|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
1258-1381 |
1.45e-46 |
|
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: 164.09 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 1258 MDLRWQIHHREKNWNREKVELLERLDNERQEWGRQKEELLWRVEQLQKEKSPRRS------------GSFLCSPREDDNR 1325
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRKinmnerakvidgEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958805815 1326 PYPHQGSLHPSR--PVSMWPCEDTDSIPFEDRPLSKLKESDRCSASENLYLDALSLDD 1381
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
622-714 |
3.36e-42 |
|
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: 149.76 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 622 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQESGWLGDGVSKGPGAS--APLQEELKSARLQIDE 699
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSreAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1958805815 700 LSGKVLKLQCENRLL 714
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
493-587 |
1.67e-37 |
|
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: 136.27 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 493 DSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASI 572
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1958805815 573 LGRKIVELEVENRGL 587
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-648 |
2.04e-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: 72.78 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:TIGR02168 689 LEEKIAELEKALAELRKE-LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DvsvRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQ---ALQNELERLRESSLKRRGSREIYKEKKLVNQDDSADLK 498
Cdd:TIGR02168 768 E---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 499 CQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstreAELKLRLKLVEEEASILGRKIV 578
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------------ALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 579 ELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMEsstELRRHLQFVEEEAELLRRSISEIE 648
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-595 |
1.61e-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: 63.15 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 345 ELDELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDVS 424
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 425 VRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLresslkRRGSREIYKEKKLVNQddsadlkcQLQFA 504
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL------RSKVAQLELQIASLNN--------EIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 505 KEEASLMRKKMAKLGREKDELEQELQKYKSLygDVDSPLPTGEAGgppstrEAELKLRLKLVEEEASILGRKIVELEVEN 584
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEE------LEELQEELERLEEALEELREELEEAEQAL 477
|
250
....*....|.
gi 1958805815 585 RGLKAEMEDIR 595
Cdd:TIGR02168 478 DAAERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-600 |
1.11e-08 |
|
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: 60.47 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 343 KDELDELRAEMEEMrDSYLEEDGYQLQELRRELDRANKNcRILQYRLRKAEQ----KSLKVAETG--QVDGEL------- 409
Cdd:TIGR02169 176 LEELEEVEENIERL-DLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGyellKEKEALERQkeAIERQLasleeel 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 410 -------------IRSLEQDLK-VAKDV-------SVRLHHELETVEEKRAKAEDDNETLRQHM---------IEVEISR 459
Cdd:TIGR02169 254 eklteeiselekrLEEIEQLLEeLNKKIkdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELedaeerlakLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 460 QALQNE-LER-LRESSLKRRGSREIYKEKKLVNQD---DSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKS 534
Cdd:TIGR02169 334 LLAEIEeLEReIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958805815 535 LYGDVDSPLPTGEAggppstREAELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHER 600
Cdd:TIGR02169 414 ELQRLSEELADLNA------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-601 |
1.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:COG1196 258 LEAELAELEAELEELRL--------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQDDSADLKCQL 501
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 502 QFAKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLRLKLVEEEASILGRKIVELE 581
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEE--------------------ALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260
....*....|....*....|
gi 1958805815 582 VENRGLKAEMEDIRVQHERE 601
Cdd:COG1196 470 EEAALLEAALAELLEELAEA 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
340-660 |
4.04e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 340 DYLKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKV 419
Cdd:COG4372 41 DKLQEELEQLREELEQAREE-LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-------LESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 420 AKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQDDS--ADL 497
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 498 KCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPST---REAELKLRLKLVEEEASILG 574
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEellEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 575 RKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQL 654
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
....*.
gi 1958805815 655 THELSK 660
Cdd:COG4372 353 NDVLEL 358
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
340-574 |
9.23e-08 |
|
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: 57.39 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 340 DYLKDELDELRAEMEEM--RDSYLEEDGYQLQELRRELDRankncRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 747 SSLEQEIENVKSELKELeaRIEELEEDLHKLEEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 418 KvakdvsvRLHHELETVEEKRakaeddnETLRQHMIEVEISRQALQNELERLRessLKRRGSREIYKEKKLvnqdDSADL 497
Cdd:TIGR02169 822 N-------RLTLEKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEA----ALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 498 KCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGD--------------VDSPLPTGEAGGPPSTREAELKLRL 563
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElkaklealeeelseIEDPKGEDEEIPEEELSLEDVQAEL 960
|
250
....*....|.
gi 1958805815 564 KLVEEEASILG 574
Cdd:TIGR02169 961 QRVEEEIRALE 971
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-710 |
2.77e-07 |
|
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: 55.84 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 435 EEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQddSADLKcQLQFAKEEASLMRKK 514
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEG--YELLK-EKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 515 MAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASI----------------LGRKIV 578
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaslersiaekereledAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 579 ELEVENRGLKAEMEDIRVQHEREGTSRDHVpgipTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHEL 658
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958805815 659 skfkfEPHQ-ESGWLGDGVSKGPGASAPLQEELKSARLQIDELSGKVLKLQCE 710
Cdd:TIGR02169 402 -----NELKrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-534 |
3.22e-07 |
|
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: 55.50 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDsyleedgyqlqELRRELDRANKNCRILQYRLRKAEqKSLKVAETG------QVD--GELIRSL 413
Cdd:pfam05483 546 LRDELESVREEFIQKGD-----------EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKcnnlkkQIEnkNKNIEEL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 414 EQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQAlQNELERLRESSLkrrgSREIYKEKKLVNQ-- 491
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKL----LEEVEKAKAIADEav 688
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958805815 492 --DDSADLKCQLQFAkEEASLMRKKMAKLGREKDELEQELQKYKS 534
Cdd:pfam05483 689 klQKEIDKRCQHKIA-EMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-767 |
3.43e-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: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 344 DELDELRAEMEEmrdsyleedgyQLQELRRELDRANKNcRILQYRLRKAEQKSLKVAetgqvdgelIRSLEQDLKVAKDV 423
Cdd:COG1196 189 ERLEDILGELER-----------QLEPLERQAEKAERY-RELKEELKELEAELLLLK---------LRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 424 SVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQDDSADLKCQLQF 503
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 504 AKEEASLMRKKMAKLGREKDELEQELQKYKslygdvdsplptgeaggppSTREAELKLRLKLVEEEASILGRKIVELEVE 583
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAE-------------------AELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 584 NRGLKAEMEDIRVQHEREGTSRDHVpgiptspfgdsmessTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSkfkf 663
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALL---------------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAE---- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 664 ephqesgwlgdgvskgpgASAPLQEELKSARLQIDELSGKVLKLQCENRLLLSNAQRCDLAAHLGLRApsprdsdAESDA 743
Cdd:COG1196 450 ------------------EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-------EADYE 504
|
410 420
....*....|....*....|....
gi 1958805815 744 GKKESDGEEGRLPQPKREGPVGGE 767
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-717 |
4.83e-07 |
|
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: 55.03 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRD------SYLEEDGYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKvaetGQVDGELIRSL 413
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTqlnqlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN----NQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 414 EQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNEL-ERLRE-SSLKRRgsREIYKE--KKLV 489
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELeEKQNEiEKLKKE--NQSYKQeiKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 490 NQddSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEaggppsTREAELKLRLKLVEEE 569
Cdd:TIGR04523 391 SQ--INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT------NQDSVKELIIKNLDNT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 570 ASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVpgipTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIED 649
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 650 HNRQLTHELSKFKFephqesgwlgdgvskgpgasaplqeELKSARL--QIDELSGKVLKLQCENRLLLSN 717
Cdd:TIGR04523 539 KISDLEDELNKDDF-------------------------ELKKENLekEIDEKNKEIEELKQTQKSLKKK 583
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-480 |
7.47e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKncrilqyRLRKAEQKSLKVAetgqvdgELIRSLEQDLKVAK 421
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLE-------ALLAALGLPLPASA 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805815 422 DVSVRLHHEletVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRE--SSLKRRGSR 480
Cdd:COG4913 380 EEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiASLERRKSN 437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-654 |
1.24e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 350 RAEMEEMRDSYLEEDGYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHH 429
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 430 ELETVEEKRAKAEDdnetLRQHMIEVEISRQALQNELERLRES-SLKRRGSREIYKEKKLVNQDDSADLKCQLqfAKEEA 508
Cdd:PTZ00121 1666 EAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKKKAEELKKAEEENKIKAEE--AKKEA 1739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 509 SLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEVENRG-- 586
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnl 1819
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958805815 587 ---LKAEMEDIRVQH--EREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFvEEEAELLRRSISEIE--DHNRQL 654
Cdd:PTZ00121 1820 vinDSKEMEDSAIKEvaDSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF-NKEKDLKEDDEEEIEeaDEIEKI 1893
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-601 |
1.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRILQYRLR---------KAEQKSL--KVAETGQVDG--- 407
Cdd:PRK03918 219 LREELEKLEKEVKE-----LEELKEEIEELEKELESLEGSKRKLEEKIReleerieelKKEIEELeeKVKELKELKEkae 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 408 ---ELIRSLEQDLKVAKDVSVRL---HHELETVEEKRAKAEDDNETLRqhmiEVEISRQALQNELERLRESSLKRRGSRE 481
Cdd:PRK03918 294 eyiKLSEFYEEYLDELREIEKRLsrlEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 482 IYKE----KKLVNQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREA 557
Cdd:PRK03918 370 KKEElerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958805815 558 ELKLRLKLVEEEASILGRKIvELEVENRGLKAEMEDIRVQHERE 601
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKE 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-581 |
2.63e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEmeemrdsyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:COG1196 321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRgsreiykEKKLVNQDDSADLKCQL 501
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-------EEEAELEEEEEALLELL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 502 QFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDvdsplptgEAGGPPSTREAELKLRLKLVEEEASILGRKIVELE 581
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD--------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
367-619 |
2.90e-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: 51.69 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 367 QLQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQDLKvakdvsvRLHHELETVEEKRAKAEDDNE 446
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKE--------------EKALLKQLA-------ALERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 447 TLRQHMIEVEISRQALQNELERLREsSLKRRGsREIYKEKK------LVNQDDSAD-------LKCQLQFAKEEASLMRK 513
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKE-ELAELL-RALYRLGRqpplalLLSPEDFLDavrrlqyLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 514 KMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGgpPSTRE---AELKLRLKLVEEEASILGRKIVELEVENRGLKAE 590
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEAL--KAERQkllARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1958805815 591 MEDIRVQHEREGTSRDH------VPGIPTSPFGDS 619
Cdd:COG4942 236 AAAAAERTPAAGFAALKgklpwpVSGRVVRRFGER 270
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
342-543 |
3.38e-06 |
|
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: 50.41 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYLEED-------------GYQLQELRRELDRANKNCRILQYRLRKAEQKS------LKVAE- 401
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEkraekaeaevaalNRRIQLLEEELERTEERLAEALEKLEEAEKAAdesergRKVLEn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 402 TGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSRE 481
Cdd:pfam00261 86 RALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958805815 482 IYKEKKLVNQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPL 543
Cdd:pfam00261 166 KASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
342-600 |
3.56e-06 |
|
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: 52.05 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRdsyleedgYQLQELRRELDRANKNCRILQYRLRKAEQkslkvaetgqvdgeLIRSLEQDLKVAK 421
Cdd:pfam05557 109 LKNELSELRRQIQRAE--------LELQSTNSELEELQERLDLLKAKASEAEQ--------------LRQNLEKQQSSLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVSVRlhheLETVEEKRAKAEDDNETLRQHMIEVEiSRQALQNELERLRESSLKRR---GSREIYKEKKlvnqddsADLK 498
Cdd:pfam05557 167 EAEQR----IKELEFEIQSQEQDSEIVKNSKSELA-RIPELEKELERLREHNKHLNeniENKLLLKEEV-------EDLK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 499 CQLQfaKEEAslMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPP----STREAELKLRLKLVEEEASILG 574
Cdd:pfam05557 235 RKLE--REEK--YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlQQREIVLKEENSSLTSSARQLE 310
|
250 260
....*....|....*....|....*.
gi 1958805815 575 RKIVELEVENRGLKAEMEDIRVQHER 600
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-654 |
9.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYLE--------EDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdGELIRSL 413
Cdd:COG4717 93 LQEELEELEEELEELEAELEElreeleklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 414 EQDLKVAK--------DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKE 485
Cdd:COG4717 169 EAELAELQeeleelleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 486 K----------KLVNQDDSAD---------LKCQLQFAKEEASLMRKKMAKLGREKDEL----------EQELQKYKSLY 536
Cdd:COG4717 249 RlllliaaallALLGLGGSLLsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleeleEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 537 GdVDSPLPTGEAGGPPST-----------REAELKLRLKLVEEEASILG-----------RKIVELEVENRGLKAEMEDI 594
Cdd:COG4717 329 G-LPPDLSPEELLELLDRieelqellreaEELEEELQLEELEQEIAALLaeagvedeeelRAALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 595 RVQHEREGTSRDHVPGIPTspFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQL 654
Cdd:COG4717 408 EEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-531 |
1.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 344 DELDELRAEMEEMRDSY--LEedgyQLQELRRELDRANKNCRILQYRLRKAEqkslkvAETGQVDGELIRSLEQDLKVAK 421
Cdd:COG4913 235 DDLERAHEALEDAREQIelLE----PIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DvsvRLHHELETVEEKRAKAEDDNETLRQHMIEVEISR-QALQNELERLRESSLKRRGSREIYKEK----KLVNQDDSAD 496
Cdd:COG4913 305 A---RLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958805815 497 L-------KCQLQFAKEEASLMRKKMAKLGREKDELEQELQK 531
Cdd:COG4913 382 FaalraeaAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-477 |
1.18e-05 |
|
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: 48.77 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDG---ElIRSLEQDLK 418
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqkE-IESLKRRIS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958805815 419 VAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRR 477
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
330-1100 |
1.90e-05 |
|
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: 49.97 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 330 REMEELRSENDYLKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRankncRILQYRLRKAEQKSLKvaetgqVDGEL 409
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE-----YLLYLDYLKLNEERID------LLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 410 IRSLEQDLKVAKDVSVRLHHELETVEEKR--AKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREiykEKK 487
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENkeEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES---EKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 488 LVNQDDSADLKCQ--LQFAKEEASLMRKKmAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppSTREAELKLRLKL 565
Cdd:pfam02463 323 KKKAEKELKKEKEeiEELEKELKELEIKR-EAEEEEEEELEKLQEKLEQLEEELLAKK---------KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 566 VEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDhvpgiptspfgDSMESSTELRRHLQFVEEEAELLRRSIS 645
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE-----------EEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 646 EIEDHNRQLTHELSKFKFEPHQESGWLGDGVSKGPGASAPLQEELKS-ARLQIDELSGKVLKLQCENRLLLSNAQRCDLA 724
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 725 AHLGLRAPSPRDSDAESDAGKKESDGEEGRlPQPKREGPVGGESDSEDMFEKTSGFGSGKPSEASEPCPTELLRVRED-- 802
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDdk 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 803 TECLVTMKLEAQRLERTVERLISDTDGFIRDSGLrgngsaspgvqgegEGSLNEPHLLETINGRMKAFRKELQAFLEQMS 882
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSL--------------EEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 883 RIVDGLSPLSHLTESSSFLSTVTSVSRDspigtLGKELGPDLQSKLREQLEWQLGQDRGDEREGLRLRATRELHRHadgd 962
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKK-----LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL---- 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 963 SGSHGLGGQSCFNLELRgspVLPEQSVSVEELQGQLQQAARLHQEETETYTNKIRKMEEDHLYALRWKELEMHSLALQNT 1042
Cdd:pfam02463 758 KKEEKEEEKSELSLKEK---ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958805815 1043 LHKRTWSDEKNMLQQELRSLKQNIFLFYVKLRWLLKHWRQGKQMEEGGEDFAESEHPE 1100
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-476 |
2.25e-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: 49.68 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 338 ENDYLKDELDELRAEMEEMRdSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLR-AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805815 418 KVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERL--RESSLKR 476
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVekELSKLQR 490
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
7-290 |
2.59e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 7 PAGGGAPDPKPqPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKdLHTRPATATPSAGRAPTPAAPRSPSLTGKAPPSPG 86
Cdd:PHA03307 152 PPAAGASPAAV-ASDAASSRQAALPLSSPEETARAPSSPPAEPP-PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 87 SPAAPGRLSRRSGVVPGAKD-------KPPPGAGARSAGGAKAAPGTRRATRAGPAEPlsrVGRPAGAEPPPALSKGRKA 159
Cdd:PHA03307 230 DDAGASSSDSSSSESSGCGWgpenecpLPRPAPITLPTRIWEASGWNGPSSRPGPASS---SSSPRERSPSPSPSSPGSG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 160 KRGPGTPPARavvppapaarvpavtlSVTSVAGTRISHTDSSSDLSDCASEPLSDEQRLLPAASSDAESGTGSSDREPLR 239
Cdd:PHA03307 307 PAPSSPRASS----------------SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPR 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958805815 240 GAPTPSSGSRGPPPGSPEPPTLLAA----------------PPVAGACLGGRSS------PGGTPSGSPGPGS 290
Cdd:PHA03307 371 PSRAPSSPAASAGRPTRRRARAAVAgrarrrdatgrfpagrPRPSPLDAGAASGafyaryPLLTPSGEPWPGS 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
337-597 |
2.89e-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: 49.30 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 337 SENDYLKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQD 416
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASR--------KIGEIEKEIEQLEQEEEKLKERLEELEED--------------LSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 417 LKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEIsrQALQNELERLRE---------SSLKRRGSREIYKEKK 487
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEEevsriearlREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 488 LvnQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLRLKLVE 567
Cdd:TIGR02169 831 L--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA--------------------ALRDLESRLGDLK 888
|
250 260 270
....*....|....*....|....*....|
gi 1958805815 568 EEASILGRKIVELEVENRGLKAEMEDIRVQ 597
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
13-317 |
4.88e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 13 PDPKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKDLHTRPATAtpsAGRAPTPAAPRSPSLtgkappsPGSPAAPG 92
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA---AQASSPPQRPRRRAA-------RPTVGSLT 2696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 93 RLSRrsgvvPGAKDKPPPGAGARSAGGAKAAPGTRRATRAGPAEPLSRVGRPAGAEPPPALSKGRKAKRgpgtpparavv 172
Cdd:PHA03247 2697 SLAD-----PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP----------- 2760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 173 ppapaarvpAVTLSVTSVAGTRISHTDSSSDLSDCASEPLSDEQRLLPAASSDAESGTGSSDREP-LRGAPTPSSGSRGP 251
Cdd:PHA03247 2761 ---------PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAaLPPAASPAGPLPPP 2831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958805815 252 PPGSPEPPTLLAAPPVAGACLGGRSSPGGTPS--GSPGPGSQEDVGGRAPPERTILGTPKEPSLGEQP 317
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
342-660 |
5.08e-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: 48.43 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSylEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKsLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:TIGR00618 224 LEKELKHLREALQQTQQS--HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVS------VRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQN---ELERLRESSLKRRGSREIyKEKKLVNQD 492
Cdd:TIGR00618 301 AVTqieqqaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREI-SCQQHTLTQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 493 DSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDvdspLPTGEAGGPPSTREAELKLrlKLVEEEASI 572
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRYAELCA--AAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 573 LGRKIVELEVENRGLKAE------MEDIRVQHEREGTSRDHV---------------------------PGIPTSPF--- 616
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEReqqlqtKEQIHLQETRKKAVVLARllelqeepcplcgscihpnparqdidnPGPLTRRMqrg 533
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958805815 617 -------GDSMESS----TELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSK 660
Cdd:TIGR00618 534 eqtyaqlETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
31-312 |
5.35e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.63 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 31 PLAERRRLHRAPSPARPFLKDLHTRPATATPSAGRAPTPAAPRSPSLTGKAPPSPGSPAAPGRLSRRSGVVPGAKDKPPP 110
Cdd:PHA03307 77 TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 111 gagarsagGAKAAPGTRRATRAGPAEPLSRVGRPAGAEPPPALSKGRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSV 190
Cdd:PHA03307 157 --------ASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 191 AGTRISHTDSS--SDLSDCASEPLSDEQRLLPA-----ASSDAESGTGSSDREPLRGAPTPSSGSRGPPPGSPEPPTLLA 263
Cdd:PHA03307 229 ADDAGASSSDSssSESSGCGWGPENECPLPRPApitlpTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958805815 264 APPVAGACLGGRSSPGGTPSGSPGPGSQEDVGGRAPPERTILGTPKEPS 312
Cdd:PHA03307 309 PSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPP 357
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
342-601 |
5.59e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEM---RDSYLEedgyQLQELRRELDRANKncrilqyrLRKAEQKSLKvaetgqvdgELIRSLEQDLK 418
Cdd:COG1340 27 LKEKRDELNEELKELaekRDELNA----QVKELREEAQELRE--------KRDELNEKVK---------ELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 419 VAKDVSvrlhhelETVEEKRAKAEDDNetlrqhmiEVEISRQALQNELERLRE----SSLKRRGSREIYK-----EKKLV 489
Cdd:COG1340 86 KLNELR-------EELDELRKELAELN--------KAGGSIDKLRKEIERLEWrqqtEVLSPEEEKELVEkikelEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 490 NQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYK----SLYGDVDSplptgeaggppSTREA-------- 557
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHeemiELYKEADE-----------LRKEAdelhkeiv 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958805815 558 ELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHERE 601
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
342-649 |
7.49e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMR-------------DSYLEEDgyqlQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGE 408
Cdd:PRK02224 211 LESELAELDEEIERYEeqreqaretrdeaDEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 409 LIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKkl 488
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 489 vnqddSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPT-----GEAGGPPSTREAELKLRL 563
Cdd:PRK02224 365 -----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElreerDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 564 KLVEEEASIL-------------GRKIVELEVENRG----LKAEMEDIRVQHERegTSRDHvpgiptspfgDSMESSTEL 626
Cdd:PRK02224 440 ERVEEAEALLeagkcpecgqpveGSPHVETIEEDRErveeLEAELEDLEEEVEE--VEERL----------ERAEDLVEA 507
|
330 340
....*....|....*....|...
gi 1958805815 627 RRHLQFVEEEAELLRRSISEIED 649
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRE 530
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
351-711 |
7.95e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 351 AEMEEMRDSYLEEDGYQLQE------LRRELDRANKNCRILQ--------YRLRKAEQKSL-------------KVAETG 403
Cdd:COG5022 734 AALEDMRDAKLDNIATRIQRairgryLRRRYLQALKRIKKIQviqhgfrlRRLVDYELKWRlfiklqpllsllgSRKEYR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 404 QVDgELIRSLEQDLKVAKDVSVRLHHELETVEE-------------KRAKAEDDNETLRQHMIEVEISRQALQNE-LERL 469
Cdd:COG5022 814 SYL-ACIIKLQKTIKREKKLRETEEVEFSLKAEvliqkfgrslkakKRFSLLKKETIYLQSAQRVELAERQLQELkIDVK 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 470 RESSLKRRGSREIYKEKKLVNQDDSaDLKCQLQFaKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeag 549
Cdd:COG5022 893 SISSLKLVNLELESEIIELKKSLSS-DLIENLEF-KTELIARLKKLLNNIDLEEGPSIEYVKLPEL-------------- 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 550 gppstreaelklrLKLVEEEASiLGRKIVELEVENrglkaEMEDIrvqHEREG-TSRDHVPGIPTSPFGDSMEsstelRR 628
Cdd:COG5022 957 -------------NKLHEVESK-LKETSEEYEDLL-----KKSTI---LVREGnKANSELKNFKKELAELSKQ-----YG 1009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 629 HLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK-FEPHQESgwlgdgVSKGPGASAPLQEELKSARLQIDelSGKVLKL 707
Cdd:COG5022 1010 ALQESTKQLKELPVEVAELQSASKIISSESTELSiLKPLQKL------KGLLLLENNQLQARYKALKLRRE--NSLLDDK 1081
|
....
gi 1958805815 708 QCEN 711
Cdd:COG5022 1082 QLYQ 1085
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-551 |
8.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEmrdsyleedgyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGElIRSLEQDLKVAK 421
Cdd:COG4913 615 LEAELAELEEELAE------------AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-IAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVSVrlhhELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQDDSADLKCQL 501
Cdd:COG4913 682 ASSD----DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958805815 502 QFAKEEASLMRKKM--------AKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGP 551
Cdd:COG4913 758 ALGDAVERELRENLeeridalrARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
338-527 |
9.46e-05 |
|
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: 47.43 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 338 ENDYLKDELDELRAE--MEEMRDSYLEEDGYQLQELRRELDRANKN--CRILQYRLRKAEQKSLKVAETgQVDGELIRSL 413
Cdd:pfam17380 390 KNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQRevRRLEEERAREMERVRLEEQER-QQQVERLRQQ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 414 EQDLKVAKDVSVRLHHELETVEEKRAKA-EDDNETLRQHMIEVEISRQALQNELERlRESSLKRRGSREIYKEKKLVNQD 492
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEE-RQKAIYEEERRREAEEERRKQQE 547
|
170 180 190
....*....|....*....|....*....|....*
gi 1958805815 493 DSADLKCQLQFAKeeASLMRKKMAKLGREKDELEQ 527
Cdd:pfam17380 548 MEERRRIQEQMRK--ATEERSRLEAMEREREMMRQ 580
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-662 |
1.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 332 MEELRSENDYLKDELDELRAEMEEMRD--SYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSlKVAETGQVDGEL 409
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK-ELKEIEEKERKL 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 410 IRSLEQDLKVAKDVSvRLHHELETVEEKRAKaeddNETLRQHMIEvEISRQAlqNELERLRESSLKRRG-----SREIYK 484
Cdd:PRK03918 479 RKELRELEKVLKKES-ELIKLKELAEQLKEL----EEKLKKYNLE-ELEKKA--EEYEKLKEKLIKLKGeikslKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 485 EKKLVNQddSADLKCQLQFAKEEASLMRKKMAKLGREK-DELEQELQKYKSLYGDVDsplptgEAGGPPSTREAELKlRL 563
Cdd:PRK03918 551 LEELKKK--LAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYL------ELKDAEKELEREEK-EL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 564 KLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREgtsrdhvpgiptsPFGDSMESSTELRRHLQFVEEEAELLRRS 643
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-------------EYEELREEYLELSRELAGLRAELEELEKR 688
|
330
....*....|....*....
gi 1958805815 644 ISEIEDHNRQLTHELSKFK 662
Cdd:PRK03918 689 REEIKKTLEKLKEELEERE 707
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-598 |
1.58e-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: 47.04 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 350 RAEME-EMRDSYLEedgyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQvdgELIRSLeQDLKVAKDvsvRLH 428
Cdd:pfam15921 592 KAQLEkEINDRRLE-----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS---ERLRAV-KDIKQERD---QLL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 429 HELETVEEKRAKAEDDNETLRQHMI----EVEISRQAL-------QNELERLRESSLKRRGSR------EIYKEKKLVNQ 491
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYEVLKRNFRnkseEMETTTNKLkmqlksaQSELEQTRNTLKSMEGSDghamkvAMGMQKQITAK 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 492 DDSAD-LKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeAGGPPSTREAELKLRLKLVEEEA 570
Cdd:pfam15921 740 RGQIDaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM--------AGELEVLRSQERRLKEKVANMEV 811
|
250 260 270
....*....|....*....|....*....|
gi 1958805815 571 SILGRKIVELEVENRGLKAEMEDIR--VQH 598
Cdd:pfam15921 812 ALDKASLQFAECQDIIQRQEQESVRlkLQH 841
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
330-654 |
2.23e-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: 46.27 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 330 REMEELRSendyLKDELDELRAEMEEMRDSYLEEDGYQLqELRRELDRankncriLQYRLRKAEQKSLKVAETGqVDGEL 409
Cdd:pfam17380 310 REVERRRK----LEEAEKARQAEMDRQAAIYAEQERMAM-ERERELER-------IRQEERKRELERIRQEEIA-MEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 410 IRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISR----QALQNELERLREsslKRRGSREIYKE 485
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRaeqeEARQREVRRLEE---ERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 486 KKLVNQDDSADLKcqlqfaKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeaggppstrEAELKLR-LK 564
Cdd:pfam17380 454 EEQERQQQVERLR------QQEEERKRKKLELEKEKRDRKRAEEQRRKIL--------------------EKELEERkQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 565 LVEEEASilgRKIVELEVENRGLKAEMEDIRVQHEREgtSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRsI 644
Cdd:pfam17380 508 MIEEERK---RKLLEKEMEERQKAIYEEERRREAEEE--RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-I 581
|
330
....*....|
gi 1958805815 645 SEIEDHNRQL 654
Cdd:pfam17380 582 VESEKARAEY 591
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
342-662 |
2.65e-04 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 45.99 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMrdsylEEDGYQLQELrrELDRankncRILQYrlrkaeQKSLKVAEtgqvdgELIRSLeqDLKVAK 421
Cdd:COG4477 227 LPDQLEELKSGYREM-----KEQGYVLEHL--NIEK-----EIEQL------EEQLKEAL------ELLEEL--DLDEAE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVSVRLHHELET---VEEKRAKA----EDDNETLRQHMIEVEISRQALQNELERLRES--------SLKRRGSREIYKEK 486
Cdd:COG4477 281 EELEEIEEEIDElydLLEKEVEAkkyvDKNQEELEEYLEHLKEQNRELKEEIDRVQQSyrlnenelEKVRNLEKQIEELE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 487 KLVNQDDSadlkcqlQFAKEEA--SLMRKKMAKLGREKDELEQELQKY----KSLygdvdsplptgeaggppstREAELK 560
Cdd:COG4477 361 KRYDEIDE-------RIEEEKVaySELQEELEEIEEQLEEIEEEQEEFseklKSL-------------------RKDELE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 561 LRLKLVEeeasilgrkivelevenrgLKAEMEDIRVQHEREgtsrdHVPGIPTSpFGDSMESSTElrrHLQFVEEEAELL 640
Cdd:COG4477 415 AREKLDE-------------------LKKKLREIKRRLEKS-----NLPGLPEE-YLEMFEEASD---EIEELSEELNEV 466
|
330 340
....*....|....*....|..
gi 1958805815 641 RRSISEIEDHNRQLTHELSKFK 662
Cdd:COG4477 467 PLNMDEVNRLLEEAEEDIETLE 488
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
5-318 |
2.88e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.93 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 5 NGPAGGG-----APDPKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPflkdlhtrPATATPSAGRAPTPAAPRSPSLtg 79
Cdd:PHA03307 69 TGPPPGPgteapANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP--------PPPTPPPASPPPSPAPDLSEML-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 80 kappspGSPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAAPGTRRATRAGP---AEPLSRVGRPAGAEPPPALSK- 155
Cdd:PHA03307 139 ------RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSsppAEPPPSTPPAAASPRPPRRSSp 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 156 ------------GRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSVAGTRISHTDSSSdlsdcASEPLSDEQRLLPAAS 223
Cdd:PHA03307 213 isasasspapapGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWE-----ASGWNGPSSRPGPASS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 224 SDAESGTG-----SSDREPLRGAPTPSSGSRGPPPGSPEPPTLLAAPPVAGAclGGRSSPGGTPSGSPGPGSQEDVGG-- 296
Cdd:PHA03307 288 SSSPRERSpspspSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGA--AVSPGPSPSRSPSPSRPPPPADPSsp 365
|
330 340
....*....|....*....|...
gi 1958805815 297 -RAPPERTILGTPKEPSLGEQPR 318
Cdd:PHA03307 366 rKRPRPSRAPSSPAASAGRPTRR 388
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
342-571 |
3.23e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEmRDSYLEEDGYQLQELRRE--------------LDRANKNCRILQyrlRKAE--QKSLKVAEtGQV 405
Cdd:pfam10174 343 LQTEVDALRLRLEE-KESFLNKKTKQLQDLTEEkstlageirdlkdmLDVKERKINVLQ---KKIEnlQEQLRDKD-KQL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 406 DG--ELIRSLEQDlkvakdvSVRLHHELETVEEKRAKAEDDNETLRQhmiEVEISRQALQNELERLRESSlkrrgsrEIY 483
Cdd:pfam10174 418 AGlkERVKSLQTD-------SSNTDTALTTLEEALSEKERIIERLKE---QREREDRERLEELESLKKEN-------KDL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 484 KEKKLVNQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRL 563
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI 560
|
....*...
gi 1958805815 564 KLVEEEAS 571
Cdd:pfam10174 561 RLLEQEVA 568
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-648 |
3.35e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 390 RKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERL 469
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 470 RESSLKRRGSREIYKEkklvnqddsadlkcQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeag 549
Cdd:COG4372 86 NEQLQAAQAELAQAQE--------------ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 550 gppSTREAELK-LRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRR 628
Cdd:COG4372 146 ---AEREEELKeLEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260
....*....|....*....|
gi 1958805815 629 HLQFVEEEAELLRRSISEIE 648
Cdd:COG4372 223 AKDSLEAKLGLALSALLDAL 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
423-720 |
3.52e-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: 45.83 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 423 VSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQDDSADLKCQLQ 502
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 503 FAKEEASLMRKKMAKLGREKDELEQELQKYkslygdvdsplptgeaggppstreaelklRLKLVEEEASILGRKIVELEV 582
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKL-----------------------------EEALNDLEARLSHSRIPEIQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 583 ENRGLKAEMEDIRvqheregtsrdhvpgiptspfgdsmESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 662
Cdd:TIGR02169 799 ELSKLEEEVSRIE-------------------------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805815 663 FEPHQESGWLGDgvskgpgasapLQEELKSARLQIDELSGKVLKLQCENRLL---LSNAQR 720
Cdd:TIGR02169 854 KEIENLNGKKEE-----------LEEELEELEAALRDLESRLGDLKKERDELeaqLRELER 903
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
367-531 |
4.11e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 367 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAE 442
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 443 DDNETLRQHMI-EVEISRQALQN---ELE-RLRE--SSLKRRGSREIYKEKKLV------------NQDDSADL-KCQLQ 502
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRLNEARREQAKAVvslrqiqhratqEKERNQELrRLQDE 638
|
170 180
....*....|....*....|....*....
gi 1958805815 503 FAKEEASLMRKKMAKLGREKDELEQELQK 531
Cdd:pfam07111 639 ARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
342-656 |
5.60e-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: 44.73 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRD-----SYLEEdgyQLQELRRELDRANK---NCRILQYRLRKAEQKSLKVAETGQVDGELIRSL 413
Cdd:pfam05557 202 LEKELERLREHNKHLNEnienkLLLKE---EVEDLKRKLEREEKyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 414 EQdlkvakdvsvrLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKlvnqdd 493
Cdd:pfam05557 279 ED-----------LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV------ 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 494 sADLKCQLQFAKEEASLMR-------KKMA------KLGREKDELEQELQKYKSLYGDVDSPLPTGE--AGG---PPSTR 555
Cdd:pfam05557 342 -RRLQRRVLLLTKERDGYRailesydKELTmsnyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEeeLGGykqQAQTL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 556 EAELKLRLK--------LVEEEASILGRKIVELEVENRGL---KAEMEDIRVQHEREGT---SRDHVPGIPTSPFGDSME 621
Cdd:pfam05557 421 ERELQALRQqesladpsYSKEEVDSLRRKLETLELERQRLreqKNELEMELERRCLQGDydpKKTKVLHLSMNPAAEAYQ 500
|
330 340 350
....*....|....*....|....*....|....*
gi 1958805815 622 SSTELRRHLQfveEEAELLRRSISEIEDHNRQLTH 656
Cdd:pfam05557 501 QRKNQLEKLQ---AEIERLKRLLKKLEDDLEQVLR 532
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
6-308 |
5.90e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 6 GPAGGGAPDPKPQPAGQHHRHHHLHP-LAERRRLHRAPSPAR----PFLKDLHTRPATATPSAGRA------PTPAAPRS 74
Cdd:PHA03307 107 TPPGPSSPDPPPPTPPPASPPPSPAPdLSEMLRPVGSPGPPPaaspPAAGASPAAVASDAASSRQAalplssPEETARAP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 75 PSLTGKAPPSPGSPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAAP----------------GTRRATRAGPAEPL 138
Cdd:PHA03307 187 SSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSsdssssessgcgwgpeNECPLPRPAPITLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 139 SRVGRPAGAEPPPALSKGRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSVAGTRISHTDSSSDLSDcaseplSDEQRL 218
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE------SSRGAA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 219 LPAASSDAESGTGSSDREPLRGAPTPSSGSRGPPPGSPEPPTLLAAPPVAGACLGG----RSSPGGTPSGSPGP-GSQED 293
Cdd:PHA03307 341 VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGrarrRDATGRFPAGRPRPsPLDAG 420
|
330
....*....|....*
gi 1958805815 294 VGGRAPPERTILGTP 308
Cdd:PHA03307 421 AASGAFYARYPLLTP 435
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1-318 |
7.11e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 1 METLNGPAGGGAPDPKPqPAGQHHRHHHLHPLAERrrlhrAPSPARPFLKDLHTRP-ATATPSAGRAP-----TPAAPRS 74
Cdd:PHA03247 2540 LEELASDDAGDPPPPLP-PAAPPAAPDRSVPPPRP-----APRPSEPAVTSRARRPdAPPQSARPRAPvddrgDPRGPAP 2613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 75 PSLTGKAPPSPGSPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAAPgTRRATR----AGPAEPLSRVGRPAG---- 146
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR-PRRARRlgraAQASSPPQRPRRRAArptv 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 147 ------AEPPP----------ALSKGRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSVAGTRISH--TDSSSDLSDCA 208
Cdd:PHA03247 2693 gsltslADPPPppptpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPAPAPP 2772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 209 SEPLSDEQRLL--PAASSDAESGTGSSDREPLRGAPTPSSGSRGPPPGSPEPPTLLAAP----PVAGACLGGRSSPGGTP 282
Cdd:PHA03247 2773 AAPAAGPPRRLtrPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPtsaqPTAPPPPPGPPPPSLPL 2852
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958805815 283 SGSPGPGSqeDVGGRAPPERtilgTPKEPSLGEQPR 318
Cdd:PHA03247 2853 GGSVAPGG--DVRRRPPSRS----PAAKPAAPARPP 2882
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
343-657 |
7.39e-04 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 44.33 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 343 KDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRAnkncRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKD 422
Cdd:COG2770 264 KDEIGELARAFNRMADSLRESIEEAEEEEELAEAEL----ARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 423 VSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREiykekkLVNQDDSADLKCQLQ 502
Cdd:COG2770 340 LLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAAL------AAALLLLELALEELV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 503 FAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEV 582
Cdd:COG2770 414 LALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLE 493
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958805815 583 ENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHE 657
Cdd:COG2770 494 EEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLL 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-1312 |
9.06e-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: 44.28 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 1156 GPLSKQVVENQQLFRALKALLEDFRSELREDEHARLRLQQQYASdkaawdvewavLKCRLEQLEEKTEKSLGELDSSAEG 1235
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-----------LEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 1236 KGALKKEREVHQKLLADSHGLVMDLRWQIHHREKNWNREKVEL------LERLDNERQEWGRQKEELLWRVEQLQKEKSP 1309
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
...
gi 1958805815 1310 RRS 1312
Cdd:TIGR02168 426 LLK 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
426-657 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 426 RLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQnELERLRESSLKRRG-SREIY-KEKKLV----NQDDSADLKC 499
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASaEREIAeLEAELErldaSSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 500 QLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTReAELKLRL------KLVEEEASIL 573
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-ALLEERFaaalgdAVERELRENL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 574 GRKIVELEVENRGLKAEMEDIRVQHEREGTSrdhvpgiPTSPFGDSMESSTELRRHLQFVEEE---------AELLRR-S 643
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAFNREWPA-------ETADLDADLESLPEYLALLDRLEEDglpeyeerfKELLNEnS 844
|
250
....*....|....
gi 1958805815 644 ISEIEDHNRQLTHE 657
Cdd:COG4913 845 IEFVADLLSKLRRA 858
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-585 |
1.18e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 341 YLKDELDELRAEMEEMRDsYLEEdgyQLQELRRELDRANKncRILQYRlrkAEQKSLKVAETGQVDGELIRSLEQDLKVA 420
Cdd:COG3206 161 YLEQNLELRREEARKALE-FLEE---QLPELRKELEEAEA--ALEEFR---QKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 421 KDVSVRLHHELETVEEKRAKAEDDNETLRQHmieveisrQALQNELERLRESSLKRRGSREIYkekklvnQDDSADLKcQ 500
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS--------PVIQQLRAQLAELEAELAELSARY-------TPNHPDVI-A 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 501 LQfaKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLRLKLVEEEASILGRKIVEL 580
Cdd:COG3206 296 LR--AQIAALRAQLQQEAQRILASLEAELEALQA--------------------REASLQAQLAQLEARLAELPELEAEL 353
|
....*
gi 1958805815 581 EVENR 585
Cdd:COG3206 354 RRLER 358
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-531 |
1.52e-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: 43.56 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEmRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEqksLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:pfam05483 592 LENKCNNLKKQIEN-KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE---LELASAKQKFEEIIDNYQKEIEDKK 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 422 DVSVRLHHELEtveekRAKAEDDNETLRQHMIEVEISRQ-----ALQNELERLRESSLKRRGSR-EIYKEKKLVNQDDSA 495
Cdd:pfam05483 668 ISEEKLLEEVE-----KAKAIADEAVKLQKEIDKRCQHKiaemvALMEKHKHQYDKIIEERDSElGLYKNKEQEQSSAKA 742
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958805815 496 DLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQK 531
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
342-470 |
1.57e-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: 43.30 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYL--EEDGYQLQELRRELDRANKNCRILQYRLRKAEQ-------------KSLKVAETGQVD 406
Cdd:pfam06160 303 AEEQNKELKEELERVQQSYTlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayselqeeleeilEQLEEIEEEQEE 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 407 G-ELIRSLEQDLKVAKDVSVRLHHELETVeeKRaKAEDDN-----ETLRQHMIEVEISRQALQNELERLR 470
Cdd:pfam06160 383 FkESLQSLRKDELEAREKLDEFKLELREI--KR-LVEKSNlpglpESYLDYFFDVSDEIEDLADELNEVP 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
337-649 |
2.17e-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: 43.24 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 337 SENDYLKDELDEL-RAEME-EMRDSYLEEdgyQLQELRRELDRANKNCRILQYRLRKAEqkslkvAETGQVDGELIRSLE 414
Cdd:pfam01576 384 SENAELQAELRTLqQAKQDsEHKRKKLEG---QLQELQARLSESERQRAELAEKLSKLQ------SELESVSSLLNEAEG 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 415 QDLKVAKDVSV---RLHHELETV-EEKRAK---------AEDDNETLRQHMIEVEISRQALQNELERLRE--SSLKRR-- 477
Cdd:pfam01576 455 KNIKLSKDVSSlesQLQDTQELLqEETRQKlnlstrlrqLEDERNSLQEQLEEEEEAKRNVERQLSTLQAqlSDMKKKle 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 478 ---GSREIYKEKKLVNQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDV-------DSPLPTGE 547
Cdd:pfam01576 535 edaGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLekkqkkfDQMLAEEK 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 548 AGGPPSTRE---AELKLRLKlvEEEASILGR-------KIVELEVENRGLKAEMEDIRvqheregTSRDhvpgiptspfg 617
Cdd:pfam01576 615 AISARYAEErdrAEAEAREK--ETRALSLARaleealeAKEELERTNKQLRAEMEDLV-------SSKD----------- 674
|
330 340 350
....*....|....*....|....*....|..
gi 1958805815 618 DSMESSTELRRHLQFVEEEAELLRRSISEIED 649
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELED 706
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
430-703 |
2.48e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 430 ELETVEEKRAKAEDDNETL----RQHMIEVEISR-QALQNELERLRESSLKRR-GSREIYKEKKLVNQDDSADLKCQLQF 503
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDMLlvvpRAELLQNRLEEcLQERAELLQAQEAANRQReKEKERYKRDREQWERQRRELESRVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 504 AKEEaslmrkkmakLGREKDELEQELQKYKSLygdVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEVE 583
Cdd:pfam07888 85 LKEE----------LRQSREKHEELEEKYKEL---SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 584 NRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTE---LRRHLQFVEEEAELLRRSISEIED-----HNRQLT 655
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEfqeLRNSLAQRDTQVLQLQDTITTLTQklttaHRKEAE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958805815 656 HELSKFKFEPHQE--------SGWLGDGVSKGPGASAPLQEELKSARLQIDELSGK 703
Cdd:pfam07888 232 NEALLEELRSLQErlnaserkVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-595 |
2.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAE--QKSLKVAEtgqvdgELIRSLEQDLKv 419
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELE------KKLDELEEELA- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 420 akdvsvRLHHELEtvEEKRAKAEDDNETLRQ------HMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQDD 493
Cdd:PRK03918 574 ------ELLKELE--ELGFESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 494 SADLK-CQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeaggppstREaELKLRLKLVEEEASI 572
Cdd:PRK03918 646 RKELEeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR-------------------RE-EIKKTLEKLKEELEE 705
|
250 260
....*....|....*....|...
gi 1958805815 573 LGRKIVELEVENRGLkAEMEDIR 595
Cdd:PRK03918 706 REKAKKELEKLEKAL-ERVEELR 727
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
340-534 |
3.08e-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: 42.53 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 340 DYLKDELDELRAEMEEMrdsylEEDGYQL--QELRRELDRankncrilqyrLRKAEQKSLKVAETGQVDG--ELIRSLEQ 415
Cdd:pfam06160 207 TELPDQLEELKEGYREM-----EEEGYALehLNVDKEIQQ-----------LEEQLEENLALLENLELDEaeEALEEIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 416 DLKvakdvsvRLHHELETveEKRAKAE-DDN-ETLRQHMIEVEISRQALQNELERLRES-------------------SL 474
Cdd:pfam06160 271 RID-------QLYDLLEK--EVDAKKYvEKNlPEIEDYLEHAEEQNKELKEELERVQQSytlnenelervrglekqleEL 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805815 475 KRR--GSREIYKEKKLVN---QDDSADLKCQLQFAKEEASLMRKKMAKLgrEKDELE--QELQKYKS 534
Cdd:pfam06160 342 EKRydEIVERLEEKEVAYselQEELEEILEQLEEIEEEQEEFKESLQSL--RKDELEarEKLDEFKL 406
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
343-703 |
3.24e-03 |
|
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: 42.73 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 343 KDELDELR---AEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLkv 419
Cdd:TIGR00606 244 ENELDPLKnrlKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL-- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 420 akdvsVRLHHELETVEEKR-----AKAEDDNETLRQHM-----------IEVEISRQALQNELERLRES----------- 472
Cdd:TIGR00606 322 -----VDCQRELEKLNKERrllnqEKTELLVEQGRLQLqadrhqehiraRDSLIQSLATRLELDGFERGpfserqiknfh 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 473 SLKRRGSREiykEKKLVNQDdSADLKCQLQFAKEEASLMRKKMAKLGR------EKDELEQELQKYKSLYG--------- 537
Cdd:TIGR00606 397 TLVIERQED---EAKTAAQL-CADLQSKERLKQEQADEIRDEKKGLGRtielkkEILEKKQEELKFVIKELqqlegssdr 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 538 --DVDSPLPTGEAGGPPSTREAE---LKLRLKLVEEEASILGRKIVELEVENRGLKAEME-------------------- 592
Cdd:TIGR00606 473 ilELDQELRKAERELSKAEKNSLtetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTtrtqmemltkdkmdkdeqir 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 593 DIRVQHEREGTSRdhVPGIPTSP-FGDSMESsteLRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQESGW 671
Cdd:TIGR00606 553 KIKSRHSDELTSL--LGYFPNKKqLEDWLHS---KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
410 420 430
....*....|....*....|....*....|....
gi 1958805815 672 LGDGVSKGPGAS--APLQEELKSARLQIDELSGK 703
Cdd:TIGR00606 628 LFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGA 661
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
336-699 |
3.63e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 336 RSENDYLKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRIlQYRLRKAEQKSLKVAETGQvdGELIRSLEQ 415
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQIND-----LESKIQNQEKLNQQKDEQIKKLQQ-EKELLEKEIERLKETIIKN--NSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 416 DLkvakdvsvrlhHELET-VEEKRAKAEDDNETLRQHMIEVEISRQALQN---ELERlRESSLKrrgsrEIYKEKKlvnq 491
Cdd:TIGR04523 448 QD-----------SVKELiIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkELKS-KEKELK-----KLNEEKK---- 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 492 ddsaDLKCQLQFAKEEASLMRKKMAKLGREKDELEQELqkyKSLYGDVDsplptgeaggppstreaELKLRLK--LVEEE 569
Cdd:TIGR04523 507 ----ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDLEDELN-----------------KDDFELKkeNLEKE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 570 ASILGRKIVELEVENRGLKA---EMEDIRVQHEREgtsrdhvpgiptspfgdsmesSTELRRHLQFVEEEAELLRRSISE 646
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKE---------------------KKDLIKEIEEKEKKISSLEKELEK 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958805815 647 IEDHNRQLTHELSKFKFephqesgwlgdgvskgpgASAPLQEELKSARLQIDE 699
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKS------------------KKNKLKQEVKQIKETIKE 656
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-710 |
3.97e-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: 42.35 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 384 ILQYRLRK--AEQKslkvaetgqvdgelIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAE---DDNETLRQHMIEVEIS 458
Cdd:TIGR02168 167 ISKYKERRkeTERK--------------LERTRENLDRLEDILNELERQLKSLERQAEKAErykELKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 459 R-QALQNELERLRESslkrrgsreiykekKLVNQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYG 537
Cdd:TIGR02168 233 RlEELREELEELQEE--------------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 538 DVDSPLPTGEAggppstREAELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHER---EGTSRDHVPGIPTS 614
Cdd:TIGR02168 299 RLEQQKQILRE------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESleaELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 615 PFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKF---------------KFEPHQESGWLGDGVSKG 679
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieellkkleeaeLKELQAELEELEEELEEL 452
|
330 340 350
....*....|....*....|....*....|.
gi 1958805815 680 PGASAPLQEELKSARLQIDELSGKVLKLQCE 710
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1158-1304 |
4.35e-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: 42.35 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 1158 LSKQVVENQQLFRALKALLEDFRSELRE--DEHARLRL--------QQQYASDKAAWDVEWAVLKCRLEQLEEKTEKSLG 1227
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDElrAELTLLNEeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 1228 ELDSSAEGKGALKKEREVHQKLLADSHGLVMDLRWQIH---HREKNWNREKVEL---LERLDNERQEWGRQKEELLWRVE 1301
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEelsEELRELESKRSELrreLEELREKLAQLELRLEGLEVRID 939
|
...
gi 1958805815 1302 QLQ 1304
Cdd:TIGR02168 940 NLQ 942
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
491-758 |
5.14e-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: 41.29 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 491 QDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLRLKLVEEEA 570
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------------ARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 571 SILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDH 650
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 651 NRQLTHELSKfkfephqesgwLGDGVSKGPGASAPLQEELKSARLQIDELSGKVLKLQCENRLLLSNAQRCD--LAAHLG 728
Cdd:COG4942 166 RAELEAERAE-----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEalIARLEA 234
|
250 260 270
....*....|....*....|....*....|
gi 1958805815 729 LRAPSPRDSDAESDAGKKesdgeeGRLPQP 758
Cdd:COG4942 235 EAAAAAERTPAAGFAALK------GKLPWP 258
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
340-596 |
5.16e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 340 DYLKDELDELRAEMEEMrdSYLEEDgyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQV---DGELIRSLEQD 416
Cdd:PRK01156 169 DKLKDVIDMLRAEISNI--DYLEEK---LKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 417 LKVAKDVSVRLHHELETVEEKRAKAEDDNETLR----QHMievEISRQALQNELERLREsSLKRRGSREIYKE-----KK 487
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKeleeRHM---KIINDPVYKNRNYIND-YFKYKNDIENKKQilsniDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 488 LVNQDDSADLKCQ-LQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSplptgeaggPPSTREAELKLRLKLV 566
Cdd:PRK01156 320 EINKYHAIIKKLSvLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIES---------LKKKIEEYSKNIERMS 390
|
250 260 270
....*....|....*....|....*....|
gi 1958805815 567 EEEASILGRKIVELEVenrgLKAEMEDIRV 596
Cdd:PRK01156 391 AFISEILKIQEIDPDA----IKKELNEINV 416
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-470 |
5.33e-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: 41.97 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLR--KAEQKSLK--VAETGQVDGELIRSL-EQD 416
Cdd:TIGR02168 356 LEAELEELEAELEELESR-LEELEEQLETLRSKVAQLELQIASLNNEIErlEARLERLEdrRERLQQEIEELLKKLeEAE 434
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958805815 417 LKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLR 470
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
343-693 |
5.65e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 343 KDELDELRAEMEEMRDSYLEEDGYQ------LQELRRELDRANKNCRILQYRLRKAEqkslkvaETGQVDGELIRSLEQD 416
Cdd:pfam07111 330 RDSVKQLRGQVAELQEQVTSQSQEQailqraLQDKAAEVEVERMSAKGLQMELSRAQ-------EARRRQQQQTASAEEQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 417 LKVA----KDVSVRLHHELETVEEKRAKAEDDNETL-----RQHMIEVEISRQA----------------------LQNE 465
Cdd:pfam07111 403 LKFVvnamSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrKVHTIKGLMARKValaqlrqescpppppappvdadLSLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 466 LERLRESslKRRGSREIYKEKKLVNQddsadlkcQLQFAKEEASLMRKKMAKLGREkdeLEQELQKYKSLYGDVDSPLPT 545
Cdd:pfam07111 483 LEQLREE--RNRLDAELQLSAHLIQQ--------EVGRAREQGEAERQQLSEVAQQ---LEQELQRAQESLASVGQQLEV 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 546 GEAGGPPSTREAElKLRLKLVEEE---ASILGRKIVELEVENR----GLKAEMEDIRVQHEREGTSRDHVPGIPTSpfgd 618
Cdd:pfam07111 550 ARQGQQESTEEAA-SLRQELTQQQeiyGQALQEKVAEVETRLReqlsDTKRRLNEARREQAKAVVSLRQIQHRATQ---- 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 619 SMESSTELRR-HLQFVEEEAELLRRSISEIE-DHN---RQLTHELSKFKFEPHQESGWLGDGVSKGPGASAPLQEELKSA 693
Cdd:pfam07111 625 EKERNQELRRlQDEARKEEGQRLARRVQELErDKNlmlATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASA 704
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-471 |
5.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 340 DYLKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQkslkvaETGQVDGELIRsLEQDLKV 419
Cdd:COG4913 664 ASAEREIAELEAELER-----LDASSDDLAALEEQLEELEAELEELEEELDELKG------EIGRLEKELEQ-AEEELDE 731
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958805815 420 AKDVSVRLHHELETVE----EKRAKAEDDNETLRQHMIEVEISRQALQNELERLRE 471
Cdd:COG4913 732 LQDRLEAAEDLARLELrallEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
342-535 |
6.98e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRD---------SYLEEDGYQLQELRRELDRankncriLQYR-----LRKAEQKSLkVAEtgqvdg 407
Cdd:COG1340 76 LKEERDELNEKLNELREeldelrkelAELNKAGGSIDKLRKEIER-------LEWRqqtevLSPEEEKEL-VEK------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 408 elIRSLEQDLKVAKDvSVRLHHELETVEEKRAKAEDDNETLRQHMieveisrQALQNELERLRESSLKRRGSR-EIYKE- 485
Cdd:COG1340 142 --IKELEKELEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKI-------KELAEEAQELHEEMIELYKEAdELRKEa 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958805815 486 ----KKLVNQDDSAD--------LKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSL 535
Cdd:COG1340 212 delhKEIVEAQEKADelheeiieLQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
342-474 |
8.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 342 LKDELDELRAEMEEMRDSYLEEDGyQLQELRRELdrankncrilqyrlrkAEQKSLKVAETGQVdgelIRSLEQDLKVAK 421
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHP-DVIALRAQI----------------AALRAQLQQEAQRI----LASLEAELEALQ 326
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958805815 422 DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSL 474
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
344-598 |
9.39e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 344 DELDELRAEMEEMRDSYLEEdgyqLQELRrELDRANKN----CRILQYRLRKaeqkslKVAETGQVDGELIRSLEQDLKV 419
Cdd:PRK04778 108 NEIESLLDLIEEDIEQILEE----LQELL-ESEEKNREeveqLKDLYRELRK------SLLANRFSFGPALDELEKQLEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 420 AKDvsvrlhhELETVEEKRA------------KAEDDNETLRQHMIEV-EISRQaLQNEL-ERLREssLKRrGSREiyke 485
Cdd:PRK04778 177 LEE-------EFSQFVELTEsgdyveareildQLEEELAALEQIMEEIpELLKE-LQTELpDQLQE--LKA-GYRE---- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805815 486 kkLVNQD---DSADLKCQLQFAKEEASLMRKKMAKLgrEKDELEQELQ----KYKSLYgdvdsplptgeaggppSTREAE 558
Cdd:PRK04778 242 --LVEEGyhlDHLDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEeiqeRIDQLY----------------DILERE 301
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958805815 559 LKLRlKLVEEEASILGRKIVELEVENRGLKAEMEdiRVQH 598
Cdd:PRK04778 302 VKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEID--RVKQ 338
|
|
| |
