkt 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 223 ---KVESLQEEIAFLKKLHDEEIQELQA-----QIQEQHVQIDVDVSKPDLTA-------ALRDVRQQYESVAAKNLQEa 287
Cdd:pfam15921 665 srnELNSLSEDYEVLKRNFRNKSEEMETttnklKMQLKSAQSELEQTRNTLKSmegsdghAMKVAMGMQKQITAKRGQI- 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 288 eEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFA----------LEAAN 357
Cdd:pfam15921 744 -DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnmevaldkasLQFAE 822
|
330 340
....*....|....*....|....*..
gi 14389299 358 YQDTIGRLQDEIQNMKEEMARHLREYQ 384
Cdd:pfam15921 823 CQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-348 |
1.95e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 104 KVELQELNDRFAnyidKVRFLEQQNKILLAELEQLKGQGKS-RLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDI 182
Cdd:COG3096 791 RAERDELAEQYA----KASFDVQKLQRLHQAFSQFVGGHLAvAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 183 MRLREKLQeeMLQReeaestLQSFRQDVDNASLA-RLD-LERKVESLQEEIAFLKKlHDEEIQELQAQIQ------EQHV 254
Cdd:COG3096 867 DQLKEQLQ--LLNK------LLPQANLLADETLAdRLEeLREELDAAQEAQAFIQQ-HGKALAQLEPLVAvlqsdpEQFE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 255 QIDVDVSkpDLTAALRDVRQQ---------------YESVAAKNLQEAE--EWYKSKFADLSEAANRNNDALRQAKQESN 317
Cdd:COG3096 938 QLQADYL--QAKEQQRRLKQQifalsevvqrrphfsYEDAVGLLGENSDlnEKLRARLEQAEEARREAREQLRQAQAQYS 1015
|
250 260 270
....*....|....*....|....*....|.
gi 14389299 318 EYRRQVQSLTCEVDALKGTNESLERQMREME 348
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEELG 1046
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
78-355 |
1.99e-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: 43.79 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 78 RLLQDSVDFSLADAINTEFKNTRTNEKVElqELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRE- 156
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENAN--NLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKREt 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 157 ---LRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQRE--EAESTLQSFRQDVDNAslaRLDLERKVESLQEEI 231
Cdd:COG5185 335 etgIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEI---PQNQRGYAQEILATL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 232 AFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPD-LTAALRDVRQQYESVAAKNLQEAeewYKSKFADLSEAANRNNDALR 310
Cdd:COG5185 412 EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeLISELNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELT 488
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 14389299 311 QAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEA 355
Cdd:COG5185 489 QIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-388 |
2.31e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 104 KVELQELNDRFANYI----DKVRFLEQQNKILLAELEQL--KGQGKSRLGDLYEEEMRELRRQVDQLTNDKARvevERDN 177
Cdd:TIGR00606 690 EAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMlgLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR---LKND 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 178 LAEDimrlrEKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKlhDEEIQELQAQIQEQHVQID 257
Cdd:TIGR00606 767 IEEQ-----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 258 VDVSKPDLTAALRDVRQQyesvAAKNLQEAEEWYKSKFADLSEAANRNndalRQAKQESNEYRRQVQSLTCEVDALKGTN 337
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQE----QIQHLKSKTNELKSEKLQIGTNLQRR----QQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 14389299 338 ESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLN 388
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-430 |
3.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 211 DNASLARLDLERKVESLQEEIAFLKklhdEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAK--NLQEAE 288
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELE----EKIAELEKALAELRKELE------ELEEELEQLRKELEELSRQisALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 289 EWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEaanyQDTIGRLQDE 368
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL----REALDELRAE 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14389299 369 IQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLES 430
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-399 |
4.23e-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: 42.80 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 110 LNDRFANYIDKVRFLEQQNkillAELEQLKgqgkSRLgDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEdimrlREKL 189
Cdd:pfam15921 498 VSDLTASLQEKERAIEATN----AEITKLR----SRV-DLKLQELQHLKNEGDHLRNVQTECEALKLQMAE-----KDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 190 QEemLQREEAESTLQSFRQ--------DVDNASLARLDLERKVEslQEEIAFLKKLHDEEIQELQAQIQEQHVQ-IDVDV 260
Cdd:pfam15921 564 IE--ILRQQIENMTQLVGQhgrtagamQVEKAQLEKEINDRRLE--LQEFKILKDKKDAKIRELEARVSDLELEkVKLVN 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 261 SKPDLTAALRDVRQQYESVAAK---------NLQEAEEWYKSKFADLSEaanrnndalrQAKQESNEYRRQVQSLTCEVD 331
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEvktsrnelnSLSEDYEVLKRNFRNKSE----------EMETTTNKLKMQLKSAQSELE 709
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14389299 332 ALKGTNESLER---QMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIAT 399
Cdd:pfam15921 710 QTRNTLKSMEGsdgHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST 780
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-382 |
4.51e-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: 42.70 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 92 INTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKiLLAELEQLKGQGKSRLGDL------------------YEEE 153
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-KIKELEKQLNQLKSEISDLnnqkeqdwnkelkselknQEKK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 154 MRELRRQVDQ-------LTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVES 226
Cdd:TIGR04523 323 LEEIQNQISQnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 227 -------LQEEIAFLKK---LHDEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYesvaaKNLQEAEEWYKSKFA 296
Cdd:TIGR04523 403 qeklnqqKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK------DLTNQDSVKELII-----KNLDNTRESLETQLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 297 DLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEN---FALEAANYQDTIGRLQDEIQNMK 373
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKiekLESEKKEKESKISDLEDELNKDD 551
|
....*....
gi 14389299 374 EEMARHLRE 382
Cdd:TIGR04523 552 FELKKENLE 560
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
124-407 |
4.57e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 124 LEQQNKILLAELEQLKGQGKSRLGDL--YEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEmlqrEEAES 201
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL----SEAED 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 202 TLqsfrqdvdnaslaRLDLERKVESLQEEIAFLKK-LHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVA 280
Cdd:TIGR00618 609 ML-------------ACEQHALLRKLQPEQDLQDVrLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELL 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 281 AKNLQE--AEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGT--------NESLERQMREMEEN 350
Cdd:TIGR00618 676 ASRQLAlqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDlaaredalNQSLKELMHQARTV 755
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14389299 351 -----FALEAANYQDTIG-RLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGE 407
Cdd:TIGR00618 756 lkartEAHFNNNEEVTAAlQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-416 |
4.94e-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: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 150 YEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSfrqdvdnaslarldLERKVESLQE 229
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ--------------LEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 230 EIAFLKKLHDEEIQELQAQIQEQHvqiDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDAL 309
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 310 R--------------QAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREME---ENFALEAANYQDTIGRLQDEIQNM 372
Cdd:TIGR02169 815 ReieqklnrltlekeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeelEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 14389299 373 KEEMARHLREYQDL---LNVKMALDIEIATYRKLLEGEESRISLPLP 416
Cdd:TIGR02169 895 EAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
106-262 |
5.65e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 106 ELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRL 185
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14389299 186 REKLQEEMLQREEaesTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKklhdEEIQELQAQIQEQHVQIDVDVSK 262
Cdd:pfam09787 81 EAQQQEEAESSRE---QLQELEEQLATERSARREAEAELERLQEELRYLE----EELRRSKATLQSRIKDREAEIEK 150
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-412 |
6.83e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 87 SLADAINTEFKNTRT------NEKVELQELNDRFANYIDKVRfleqqNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQ 160
Cdd:TIGR04523 152 KELEKLNNKYNDLKKqkeeleNELNLLEKEKLNIQKNIDKIK-----NKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 161 VDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDE 240
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 241 EI-QELQAQIQEQHVQIDVDVSKPDLT-AALRDVRQQYESVaAKNLQEAEEWYKSKFADLSEaanrNNDALRQAKQESNE 318
Cdd:TIGR04523 307 DWnKELKSELKNQEKKLEEIQNQISQNnKIISQLNEQISQL-KKELTNSESENSEKQRELEE----KQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 319 YRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQdtigRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIA 398
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE----LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
330
....*....|....
gi 14389299 399 TYRKLLEGEESRIS 412
Cdd:TIGR04523 458 NLDNTRESLETQLK 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-255 |
7.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 106 ELQELNDRFANYIDKVRFLEQQnkILLAELEQLKGQGKSRLGDLyEEEMRELRRQVDQLtndkARVEVERDNLAEDIMRL 185
Cdd:COG4717 103 ELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAEL-PERLEELEERLEEL----RELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14389299 186 REKLQEEMLQ-REEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQ 255
Cdd:COG4717 176 QEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
169-281 |
8.86e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 169 ARVEVERDNLAEDIMRLREKLQEEMLQREEAEstlqsfrQDVDNASLARLD-LERKVESLQEEIAFLK------KLHDEE 241
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALK-------KEQDEASFERLAeLRDELAELEEELEALKarweaeKELIEE 472
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 14389299 242 IQELQAQIQEQHVQIdvdvskPDLTAALRDVRQQYESVAA 281
Cdd:COG0542 473 IQELKEELEQRYGKI------PELEKELAELEEELAELAP 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-246 |
9.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 104 KVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKgqgkSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDNLAEDIM 183
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLR----SKVAQL-ELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14389299 184 RLREKLQEemLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQ 246
Cdd:TIGR02168 425 ELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
90-248 |
1.40e-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: 40.90 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 90 DAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKI--LLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTND 167
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 168 KARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQA 247
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 14389299 248 Q 248
Cdd:COG4942 239 A 239
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
104-382 |
1.46e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 104 KVELQELNDRFANYIDKVRFLEQQNKI---LLAELEQLKGQGKSRLGDLYEE---EMRELRRQVDQLTNDKARVEVERDN 177
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTynkNIEEQRKKNGENIARKQNKYDElveEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 178 LAEDIMRLREklqeemlqreeaestlqsfrqdvdnaslARLDLERKVESLQEEIAFLKKlHDEEIQELQAQIQEQHVQID 257
Cdd:PHA02562 253 PSAALNKLNT----------------------------AAAKIKSKIEQFQKVIKMYEK-GGVCPTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 258 VDVSKPDLTAALRDVRQQYEsvaakNLQEAEewykSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGtn 337
Cdd:PHA02562 304 IKDKLKELQHSLEKLDTAID-----ELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA-- 372
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 14389299 338 eslerqmremeenfalEAANYQDTIGRLQDEIQNMKEEMARHLRE 382
Cdd:PHA02562 373 ----------------EFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
119-379 |
1.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 119 DKVRFLEQQNKILLAELEQL---KGQGKSRLGDLYE---------EEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLR 186
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYeeqREQARETRDEADEvleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 187 EKLQE------EML---------------QREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHD---EEI 242
Cdd:PRK02224 286 ERLEEleeerdDLLaeaglddadaeaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelrEEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 243 QELQAQIQEQHVQIDVDVSK-PDLTAALRDVRQQYESVA-------------AKNLQEAEEWYKSKFADLSEAANRNNDA 308
Cdd:PRK02224 366 AELESELEEAREAVEDRREEiEELEEEIEELRERFGDAPvdlgnaedfleelREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 309 LR-----------QAKQES------NEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEaanyqDTIGRLQDEIQN 371
Cdd:PRK02224 446 EAlleagkcpecgQPVEGSphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE-----DRIERLEERRED 520
|
....*...
gi 14389299 372 MKEEMARH 379
Cdd:PRK02224 521 LEELIAER 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-384 |
1.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 174 ERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDE-EIQELQAQIQEQ 252
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 253 HVQIDVDvSKPDLTAALRDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDAlrQAKQESNEYRRQVQSLTCEVDA 332
Cdd:COG4717 376 LAEAGVE-DEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14389299 333 LKGTNESLERQMREMEEnfaleaanyQDTIGRLQDEIQNMKEEMARHLREYQ 384
Cdd:COG4717 451 LREELAELEAELEQLEE---------DGELAELLQELEELKAELRELAEEWA 493
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
150-251 |
2.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 150 YEEEMRELRRQVDQLtndkaRVEVERdnlaedimrLREKLQEEMLQREEAESTLQSFRQDVDnaslARLDLERKVESLQE 229
Cdd:COG2433 411 EEEEIRRLEEQVERL-----EAEVEE---------LEAELEEKDERIERLERELSEARSEER----REIRKDREISRLDR 472
|
90 100
....*....|....*....|....*
gi 14389299 230 EIAFLKKLHDEE---IQELQAQIQE 251
Cdd:COG2433 473 EIERLERELEEErerIEELKRKLER 497
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-332 |
2.03e-03 |
|
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: 39.52 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 169 ARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDE-----EIQ 243
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 244 ELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQV 323
Cdd:COG1579 93 ALQKEIESLKRRIS------DLEDEILELMERIEE-LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 14389299 324 QSLTCEVDA 332
Cdd:COG1579 166 EELAAKIPP 174
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
150-257 |
2.78e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.65 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 150 YEEEMRELRRQVDQLTNDKARVEVERDNLAEdIMRLREKLQEEMLQREEAESTLQSFR----------QDVDNASLARLD 219
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELGAEAE-IAAAEAQLAAAQAQLDLAQRELERYQalykkgavsqQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 14389299 220 LERKVESLQEEIAFLKKLHD--EEIQELQAQIQEQHVQID 257
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLReeEELAAAQAQVAQAEAALA 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
132-281 |
4.63e-03 |
|
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: 38.75 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 132 LAELEQLKGQGKSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREK-------------------LQEE 192
Cdd:COG1579 19 LDRLEHRLKELPAELAEL-EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqlgnvrnnkeyeaLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 193 M----LQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSK--PDLT 266
Cdd:COG1579 98 IeslkRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKipPELL 177
|
170
....*....|....*
gi 14389299 267 AALRDVRQQYESVAA 281
Cdd:COG1579 178 ALYERIRKRKNGLAV 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-343 |
4.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 154 MRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAF 233
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 234 L-----KKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDA 308
Cdd:COG4717 128 LplyqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 14389299 309 LRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQ 343
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-281 |
7.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 103 EKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKG--QGKSRLGDLYE--EEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 179 AEDIMRLREKLQEemlqREEAESTLQSFRQDVDNASLARL-DLERKVESLQEEIAFLKklhdEEIQELQAQIQEQHVQID 257
Cdd:COG4717 159 RELEEELEELEAE----LAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAELE----EELEEAQEELEELEEELE 230
|
170 180
....*....|....*....|....
gi 14389299 258 VDVSKPDLTAALRDVRQQYESVAA 281
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLI 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
126-349 |
7.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 126 QQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEvERDNLAEDIMRLREKLQE-----EMLQR--EE 198
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQ-QHGNALAQLEPIVSVLQSdpeqfEQLKQdyQQ 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 199 AESTLQSFRQDVDnaSLARLDLERKVESLQEEIAFLkklhdEEIQELQAQIQEQHVQIDVDVSKpdLTAALRDVRQQYE- 277
Cdd:PRK04863 947 AQQTQRDAKQQAF--ALTEVVQRRAHFSYEDAAEML-----AKNSDLNEKLRQRLEQAEQERTR--AREQLRQAQAQLAq 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389299 278 ------------SVAAKNLQEAEEwyksKFADL-----SEAANRN-------NDALRQAKQESNEYRRQVQSLTCEVDAL 333
Cdd:PRK04863 1018 ynqvlaslkssyDAKRQMLQELKQ----ELQDLgvpadSGAEERArarrdelHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
250
....*....|....*.
gi 14389299 334 KGTNESLERQMREMEE 349
Cdd:PRK04863 1094 TKKLRKLERDYHEMRE 1109
|
|
| |
