|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
102-410 |
2.44e-132 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 384.66 E-value: 2.44e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 102 NEKVELQELNDRFANYIDKVRFLEQQNKIL---LAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLetkISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 179 TEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDV 258
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 259 DVS-KPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTN 337
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380787893 338 ESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESR 410
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
14-101 |
5.57e-20 |
|
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: 83.98 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 14 MFGGPGTASRPSSSRSYVTTSTrtyslgsalrpSTSRSLYASSPGGVYATRSSAVRLRSSVPgvRLLQDSVDFSLADAIN 93
Cdd:pfam04732 9 MFGDSSSSRPSYSSSSGSRSVS-----------SRSYSRSSSSSPSSSSRRSSRSSSRSSYP--SLAADSLDFSLADALN 75
|
....*...
gi 380787893 94 TEFKNTRT 101
Cdd:pfam04732 76 QEFKATRT 83
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-413 |
2.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 131 LLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDV 210
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 211 DNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQID-VDVSKPDLTAALRDVRQQYESVAAKNLQEAEE 289
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEeLEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 290 wykskFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEN---FAVEAANYQDTIGRLQ 366
Cdd:COG1196 374 -----LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaeLEEEEEEEEEALEEAA 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 380787893 367 DEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISL 413
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-423 |
5.21e-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: 68.16 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 95 EFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLK---------GQGKSRLGDLYEEEMRELRRQVDQLT 165
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrkeLEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 166 NDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIaflkKLHEEEIQEL 245
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 246 QAQIQEQHVQIDvdvskpDLTAALRDVRQQyesvaAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQS 325
Cdd:TIGR02168 823 RERLESLERRIA------ATERRLEDLEEQ-----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 326 LTCEVDALKGTNESLERQMREME---ENFAVEAANYQDTIGRLQDEIQNMKEEMArhlREYQDLLNVKMALDIEIATYRK 402
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRrelEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEE 968
|
330 340
....*....|....*....|.
gi 380787893 403 LLEGEESRISLPLPNFSSLNL 423
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNL 989
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-412 |
1.65e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 137 QLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLA 216
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 217 RLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDVDV-SKPDLTAALRDVRQQYESVAAK--NLQEAEEWYKS 293
Cdd:TIGR02168 297 ISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAeELAELEEKLEELKEELESLEAEleELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 294 KFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFavEAANYQDTIGRLqDEIQNMK 373
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAEL-EELEEEL 449
|
250 260 270
....*....|....*....|....*....|....*....
gi 380787893 374 EEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRIS 412
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
132-465 |
8.42e-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: 61.29 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 132 LAELEQLKGQGKSRLGD---LYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEM--LQREEAENTLQSF 206
Cdd:pfam15921 319 LSDLESTVSQLRSELREakrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLadLHKREKELSLEKE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 207 RQ----DVDNASLARLD-LERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQI---DVDVSK-PDLTAALRD----VR 273
Cdd:pfam15921 399 QNkrlwDRDTGNSITIDhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIqgkNESLEKvSSLTAQLEStkemLR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 274 QQYESVAAKNLqeAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEnFAV 353
Cdd:pfam15921 479 KVVEELTAKKM--TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 354 EAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRklLEGEESRIslpLPNFSSLNLRETN------ 427
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR--LELQEFKI---LKDKKDAKIRELEarvsdl 630
|
330 340 350
....*....|....*....|....*....|....*....
gi 380787893 428 -LDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDL 465
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-370 |
1.02e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 95 EFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLY---------EEEMRELRRQVDQLT 165
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarlEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 166 NDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQEL 245
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 246 QAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWyKSKFADLSEAANRNNDALRQAKQESNEYRRQVQS 325
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-EEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 380787893 326 LTCEVDALKGTNESLERQmREMEENFAVEAANYQDTIGRLQDEIQ 370
Cdd:COG1196 475 LEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-405 |
1.80e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 150 YEEEMRELRRQVDQLtndkarveverdnltEDIMRLREKLQEEMLQREEAENTLQSFRQDVDnaslarldlERKVESLQE 229
Cdd:COG4913 240 AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 230 EIAFLkklhEEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAKNLQEAEewykskfADLSEAanrnNDAL 309
Cdd:COG4913 296 ELEEL----RAELARLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQLE-------REIERL----EREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 310 RQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNV 389
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250
....*....|....*.
gi 380787893 390 KMALDIEIATYRKLLE 405
Cdd:COG4913 435 KSNIPARLLALRDALA 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-388 |
4.98e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 148 DLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLR--EKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERkve 225
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA--- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 226 sLQEEIAFLKKLH---EEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAA 302
Cdd:COG4913 690 -LEEQLEELEAELeelEEELDELKGEIGRLEKELE------QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 303 NRnndalrqaKQESNEYRRQVQSLTcevDALKGTNESLERQMREMEENFAVEAANYQDTIG------RLQDEIQNmkEEM 376
Cdd:COG4913 763 VE--------RELRENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADLEslpeylALLDRLEE--DGL 829
|
250
....*....|..
gi 380787893 377 ARHLREYQDLLN 388
Cdd:COG4913 830 PEYEERFKELLN 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-416 |
8.06e-07 |
|
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: 50.92 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 179 TEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKK---LHEEEIQELQAQIQEQHVQ 255
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 256 IDV--DVSKPDLTAALRDVRQQYESVAAkNLQEAEEWYKSkFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDAL 333
Cdd:COG4942 99 LEAqkEELAELLRALYRLGRQPPLALLL-SPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 334 KGTNESLERQMREMEEnfavEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEG---EESR 410
Cdd:COG4942 177 EALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAagfAALK 252
|
....*.
gi 380787893 411 ISLPLP 416
Cdd:COG4942 253 GKLPWP 258
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-306 |
8.73e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 100 RTNEKVE-LQELNDRFANYIDKVRFLEQQNkillAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:COG4913 246 DAREQIElLEPIRELAERYAAARERLAELE----YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 179 TEDIMRLREKLQEEMLQR-EEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAflkkLHEEEIQELQAQIQEQhvqid 257
Cdd:COG4913 322 REELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLP----ASAEEFAALRAEAAAL----- 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 380787893 258 vdvsKPDLTAALRDVRQQYESvAAKNLQEAEEWYKSKFADLSEAANRNN 306
Cdd:COG4913 393 ----LEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASLERRKS 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-378 |
9.79e-07 |
|
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: 50.92 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 151 EEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLqeemlqrEEAENTLQSFRQDVDnaslarlDLERKVESLQEE 230
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELA-------ALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 231 IAFLKKLHEEEIQELQAQI-----QEQHVQIDVDVSKPDLTAALRdvRQQYESVAAKNLQEAEEWYKSKFADLseaaNRN 305
Cdd:COG4942 92 IAELRAELEAQKEELAELLralyrLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAEL----AAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380787893 306 NDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMAR 378
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-325 |
2.73e-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: 49.38 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 98 NTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRlgdlyEEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-----ARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 178 LTEDIMRLREKLQEEM--LQREEAENTL------QSFRQDVDNASL------ARLDLERKVESLQEEIAFLKKLHEEEIQ 243
Cdd:COG4942 95 LRAELEAQKEELAELLraLYRLGRQPPLalllspEDFLDAVRRLQYlkylapARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 244 ELQAQIQEQHVQIdvdvskpdltAALRDVRQQYESVAAKnLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQV 323
Cdd:COG4942 175 ELEALLAELEEER----------AALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 380787893 324 QS 325
Cdd:COG4942 244 PA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-388 |
3.51e-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: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 101 TNEKVELQELNDRFANYIDKVRFLEQQnkilLAELEQLKGQGKSRLGDLYEEEMRElrrQVDQLTNDKARVEVERDNLTE 180
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEAR----IEELEEDLHKLEEALNDLEARLSHS---RIPEIQAELSKLEEEVSRIEA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 181 DIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQE---QHVQID 257
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL----EEELEELEAALRDlesRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 258 VDVSkpDLTAALRDVRQQYESVAAKnLQEAEEWYKSKFADLsEAANRNNDALRQAKQESNEYRRQVQSLtcevDALKGTN 337
Cdd:TIGR02169 889 KERD--ELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKL-EALEEELSEIEDPKGEDEEIPEEELSL----EDVQAEL 960
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 380787893 338 ESLERQMREMEE--NFAVEaaNYQDTIGRLqDEIQNMKEEMARHLREYQDLLN 388
Cdd:TIGR02169 961 QRVEEEIRALEPvnMLAIQ--EYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-412 |
3.57e-06 |
|
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: 49.63 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 87 SLADAINTEFKNTRT------NEKVELQELNDRFANYIDKVRfleqqNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQ 160
Cdd:TIGR04523 152 KELEKLNNKYNDLKKqkeeleNELNLLEKEKLNIQKNIDKIK-----NKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 161 VDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE 240
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 241 EI-QELQAQIQEQHVQIDVDVSKPDLT-AALRDVRQQYESVaAKNLQEAEEWYKSKFADLSEaanrNNDALRQAKQESNE 318
Cdd:TIGR04523 307 DWnKELKSELKNQEKKLEEIQNQISQNnKIISQLNEQISQL-KKELTNSESENSEKQRELEE----KQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 319 YRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQdtigRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIA 398
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE----LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
330
....*....|....
gi 380787893 399 TYRKLLEGEESRIS 412
Cdd:TIGR04523 458 NLDNTRESLETQLK 471
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
98-378 |
3.80e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 98 NTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKgqgksrlgdlyeEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA------------EKRDELNAQVKELREEAQELREKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 178 LTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLD---LERKVESLQEEI--AFLKKLHE----EEIQELQAQ 248
Cdd:COG1340 69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQqtEVLSPEEEkelvEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 249 IQEQHVQIDVDVSKPDLTAALRDVRQQYESvaaknlqeaeewYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTC 328
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEE------------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 380787893 329 EVDALKGTNESLERQMREMEEnfavEAANYQDTIGRLQDEIQNMKEEMAR 378
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQK----ELRELRKELKKLRKKQRALKREKEK 262
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-359 |
4.21e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 110 LNDRFANYIDKVRFLEQQNKILLAELEQLkgqgksrlgdlyEEEMRELRRQvdqltNDKARVEVERDNLTEDIMRLREKL 189
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA------------EAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 190 QEEMLQREEAENTLQSFRQ--DVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDvdvskpDLTA 267
Cdd:COG3206 229 AEARAELAEAEARLAALRAqlGSGPDALPELLQSPVIQQLRAQLAEL----EAELAELSARYTPNHPDVI------ALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 268 ALRDVRQQYESVAAKNLQEAE---EWYKSKFADLSEAANRNNDALRQAKQESNEYRRqvqsLTCEVDALKGTNESLERQM 344
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEaelEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRL 374
|
250
....*....|....*
gi 380787893 345 REMEENFAVEAANYQ 359
Cdd:COG3206 375 EEARLAEALTVGNVR 389
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
162-349 |
5.97e-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: 47.07 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 162 DQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEE 241
Cdd:pfam14988 25 NQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 242 IQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQqyesvaaknlqeaeEWYKSKFADLSEAANRNNDALRQAKQESNEYRR 321
Cdd:pfam14988 105 DREAHLQFLKEKALLEKQLQELRILELGERATR--------------ELKRKAQALKLAAKQALSEFCRSIKRENRQLQK 170
|
170 180
....*....|....*....|....*...
gi 380787893 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 |
6.41e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 118 IDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQRE 197
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 198 EAENTLQSFRQDVDnaslarlDLERKVESLQEEIAFLKklheEEIQELQAQIQEqhvqidVDVSkpdlTAALRDvrqqye 277
Cdd:TIGR02169 333 KLLAEIEELEREIE-------EERKRRDKLTEEYAELK----EELEDLRAELEE------VDKE----FAETRD------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 278 svAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAA- 356
Cdd:TIGR02169 386 --ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAd 463
|
250 260
....*....|....*....|....*....
gi 380787893 357 --NYQDTIGRLQDEIQNMKEEMARHLREY 383
Cdd:TIGR02169 464 lsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-341 |
1.04e-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: 48.14 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 90 DAINTEFKNTRTNEKVELQElndRFANYIDKVRFLEQQNKILLAELEQLKGQGKSrlgdlYEEEMRELRRQVDQLTNDKA 169
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRVKE---KIGELEAEIASLERSIAEKERELEDAEERLAK-----LEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 170 RVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFL---KKLHEEEIQELQ 246
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELADLN 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 247 AQIQEQHVQI-DVDVSKPDLTAALRDVRQQYESVAAKnlqeaEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQS 325
Cdd:TIGR02169 427 AAIAGIEAKInELEEEKEDKALEIKKQEWKLEQLAAD-----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
250
....*....|....*.
gi 380787893 326 LTCEVDALKGTNESLE 341
Cdd:TIGR02169 502 SEERVRGGRAVEEVLK 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-342 |
1.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 104 KVELQELNDRFANY--IDKVRFLEQQNKILLAELEQLKGQgKSRLgDLYEEEMRELRRQVDQLTNDKARVEVERDNLTED 181
Cdd:COG4913 637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAE-LERL-DASSDDLAALEEQLEELEAELEELEEELDELKGE 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 182 IMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLD-----------LERKVESLQEEIAFLKKL---HEEEIQELQA 247
Cdd:COG4913 715 IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavERELRENLEERIDALRARlnrAEEELERAMR 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 248 QIQEQHVQIDVDVSkPDLtAALRDVRQQYESVAAKNLQEAEEwyksKFADLSEAANRNN--DALRQAKQESNEYRRQVQS 325
Cdd:COG4913 795 AFNREWPAETADLD-ADL-ESLPEYLALLDRLEEDGLPEYEE----RFKELLNENSIEFvaDLLSKLRRAIREIKERIDP 868
|
250
....*....|....*..
gi 380787893 326 LtcevdalkgtNESLER 342
Cdd:COG4913 869 L----------NDSLKR 875
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-382 |
2.07e-05 |
|
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: 46.94 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 92 INTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKiLLAELEQLKGQGKSRLGDL------------------YEEE 153
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-KIKELEKQLNQLKSEISDLnnqkeqdwnkelkselknQEKK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 154 MRELRRQVDQ-------LTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVES 226
Cdd:TIGR04523 323 LEEIQNQISQnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 227 -------LQEEIAFLKK---LHEEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYesvaaKNLQEAEEWYKSKFA 296
Cdd:TIGR04523 403 qeklnqqKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK------DLTNQDSVKELII-----KNLDNTRESLETQLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 297 DLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEN---FAVEAANYQDTIGRLQDEIQNMK 373
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKiekLESEKKEKESKISDLEDELNKDD 551
|
....*....
gi 380787893 374 EEMARHLRE 382
Cdd:TIGR04523 552 FELKKENLE 560
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-385 |
2.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 181 DIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDvdv 260
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 261 skpdltaalRDVRQQYES----------VAAKNLQEaeewYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEV 330
Cdd:COG3883 90 ---------ERARALYRSggsvsyldvlLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 380787893 331 DALKGTNESLERQMREMEENFAvEAANYQDTIGRLQDEIQNMKEEMARHLREYQD 385
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
152-242 |
2.65e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 152 EEMRELRRQVDQLTNDKARVEVERD--------NLTEDIMRLREKLqEEMLQREEAE----NTLQSFRQDVDNASLARLD 219
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEEL-EALKARWEAEkeliEEIQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|...
gi 380787893 220 LERKVESLQEEIAFLKKLHEEEI 242
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-274 |
3.16e-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: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 78 RLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDL--YEEEMR 155
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 156 ELRRQVDQLTNDKARVEV-------ERDNLTEDI-------MRLREKLQEEMLQREEAENTLQSFRQDVDN-----ASLA 216
Cdd:TIGR02168 870 ELESELEALLNERASLEEalallrsELEELSEELreleskrSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEY 949
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380787893 217 RLDLE-----------------RKVESLQEEIAFLKKLHEEEIQELQAQIQEqhvQIDVDVSKPDLTAALRDVRQ 274
Cdd:TIGR02168 950 SLTLEeaealenkieddeeearRRLKRLENKIKELGPVNLAAIEEYEELKER---YDFLTAQKEDLTEAKETLEE 1021
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
124-389 |
5.31e-05 |
|
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: 45.73 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 124 LEQQNKILLAELEQLKGQGKSRLGDL--YEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLR--------------E 187
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlteklseaedmlaC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 188 KLQEEMLQREEAENTLQ--------SFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQE-QHVQIDV 258
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDvrlhlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKmQSEKEQL 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 259 DVSKPDLTAALRDVRQQYESVaAKNLQEAEEWYKSKFADLSEaANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNE 338
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSD-LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 380787893 339 SLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNV 389
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNL 821
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
64-382 |
7.62e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 64 RSSAVRLRSSVPGVRLlQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQnkILLaeLEQLKGQGK 143
Cdd:PLN02939 81 RTVMELPQKSTSSDDD-HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKN--ILL--LNQARLQAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 144 SRLGDLYEEEmRELRRQVDQL------TNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAEntlqsfRQDVDNASLAR 217
Cdd:PLN02939 156 EDLEKILTEK-EALQGKINILemrlseTDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATE------GLCVHSLSKEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 218 LDLERKVESLQEEIAFLKK--LHEEEIQELQAQIQEQHVQIDVDVSKPD--LTAALRDVRQ----QYESVAAK--NLQEA 287
Cdd:PLN02939 229 DVLKEENMLLKDDIQFLKAelIEVAETEERVFKLEKERSLLDASLRELEskFIVAQEDVSKlsplQYDCWWEKveNLQDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 288 EEWYKSKFADLSEAANRNND------ALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVeaanYQDT 361
Cdd:PLN02939 309 LDRATNQVEKAALVLDQNQDlrdkvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL----YQES 384
|
330 340
....*....|....*....|.
gi 380787893 362 IGRLQDEIQNMKEEMARHLRE 382
Cdd:PLN02939 385 IKEFQDTLSKLKEESKKRSLE 405
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-466 |
1.02e-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: 45.04 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 104 KVELQELNDRFANYI----DKVRFLEQQNKILLAELEQL--KGQGKSRLGDLYEEEMRELRRQVDQLTNDKARvevERDN 177
Cdd:TIGR00606 690 EAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMlgLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR---LKND 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 178 LTEDimrlrEKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKlhEEEIQELQAQIQEQHVQID 257
Cdd:TIGR00606 767 IEEQ-----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 258 VDVSKPDLTAALRDVRQQyesvAAKNLQEAEEWYKSKFADLSEAANRNndalRQAKQESNEYRRQVQSLTCEVDALKGTN 337
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQE----QIQHLKSKTNELKSEKLQIGTNLQRR----QQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 338 ESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLN--------VKMALDIEIATYRKLLEGEES 409
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEK 991
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380787893 410 R-------ISLPLPNFSSLNLRETNL-DSLPLVDTHSKRTLLIKTVETRDGQV----INETSQHHDDLE 466
Cdd:TIGR00606 992 HqekinedMRLMRQDIDTQKIQERWLqDNLTLRKRENELKEVEEELKQHLKEMgqmqVLQMKQEHQKLE 1060
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-416 |
1.20e-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: 44.67 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 150 YEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSfrqdvdnaslarldLERKVESLQE 229
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ--------------LEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 230 EIAFLKKLHEEEIQELQAQIQEQHvqiDVDVSKPDLTAALRDVRQQYESVAAK-----------NLQEAEEWYK---SKF 295
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARlshsripeiqaELSKLEEEVSrieARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 296 ADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREME---ENFAVEAANYQDTIGRLQDEIQNM 372
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeelEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 380787893 373 KEEMARHLREYQDL---LNVKMALDIEIATYRKLLEGEESRISLPLP 416
Cdd:TIGR02169 895 EAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
119-414 |
1.28e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 119 DKVRFLEQQNKilLAELEQLKGQGKSRLGDLYEEEMR---ELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQ 195
Cdd:pfam17380 307 EKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERmamERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 196 REEAENTlQSFRQDVDNAslarldleRKVESLQEEIAFLKKLHEEEIQELQAQiQEQHVQIDVDVSKPDLTAALRDVRQ- 274
Cdd:pfam17380 385 MERQQKN-ERVRQELEAA--------RKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQREVRRLEEERAREMERVRLe 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 275 -QYESVAAKNLQEAEEWYKSKFADLseaanrnnDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQM--REMEENf 351
Cdd:pfam17380 455 eQERQQQVERLRQQEEERKRKKLEL--------EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLleKEMEER- 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380787893 352 avEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKM------ALDIEIATYRKLLEGEESRISLP 414
Cdd:pfam17380 526 --QKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEersrleAMEREREMMRQIVESEKARAEYE 592
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-386 |
1.40e-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: 44.56 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 104 KVELQELNDRFAnyidKVRFLEQQNKILLAELEQLKGQGKS-RLGDLYEEEMRELRRQvdqltndkaRVEVERD--NLTE 180
Cdd:COG3096 791 RAERDELAEQYA----KASFDVQKLQRLHQAFSQFVGGHLAvAFAPDPEAELAALRQR---------RSELERElaQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 181 DIMRLREKLqEEMLQREEAENTLQSFRQDVDNASLA-RLD-LERKVESLQEEIAFLKKlHEEEIQELQAQIQ------EQ 252
Cdd:COG3096 858 QEQQLRQQL-DQLKEQLQLLNKLLPQANLLADETLAdRLEeLREELDAAQEAQAFIQQ-HGKALAQLEPLVAvlqsdpEQ 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 253 HVQIDVDVSkpDLTAALRDVRQQ---------------YESVAAKNLQEAE--EWYKSKFADLSEAANRNNDALRQAKQE 315
Cdd:COG3096 936 FEQLQADYL--QAKEQQRRLKQQifalsevvqrrphfsYEDAVGLLGENSDlnEKLRARLEQAEEARREAREQLRQAQAQ 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 316 SNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAAN----------------------YQDTIGRLQDEIQNMK 373
Cdd:COG3096 1014 YSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEErarirrdelheelsqnrsrrsqLEKQLTRCEAEMDSLQ 1093
|
330
....*....|...
gi 380787893 374 EEMARHLREYQDL 386
Cdd:COG3096 1094 KRLRKAERDYKQE 1106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-411 |
1.72e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 180 EDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQID-V 258
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAsL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 259 DVSKPDLTAALRDVRQQYESVAAKNLQEAEE----------WYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTC 328
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 329 EVDALKGTNESLERQMRE-------MEENFAVEAANYQDTIGRLQD-----------------EIQNMKEEMARHLREYQ 384
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEvdkefaetrdelkdyreKLEKLKREINELKRELD 409
|
250 260
....*....|....*....|....*..
gi 380787893 385 DLLNVKMALDIEIATYRKLLEGEESRI 411
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
119-400 |
1.87e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 119 DKVRFLEQQNKILLAELEQLKGQGKsrlgdLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDI----MRLREKLQEEML 194
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 195 QREEAENTLQSFRQdvdnaslARLDLERKVESLQEEIAFLKKLHE-----EEIQELQAQIQEqhvqidvdvskpdLTAAL 269
Cdd:PHA02562 249 DIEDPSAALNKLNT-------AAAKIKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITK-------------IKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 270 RDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQesneyrrqvqSLTCEVDALKgtneslerqmremee 349
Cdd:PHA02562 309 KELQHSLE--KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQ----------SLITLVDKAK--------------- 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 380787893 350 nfAVEAAnyqdtIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATY 400
Cdd:PHA02562 362 --KVKAA-----IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
106-256 |
2.17e-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: 43.21 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 106 ELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRL 185
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380787893 186 REKLQEEMLQREEaenTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQI 256
Cdd:pfam09787 81 EAQQQEEAESSRE---QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEI 148
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-255 |
2.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 106 ELQELNDRFANYIDKVRFLEQQnkILLAELEQLKGQGKSRLGDLyEEEMRELRRQVDQLtndkARVEVERDNLTEDIMRL 185
Cdd:COG4717 103 ELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAEL-PERLEELEERLEEL----RELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380787893 186 REKLQEEMLQ-REEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQ 255
Cdd:COG4717 176 QEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL----EEELEQLENELEAAALE 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
104-382 |
2.78e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 104 KVELQELNDRFANYIDKVRFLEQQNKI---LLAELEQLKGQGKSRLGDLYEE---EMRELRRQVDQLTNDKARVEVERDN 177
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTynkNIEEQRKKNGENIARKQNKYDElveEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 178 LTEDIMRLREklqeemlqreeaentlqsfrqdvdnaslARLDLERKVESLQEEIAFLKKLHE-----EEIQELQAQIQEq 252
Cdd:PHA02562 253 PSAALNKLNT----------------------------AAAKIKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITK- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 253 hvqidvdvskpdLTAALRDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDA 332
Cdd:PHA02562 304 ------------IKDKLKELQHSLE--KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 380787893 333 LKGtneslerqmremeenfavEAANYQDTIGRLQDEIQNMKEEMARHLRE 382
Cdd:PHA02562 370 LQA------------------EFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
148-257 |
3.18e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.11 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 148 DLYEEEM----RELRRQVDQLTNDKARVEVERDNLTEDIMRLREKL------QEEMLQReeAENTLQSFRQDVDNASLAR 217
Cdd:pfam10168 553 DLAREEIqkrvKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYeeikdkQEKLMRR--CKKVLQRLNSQLPVLSDAE 630
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 380787893 218 LDLERKVESLQEEIAFLKKlheeEIQELQAQIQEQHVQID 257
Cdd:pfam10168 631 REMKKELETINEQLKHLAN----AIKQAKKKMNYQRYQIA 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-384 |
3.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 174 ERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE-EIQELQAQIQEQ 252
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 253 HVQIDVDvSKPDLTAALRDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDAlrQAKQESNEYRRQVQSLTCEVDA 332
Cdd:COG4717 376 LAEAGVE-DEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 380787893 333 LKGTNESLERQMREMEEnfaveaanyQDTIGRLQDEIQNMKEEMARHLREYQ 384
Cdd:COG4717 451 LREELAELEAELEQLEE---------DGELAELLQELEELKAELRELAEEWA 493
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
119-379 |
3.39e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 119 DKVRFLEQQNKILLAELEQL---KGQGKSRLGDLYE---------EEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLR 186
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYeeqREQARETRDEADEvleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 187 EKLQE------EML---------------QREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFL----KKLHEE- 240
Cdd:PRK02224 286 ERLEEleeerdDLLaeaglddadaeaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLeeraEELREEa 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 241 -----EIQELQAQIQEQHVQI-DVDVSKPDLTAALRDVRQQYESVA------AKNLQEAEEWYKSKFADLSEAANRNNDA 308
Cdd:PRK02224 366 aelesELEEAREAVEDRREEIeELEEEIEELRERFGDAPVDLGNAEdfleelREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 309 LR-----------QAKQES------NEYRRQVQSLTCEVDALKGTNESLERQMREMEEnfAVEAAnyqDTIGRLQDEIQN 371
Cdd:PRK02224 446 EAlleagkcpecgQPVEGSphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED--LVEAE---DRIERLEERRED 520
|
....*...
gi 380787893 372 MKEEMARH 379
Cdd:PRK02224 521 LEELIAER 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-428 |
3.66e-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: 43.12 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 211 DNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAK--NLQEAE 288
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEEL----EEKIAELEKALAELRKELE------ELEEELEQLRKELEELSRQisALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 289 EWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEEnfavEAANYQDTIGRLQDE 368
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----ELKALREALDELRAE 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 369 IQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNL 428
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
169-281 |
4.52e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 169 ARVEVERDNLTEDIMRLREKLQEEMLQREEAENtlqsfrqDVDNASLARLD-LERKVESLQEEIAFLKKLHEEE------ 241
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKK-------EQDEASFERLAeLRDELAELEEELEALKARWEAEkeliee 472
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 380787893 242 IQELQAQIQEQHVQIdvdvskPDLTAALRDVRQQYESVAA 281
Cdd:COG0542 473 IQELKEELEQRYGKI------PELEKELAELEEELAELAP 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-258 |
6.13e-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: 42.35 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 104 KVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKgqgkSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDNLTEDIM 183
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLR----SKVAQL-ELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380787893 184 RLREKLQEemLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDV 258
Cdd:TIGR02168 425 ELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEA----EQALDAAERELAQLQARLDS 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
90-384 |
6.45e-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: 42.41 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 90 DAINTEFKNTRTNEKVELQELNdRFANYIDKVRFLEqqnkillAELEQLKGQ--GKSRLGDLYEEEMRELRRQVDQLTND 167
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQ-------TECEALKLQmaEKDKVIEILRQQIENMTQLVGQHGRT 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 168 KARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDL-----ER-------------------- 222
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagsERlravkdikqerdqllnevkt 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 223 ---KVESLQEEIAFLKKLHEEEIQELQA-----QIQEQHVQIDVDVSKPDLTA-------ALRDVRQQYESVAAKNLQea 287
Cdd:pfam15921 665 srnELNSLSEDYEVLKRNFRNKSEEMETttnklKMQLKSAQSELEQTRNTLKSmegsdghAMKVAMGMQKQITAKRGQ-- 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 288 EEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFA----------VEAAN 357
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnmevaldkasLQFAE 822
|
330 340
....*....|....*....|....*..
gi 380787893 358 YQDTIGRLQDEIQNMKEEMARHLREYQ 384
Cdd:pfam15921 823 CQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
150-251 |
1.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 150 YEEEMRELRRQVDQLtndkaRVEVERdnltedimrLREKLQEEMLQREEAENTLQSFRQDVDnaslARLDLERKVESLQE 229
Cdd:COG2433 411 EEEEIRRLEEQVERL-----EAEVEE---------LEAELEEKDERIERLERELSEARSEER----REIRKDREISRLDR 472
|
90 100
....*....|....*....|....*
gi 380787893 230 EIAFLKK-LHEEE--IQELQAQIQE 251
Cdd:COG2433 473 EIERLEReLEEERerIEELKRKLER 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-281 |
1.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 103 EKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKG--QGKSRLGDLYE--EEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 179 TEDIMRLREKLQEemlqREEAENTLQSFRQDVDNASLARL-DLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQID 257
Cdd:COG4717 159 RELEEELEELEAE----LAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAEL----EEELEEAQEELEELEEELE 230
|
170 180
....*....|....*....|....
gi 380787893 258 VDVSKPDLTAALRDVRQQYESVAA 281
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLI 254
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
92-408 |
1.75e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 92 INTEFKNTRTNE-KVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRL--GDLYEEEMRELRrqvDQLTNDK 168
Cdd:PRK01156 402 IDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgTTLGEEKSNHII---NHYNEKK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 169 ARVEVERDNLTEDIMRLREKLQ-----EEMLQREEAENTLQSFRQdvdnaslaRLDLERKVESLQEEIAFLKKLHeEEIQ 243
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVdlkkrKEYLESEEINKSINEYNK--------IESARADLEDIKIKINELKDKH-DKYE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 244 ELQAQIQEQHVQiDVDVSKPDLTAALrdvrQQYESVAAKNLQEAEEWYKSKFADLSEAANR-----------NNDALRQA 312
Cdd:PRK01156 550 EIKNRYKSLKLE-DLDSKRTSWLNAL----AVISLIDIETNRSRSNEIKKQLNDLESRLQEieigfpddksyIDKSIREI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 313 KQESNEYRRQ---VQSLTCEVDALKGTNESLERQMREMEE------NFAVEAANYQDTIGRLQDEIQNMKEEMARHLREY 383
Cdd:PRK01156 625 ENEANNLNNKyneIQENKILIEKLRGKIDNYKKQIAEIDSiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
330 340
....*....|....*....|....*
gi 380787893 384 QDLLNVKMALDIEIATYRKLLEGEE 408
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-399 |
1.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 106 ELQELNDRFA---NYIDKVRFLEQQNKILLAELEQLKGQ---GKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLT 179
Cdd:COG4717 140 ELAELPERLEeleERLEELRELEEELEELEAELAELQEEleeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 180 EDIMRLREKLQ--EEMLQREEAENTLQSFRQDVDNAS-------------------------------LARLDLERKVES 226
Cdd:COG4717 220 EELEELEEELEqlENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgllaLLFLLLAREKAS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 227 LQEEIAFLKKLHE-EEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEewykskfADLSEAANRN 305
Cdd:COG4717 300 LGKEAEELQALPAlEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-------LQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 306 NDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTigRLQDEIQNMKEEMARHLREYQD 385
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE 450
|
330
....*....|....
gi 380787893 386 LLNVKMALDIEIAT 399
Cdd:COG4717 451 LREELAELEAELEQ 464
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
90-248 |
1.99e-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: 40.52 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 90 DAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKI--LLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTND 167
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 168 KARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQA 247
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 380787893 248 Q 248
Cdd:COG4942 239 A 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
132-282 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 132 LAELEQLKGQGKSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENT--LQSFRQD 209
Cdd:COG1579 19 LDRLEHRLKELPAELAEL-EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380787893 210 VDNASLARLDLERKVESLQEEIAFLKKL---HEEEIQELQAQIQEQHVQIDVDVSkpDLTAALRDVRQQYESVAAK 282
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEElaeLEAELAELEAELEEKKAELDEELA--ELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-332 |
3.03e-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: 39.14 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 169 ARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE-----EIQ 243
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 244 ELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQV 323
Cdd:COG1579 93 ALQKEIESLKRRIS------DLEDEILELMERIEE-LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 380787893 324 QSLTCEVDA 332
Cdd:COG1579 166 EELAAKIPP 174
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
150-257 |
3.66e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.26 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 150 YEEEMRELRRQVDQLTNDKARVEVERDNlTEDIMRLREKLQEEMLQREEAENTLQSFR----------QDVDNASLARLD 219
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsqQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 380787893 220 LERKVESLQEEIAFLKKLH--EEEIQELQAQIQEQHVQID 257
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLreEEELAAAQAQVAQAEAALA 199
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
108-279 |
4.06e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 108 QELNDRFANYIDKVRFLEQQNKILLAELEQLK-----GQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDI 182
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQqsytlNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 183 MRLREKLQEEMLQREEAENTLQSFRQDVDNA--SLARLDLE-----RKVE-----SLQEEIAFLKKLHEEEIQELQAQIq 250
Cdd:pfam06160 367 EEILEQLEEIEEEQEEFKESLQSLRKDELEAreKLDEFKLElreikRLVEksnlpGLPESYLDYFFDVSDEIEDLADEL- 445
|
170 180
....*....|....*....|....*....
gi 380787893 251 eQHVQIDVDVSKPDLTAALRDVRQQYESV 279
Cdd:pfam06160 446 -NEVPLNMDEVNRLLDEAQDDVDTLYEKT 473
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
163-378 |
4.17e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 163 QLTNDKARVEVERDNLTEDIMRLREKLQEEmlqreeaentLQSFRQDVDnaslarlDLERKVESLQEEIAFLKKLH---E 239
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQQQREEE----------LEELQEQLE-------DLESSIQELEKEIKKLESSIkqvE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 240 EEIQELQAQIQEQhvQIDVDVSK------PDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAAnrnndALRQAK 313
Cdd:pfam05667 370 EELEELKEQNEEL--EKQYKVKKktldllPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYR-----ALKEAK 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380787893 314 QE-SNEYRRQVQSLtcevdalkgtnESLERQMREMEEnfavEAANYQDTIGRLQDEIQNMKEEMAR 378
Cdd:pfam05667 443 SNkEDESQRKLEEI-----------KELREKIKEVAE----EAKQKEELYKQLVAEYERLPKDVSR 493
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-409 |
4.19e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 159 RQVDQLTNDKARVEVER----DNLTEDIMRLR---EKLQEEMLQREEAENTLQSFRQDVdnaslarLDLERKVESLQEEI 231
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwirdIQAIAGIMKIRpefTKLQQEFNTLESAELRLSHLHFGY-------KSDETLIASRQEER 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 232 AFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDltAALRDVRQQYESVAAKNLQEAEEWYKSKFADLS---------EAA 302
Cdd:pfam12128 282 QETSAELNQLLRTLDDQWKEKRDELNGELSAAD--AAVAKDRSELEALEDQHGAFLDADIETAAADQEqlpswqselENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 303 NRNNDALRQAKQ---ESNEYRRQVQSLTCeVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARH 379
Cdd:pfam12128 360 EERLKALTGKHQdvtAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEE 438
|
250 260 270
....*....|....*....|....*....|.
gi 380787893 380 LREYQDLL-NVKMALDIEIATYRKLLEGEES 409
Cdd:pfam12128 439 EYRLKSRLgELKLRLNQATATPELLLQLENF 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-289 |
4.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 118 IDKVRFLEQQNKILLAELEQLKgQGKSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDN--LTEDIMRLREKLQEEMLQ 195
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYA-ELQEELEEL-EEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 196 REEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQI-DVDVSKPDLTAALRDVRQ 274
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 380787893 275 QYESVAAKNLQEAEE 289
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
126-357 |
5.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 126 QQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEdIMRLREKLQE-----EMLQR--EE 198
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSdpeqfEQLKQdyQQ 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 199 AENTLQSFRQDVDnaSLARLDLERKVESLQEEIAFLkklheEEIQELQAQIQEQHVQIDVDVSKpdLTAALRDVRQQYE- 277
Cdd:PRK04863 947 AQQTQRDAKQQAF--ALTEVVQRRAHFSYEDAAEML-----AKNSDLNEKLRQRLEQAEQERTR--AREQLRQAQAQLAq 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 278 ------------SVAAKNLQEAEEwyksKFADL-----SEAANRN-------NDALRQAKQESNEYRRQVQSLTCEVDAL 333
Cdd:PRK04863 1018 ynqvlaslkssyDAKRQMLQELKQ----ELQDLgvpadSGAEERArarrdelHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
250 260
....*....|....*....|....
gi 380787893 334 KGTNESLERQMREMEEnfAVEAAN 357
Cdd:PRK04863 1094 TKKLRKLERDYHEMRE--QVVNAK 1115
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
151-347 |
6.57e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 151 EEEMRELRRQvdqltndkaRVEVERdnlteDIMRLREKLQEEMLQREEAENTLQSFRQDVDNAS-LARLDLERKVESLQE 229
Cdd:PRK04863 836 EAELRQLNRR---------RVELER-----ALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlLADETLADRVEEIRE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 230 EIAFLKK-------------LHEEEIQELQ------AQIQEQHVQIDVDVSKPDLTA-ALRDVRQQ-----YESvAAKNL 284
Cdd:PRK04863 902 QLDEAEEakrfvqqhgnalaQLEPIVSVLQsdpeqfEQLKQDYQQAQQTQRDAKQQAfALTEVVQRrahfsYED-AAEML 980
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380787893 285 ---QEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREM 347
Cdd:PRK04863 981 aknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-251 |
7.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 95 EFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKsRLGDL--YEEEMRELRRQVDQLTNDKARVE 172
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELkeKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380787893 173 VERDNLTEDIMRLREKLQEemlqREEAENTLQsfrqdvdnaslarlDLERKVESLQEEIAFLKKLHE--EEIQELQAQIQ 250
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKE----LEEKEERLE--------------ELKKKLKELEKRLEELEERHElyEEAKAKKEELE 375
|
.
gi 380787893 251 E 251
Cdd:PRK03918 376 R 376
|
|
| |
