|
Name |
Accession |
Description |
Interval |
E-value |
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
110-632 |
0e+00 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 537.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 110 FLSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPG-LTAKKLLLLQSQLEQLQEENFRLES 188
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtPGGKKYLLLQKQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 189 SREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEER 268
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 269 NAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREA 348
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 349 NEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRL-CQQEAADRERQEELQRHLEEANRAR 427
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 428 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSST-RR 506
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLaQK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 507 IEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPptVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQ 586
Cdd:pfam05622 401 IDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNP--ASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1732634032 587 EEKLLISAWYSMGMALEHRAGEEHAP---AHAQSFLAQQRLATNARRGP 632
Cdd:pfam05622 479 EEKLIVTAWYNMGMALHRKAIEERLAglsSPGQSFLARQRQATNARRGL 527
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-529 |
1.49e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 190 REDDRLRclELEREVAELQ-QRNQAltslsQEAQALKDEmdelrqssERARQLEATLNSCRRRLGELQELRRQVRQLEER 268
Cdd:COG1196 190 RLEDILG--ELERQLEPLErQAEKA-----ERYRELKEE--------LKELEAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 269 NAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfecrnLEEKCDLVTKEKERLLTERDSLREA 348
Cdd:COG1196 255 LEELEAELAELEAELEE---LRLELEELELELEEAQAEEYELLAELAR-------LEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 349 NEELRcAQLQprgLAQADLSLdptpsgLENLAAEILpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARH 428
Cdd:COG1196 325 LAELE-EELE---ELEEELEE------LEEELEEAE-EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 429 GLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTRRIE 508
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340
....*....|....*....|.
gi 1732634032 509 ELQDSLQKKDADLRAMEERYR 529
Cdd:COG1196 474 LLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-526 |
1.12e-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: 71.63 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLR--CLELEREVAELQQrnqALTSLSQEAQALKDEMDELRQSSERA-RQLEATLNSCRRRLGELQELRRQ 261
Cdd:TIGR02168 672 ILERRREIEELEekIEELEEKIAELEK---ALAELRKELEELEEELEQLRKELEELsRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 262 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfecRNLEEKCDLVTKEKERLLTE 341
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR------EALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 342 RDSLREANEELRCAQLQPRGLAQ--ADLSLDptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRH 419
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEqiEELSED-----IESLAAEI--EELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 420 LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEqggktedptlLKRKLEDHLQKLHEadlELQRKREYIEELEPP 499
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEG----------LEVRIDNLQERLSE---EYSLTLEEAEALENK 962
|
330 340 350
....*....|....*....|....*....|..
gi 1732634032 500 TDSSTRRIEELQDSLQKK-----DADLRAMEE 526
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKikelgPVNLAAIEE 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-621 |
4.40e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 320 ECRNLEEKCDLVTKEKERLLTERDSLREANEELRcaqlqpRGLAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLEN 399
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLR------KELEELSRQISALRKDLARLEAEV--EQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 400 KRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGG----KTEDPTLLKRKLEDH 475
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 476 LQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEpkqrpptVVSPE 555
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-------ELESK 909
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732634032 556 FHTLRSQLWERNLRIRQMEMDYEKSR-RRQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQ 621
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
60-86 |
8.24e-12 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 63.42 E-value: 8.24e-12
10 20
....*....|....*....|....*..
gi 1732634032 60 EEYIQRIMTLEESVQHVVMEAIQELMT 86
Cdd:cd22222 121 EEYIQAIMGLEESVQHVVMEAIQELMS 147
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
60-88 |
8.88e-12 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 63.20 E-value: 8.88e-12
10 20
....*....|....*....|....*....
gi 1732634032 60 EEYIQRIMTLEESVQHVVMEAIQELMTKD 88
Cdd:pfam19047 123 QEYIQQIMTLEESVQHVVMTAIQELMSKD 151
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-456 |
2.50e-11 |
|
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: 67.02 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 186 LESSREDDRLRCLELEREVAELQQRNQALTSlsQEAQALKDEMDELrqSSERArQLEATLNSCRRRLGELQELRRQ-VRQ 264
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGEL--EAEIA-SLERSIAEKERELEDAEERLAKlEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 265 LEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 344
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 345 LREANEELRCAQLQPRG-LAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEA 423
Cdd:TIGR02169 411 LQEELQRLSEELADLNAaIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
250 260 270
....*....|....*....|....*....|...
gi 1732634032 424 NRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 456
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-526 |
3.37e-11 |
|
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: 66.63 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 202 REVAELQQRNQALTSLSQEAQALKDEMDELRQsseRARQLEATLNSCRRRLGELQelrRQVRQLEERNAGHAERTRQLEE 281
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN---RLDELSQELSDASRKIGEIE---KEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 282 ELRragSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDlvtkeKERLLTERDSLREANEELRCAQLQPRG 361
Cdd:TIGR02169 745 DLS---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 362 LAQADLSLDptpsgLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQL 441
Cdd:TIGR02169 817 IEQKLNRLT-----LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 442 SELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSstrrIEELQDSLQKKDADL 521
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----LEDVQAELQRVEEEI 967
|
....*
gi 1732634032 522 RAMEE 526
Cdd:TIGR02169 968 RALEP 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-464 |
1.73e-10 |
|
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: 64.31 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQALKDE-MDELRQSSERARQLEATLNSCRRRLGEL-QELRRQVRQLEERNAGHAERT 276
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 277 RQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRcAQ 356
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-NE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 357 LQ--PRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEaadrERQEELQRHLEEANRARHGLEAQQ 434
Cdd:TIGR02168 402 IErlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ----EELERLEEALEELREELEEAEQAL 477
|
250 260 270
....*....|....*....|....*....|
gi 1732634032 435 RLNQQQLSELRAQVEELQKALQEQGGKTED 464
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
60-88 |
4.34e-10 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 58.32 E-value: 4.34e-10
10 20
....*....|....*....|....*....
gi 1732634032 60 EEYIQRIMTLEESVQHVVMEAIQELMTKD 88
Cdd:cd22225 122 QEHIQNIMTLEESVQHVVMTAIQELMSKE 150
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
60-87 |
5.22e-10 |
|
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411798 Cd Length: 150 Bit Score: 58.35 E-value: 5.22e-10
10 20
....*....|....*....|....*...
gi 1732634032 60 EEYIQRIMTLEESVQHVVMEAIQELMTK 87
Cdd:cd22227 123 QEHIQQIMTLEESVQHVVMEAIQELLTK 150
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-563 |
7.43e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSRED-DRLRCL--ELEREVAELQQrnQAltSLSQEAQALKDEMDELrqsserarQLEATLNSCRRRLGELQELRRQ 261
Cdd:TIGR02168 180 KLERTRENlDRLEDIlnELERQLKSLER--QA--EKAERYKELKAELREL--------ELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 262 VRQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTE 341
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEE---LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 342 RDSLREANEELRCAqlqprglaqadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLE 421
Cdd:TIGR02168 325 LEELESKLDELAEE--------------------LAELEEKL--EELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 422 EANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEqggktedptlLKRKLEDHLQKLHEADLElqrkrEYIEELEpptd 501
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----------LQQEIEELLKKLEEAELK-----ELQAELE---- 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732634032 502 sstrRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPkqrpptvvspEFHTLRSQL 563
Cdd:TIGR02168 444 ----ELEEELEELQEELERLEEALEELREELEEAEQALDAAER----------ELAQLQARL 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-526 |
4.21e-09 |
|
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: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 111 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESApgLTAKKLLLLQSQLEQLQEENFRLESSR 190
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL--EAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 191 EDDRLRCLELEREVAELQQRNQALtsLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNA 270
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 271 GHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEK------------WLFECRNLEEKC------DLVT 332
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligVEAAYEAALEAAlaaalqNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 333 KEKERLLTERDSLREAN----EELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC----- 403
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVaarle 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 404 -----------------------------------QQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQV 448
Cdd:COG1196 634 aalrravtlagrlrevtlegeggsaggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732634032 449 EELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQrkrEYIEELEPPTDSSTRRIEELQDSLQKKDA-DLRAMEE 526
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA---LEELPEPPDLEELERELERLEREIEALGPvNLLAIEE 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-533 |
8.41e-09 |
|
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: 58.93 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 220 EAQALKDEMDELRQSSERARQLEATLNSCRRRLGE--LQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQR 297
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerEKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 298 RQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTE------------RDSLREANEELRCAQLQprgLAQA 365
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeleaeiaslERSIAEKERELEDAEER---LAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 366 DLSLDPTPSGLENLAAEI----------------LPAELRETLVRLQ---LENKRLCQQEAADRERQEELQRHLEEANRA 426
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIeeerkrrdklteeyaeLKEELEDLRAELEevdKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 427 RHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTL----LKRKLEDHLQKLHEADLELQRKREYIEELEpptds 502
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALeikkQEWKLEQLAADLSKYEQELYDLKEEYDRVE----- 482
|
330 340 350
....*....|....*....|....*....|.
gi 1732634032 503 stRRIEELQDSLQKKDADLRAMEERYRRYVD 533
Cdd:TIGR02169 483 --KELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-543 |
2.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 336 ERLLTERDSLREANEELRCAQLQPRGLAQadlsldptpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAadRERQEE 415
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-----------IRELAERY--AAARERLAELEYLRAALRLWFA--QRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 416 LQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPtlLKRKLEDHLQKLHEADLELQRKREYIEE 495
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732634032 496 LEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLE 543
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
60-87 |
9.74e-08 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 51.89 E-value: 9.74e-08
10 20
....*....|....*....|....*...
gi 1732634032 60 EEYIQRIMTLEESVQHVVMEAIQELMTK 87
Cdd:cd22226 126 QEYIQTIMMMEESVQHVVMTAIQELMSK 153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-353 |
1.16e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERA-----------------RQLEATLNSCRRRLGELQELRRQ 261
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidvasaereiAELEAELERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 262 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE-KERLLT 340
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEE 773
|
170
....*....|...
gi 1732634032 341 ERDSLREANEELR 353
Cdd:COG4913 774 RIDALRARLNRAE 786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-628 |
4.12e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 187 ESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQAlKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE 266
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 267 ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 346
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 347 EANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKrlcqqeAADRERQEELQRHLEEANRA 426
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK------AEEAKKAEEAKKKAEEAKKA 1472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 427 RhglEAQQRLNQ-QQLSELRAQVEELQKALQEQGGKTEDptllkRKLEDHLQKLHEADL--ELQRKREYIEELEPPTDSS 503
Cdd:PTZ00121 1473 D---EAKKKAEEaKKADEAKKKAEEAKKKADEAKKAAEA-----KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 504 TRRIEELQDSLQ-KKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRR 582
Cdd:PTZ00121 1545 KKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1732634032 583 RQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLATNA 628
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-450 |
5.42e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQsserARQLEATLNSCRRRLgELQELRRQVRQLEERNAGHAERTRQ 278
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAE----LEYLRAALRLWFAQR-RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 279 LEEELRRAGSLRAQLEAQRRQvqelQGQWQEEAmkaekwlfecrnLEEKCDLVTKEKERLLTERDSLREAneelrcaqlq 358
Cdd:COG4913 314 LEARLDALREELDELEAQIRG----NGGDRLEQ------------LEREIERLERELEERERRRARLEAL---------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 359 prgLAQADLSLDPTPSGLENLAaeilpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQ 438
Cdd:COG4913 368 ---LAALGLPLPASAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
250
....*....|..
gi 1732634032 439 QQLSELRAQVEE 450
Cdd:COG4913 440 ARLLALRDALAE 451
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-458 |
6.31e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQaltSLSQEAQALKDEMDELRQSSERARQLE-----ATLNSCRRRLGELQELRRQVRQleernagHA 273
Cdd:PRK04863 848 ELERALADHESQEQ---QQRSQLEQAKEGLSALNRLLPRLNLLAdetlaDRVEEIREQLDEAEEAKRFVQQ-------HG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 274 ERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMK--AEKWLFECRN----------LEEKCDLVTKEKERLLTE 341
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafALTEVVQRRAhfsyedaaemLAKNSDLNEKLRQRLEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 342 RDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLEnkrlcqQEAADRERQEELQRHLE 421
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQE-LKQELQDLGVPADSG------AEERARARRDELHARLS 1070
|
250 260 270
....*....|....*....|....*....|....*..
gi 1732634032 422 EANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQ 458
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-457 |
8.94e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 111 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQnlaQENAALRERVGRSEVESAPGltAKKLLLLQSQLEQLQEENFRLESSR 190
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 191 EDDRLRCLELEREVAELQQR-NQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQ-ELRRQVRQLEER 268
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 269 NaghaERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfECRNLEEKCDLVTKEKERLLTERDSLREA 348
Cdd:TIGR02168 851 S----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 349 NE---------ELRCAQLQPRGLAQADLSLDPTPSGLENLAAEilPAELRETLVRLQLENKRL-------CQQEAADRER 412
Cdd:TIGR02168 924 LAqlelrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKELgpvnlaaIEEYEELKER 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1732634032 413 QEELQRHLEEANRARHGLE-AQQRLNQQQLSELRAQVEELQKALQE 457
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEeAIEEIDREARERFKDTFDQVNENFQR 1047
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-556 |
1.02e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 112 SEEVEEGDHLQQHYLDLERQLLLLSEEKQNlAQENAALRERVGRSEVESAPGLtaKKLLLLQSQLEQLQEENFRLESSRE 191
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 192 DDRLRCLELEREVAELQQRNQALTSLSQEAQALKDE---MDELRQSSERARQLEATLNSCRRRLGELQELRR-------- 260
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenkik 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 261 --QVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfECRNLEEKCDLVTKEKERl 338
Cdd:PTZ00121 1663 aaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKK- 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 339 ltERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRER-QEELQ 417
Cdd:PTZ00121 1738 --EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiIEGGK 1815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 418 RHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQ-------EQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKR 490
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFnknnengEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732634032 491 EYIEELEPPTDSSTRRIEELQDSLQKkdadlramEERYRRYVDKARTVIQTLEPKQRPPTVVSPEF 556
Cdd:PTZ00121 1896 DDIEREIPNNNMAGKNNDIIDDKLDK--------DEYIKRDAEETREEIIKISKKDMCINDFSSKF 1953
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-636 |
1.07e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 190 REDDRLRCLELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLG--ELQELRRQVRQLEE 267
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAE---LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 268 RNAGHAERTRQLEEELRRAG----SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKcdlVTKEKERLLTERD 343
Cdd:COG4913 353 ELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 344 SLREANEELRCAQLQPRGLAQADLSLDPT-----------------------------------PSGLENLAAEILPAEL 388
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVNRLH 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 389 RETLVRLQL--ENKRLCQQEAADR-------------------------------ERQEELQRH--------LEEANRAR 427
Cdd:COG4913 510 LRGRLVYERvrTGLPDPERPRLDPdslagkldfkphpfrawleaelgrrfdyvcvDSPEELRRHpraitragQVKGNGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 428 HGLEAQQRL---------NQQQLSELRAQVEELQKALQEQGGKTEdptllkrKLEDHLQKLHEADLELQRKREYIEELEp 498
Cdd:COG4913 590 HEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLE-------ALEAELDALQERREALQRLAEYSWDEI- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 499 PTDSSTRRIEELQD---SLQKKDADLRAMEERyrryVDKARTVIQTLEpkqrpptvvsPEFHTLRSQLWERNLRIRQMEM 575
Cdd:COG4913 662 DVASAEREIAELEAeleRLDASSDDLAALEEQ----LEELEAELEELE----------EELDELKGEIGRLEKELEQAEE 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634032 576 DYEKSRRRQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFLAQQRLATNARRGPLGRQ 636
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-590 |
1.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALtslsQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGEL----QELRRQVRQLEERNAGHAE 274
Cdd:COG4717 99 ELEEELEELEAELEEL----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerlEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 275 RTRQLEEELRRAG-SLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERlLTERDSLREANEELR 353
Cdd:COG4717 175 LQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 354 CAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQ 433
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 434 QRLNQ--------QQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEpptdSSTR 505
Cdd:COG4717 334 LSPEEllelldriEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE----ELEE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 506 RIEELQDSLQK--KDADLRAMEERYRRYVDKARTVIQTLEpkqrpptvvspefhTLRSQLWERNLRIRQMEMDYEKSRRR 583
Cdd:COG4717 410 QLEELLGELEEllEALDEEELEEELEELEEELEELEEELE--------------ELREELAELEAELEQLEEDGELAELL 475
|
....*..
gi 1732634032 584 QEQEEKL 590
Cdd:COG4717 476 QELEELK 482
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
60-85 |
1.93e-06 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 47.66 E-value: 1.93e-06
10 20
....*....|....*....|....*.
gi 1732634032 60 EEYIQRIMTLEESVQHVVMEAIQELM 85
Cdd:cd22211 119 EEYIARIQQLDESTQAELMLIIQEVL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-594 |
2.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 370 DPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVE 449
Cdd:TIGR02168 666 AKTNSSILERRREI--EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 450 ELQKALQEQGGKTEDptlLKRKLEDHLQKLHEADLELQRKREYIEELEPptdsstrRIEELQDSLQKKDADLRAMEERYR 529
Cdd:TIGR02168 744 QLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732634032 530 RYVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISA 594
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
263-500 |
2.10e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 263 RQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELQGQWQEEAMKAEKwlfecRNLEEKCDLVTKEKERLLTER 342
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 343 DSLREANEELRcAQLQPRGLAQADLSLDPTPSGLENLAAEiLPAELRETLVRLQLENKRLC----QQEAADRERQEELQR 418
Cdd:COG3206 236 AEAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIalraQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 419 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEP 498
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
..
gi 1732634032 499 PT 500
Cdd:COG3206 394 AV 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-450 |
2.16e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 112 SEEVEEGDHLQQhyldlERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQLqeenfRLESSRE 191
Cdd:PTZ00121 1466 AEEAKKADEAKK-----KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK-----KAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 192 DDRLRCLELEREVAELQQ-----RNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE 266
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 267 ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLR 346
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 347 EANEELRCAQLQPRGLAQadlsldptpsglENLAAEILPAELRETLVRLQlenkRLCQQEAADRERQEELQRHLEEANRA 426
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAE------------EKKKAEELKKAEEENKIKAE----EAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
330 340
....*....|....*....|....
gi 1732634032 427 RHGLEAQQRLNQQQLSELRAQVEE 450
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
187-589 |
2.25e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 187 ESSREDDRLRCLELEREVAELQQRNQALTSLSQ----EAQALKDEMDELrqsSERARQLEATLNSCRRRLGELQE----L 258
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 259 RRQVRQLEERNAGHAERTRQLEEELRRAgslRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKER- 337
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEl 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 338 ----------LLTERDSLREAN---EELRCAQL-QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLC 403
Cdd:PRK02224 425 rereaeleatLRTARERVEEAEallEAGKCPECgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 404 QQEAADRERQEELQRHLEEANRARHGLEAQQRLnqqQLSELRAQVEELQKALQEqggKTEDPTLLKRKLEDHLQKLHEAD 483
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRE---RAEELRERAAELEAEAEE---KREAAAEAEEEAEEAREEVAELN 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 484 LELQRKREYIEELEpptdsstrRIEELQDSLQKKDADLRAMEERyrryvdkaRTVIQTLEPKQRpptvvspefhtlrSQL 563
Cdd:PRK02224 579 SKLAELKERIESLE--------RIRTLLAAIADAEDEIERLREK--------REALAELNDERR-------------ERL 629
|
410 420
....*....|....*....|....*.
gi 1732634032 564 WERNLRIRQMEMDYEKSRRRQEQEEK 589
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDK 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-591 |
4.30e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLRCLELEREV--AELQQRNQALTSLSQEAQALKDEMDELRQS--------SERARQLEATLNSCRRRLGE 254
Cdd:COG1196 308 EERRRELEERLEELEEELAEleEELEELEEELEELEEELEEAEEELEEAEAElaeaeealLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 255 LQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKE 334
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 335 KERLLTE-RDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLcQQEAADRERQ 413
Cdd:COG1196 468 LLEEAALlEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 414 EELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQggktEDPTLLKRKLEDHLQKLHEADLELQRKREYI 493
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA----LARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 494 EELEPPT---DSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRpptvvspefhtLRSQLWERNLRI 570
Cdd:COG1196 623 LGRTLVAarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA-----------ELEELAERLAEE 691
|
410 420
....*....|....*....|.
gi 1732634032 571 RQMEMDYEKSRRRQEQEEKLL 591
Cdd:COG1196 692 ELELEEALLAEEEEERELAEA 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
111-531 |
5.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 111 LSEEVEEGDHLQQHYLDLERQLLLLSEEKQNLAQENAALRERVGRSEVESAPGLTAKKLLLLQSQLEQlqeenfrlessr 190
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE------------ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 191 EDDRLRclELEREVAELQQRNQALTSLSQEAQALKDEMDELRQ--SSERARQLEATLNSCRRRLGELQELRRQVRQLEER 268
Cdd:COG4717 144 LPERLE--ELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 269 NAGHAERTRQLEEELRRAGSLRAQLEAQRRQ-----VQELQGQWQEEAMKAEKWL-FECRNLEEKCDLVTKEKERLLTER 342
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLliaaaLLALLGLGGSLLSLILTIAgVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 343 DSLREANEELRCAQLQPRGLAQ--ADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHL 420
Cdd:COG4717 302 KEAEELQALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 421 EEANRARHGLEAQQRLNQ--QQLSELRAQVEELQKALQEQGGKTEDPTL------LKRKLEDHLQKLHEADLELQRKREY 492
Cdd:COG4717 382 EDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLEALDEEELeeeleeLEEELEELEEELEELREELAELEAE 461
|
410 420 430
....*....|....*....|....*....|....*....
gi 1732634032 493 IEELEpptdsSTRRIEELQDSLQKKDADLRAMEERYRRY 531
Cdd:COG4717 462 LEQLE-----EDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-588 |
5.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 387 ELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPT 466
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 467 LlkRKLEDHLQKLHEadlELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQ 546
Cdd:TIGR02169 793 I--PEIQAELSKLEE---EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732634032 547 RPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEE 588
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
213-457 |
1.00e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 213 ALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRL-GELQELRRQVRQLEERNAGHAERTRQLEEELRRagsLRA 291
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALlKQLAALERRIAALARRIRALEQELAALEAELAE---LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 292 QLEAQRRQVQELQGQWQEEAMKAEKwlfecrnleekcdLVTKEKERLLTERDSLREANEELRCAqlqpRGLAQADLSLdp 371
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYR-------------LGRQPPLALLLSPEDFLDAVRRLQYL----KYLAPARREQ-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 372 tpsgLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEEL 451
Cdd:COG4942 152 ----AEELRADL--AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*.
gi 1732634032 452 QKALQE 457
Cdd:COG4942 226 EALIAR 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
219-384 |
1.60e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 219 QEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQ-- 296
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaa 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 297 ---------RRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLV----------------TKEKERLLT-ERDSLREANE 350
Cdd:COG3096 575 eaveqrselRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadsqevtaamqqLLEREREATvERDELAARKQ 654
|
170 180 190
....*....|....*....|....*....|....*
gi 1732634032 351 ELrcaQLQPRGLAQADLSLDPTPSGL-ENLAAEIL 384
Cdd:COG3096 655 AL---ESQIERLSQPGGAEDPRLLALaERLGGVLL 686
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-538 |
1.61e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQALKDEMDELR----QSSERARQLEATLNSCRRRLGE--LQELRRQVRQLEERNAGH 272
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEarieELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 273 AERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEamKAEkwlfecrnLEEKCDLVTKEKERLLTErdslreaneel 352
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--IKS--------IEKEIENLNGKKEELEEE----------- 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 353 rcaqlqprglaqadlsldptpsgLENLAAEIlpAELRETLVRLQlenkrlcqqeaadRERqEELQRHLEEANRARHGLEA 432
Cdd:TIGR02169 870 -----------------------LEELEAAL--RDLESRLGDLK-------------KER-DELEAQLRELERKIEELEA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 433 QQRLNQQQLSELRAQVEELQKALQEQGgktedpTLLKRKLEDHLQKLHEADLELQRKR--EYIEELEPPT-------DSS 503
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE------DPKGEDEEIPEEELSLEDVQAELQRveEEIRALEPVNmlaiqeyEEV 984
|
330 340 350
....*....|....*....|....*....|....*
gi 1732634032 504 TRRIEELQDSLQKKDADLRAMEERYRRYVDKARTV 538
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
137-536 |
1.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 137 EEKQNLAQEnaALRERVGRSEVESAPGLTAKKLLLLQSQLEQLQEENFR-LESSREDDRLRCLELEREVAELQQRNQALT 215
Cdd:PTZ00121 1094 EEAFGKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARkAEEARKAEDAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 216 SLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNA---GHAERTRQLEEELRRAGSLRAQ 292
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 293 LEAQRRQVQELQGQWQ-------EEAMKAEkwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQA 365
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARrqaaikaEEARKAD----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 366 DLSLDPTPSGLENL--AAEILPAELRETLVRLQLENKRlcqQEAADRERQEELQRHLEEANRARHGLEAQQRlnQQQLSE 443
Cdd:PTZ00121 1328 KKKADAAKKKAEEAkkAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 444 LRAQVEELQKALQEQGGKTEdptlLKRKLEDhLQKLHEADLELQRKREyIEELEPPTDSSTRRIEELQDSLQKKDADLRA 523
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADE----AKKKAEE-KKKADEAKKKAEEAKK-ADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
410
....*....|...
gi 1732634032 524 MEERYRRYVDKAR 536
Cdd:PTZ00121 1477 KKAEEAKKADEAK 1489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-588 |
2.35e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDElrqsSERARQ-LEATLNSCRRRLGELQELRRQVR 263
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAE----TEREREeLAEEVRDLRERLEELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 264 QLEERNAGHAERTRQLEEEL-RRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTER 342
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELeDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 343 DSLREANEELRCAqlqprgLAQADLSLDPTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEE 422
Cdd:PRK02224 380 EDRREEIEELEEE------IEELRERFGDAPVDLGNAEDFL--EELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 423 ANRARHGLE----------AQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREY 492
Cdd:PRK02224 452 GKCPECGQPvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 493 IEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERyrryVDKARTVIQTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQ 572
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDE 607
|
410
....*....|....*.
gi 1732634032 573 MEMDYEKSRRRQEQEE 588
Cdd:PRK02224 608 IERLREKREALAELND 623
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
217-590 |
7.01e-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: 46.12 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 217 LSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLE-------------------ERNAGHAERTR 277
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeavleetqerinrarkaAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 278 QLEE-------ELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLE---EKCDLVTKEKERLLTERDSLRE 347
Cdd:TIGR00618 304 QIEQqaqrihtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRdahEVATSIREISCQQHTLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 348 ANEELRCAQLQPRGLAQADLSLDptpsgleNLAAEILPAELRETLVRLQLenKRLCQQEAADRERQEELQRHLEEANRAR 427
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRDLQGQL--AHAKKQQELQQRYAELCAAAITCTAQCE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 428 HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTR-- 505
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRge 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 506 -RIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSPEFHTLRsQLWERNLRIRQMEMDYEKSRRRQ 584
Cdd:TIGR00618 535 qTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACE 613
|
....*.
gi 1732634032 585 EQEEKL 590
Cdd:TIGR00618 614 QHALLR 619
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-591 |
7.94e-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: 45.83 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 381 AEILPAELRETLVRLQLE-NKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRlnqqQLSELRAQVEELQKALQEQG 459
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRRErEKAERYQALLKEKREYEGYELLKEKEALERQKEAIER----QLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 460 GKTEDPTLLKRKLEDHLQKLHEAdlELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVI 539
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732634032 540 QTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLL 591
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
196-527 |
8.84e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 196 RCLELEREVAELQQRNQALTslsQEAQALKDEMDELRQsserARQLEATLNSCRRRLGELQE-LRRQVRQLEERNAGHAE 274
Cdd:COG3096 307 RLVEMARELEELSARESDLE---QDYQAASDHLNLVQT----ALRQQEKIERYQEDLEELTErLEEQEEVVEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 275 RTRQLEEELRRAGSLRAQLEAQRRQVQELQ---GQWQEeamkAEKWLFECRNLEEKCDL-VTKEKERLLTERDSLREANE 350
Cdd:COG3096 380 AEARLEAAEEEVDSLKSQLADYQQALDVQQtraIQYQQ----AVQALEKARALCGLPDLtPENAEDYLAAFRAKEQQATE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 351 ELRCAQlQPRGLAQADLS------------LDPTPSG---------------LENLA--AEILPAELRETLVRLQLEN-- 399
Cdd:COG3096 456 EVLELE-QKLSVADAARRqfekayelvckiAGEVERSqawqtarellrryrsQQALAqrLQQLRAQLAELEQRLRQQQna 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 400 ----KRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQ--------------------KAL 455
Cdd:COG3096 535 erllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRarikelaarapawlaaqdalERL 614
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732634032 456 QEQGGKT-EDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEpptdsstRRIEELQDSLQKKDADLRAMEER 527
Cdd:COG3096 615 REQSGEAlADSQEVTAAMQQLLEREREATVERDELAARKQALE-------SQIERLSQPGGAEDPRLLALAER 680
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
254-353 |
1.02e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 254 ELQELRRQVRQLE-ERNAGHAERTRQLEEelrRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVT 332
Cdd:COG0542 412 ELDELERRLEQLEiEKEALKKEQDEASFE---RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|.
gi 1732634032 333 KEKERLLTERDSLREANEELR 353
Cdd:COG0542 489 ELEKELAELEEELAELAPLLR 509
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
198-564 |
1.24e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.34 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 198 LELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTR 277
Cdd:COG4995 79 ALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 278 QLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQL 357
Cdd:COG4995 159 AAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 358 QPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLN 437
Cdd:COG4995 239 ALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 438 QQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQDSLQKK 517
Cdd:COG4995 319 LLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAA 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1732634032 518 DADLRAMEERYRRYVDKARTVIQTLEPKQRPPTVVSP-EFHTLRSQLW 564
Cdd:COG4995 399 ALLALAAAQLLRLLLAALALLLALAAYAAARLALLALiEYIILPDRLY 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
312-524 |
1.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 312 MKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRET 391
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 392 LVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRlnqqQLSELRAQVEELQKALQEQGGKTEDPTL---- 467
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEeelq 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732634032 468 -LKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAM 524
Cdd:COG4717 196 dLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
184-530 |
1.71e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 184 FRLESSREDDRLRCLELEREVAELqqrNQALTSLSQEAQALKDEMdelrQSSERARQLEATLNSCRRRLGELQE-LRRQV 262
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAEL---NEAESDLEQDYQAASDHL----NLVQTALRQQEKIERYQADLEELEErLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 263 RQLEERNAGHAERTRQLEEELRRAGSLRAQL--------EAQRRQVQELQGQWQEEamKAEKWL----FECRNLEEKCD- 329
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldVQQTRAIQYQQAVQALE--RAKQLCglpdLTADNAEDWLEe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 330 LVTKEKErlLTERdsLREANEELRCAQLQPRGLAQAdLSLdptpsgLENLAAEILPAE----LRETLVRLQlENKRLCQQ 405
Cdd:PRK04863 447 FQAKEQE--ATEE--LLSLEQKLSVAQAAHSQFEQA-YQL------VRKIAGEVSRSEawdvARELLRRLR-EQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 406 EAADRERQEELQRHLEEANRARHGL-EAQQRLN---------QQQLSELRAQVEELQKALQEQGgktEDPTLLKRKLED- 474
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLaEFCKRLGknlddedelEQLQEELEARLESLSESVSEAR---ERRMALRQQLEQl 591
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634032 475 -----HLQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRR 530
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAA 652
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
188-534 |
1.87e-04 |
|
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: 44.96 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 188 SSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEE 267
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 268 RNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLRE 347
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 348 ANEElrcaQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRAR 427
Cdd:pfam02463 812 EEAE----LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 428 --HGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTR 505
Cdd:pfam02463 888 leSKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
330 340
....*....|....*....|....*....
gi 1732634032 506 RIEELQDSLQKKDADLRAMEERYRRYVDK 534
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-567 |
2.08e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLRCLELEREVAELQQRNQALT----SLSQEAQALKDEMDELRqssERARQLEATLNSCRR----RLGELQ 256
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNeeaeSLREDADDLEERAEELR---EEAAELESELEEAREavedRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 257 ELRRQVRQLEERNA-------GHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQwqEEAMKAEKWLFEC-RNLEEKC 328
Cdd:PRK02224 388 ELEEEIEELRERFGdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEE--AEALLEAGKCPECgQPVEGSP 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 329 DLVTKE-----KERLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKR-- 401
Cdd:PRK02224 466 HVETIEedrerVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRer 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 402 -------LCQQEAADRERQEELQRHLEEA---NRARHGL-EAQQRLNQ------------QQLSELRAQVEELQKALQEQ 458
Cdd:PRK02224 546 aaeleaeAEEKREAAAEAEEEAEEAREEVaelNSKLAELkERIESLERirtllaaiadaeDEIERLREKREALAELNDER 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 459 GGKTEDPTLLKRKLEDHLQ--KLHEADLELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKAR 536
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDeaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
410 420 430
....*....|....*....|....*....|.
gi 1732634032 537 TViQTLEPKQRPPTVVSPEFHTLRSQLWERN 567
Cdd:PRK02224 706 RV-EALEALYDEAEELESMYGDLRAELRQRN 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-589 |
2.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSS---ERARQLEATLNSCRRRLGELqELRRQ 261
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGL-TPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 262 VRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQG----------------------QWQEEAMKAEKWLF 319
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleEYTAELKRIEKELK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 320 ECRNLEEKCDLVTKEKERLLTERD---SLREANEELRCAQLQPRGLAQADLSldptpsglenlAAEILPAELRETLVRLQ 396
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESeliKLKELAEQLKELEEKLKKYNLEELE-----------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 397 LENKRLcqqeAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELR-AQVEELQKALQEQGGKTEDPTLLK---RKL 472
Cdd:PRK03918 539 GEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKdaeKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 473 EDHLQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDadlraMEERYRRYVDKARtviqtlepkqrpptvv 552
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE-----YEELREEYLELSR---------------- 673
|
410 420 430
....*....|....*....|....*....|....*..
gi 1732634032 553 spEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEK 589
Cdd:PRK03918 674 --ELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
191-481 |
2.50e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 191 EDDRLRCLELEREVAELQQRNQaltsLSQEAQALKDEMDELRQSSERARQLEATLNS--------------------CRR 250
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ----LAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrqqekierYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 251 RLGELQE-LRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQ---GQWQEeamkAEKWLFECRNLEE 326
Cdd:COG3096 355 DLEELTErLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQtraIQYQQ----AVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 327 KCDL-VTKEKERLLTERDSLREANEELRCAQlQPRGLAQADLS-LDPTPSGLENLAAEILPAELRET---LVRLQLENKR 401
Cdd:COG3096 431 LPDLtPENAEDYLAAFRAKEQQATEEVLELE-QKLSVADAARRqFEKAYELVCKIAGEVERSQAWQTareLLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 402 LCQQEAADRERQEELQRHLEEANRARHGLEA-QQRLNQQ---------QLSELRAQVEELQKALQEQGgktEDPTLLKRK 471
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQldaaeeleeLLAELEAQLEELEEQAAEAV---EQRSELRQQ 586
|
330
....*....|
gi 1732634032 472 LEDHLQKLHE 481
Cdd:COG3096 587 LEQLRARIKE 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
380-543 |
2.74e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 380 AAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRH---LEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQ 456
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 457 EQGGKTED--PTLLKRKLEDHLQKLHEAD--LELQRKREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYV 532
Cdd:COG4942 101 AQKEELAEllRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170
....*....|.
gi 1732634032 533 DKARTVIQTLE 543
Cdd:COG4942 181 AELEEERAALE 191
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
414-526 |
3.54e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 414 EELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKaLQEQGGKTEDPTLLKR--KLEDHLQKLHEADLELQRKRE 491
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNK-LLPQANLLADETLADRleELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1732634032 492 YIEELEP--------PT--DSSTRRIEELQDSLQKKDADLRAMEE 526
Cdd:COG3096 918 ALAQLEPlvavlqsdPEqfEQLQADYLQAKEQQRRLKQQIFALSE 962
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-519 |
5.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQ 264
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 265 LEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDL------VTKEKERL 338
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakaKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 339 LTERD--SLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAaeilpAELRETLVRLQLENKR--LCQQEAADRERQE 414
Cdd:PRK03918 378 KKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI-----KELKKAIEELKKAKGKcpVCGRELTEEHRKE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 415 ELQRHLEEANRarhgLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKrKLEDHLQKLHEADLE-LQRKREYI 493
Cdd:PRK03918 453 LLEEYTAELKR----IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEY 527
|
330 340
....*....|....*....|....*.
gi 1732634032 494 EELEPPTDSSTRRIEELQDSLQKKDA 519
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
229-510 |
7.73e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 229 DELRQSSERARQLEATLnSCRRrlgelqELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQR---------RQ 299
Cdd:PRK04863 273 DYMRHANERRVHLEEAL-ELRR------ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqtaLR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 300 VQELQGQWQEEAMKAEKwlfecrNLEEKCDLVTKEKERLLTERDSLREANEELRCAQ------------LQPRGL----- 362
Cdd:PRK04863 346 QQEKIERYQADLEELEE------RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 363 ------AQADLSLDP-TPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADR------------------------- 410
Cdd:PRK04863 420 vqalerAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlvrkiagevsrseawdvar 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 411 --ERQEELQRHL---EEANRARHGlEAQQRLNQQQlselrAQVEELQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLE 485
Cdd:PRK04863 500 elLRRLREQRHLaeqLQQLRMRLS-ELEQRLRQQQ-----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
330 340
....*....|....*....|....*
gi 1732634032 486 LQRKREYIEELEPPTDSSTRRIEEL 510
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRL 598
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
259-540 |
9.14e-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: 42.42 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 259 RRQVRQLEERNAGHAERTRQLEEelrragSLRAQLEAQRRQVQeLQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERL 338
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEE------AEKARQAEMDRQAA-IYAEQERMAMERERELERIRQEERKRELERIRQEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 339 LTERDSLREAnEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPAELREtlvrlqLENKRLCQQEAadreRQEELQR 418
Cdd:pfam17380 371 AMEISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE------MEQIRAEQEEA----RQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 419 HLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDptllKRKLEDHLQKLHEADLElQRKREYIEElEP 498
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKELE-ERKQAMIEE-ER 513
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1732634032 499 PTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVIQ 540
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
194-309 |
9.15e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 194 RLRcLELEREVAELQQRNQALTSLSQEAQALKDEMDELrqSSERARQLEAtlnscrrrlgELQELRRQVRQLEERNagHA 273
Cdd:COG0542 401 RVR-MEIDSKPEELDELERRLEQLEIEKEALKKEQDEA--SFERLAELRD----------ELAELEEELEALKARW--EA 465
|
90 100 110
....*....|....*....|....*....|....*.
gi 1732634032 274 ERtrqleEELRRAGSLRAQLEAQRRQVQELQGQWQE 309
Cdd:COG0542 466 EK-----ELIEEIQELKEELEQRYGKIPELEKELAE 496
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
199-512 |
1.02e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEaqaLKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERNAGHAERTRQ 278
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNR---SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 279 LEEELRRAGSLRAQLE---AQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTERDSLREANEELRCA 355
Cdd:TIGR00618 637 CSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 356 QLQPRGLAQADLSLDPTPSGLENLAAEILP---AELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEA 432
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKelmHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 433 QQRLNQQQLSELRAQVEE-LQKALQEQGGKTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQ 511
Cdd:TIGR00618 797 DTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
.
gi 1732634032 512 D 512
Cdd:TIGR00618 877 K 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
199-317 |
1.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRnqaLTSLSQEAQALKDEMDELRQS-SERARQLEATLNSCRRRL-GELQELRRQVRQLEERNAGHAERT 276
Cdd:COG3206 274 ELEAELAELSAR---YTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALqAREASLQAQLAQLEARLAELPELE 350
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1732634032 277 RQLEEELRRAGSLRAQLEAQRRQVQELQgqwQEEAMKAEKW 317
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEAR---LAEALTVGNV 388
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
199-520 |
1.84e-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: 41.54 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSER--ARQLEATLNSCRRRLGELQ-----------ELRRQVRQL 265
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQnqisqnnkiisQLNEQISQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 266 E----ERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLTE 341
Cdd:TIGR04523 348 KkeltNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 342 RDSLREANEELrcaQLQPRGLAQADLSLDPTPSGLENLAaEILPAELRETL-----VRLQLENKrlcQQEAADRERQeel 416
Cdd:TIGR04523 428 IERLKETIIKN---NSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSrsinkIKQNLEQK---QKELKSKEKE--- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 417 qrhLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDptlLKRKLEDHLQKLHEADLE--LQRKREYIE 494
Cdd:TIGR04523 498 ---LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDFELKKENLEkeIDEKNKEIE 571
|
330 340
....*....|....*....|....*.
gi 1732634032 495 ELEPPTDSSTRRIEELQDSLQKKDAD 520
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKE 597
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
198-372 |
2.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 198 LELEREVAELQQRNQAltslSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQVRQLEERN-------- 269
Cdd:PRK04863 479 YQLVRKIAGEVSRSEA----WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknldded 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 270 ---AGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKWL----------------FECRNLEEKCDL 330
Cdd:PRK04863 555 eleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLaaqdalarlreqsgeeFEDSQDVTEYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732634032 331 VTKEKERLLT-ERDSLREANEELrcaQLQPRGLAQADLSLDPT 372
Cdd:PRK04863 635 QLLERERELTvERDELAARKQAL---DEEIERLSQPGGSEDPR 674
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
185-534 |
2.30e-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: 41.25 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 185 RLESSREDDRLRCLELEREVAELQQRN----------QALTSLSQEAQALKDEMDELRQSSERARQLEATLNS-CRRRLG 253
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTkfknnkevelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFlLQAREK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 254 ELQELRRQVRQLEERNAGHAERTRQLEEELRRAGSLRAQLEAqrrQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTK 333
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA---HCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 334 EKERLLTERDSLREANEELR--CAQLQPRGLAQAD---LSLDPTPSGLENLAAEILPAELRETLVRLQLENKrlcqqeaa 408
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRdeLESVREEFIQKGDevkCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL-------- 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 409 dRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKlEDHLQKLHEADLelqr 488
Cdd:pfam05483 600 -KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKL---- 673
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1732634032 489 kREYIEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDK 534
Cdd:pfam05483 674 -LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDK 718
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
184-353 |
2.76e-03 |
|
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: 40.88 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 184 FRLESSREDDRLRC-LELEREVAELQQRNQaltslsQEAQALKDEMDELRQSSERARQLEAtlnscRRRLGELQELRRQV 262
Cdd:pfam17380 383 LQMERQQKNERVRQeLEAARKVKILEEERQ------RKIQQQKVEMEQIRAEQEEARQREV-----RRLEEERAREMERV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 263 RQLEERNAGHAERTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEEAMKAEKW-LFECRNLEEKCDLVTKEKERLLTE 341
Cdd:pfam17380 452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQaMIEEERKRKLLEKEMEERQKAIYE 531
|
170
....*....|..
gi 1732634032 342 RDSLREANEELR 353
Cdd:pfam17380 532 EERRREAEEERR 543
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-528 |
2.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 194 RLRCLELEREVAELQQRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNS-------CRRRLGE------LQELRR 260
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvCGRELTEehrkelLEEYTA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 261 QVRQLEERNAGHAERTRQLEEELRRagsLRAQLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEKCDLVTKEKERLLT 340
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRE---LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 341 ERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEILPA-----------------------ELRETLVRLQL 397
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeleerlkelepfyneylELKDAEKELER 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 398 ENKRLCQQEAADRERQEELQRHLEEANRARHGL-EAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHL 476
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELeELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1732634032 477 QKLHEADLELQRKREYIEELEpptdsstRRIEELQDsLQKKDADLRAMEERY 528
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLE-------KALERVEE-LREKVKKYKALLKER 740
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
199-495 |
3.29e-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: 40.54 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQALKDEmdELRQS---SERARQLEATLNSCRRRLGELQELRRQV-RQLEERNAGHAE 274
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQLSD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 275 RTRQLEEElrrAGSLRAQLEAQRRQVQELQGQWQEEAMKAEkwlfECRNLEEKCDLVTKEKERLLTERDSLREANEELRC 354
Cdd:pfam01576 529 MKKKLEED---AGTLEALEEGKKRLQRELEALTQQLEEKAA----AYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 355 AQ------LQPRGLAQADLSLDPTPSGLENLAAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARH 428
Cdd:pfam01576 602 KQkkfdqmLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH 681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732634032 429 GLEAQQRLNQQQLSELRAQVEELQKALQEqggkTEDPTLlkrKLEDHLQKLH-EADLELQRKREYIEE 495
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQA----TEDAKL---RLEVNMQALKaQFERDLQARDEQGEE 742
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
183-591 |
4.56e-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: 40.09 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 183 NFRLESSREDDRLRCLELEREVAELQ-QRNQALTSLSQEAQALKDEMDELRQSSERARQLEATLNSCRRRLGELQELRRQ 261
Cdd:pfam05483 214 HFKLKEDHEKIQHLEEEYKKEINDKEkQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 262 VRQLEERNAGHAERT----RQLEEELRRAGSLRAQL-EAQRRQVQELQGQWQEEAMKAEKWLFECRNLEEkcdLVTKEKE 336
Cdd:pfam05483 294 LTKELEDIKMSLQRSmstqKALEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 337 RLLTERDSLREANEELRCAQLQPRGLAQADLSLDPTPSGLENLAAEilpaelRETLVRlqlENKRLCQQEAADRERQEEL 416
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLD---EKKQFEKIAEELKGKEQEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 417 QRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKL----EDHLQKLHEADLELQRKREY 492
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQED 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 493 IEELEPPTDSSTRRIEELQDSLQKKDADLRAMEERYRRYVDK-----------ARTVIQTLEPKQRPPTVVSPEFHTLRS 561
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkckldkseenARSIEYEVLKKEKQMKILENKCNNLKK 601
|
410 420 430
....*....|....*....|....*....|
gi 1732634032 562 QLWERNLRIRQMEMDYEKSRRRQEQEEKLL 591
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
279-528 |
4.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 279 LEEELRRAGSLRAQLEAQRRQVQELQGQWQEE-AMKAEKWLFECRN-LEEKCDLVTKEKERLLTERDSLREANEElrcaq 356
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQiEEKEEKDLHERLNgLESELAELDEEIERYEEQREQARETRDE----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 357 lqprglaqADLSLD---PTPSGLENLAAEIlpAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEAnRARHGLE-A 432
Cdd:PRK02224 239 --------ADEVLEeheERREELETLEAEI--EDLRETIAETEREREELAEEVRDLRERLEELEEERDDL-LAEAGLDdA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 433 QQRLNQQQLSELRAQVEELQKALQEQggkTEDPTLLKRKLEDHLQKLHEADLELQRKREYIEELEPPTDSSTRRIEELQD 512
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEEC---RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
250
....*....|....*.
gi 1732634032 513 SLQKKDADLRAMEERY 528
Cdd:PRK02224 385 EIEELEEEIEELRERF 400
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
199-537 |
6.77e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 199 ELEREVAELQQRNQALTSLSQEAQ----ALKDEMDELRQSSERARQ-LEATLNSCRRRLGELQELRRQVrqleernagha 273
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEeqlvQANGELEKASREETFARTaLKNARLDLRRLFDEKQSEKDKK----------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 274 erTRQLEEELRRAGSLRAQLEAQRRQVQELQGQWQEE---------AMKAEKWLFECRNLEEKCDLVTKEKERLLTERDS 344
Cdd:pfam12128 670 --NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkrearTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 345 LREANEELRCAQLQPRGL-AQADLSLDptpSGLENLAAEILPAELRETLVR--LQLENKRLCQQEAADRERQEELQRHLE 421
Cdd:pfam12128 748 ELKALETWYKRDLASLGVdPDVIAKLK---REIRTLERKIERIAVRRQEVLryFDWYQETWLQRRPRLATQLSNIERAIS 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 422 EANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEQGGKTEDPTLLKRKLEDHlQKLHEADLELQRKREYIEELEPPTD 501
Cdd:pfam12128 825 ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED-ANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350
....*....|....*....|....*....|....*...
gi 1732634032 502 SSTRRIEELQDSLQKKDADLRAME--ERYRRYVDKART 537
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGlaETWESLREEDHY 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-630 |
7.03e-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: 39.65 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 380 AAEILPAELRETLVRLQLENKRLCQQEAADRERQEELQRHLEEANRARHGLEAQQRLNQQQLSELRAQVEELQKALQEqg 459
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 460 gktedptllkrkledHLQKLHEADLELQRKREYIEELEPptdsstrRIEELQDSLQKKDADLRAMEERYRRYVDKARTVI 539
Cdd:TIGR02168 328 ---------------LESKLDELAEELAELEEKLEELKE-------ELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 540 QTLEPKQRPPTVVSPEFHTLRSQLWERNLRIRQMEMDYEKSRRRQEQEEKLLISAWYSMGMALEHRAGEEHAPAHAQSFL 619
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250
....*....|.
gi 1732634032 620 AQQRLATNARR 630
Cdd:TIGR02168 466 LREELEEAEQA 476
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
184-539 |
8.02e-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: 39.32 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 184 FRLESSRedDRLRCLElerEVAELQQRNqaLTSLSQEAQALKDEMDELRQSSERA----RQLEATLNSCRRRLGELQELR 259
Cdd:pfam05483 261 FLLEESR--DKANQLE---EKTKLQDEN--LKELIEKKDHLTKELEDIKMSLQRSmstqKALEEDLQIATKTICQLTEEK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 260 R-QVRQLEERNAGHAERTRQLE------EELRRAGSLRaqLEAQRRQVQELQGQWQEEAMKAEKWLFECRNLE---EKCD 329
Cdd:pfam05483 334 EaQMEELNKAKAAHSFVVTEFEattcslEELLRTEQQR--LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvelEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 330 LVTKEKERLLTERDSLREANEELRCAQLQPRGLAQA------DLSLDPTPSG---------LENLAAEILPAELRETLV- 393
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihDLEIQLTAIKtseehylkeVEDLKTELEKEKLKNIELt 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 394 ----RLQLENKRLCQQEAadrERQEELQRHLEEANRARHGLE---AQQRLNQQQLSELRAQVEELQKALQEQGG------ 460
Cdd:pfam05483 492 ahcdKLLLENKELTQEAS---DMTLELKKHQEDIINCKKQEErmlKQIENLEEKEMNLRDELESVREEFIQKGDevkckl 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634032 461 -KTEDPTL----------------------LKRKLED---HLQKLHEADLELQRKREY-----------IEELEPPTDSS 503
Cdd:pfam05483 569 dKSEENARsieyevlkkekqmkilenkcnnLKKQIENknkNIEELHQENKALKKKGSAenkqlnayeikVNKLELELASA 648
|
410 420 430
....*....|....*....|....*....|....*.
gi 1732634032 504 TRRIEELQDSLQKKDADLRAMEERYRRYVDKARTVI 539
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
|
| |
