|
Name |
Accession |
Description |
Interval |
E-value |
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
504-593 |
2.47e-35 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 130.11 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 504 SLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYRSEHELDVTLSED-----SCSVLSEPSQEELAAAKLQIGE 578
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDgegggSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 257467641 579 LSGKVKKLQYENRVL 593
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
378-472 |
5.00e-33 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 123.56 E-value: 5.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 378 DSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHLKLVEEEANL 457
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 257467641 458 LSRRIVELEVENRGL 472
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
1065-1203 |
1.50e-26 |
|
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365.
Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 106.69 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1065 MELTRQLQLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAEPW-VLKHSDMEKQDnsWKEARSEKTHDKE 1143
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRrKINMNERAKVI--DGEKFVPDQKESS 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1144 GVSEAELGGTGLKRTKSVSSMSEFESLLDCSPYLAGGDARNKKLPNGPAFAFVSTEPVEP 1203
Cdd:pfam14818 79 SPPFPDSGQCEFPRMNHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-541 |
3.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEmLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQT-GQVDGE 292
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 293 LIRGLEQDVKVSKDISmRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSlgktdkk 372
Cdd:TIGR02168 756 LTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE------- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 373 pTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSlygDLDAALsaEELAdaphsretELKVHLKLVE 452
Cdd:TIGR02168 828 -SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALL--NERA--------SLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 453 EEANLLSRRIVELEVENRGLRAEMDDMKDHGGgggpEARLAFSSLGGECGESLAELRRH----LQFVEEEAELLRRSSAE 528
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEysltLEEAEALENKIEDDEEE 969
|
330
....*....|...
gi 257467641 529 LEDQNKLLLNELA 541
Cdd:TIGR02168 970 ARRRLKRLENKIK 982
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
214-536 |
2.01e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGEL 293
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 294 IRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTDKKP 373
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 374 TAQEDSADL---KCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHLKL 450
Cdd:pfam02463 403 EEKEAQLLLelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 451 VEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELE 530
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
....*.
gi 257467641 531 DQNKLL 536
Cdd:pfam02463 563 RQKLVR 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-531 |
2.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEMLEMRDVYmEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDG 291
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 292 ELIRGLEQDVKvskdismRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTDK 371
Cdd:COG1196 330 EELEELEEELE-------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 372 KPTAQEDSADLKCQLHFAKEESALMcKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKvhlklv 451
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELE-EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL------ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 452 EEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELED 531
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
212-587 |
5.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEMLEMRDVYM--EEDVYQLQELRQQLDQAsktcrilqyrlrkaerRSLRAAQTGQV 289
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEEL----------------ERLKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 290 DGELIRGLEQDVKVSKDISmrlhKELEVVEKKRMRLEEENEGLRQRLIETELAKQ---VLQTELDRPREHSLKKRGTRSL 366
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIE----EEISKITARIGELKKEIKELKKAIEELKKAKGkcpVCGRELTEEHRKELLEEYTAEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 367 GKTDKKptaqedsadlkcqlhfaKEESAlmcKKLTKLAKENDSMKEELLKYRSLygdldaaLSAEELADAPHSRETELKV 446
Cdd:PRK03918 462 KRIEKE-----------------LKEIE---EKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKLKK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 447 H----LKLVEEEANLLSRRIVELEVENRGLRAEMDDMKdhgggggpearlafsslggECGESLAELRRHLQFVEEE-AEL 521
Cdd:PRK03918 515 YnleeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-------------------ELKKKLAELEKKLDELEEElAEL 575
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257467641 522 LRRSSA---ELEDQNKLLLNELAKY--------RSEHELDVTLSE-DSCSVLSEPSQEELAAAKLQIGELSGKVKKLQ 587
Cdd:PRK03918 576 LKELEElgfESVEELEERLKELEPFyneylelkDAEKELEREEKElKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
998-1115 |
1.75e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 998 LTELQQQFAKAKATWETERAELKGHASQMELKAGKGASERPGPDWK------AALQREREEQQHLLAESYSAVMELTRQL 1071
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQqlraqlAELEAELAELSARYTPNHPDVIALRAQI 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 257467641 1072 QLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAE 1115
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
28-211 |
1.03e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 28 SHRAPSPaRPKDVAGWSLAkGRRGTGPGSATACGTASSARPDKKGRAVAPGtrGTGPRVAGVRtgvrAKGRPRPGTGPRP 107
Cdd:PHA03307 76 GTEAPAN-ESRSTPTWSLS-TLAPASPAREGSPTPPGPSSPDPPPPTPPPA--SPPPSPAPDL----SEMLRPVGSPGPP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 108 PPPPPSLTDSSSEVSDCASEEARQLGLELALSSDAESAAGGPAGTRTG-QPPQPAQSGQQPPRPPASPDEPSVAASSVGS 186
Cdd:PHA03307 148 PAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPsTPPAAASPRPPRRSSPISASASSPAPAPGRS 227
|
170 180
....*....|....*....|....*
gi 257467641 187 SRLPLSASlAFSDLTEEMLDCGPGG 211
Cdd:PHA03307 228 AADDAGAS-SSDSSSSESSGCGWGP 251
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
814-1109 |
3.99e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 814 SEIKDLQLVLAEAHDSLRGLQEQLS-QERQLRK--EEADSFNQKMVQLKEDQQRallrrefelqSLSLQRRLEQKF---- 886
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKlQDENLKEliEKKDHLTKELEDIKMSLQR----------SMSTQKALEEDLqiat 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 887 -----WSQEKNILVQESQQFK--HNFLLLFMK-----LRWFLKRWRQGkvLPSEEDDF------LEVNSMKELYLLMEEE 948
Cdd:pfam05483 324 kticqLTEEKEAQMEELNKAKaaHSFVVTEFEattcsLEELLRTEQQR--LEKNEDQLkiitmeLQKKSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 949 EMNAQHSDNKACTGESWTQNTPNECIKTLA-DMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELKGHASQME 1027
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1028 LKAGKGASERPGPDwKAALqrereEQQHLLAESYSAVMELTRQLQLSERHWSQEK--LQLVERLQGEKQQVEQQVKELQN 1105
Cdd:pfam05483 482 KEKLKNIELTAHCD-KLLL-----ENKELTQEASDMTLELKKHQEDIINCKKQEErmLKQIENLEEKEMNLRDELESVRE 555
|
....
gi 257467641 1106 RLSQ 1109
Cdd:pfam05483 556 EFIQ 559
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
989-1150 |
8.41e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 989 WLLQDErrgltELQQQFAKAKATWETERAELKGHASQMELKAGKGASERpgpdwkAALQREREEQQHLLAESYSAVMELT 1068
Cdd:COG1196 230 LLLKLR-----ELEAELEELEAELEELEAELEELEAELAELEAELEELR------LELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1069 RQLQLSERHwsqekLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAEPWVLKHSDMEKQDNSWKEARSEKTHDKEGVSEA 1148
Cdd:COG1196 299 RLEQDIARL-----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
..
gi 257467641 1149 EL 1150
Cdd:COG1196 374 LA 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
452-664 |
8.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 452 EEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEA------RLAFSSLGGECGESLAELRRHLQFVEEEAELLRRS 525
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 526 SAELEDQNKLLLNELAKYRSEHELDVTLSEDSCSVLSEpSQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQ------- 598
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-LEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrerea 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257467641 599 --RCDLASCQSTRPMLETDAEAGDSAQCvpaplGETLE--PHAARLCRARE-----AEALPGLREQAALVSKAID 664
Cdd:PRK02224 430 elEATLRTARERVEEAEALLEAGKCPEC-----GQPVEgsPHVETIEEDRErveelEAELEDLEEEVEEVEERLE 499
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
504-593 |
2.47e-35 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 130.11 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 504 SLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYRSEHELDVTLSED-----SCSVLSEPSQEELAAAKLQIGE 578
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDgegggSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 257467641 579 LSGKVKKLQYENRVL 593
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
378-472 |
5.00e-33 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 123.56 E-value: 5.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 378 DSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHLKLVEEEANL 457
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 257467641 458 LSRRIVELEVENRGL 472
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
1065-1203 |
1.50e-26 |
|
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365.
Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 106.69 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1065 MELTRQLQLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAEPW-VLKHSDMEKQDnsWKEARSEKTHDKE 1143
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRrKINMNERAKVI--DGEKFVPDQKESS 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1144 GVSEAELGGTGLKRTKSVSSMSEFESLLDCSPYLAGGDARNKKLPNGPAFAFVSTEPVEP 1203
Cdd:pfam14818 79 SPPFPDSGQCEFPRMNHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-541 |
3.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEmLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQT-GQVDGE 292
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 293 LIRGLEQDVKVSKDISmRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSlgktdkk 372
Cdd:TIGR02168 756 LTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE------- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 373 pTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSlygDLDAALsaEELAdaphsretELKVHLKLVE 452
Cdd:TIGR02168 828 -SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALL--NERA--------SLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 453 EEANLLSRRIVELEVENRGLRAEMDDMKDHGGgggpEARLAFSSLGGECGESLAELRRH----LQFVEEEAELLRRSSAE 528
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEysltLEEAEALENKIEDDEEE 969
|
330
....*....|...
gi 257467641 529 LEDQNKLLLNELA 541
Cdd:TIGR02168 970 ARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-587 |
9.49e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 294 IRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREhslkkrgtrslgktdKKP 373
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---------------EVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 374 TAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELA-DAPHSRETELKVHLKLVE 452
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAlDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 453 EEANLLSRRIVELEVENRGLRAEMDDMKdhgggggpEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELEDQ 532
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELS--------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 257467641 533 NKLLLNELAKYRSE-HELDVTLSEDscsvlsepsQEELAAAKLQIGELSGKVKKLQ 587
Cdd:TIGR02168 896 LEELSEELRELESKrSELRRELEEL---------REKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
214-536 |
2.01e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGEL 293
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 294 IRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTDKKP 373
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 374 TAQEDSADL---KCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHLKL 450
Cdd:pfam02463 403 EEKEAQLLLelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 451 VEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELE 530
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
....*.
gi 257467641 531 DQNKLL 536
Cdd:pfam02463 563 RQKLVR 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-531 |
2.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEMLEMRDVYmEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDG 291
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 292 ELIRGLEQDVKvskdismRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTDK 371
Cdd:COG1196 330 EELEELEEELE-------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 372 KPTAQEDSADLKCQLHFAKEESALMcKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKvhlklv 451
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELE-EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL------ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 452 EEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELED 531
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
212-587 |
5.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEMLEMRDVYM--EEDVYQLQELRQQLDQAsktcrilqyrlrkaerRSLRAAQTGQV 289
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEEL----------------ERLKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 290 DGELIRGLEQDVKVSKDISmrlhKELEVVEKKRMRLEEENEGLRQRLIETELAKQ---VLQTELDRPREHSLKKRGTRSL 366
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIE----EEISKITARIGELKKEIKELKKAIEELKKAKGkcpVCGRELTEEHRKELLEEYTAEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 367 GKTDKKptaqedsadlkcqlhfaKEESAlmcKKLTKLAKENDSMKEELLKYRSLygdldaaLSAEELADAPHSRETELKV 446
Cdd:PRK03918 462 KRIEKE-----------------LKEIE---EKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKLKK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 447 H----LKLVEEEANLLSRRIVELEVENRGLRAEMDDMKdhgggggpearlafsslggECGESLAELRRHLQFVEEE-AEL 521
Cdd:PRK03918 515 YnleeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-------------------ELKKKLAELEKKLDELEEElAEL 575
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257467641 522 LRRSSA---ELEDQNKLLLNELAKY--------RSEHELDVTLSE-DSCSVLSEPSQEELAAAKLQIGELSGKVKKLQ 587
Cdd:PRK03918 576 LKELEElgfESVEELEERLKELEPFyneylelkDAEKELEREEKElKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-477 |
9.36e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEMLEMRDvymEEDVYQ--LQELRQQLDQASKTCRILQYRLRKAERRSLRAaqtgqv 289
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEE---EIEELQkeLYALANEISRLEQQKQILRERLANLERQLEEL------ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 290 dGELIRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDrprehslkkrgtrslgkt 369
Cdd:TIGR02168 322 -EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE------------------ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 370 dkkpTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSREtELKVHLK 449
Cdd:TIGR02168 383 ----TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-ELQEELE 457
|
250 260
....*....|....*....|....*...
gi 257467641 450 LVEEEANLLSRRIVELEVENRGLRAEMD 477
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELA 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-1137 |
1.71e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 251 QLQELRQQLDQASKTCRILQYRLRKAERRSLRAaQTGQVDGELIRGLEQDVKVSKDISmRLHKELEVVEKKRMRLEEENE 330
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQE-ELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 331 GLRQRLIETELAKQVLQTELDRPrEHSLKKRGTRSLGKTDKKPTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSM 410
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 411 KEELLKYRSLYGDLDAALSAEELadaphsRETELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDdmkdhgggggpea 490
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLEL------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------------- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 491 RLAFSSLGGECGES---LAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYRSEHELDVTLSEDscsvLSEPSQE 567
Cdd:TIGR02168 432 EAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 568 --ELAAAKLQIGELSGkvkklqyenrvLLSNLQRCDlascqstrPMLETDAEA--GDSAQcvpAPLGETLEphAARLCRA 643
Cdd:TIGR02168 508 vkALLKNQSGLSGILG-----------VLSELISVD--------EGYEAAIEAalGGRLQ---AVVVENLN--AAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 644 REAEALPGLREQAALVSKAIDVLVAD----ANGFSVGLRLCLDNECADLRLHEA-----------PDNSEGPRDAKLIHA 708
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNdreiLKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDLDNALELAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 709 iLVRLSVLQQELnaFTRKADVALGSSGKEQpepfpalpalGSQGPAKEImlsKDLGsdfqppdfRDLLEWEPRIREAfrt 788
Cdd:TIGR02168 644 -GYRIVTLDGDL--VRPGGVITGGSAKTNS----------SILERRREI---EELE--------EKIEELEEKIAEL--- 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 789 gdleskpdpSRNFRPYRAEDNDsYASEIKDLQLVLAEAHDSLRGLQEQLSQERQLRKEEADSFNQKMVQLKE-DQQRALL 867
Cdd:TIGR02168 697 ---------EKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 868 RREFELQSLSLQRrLEQKFWSQEKNILVQESQqfkhnflllfmklrwflkrwrqgkvLPSEEDDFLEVNsmkelyllmee 947
Cdd:TIGR02168 767 EERLEEAEEELAE-AEAEIEELEAQIEQLKEE-------------------------LKALREALDELR----------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 948 eemnAQHSDNKACTGEswTQNTPNECIKTLADMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELKGHasqme 1027
Cdd:TIGR02168 810 ----AELTLLNEEAAN--LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL----- 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1028 LKAGKGASERpgpdwKAALQREREEQQHLLAESYSAVMELTRQLQLSERHWSQEKLQLverlqgekQQVEQQVKELQNRL 1107
Cdd:TIGR02168 879 LNERASLEEA-----LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL--------EGLEVRIDNLQERL 945
|
890 900 910
....*....|....*....|....*....|
gi 257467641 1108 SQLQKAAEPWVLKHsdMEKQDNSWKEARSE 1137
Cdd:TIGR02168 946 SEEYSLTLEEAEAL--ENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-1118 |
1.36e-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: 50.06 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 253 QELRQQLDQASKtcrILQYRLRKAE-RRSLRAAQTG--QVDGeLIRGLEQDVKvskdismRLHKELEVVEKKRmRLEEEN 329
Cdd:TIGR02168 155 EERRAIFEEAAG---ISKYKERRKEtERKLERTRENldRLED-ILNELERQLK-------SLERQAEKAERYK-ELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 330 EGLRQRLIETELakQVLQTELDRPREhSLKKRGTRSLGKTDKKPTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDS 409
Cdd:TIGR02168 223 RELELALLVLRL--EELREELEELQE-ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 410 MKEELLKYRSLYGDLDAALSAEELadaphsRETELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKdhgggggpe 489
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEA------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 490 arlafsslggecgESLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKY-----RSEHELDVTLSEDScSVLSEP 564
Cdd:TIGR02168 365 -------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLearleRLEDRRERLQQEIE-ELLKKL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 565 SQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQRCDLASCQSTRPMLETDAEagdsaqcvpaplgetLEPHAARLcrar 644
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE---------------LAQLQARL---- 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 645 eaEALPGLREQAALVSKAIDVLVADANGFSV-------------GLRLCLDNECADLRLHEAPDNSEgprDAKLIHAILV 711
Cdd:TIGR02168 492 --DSLERLQENLEGFSEGVKALLKNQSGLSGilgvlselisvdeGYEAAIEAALGGRLQAVVVENLN---AAKKAIAFLK 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 712 -----RLSVLqqELNAFT-RKADVALGSSGKEQPEPFPALPALGSQGPAKEIMLSKDLGSDFQPPDFRDLLEWEPRIREA 785
Cdd:TIGR02168 567 qnelgRVTFL--PLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 786 FR----TGDLESkPDPSRNFRPYRAEDND-SYASEIKDLQLVLAEAHDSLRGLQEQLSQERQLRkEEADSFNQKMVQLKE 860
Cdd:TIGR02168 645 YRivtlDGDLVR-PGGVITGGSAKTNSSIlERRREIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELE 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 861 DQQRALLRREFELQSLSLQRRLEQKFWSQEkNILVQESQQFKHNFLLLFMKLRWFLKRWRQGKVlpSEEDDFLEVNSmKE 940
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIE--ELEAQIEQLKE-EL 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 941 LYLLMEEEEMNAQHSDNKACTGEswTQNTPNECIKTLADMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELK 1020
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAAN--LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1021 GHasqmeLKAGKGASERpgpdwKAALQREREEQQHLLAESYSAVMELTRQLQLSERHWSQEKLQLvERLQGEKQQVEQQV 1100
Cdd:TIGR02168 877 AL-----LNERASLEEA-----LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL-EGLEVRIDNLQERL 945
|
890
....*....|....*...
gi 257467641 1101 KELQNRLSQLQKAAEPWV 1118
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKI 963
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
208-349 |
2.19e-05 |
|
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: 48.22 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 208 GPGGLVRELEELRSENDYLKDE-------IEELRAEMLEMRDVYMEEdvyqLQELRQQLDQASKTCRILQYRLRKAERRS 280
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEiqklrgqIQQLRTELQELEAQQQEE----AESSREQLQELEEQLATERSARREAEAEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 281 LRAAQTgqvdgelIRGLEQDVKVSKDISMRLHKELEV-VEKKRMRL---------EEENEGLRQRLIETELAKQV----L 346
Cdd:pfam09787 117 ERLQEE-------LRYLEEELRRSKATLQSRIKDREAeIEKLRNQLtsksqssssQSELENRLHQLTETLIQKQTmleaL 189
|
...
gi 257467641 347 QTE 349
Cdd:pfam09787 190 STE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-596 |
2.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQ-LQELRQQLDQASKtcRILQYRLRKAERRSLRAAQTgQVD 290
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQeLEALEAELAELPE--RLEELEERLEELRELEEELE-ELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 291 GELIRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTD 370
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 371 KKP-----------TAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLygDLDAALSAEELADAPhs 439
Cdd:COG4717 250 LLLliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL--PALEELEEEELEELL-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 440 reTELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKDHgggggpEARLAFSSLGGECG-ESLAELRRHLQFVEEE 518
Cdd:COG4717 326 --AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE------ELEQEIAALLAEAGvEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 519 AELLRR---SSAELEDQNKLLLnELAKYRSEHELDVTLSEdscsvlsepSQEELAAAKLQIGELSGKVKKLQYENRVLLS 595
Cdd:COG4717 398 QELKEEleeLEEQLEELLGELE-ELLEALDEEELEEELEE---------LEEELEELEEELEELREELAELEAELEQLEE 467
|
.
gi 257467641 596 N 596
Cdd:COG4717 468 D 468
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-556 |
2.89e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 226 LKDEIEELRAEMLEMRDVYMEEdvyQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGELIRgleqdvkvsk 305
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEA---ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 306 dismRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRprehslkkrgtrslgktdkkptAQEDSADLKCQ 385
Cdd:COG1196 285 ----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE----------------------LEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 386 LHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELAD-APHSRETELKVHLKLVEEEANLLSRRIVE 464
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELlEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 465 LEVENRGLRAEMDDMKdhgggggpEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYR 544
Cdd:COG1196 419 LEEELEELEEALAELE--------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330
....*....|..
gi 257467641 545 SEHELDVTLSED 556
Cdd:COG1196 491 ARLLLLLEAEAD 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
212-481 |
3.27e-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: 48.91 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 212 LVRELEELRSENDYLKDEIEELRAEM--LEMRDVYMEEDVYQLQELRQQLDqasktcrilqyrlrkaerRSLRAAQTGQV 289
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELkeLEARIEELEEDLHKLEEALNDLE------------------ARLSHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 290 DGELiRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETElakqvLQTELDRPREHSLKKRgTRSLGKT 369
Cdd:TIGR02169 797 QAEL-SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-----EQIKSIEKEIENLNGK-KEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 370 DKKPTAQEdsADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEEladaphSRETELKVHLK 449
Cdd:TIGR02169 870 LEELEAAL--RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE------EELSEIEDPKG 941
|
250 260 270
....*....|....*....|....*....|...
gi 257467641 450 -LVEEEANLLSRRIVELEVENrgLRAEMDDMKD 481
Cdd:TIGR02169 942 eDEEIPEEELSLEDVQAELQR--VEEEIRALEP 972
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
998-1115 |
1.75e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 998 LTELQQQFAKAKATWETERAELKGHASQMELKAGKGASERPGPDWK------AALQREREEQQHLLAESYSAVMELTRQL 1071
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQqlraqlAELEAELAELSARYTPNHPDVIALRAQI 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 257467641 1072 QLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAE 1115
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
216-599 |
2.40e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 216 LEELRSENDYLKDEIEELRAEMLEMRDVYM-EEDVY-QLQELRQQLDQASKTCRILQYRLRKAERRSlraaqtgqvdgEL 293
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKrTENIEeLIKEKEKELEEVLREINEISSELPELREEL-----------EK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 294 IRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGK----- 368
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeey 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 369 TDKKPTAQEDSADLKCQLHFAKEEsalmCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHL 448
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 449 KL-----VEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGgggpEARLAFSSL---GGEC------------GESLAEL 508
Cdd:PRK03918 382 TGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIK----ELKKAIEELkkaKGKCpvcgrelteehrKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 509 RRHLQFVEEE----AELLRRSSAELEDQNKLLLNE--LAKYRSEHELDVTLSEDscsvLSEPSQEELAAAKLQIGELSGK 582
Cdd:PRK03918 458 TAELKRIEKElkeiEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEK----LKKYNLEELEKKAEEYEKLKEK 533
|
410
....*....|....*..
gi 257467641 583 VKKLQYENRVLLSNLQR 599
Cdd:PRK03918 534 LIKLKGEIKSLKKELEK 550
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-539 |
2.44e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 192 SASLAFSDLTEEmldcgPGGLVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDvyQLQ------ELRQQLDQASKT 265
Cdd:PRK02224 395 ELRERFGDAPVD-----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAE--ALLeagkcpECGQPVEGSPHV 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 266 CRILQYRLRKAERRSLRA---AQTGQVDGELIRgLEQDVKVSKDISMRLHKE---LEVVEKKRMRLEEENE---GLRQRL 336
Cdd:PRK02224 468 ETIEEDRERVEELEAELEdleEEVEEVEERLER-AEDLVEAEDRIERLEERRedlEELIAERRETIEEKREraeELRERA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 337 IETELAKQVLQTELDRPREHSLKKRGT-----RSLGKTDKKPTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMK 411
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 412 EELLKYRSLYGDLDAALSAEELADAPHSREtELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKdhgggggpEAR 491
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARIEEAREDKE-RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE--------ELR 697
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 257467641 492 lafsslggECGESLAELRRHLQFVEEEAELL----RRSSAELEDQN----KLLLNE 539
Cdd:PRK02224 698 --------ERREALENRVEALEALYDEAEELesmyGDLRAELRQRNvetlERMLNE 745
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
196-531 |
3.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 196 AFSDLTEEMLDCGPGGLVRELEELRSENDYLKDEIEELraemlemrdvymEEDVYQLQELRQQLDQasktcRILQYRLRK 275
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY------------EEQREQARETRDEADE-----VLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 276 AERRSLRAAqtgqvdgelIRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRL------IET-ELAKQVLQT 348
Cdd:PRK02224 251 EELETLEAE---------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadAEAvEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 349 ELDRPREHSLKKRgTRSLGKTDKKPTAQEDSADLKCQLHFAKEESAlmckkltKLAKENDSMKEELLKYRSLYGDLDAAL 428
Cdd:PRK02224 322 RDEELRDRLEECR-VAAQAHNEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 429 SA--EELADAPHSREtELKVHLKLVEEEANLLSRRIVELEVENRGLR---AEMDDMKDHGG--------GGGPEARLAfs 495
Cdd:PRK02224 394 EElrERFGDAPVDLG-NAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAGKcpecgqpvEGSPHVETI-- 470
|
330 340 350
....*....|....*....|....*....|....*.
gi 257467641 496 slgGECGESLAELRRHLQFVEEEAELLRRSSAELED 531
Cdd:PRK02224 471 ---EEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
216-590 |
3.17e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 216 LEELRSENDYLKDEIEELRAEMlEMRDVYMEEDVYQLQELRQQLDQASKTCR---ILQYRLRKAERRSLRAAQTGQvdgE 292
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQI-QRAELELQSTNSELEELQERLDLLKAKASeaeQLRQNLEKQQSSLAEAEQRIK---E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 293 LIRGL---EQDVKVSKDISMRLHK--ELEVvEKKRMR---------------LEEENEGLRQRL---------------- 336
Cdd:pfam05557 175 LEFEIqsqEQDSEIVKNSKSELARipELEK-ELERLRehnkhlnenienkllLKEEVEDLKRKLereekyreeaatlele 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 337 ---IETELA-----------------------KQVLQTELDRPREHSLKKRGTRSLGKT-----DKKPTAQEDSADLKCQ 385
Cdd:pfam05557 254 kekLEQELQswvklaqdtglnlrspedlsrriEQLQQREIVLKEENSSLTSSARQLEKArreleQELAQYLKKIEDLNKK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 386 LHFAKEESALMCKKLTKLAKENDSMKEELLKYRSlygDLDAA----------LSAEELADAPHSRETELKVHLKLVEEEA 455
Cdd:pfam05557 334 LKRHKALVRRLQRRVLLLTKERDGYRAILESYDK---ELTMSnyspqlleriEEAEDMTQKMQAHNEEMEAQLSVAEEEL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 456 NLLSRRIVELEVENRGLRAEMDdmkdhgggggpearlafSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELE----D 531
Cdd:pfam05557 411 GGYKQQAQTLERELQALRQQES-----------------LADPSYSKEEVDSLRRKLETLELERQRLREQKNELEmeleR 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 257467641 532 QNKLLLNELAKYRSEHeldvtLSEDSCSVLSEPSQEELAAAKLQIGELSGKVKKLQYEN 590
Cdd:pfam05557 474 RCLQGDYDPKKTKVLH-----LSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
974-1115 |
4.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 974 IKTLADMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELKGHASQMELKAGKGASERPGPDWKAALQR--ERE 1051
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERleELR 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257467641 1052 EQQHLLAESYSAVMELTRQLQLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAE 1115
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-362 |
6.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKtcrilqyRLRKAERRSLRAAQtgqvdgeL 293
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLEA-------L 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257467641 294 IRGLEQDVKVSKDISMRLHKE----LEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDrprehSLKKRG 362
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-----SLERRK 435
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
209-609 |
6.39e-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: 44.57 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 209 PGGLVRELEELRSENDYLKDEIEELRAEMLEMRDvymeedvyQLQELRQQLDQASKTCRILQyrlRKAERRSLRAAQTGQ 288
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK--------QRASLKEQMQEIQQSFSILT---QCDNRSKEDIPNLQN 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 289 VDGELIRGLEQDVKVSKDISMRLHKELEVVE----KKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGtr 364
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV-- 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 365 slgktdkkptaqedsadlkcqlhfakeesalmcKKLTKLAKENDSMKEELLKYRSLYGDLDaalSAEELADAPHSRETEL 444
Cdd:TIGR00618 670 ---------------------------------LPKELLASRQLALQKMQSEKEQLTYWKE---MLAQCQTLLRELETHI 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 445 KVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKDhgggggpEARLAFSSLGGECGESLAELRRHLQFVEEEAELL-- 522
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-------QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAae 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 523 ----RRSSAELEDQNKLLLNELAKYRSEHELDVTLSEdscsvlsEPSQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQ 598
Cdd:TIGR00618 787 iqffNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC-------ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK 859
|
410
....*....|.
gi 257467641 599 RCDLASCQSTR 609
Cdd:TIGR00618 860 QLAQLTQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
277-599 |
7.19e-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: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 277 ERRSL--RAAQTGQVDGELIRGLEqdvkvskdismrlhkELEVVEKKRMRLEEENEGLRQRL--IETELAK----QVLQT 348
Cdd:TIGR02169 154 ERRKIidEIAGVAEFDRKKEKALE---------------ELEEVEENIERLDLIIDEKRQQLerLRREREKaeryQALLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 349 ELDRPR--EHSLKKRGT-RSLGKTDKKPTAQEDS-ADLKCQLHFAKEESALMCKKLTKLAKE-NDSMKEELLKYRSLYGD 423
Cdd:TIGR02169 219 EKREYEgyELLKEKEALeRQKEAIERQLASLEEElEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 424 LDA---------ALSAEELADApHSRETELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKDhgggggpEARLAF 494
Cdd:TIGR02169 299 LEAeiaslersiAEKERELEDA-EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 495 SSLgGECGESLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYRSE---HELDVTLSEDSCSVLS---EPSQEE 568
Cdd:TIGR02169 371 AEL-EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINELEeekEDKALE 449
|
330 340 350
....*....|....*....|....*....|.
gi 257467641 569 LAAAKLQIGELSGKVKKLQYENRVLLSNLQR 599
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
209-587 |
9.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 209 PGGLVRELEELRSENDYLKDEIEELRAEMLEmrdvyMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQ 288
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGE-----LKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 289 vdgelIRGLEQDVKVSKDISMRLHKELEVVEKKrmrLEEENEGLRQRL-------IETELAKQVLQ------TELDRPRE 355
Cdd:PRK03918 461 -----LKRIEKELKEIEEKERKLRKELRELEKV---LKKESELIKLKElaeqlkeLEEKLKKYNLEelekkaEEYEKLKE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 356 HSLKKRG-TRSLGKTDKKPTAQEDS-ADLKCQLHFAKEESALMCKKLTKLAKEN-DSMKEELLKYRSLYGDLDaalsaeE 432
Cdd:PRK03918 533 KLIKLKGeIKSLKKELEKLEELKKKlAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYL------E 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 433 LADAPHSRETELKvHLKLVEEEANLLSRRIVELEVENRGLRAEMDdmkdhgggggpEARLAFSSLGGE-CGESLAELRRH 511
Cdd:PRK03918 607 LKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELE-----------ELEKKYSEEEYEeLREEYLELSRE 674
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257467641 512 LQFVEEEAELLRRSSAELEDQNKLLLNELAKyRSEHELDVtlsedscsvlsepsqEELAAAKLQIGELSGKVKKLQ 587
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEE-REKAKKEL---------------EKLEKALERVEELREKVKKYK 734
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
28-211 |
1.03e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 28 SHRAPSPaRPKDVAGWSLAkGRRGTGPGSATACGTASSARPDKKGRAVAPGtrGTGPRVAGVRtgvrAKGRPRPGTGPRP 107
Cdd:PHA03307 76 GTEAPAN-ESRSTPTWSLS-TLAPASPAREGSPTPPGPSSPDPPPPTPPPA--SPPPSPAPDL----SEMLRPVGSPGPP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 108 PPPPPSLTDSSSEVSDCASEEARQLGLELALSSDAESAAGGPAGTRTG-QPPQPAQSGQQPPRPPASPDEPSVAASSVGS 186
Cdd:PHA03307 148 PAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPsTPPAAASPRPPRRSSPISASASSPAPAPGRS 227
|
170 180
....*....|....*....|....*
gi 257467641 187 SRLPLSASlAFSDLTEEMLDCGPGG 211
Cdd:PHA03307 228 AADDAGAS-SSDSSSSESSGCGWGP 251
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
251-546 |
1.13e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 251 QLQELRQQLDQASKTcrilqyRLRKAERRSLRAAQTGQVDGELIRGLEQDVKVSKDISM---RLHKELEVVEKK------ 321
Cdd:pfam01576 413 QLQELQARLSESERQ------RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSlesQLQDTQELLQEEtrqkln 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 322 ---RMR-LEEENEGLRQRLIETELAK-------QVLQTELDRPREHSLKKRGTRSLGKTDKKpTAQEDSADLKCQLhfak 390
Cdd:pfam01576 487 lstRLRqLEDERNSLQEQLEEEEEAKrnverqlSTLQAQLSDMKKKLEEDAGTLEALEEGKK-RLQRELEALTQQL---- 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 391 EESALMCKKL----TKLAKENDSMKEELLKYRSLYGDL-------DAALSAEELADAPH----------SRETELKVhLK 449
Cdd:pfam01576 562 EEKAAAYDKLektkNRLQQELDDLLVDLDHQRQLVSNLekkqkkfDQMLAEEKAISARYaeerdraeaeAREKETRA-LS 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 450 LVEEEANLLSRRiVELEVENRGLRAEMDDMkdhgggggpearlafSSLGGECGESLAELRRHLQFVEEEAELLRRSSAEL 529
Cdd:pfam01576 641 LARALEEALEAK-EELERTNKQLRAEMEDL---------------VSSKDDVGKNVHELERSKRALEQQVEEMKTQLEEL 704
|
330
....*....|....*..
gi 257467641 530 EDQnkLLLNELAKYRSE 546
Cdd:pfam01576 705 EDE--LQATEDAKLRLE 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-356 |
1.18e-03 |
|
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: 43.89 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 192 SASLAFSDLTEEMLdcgpgGLVRELEELRSENDYLKDEIEELRAEMLEMRDVyMEEDVYQLQELRQQLDQASKTCRILQY 271
Cdd:TIGR02168 751 QLSKELTELEAEIE-----ELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 272 RLRKAERRSLRAAQTGQVDGELIRGLEQDV-KVSKDIS------MRLHKELEVVEKKRMRLEEENEGLRQRLI------- 337
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIeSLAAEIEeleeliEELESELEALLNERASLEEALALLRSELEelseelr 904
|
170
....*....|....*....
gi 257467641 338 ETELAKQVLQTELDRPREH 356
Cdd:TIGR02168 905 ELESKRSELRRELEELREK 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
211-352 |
1.83e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 211 GLVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVyQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVD 290
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257467641 291 GELIRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDR 352
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
214-436 |
2.66e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEMLEMRDVYME---------EDVY-----QLQELRQQLDQASKTCRILQYRLRKAERR 279
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlgEEEQlrvkeKIGELEAEIASLERSIAEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 280 SLRA--------AQTGQVDGEL------IRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQV 345
Cdd:TIGR02169 324 LAKLeaeidkllAEIEELEREIeeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 346 LQTELDRPREHSLKKRGTRSLGKTDKKpTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLD 425
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
250
....*....|...
gi 257467641 426 AALSA--EELADA 436
Cdd:TIGR02169 483 KELSKlqRELAEA 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
233-522 |
3.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 233 LRAEMLEMRDVY-----MEEDVYQLQELRQQLDQASKTCRILQyRLRKAERRSLRAAQTGQVDGELIRGLEQDvkvskdi 307
Cdd:COG4913 213 VREYMLEEPDTFeaadaLVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLW------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 308 smRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRpREHSLKKRGTRSLgktdkkptaqedsADLKCQLH 387
Cdd:COG4913 285 --FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE-LEAQIRGNGGDRL-------------EQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 388 FAKEESALMCKKLTKLakendsmkEELLkyRSLygDLDAALSAEELAD---APHSRETELKVHLKLVEEEANLLSRRIVE 464
Cdd:COG4913 349 RLERELEERERRRARL--------EALL--AAL--GLPLPASAEEFAAlraEAAALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257467641 465 LEVENRGLRAEMDDMKDHGggggpearlafSSLGGECGESLAELRRHLQFVEEE----AELL 522
Cdd:COG4913 417 LRRELRELEAEIASLERRK-----------SNIPARLLALRDALAEALGLDEAElpfvGELI 467
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
226-481 |
3.93e-03 |
|
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: 41.88 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 226 LKDEIEELRAEMLEMRDVymEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTgQVDGELIRGLEQDVKVSK 305
Cdd:TIGR00618 224 LEKELKHLREALQQTQQS--HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEET-QERINRARKAAPLAAHIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 306 DIS------MRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELdrpREHSLKKRGT-RSLGKTDKKPTAQED 378
Cdd:TIGR00618 301 AVTqieqqaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHeVATSIREISCQQHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 379 SADLKC---QLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELAdapHSRETELKVHlklVEEEA 455
Cdd:TIGR00618 378 TQHIHTlqqQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ---QRYAELCAAA---ITCTA 451
|
250 260
....*....|....*....|....*.
gi 257467641 456 NLLSRRIVELEVENRGLRAEMDDMKD 481
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQT 477
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
814-1109 |
3.99e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 814 SEIKDLQLVLAEAHDSLRGLQEQLS-QERQLRK--EEADSFNQKMVQLKEDQQRallrrefelqSLSLQRRLEQKF---- 886
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKlQDENLKEliEKKDHLTKELEDIKMSLQR----------SMSTQKALEEDLqiat 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 887 -----WSQEKNILVQESQQFK--HNFLLLFMK-----LRWFLKRWRQGkvLPSEEDDF------LEVNSMKELYLLMEEE 948
Cdd:pfam05483 324 kticqLTEEKEAQMEELNKAKaaHSFVVTEFEattcsLEELLRTEQQR--LEKNEDQLkiitmeLQKKSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 949 EMNAQHSDNKACTGESWTQNTPNECIKTLA-DMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELKGHASQME 1027
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1028 LKAGKGASERPGPDwKAALqrereEQQHLLAESYSAVMELTRQLQLSERHWSQEK--LQLVERLQGEKQQVEQQVKELQN 1105
Cdd:pfam05483 482 KEKLKNIELTAHCD-KLLL-----ENKELTQEASDMTLELKKHQEDIINCKKQEErmLKQIENLEEKEMNLRDELESVRE 555
|
....
gi 257467641 1106 RLSQ 1109
Cdd:pfam05483 556 EFIQ 559
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
214-518 |
4.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 214 RELEELRSENDYLKDEIEELRAEMLEMR---DVYMEEDVYQLQELRQQlDQASKTcrilqYRLRKAERR----SLRAAQT 286
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKkadEAKKAEEAKKADEAKKA-EEAKKA-----DEAKKAEEKkkadELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 287 GQvDGELIRGLEQDVKVSKDISMRLHK--ELEVVEKKR----MRLEEEN-----EGLRQRLIETELAKQVLQTELDRPRE 355
Cdd:PTZ00121 1557 LK-KAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARieevMKLYEEEkkmkaEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 356 HSLKKRGTRSLGKTDKKPTAQEDSADLKCQLHFAKEESALMCKKLTKlAKENDSMKEELLKYRSlygdlDAALSAEEL-- 433
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK-AEEDEKKAAEALKKEA-----EEAKKAEELkk 1709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 434 ADAPHSRETElkvHLKLVEEEAnllsrrivELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQ 513
Cdd:PTZ00121 1710 KEAEEKKKAE---ELKKAEEEN--------KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
....*
gi 257467641 514 FVEEE 518
Cdd:PTZ00121 1779 AVIEE 1783
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
294-555 |
5.14e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 294 IRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLietelakQVLQTELDRPREHslkkrgtrsLGKTDKKP 373
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRI-------QLLEEELERTEER---------LAEALEKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 374 TaqedsadlkcQLHFAKEESALMCKKLtklakENDSMKEElLKYRSLYGDLDAALSAEELADAPHS----RETELKVHLK 449
Cdd:pfam00261 67 E----------EAEKAADESERGRKVL-----ENRALKDE-EKMEILEAQLKEAKEIAEEADRKYEevarKLVVVEGDLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 450 LVEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGgggpearlAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAEL 529
Cdd:pfam00261 131 RAEERAELAESKIVELEEELKVVGNNLKSLEASEE--------KASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
250 260 270
....*....|....*....|....*....|.
gi 257467641 530 EDQNKLLLNELAKYRSEH-----ELDVTLSE 555
Cdd:pfam00261 203 EKEVDRLEDELEAEKEKYkaiseELDQTLAE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1115 |
5.90e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 991 LQDERRGLTELQQQFAKAKATWETERAELKGHASQMELKAGKGASErpgpdwKAALQREREEQQHLLAESYSAVMELTRQ 1070
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE------LEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 257467641 1071 LQLSERHWSQEKLQLVERLQgEKQQVEQQVKELQNRLSQLQKAAE 1115
Cdd:COG1196 374 LAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLE 417
|
|
| PCRF |
pfam03462 |
PCRF domain; This domain is found in peptide chain release factors. |
398-492 |
8.03e-03 |
|
PCRF domain; This domain is found in peptide chain release factors.
Pssm-ID: 460929 [Multi-domain] Cd Length: 192 Bit Score: 39.29 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 398 KKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPhsretELKvhlKLVEEEANLLSRRIVELEVENRGL---RA 474
Cdd:pfam03462 22 KRAQKLSKEYSELEPIVEAYREYKQALEDLEEAKELLEDP-----ELA---ELAEEELEELEKRLEELEEELKLLllpKD 93
|
90 100
....*....|....*....|...
gi 257467641 475 EMDDmKD-----HGGGGGPEARL 492
Cdd:pfam03462 94 PNDD-KNaileiRAGAGGDEAAL 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
989-1150 |
8.41e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 989 WLLQDErrgltELQQQFAKAKATWETERAELKGHASQMELKAGKGASERpgpdwkAALQREREEQQHLLAESYSAVMELT 1068
Cdd:COG1196 230 LLLKLR-----ELEAELEELEAELEELEAELEELEAELAELEAELEELR------LELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 1069 RQLQLSERHwsqekLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAEPWVLKHSDMEKQDNSWKEARSEKTHDKEGVSEA 1148
Cdd:COG1196 299 RLEQDIARL-----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
..
gi 257467641 1149 EL 1150
Cdd:COG1196 374 LA 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
452-664 |
8.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 452 EEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEA------RLAFSSLGGECGESLAELRRHLQFVEEEAELLRRS 525
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467641 526 SAELEDQNKLLLNELAKYRSEHELDVTLSEDSCSVLSEpSQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQ------- 598
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-LEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrerea 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257467641 599 --RCDLASCQSTRPMLETDAEAGDSAQCvpaplGETLE--PHAARLCRARE-----AEALPGLREQAALVSKAID 664
Cdd:PRK02224 430 elEATLRTARERVEEAEALLEAGKCPEC-----GQPVEgsPHVETIEEDRErveelEAELEDLEEEVEEVEERLE 499
|
|
| |
