|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
578-785 |
7.52e-104 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 319.02 E-value: 7.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 578 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADM 657
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 658 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 737
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 590122003 738 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLAHSSTLT 785
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-656 |
5.92e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 488
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 489 DLRDRLETANKQLAEKEYEGSEDTRKtISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 568
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 569 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEE 648
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 590122003 649 RILALEAD 656
Cdd:COG1196 472 AALLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-664 |
9.40e-10 |
|
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: 62.78 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 439 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQ 518
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 519 LFAKHKENQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 596
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590122003 597 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnaSEYNAAAlMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-751 |
1.60e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 464 KREALEK--AMRNKLEgeirRMHDFNRDLRDRLETANKQlAEK-----EYEGSEDTRKtISQLFAKHKENQREKEKLEAE 536
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 537 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 616
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 617 LRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 696
Cdd:COG1196 321 LEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 590122003 697 SYDTALEARIQKEEEEILMANKrclDMEGRIKTLHAQIIEKDAMIKVLQQRSRKE 751
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
440-760 |
9.13e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 440 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRDRLETANKQLAEKEYEgseDTRKTISQL 519
Cdd:TIGR02168 171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 520 FAKHKENQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 599
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 600 EQLEHRLRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 679
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEE------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 680 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 759
Cdd:TIGR02168 370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
.
gi 590122003 760 S 760
Cdd:TIGR02168 428 K 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-672 |
5.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 403 PADPF--AMVSRAQQMVEIL-SDENRN--LRQELD-GCYEKVAR-LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK 475
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 476 LEGEIRRMHDFNRDLRDRLETANKqlAEKEYEGSEDTRKTISQLfakhkenQREKEKLEAELatarstnedqrRHIEIRD 555
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEK--LEKEVKELEELKEEIEEL-------EKELESLEGSK-----------RKLEEKI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 556 QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLR---TRLERELESLRIQQRQGNSQPTNAS 632
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLE 341
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 590122003 633 EynaaaLMELLREKEERILALEADMTKWEQ-KYLEENVMRH 672
Cdd:PRK03918 342 E-----LKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
420-667 |
1.11e-04 |
|
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: 45.84 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRDR 493
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 494 LETANKQLAEKEYEGSEDTRKTISQLF------AKHKENQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 559
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 560 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 619
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 590122003 620 QQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKwEQKYLEE 667
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
182-407 |
1.89e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.14 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 182 MSLATSGVKAHPPVTSAPLSP----PQPNDLYKNATSSSEFYKAQGP-PPSQHSLKG----MEHRGPPPEYPFKGVPSQS 252
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPlqpmTQPPPPSQVSPQPLPQPSLHGQmPPMPHSLQTgpshMQHPVPPQPFPLTPQSSQS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 253 VVCKSQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARAtqdisSLSLSARNSQPHSPTSSL-TAGASSLPLLQSPPS 331
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPA-----PLSMPHIKPPPTTPIPQLpNPQSHKHPPHLSGPS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 332 -----TRLPPGQHL-----VSNQGDHSAHLSRHQqhlLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRA--QQSASY 399
Cdd:pfam03154 383 pfqmnSNLPPPPALkplssLSTHHPPSAHPPPLQ---LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSglHQVPSQ 459
|
....*...
gi 590122003 400 QPMPADPF 407
Cdd:pfam03154 460 SPFPQHPF 467
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
436-617 |
8.47e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 38.49 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 436 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrdrletANKQLAEKEYEGSEDTRKT 515
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 516 ISQLFAKHKE-NQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 577
Cdd:cd07596 66 LSKLGKAAEElSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 590122003 578 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
425-749 |
9.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 425 RNLRQELDGCYEKVARLqkvETEIQRVSEAYENLvkssskREALekAMRNKLEGEIRRMHDfnRDLRDRLETANKQLAEk 504
Cdd:PRK04863 840 RQLNRRRVELERALADH---ESQEQQQRSQLEQA------KEGL--SALNRLLPRLNLLAD--ETLADRVEEIREQLDE- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 505 eyegSEDTRKTISQlfakhkeNQREKEKLEAELATARSTNED----QRRHIEIrDQALSNAQAKVVKLEEELKKKQVYvd 580
Cdd:PRK04863 906 ----AEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQfeqlKQDYQQA-QQTQRDAKQQAFALTEVVQRRAHF-- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 581 kveKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQRQGNSQptnASEYNA--AALMELLREKEERILALEADMT 658
Cdd:PRK04863 972 ---SYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQ---LAQYNQvlASLKSSYDAKRQMLQELKQELQ 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 659 KWEQKYLEENVMRhfaldaaatVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKD 738
Cdd:PRK04863 1045 DLGVPADSGAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
330
....*....|.
gi 590122003 739 AMIKVLQQRSR 749
Cdd:PRK04863 1116 AGWCAVLRLVK 1126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
578-785 |
7.52e-104 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 319.02 E-value: 7.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 578 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADM 657
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 658 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 737
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 590122003 738 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLAHSSTLT 785
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-656 |
5.92e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 488
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 489 DLRDRLETANKQLAEKEYEGSEDTRKtISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 568
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 569 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEE 648
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 590122003 649 RILALEAD 656
Cdd:COG1196 472 AALLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-664 |
9.40e-10 |
|
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: 62.78 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 439 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQ 518
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 519 LFAKHKENQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 596
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590122003 597 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnaSEYNAAAlMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-751 |
1.60e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 464 KREALEK--AMRNKLEgeirRMHDFNRDLRDRLETANKQlAEK-----EYEGSEDTRKtISQLFAKHKENQREKEKLEAE 536
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 537 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 616
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 617 LRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 696
Cdd:COG1196 321 LEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 590122003 697 SYDTALEARIQKEEEEILMANKrclDMEGRIKTLHAQIIEKDAMIKVLQQRSRKE 751
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-663 |
1.74e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 483
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 484 HDFNRDLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 563
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 564 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQGNSQpTNASEYNAAALM 640
Cdd:TIGR02168 839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEELSEE-LRELESKRSELR 914
|
250 260
....*....|....*....|...
gi 590122003 641 ELLREKEERILALEADMTKWEQK 663
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-664 |
2.93e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLR 491
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 492 DRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEE 571
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 572 LKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynAAALMELLREKEERIL 651
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAARLL 494
|
250
....*....|...
gi 590122003 652 ALEADMTKWEQKY 664
Cdd:COG1196 495 LLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
440-760 |
9.13e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 440 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRDRLETANKQLAEKEYEgseDTRKTISQL 519
Cdd:TIGR02168 171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 520 FAKHKENQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 599
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 600 EQLEHRLRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 679
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEE------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 680 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 759
Cdd:TIGR02168 370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
.
gi 590122003 760 S 760
Cdd:TIGR02168 428 K 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-667 |
1.09e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 407 FAMVSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDf 486
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA- 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 487 nRDLRDRLETANKQLAEKEYEGSEdTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVV 566
Cdd:TIGR02169 787 -RLSHSRIPEIQAELSKLEEEVSR-IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 567 KLEEELKKKQVYVDKVEK------------------MQQALVQLQAACEKREQLEHRLRTRLERELESLR-IQQRQGNSQ 627
Cdd:TIGR02169 865 ELEEELEELEAALRDLESrlgdlkkerdeleaqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDE 944
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 590122003 628 PTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-625 |
1.36e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 405 DPFAMVSRAQQMVEILSDENRnLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 480
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 481 RRmhdfnrdLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQ-REKEKLEAELATARSTNEDQRRHIEIRDQALS 559
Cdd:COG4913 298 EE-------LRAELARLEAELERLE-ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 590122003 560 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 625
Cdd:COG4913 370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
498-668 |
5.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 498 NKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 575
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 576 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT---NASEYNAAALMELLREKEERILA 652
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 590122003 653 LEADMTKWEQKYLEEN 668
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-672 |
5.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 403 PADPF--AMVSRAQQMVEIL-SDENRN--LRQELD-GCYEKVAR-LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK 475
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 476 LEGEIRRMHDFNRDLRDRLETANKqlAEKEYEGSEDTRKTISQLfakhkenQREKEKLEAELatarstnedqrRHIEIRD 555
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEK--LEKEVKELEELKEEIEEL-------EKELESLEGSK-----------RKLEEKI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 556 QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLR---TRLERELESLRIQQRQGNSQPTNAS 632
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLE 341
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 590122003 633 EynaaaLMELLREKEERILALEADMTKWEQ-KYLEENVMRH 672
Cdd:PRK03918 342 E-----LKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
439-663 |
2.00e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 439 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRDRLETANKQLAEKEYEGSEdtrktisq 518
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYLRAA-------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 519 lfAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 598
Cdd:COG4913 281 --LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590122003 599 REqlehRLRTRLERELESLriqqrqGNSQPTNASEY--NAAALMELLREKEERILALEADMTKWEQK 663
Cdd:COG4913 357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
429-608 |
3.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 429 QELDGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRDRLETANKQLAE--K 504
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 505 EYEGSEDTRKTISQLFAKHKENQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 583
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 590122003 584 KMQQALVQLQAACEKREQLEHRLRT 608
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-666 |
4.83e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 426 NLRQELDGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMR--NKLEGEIRRMHDFNRDLRDRLETANKQLAE 503
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 504 KeyegSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 583
Cdd:TIGR02168 748 R----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 584 KMQQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNASEYNAAALMELLREKEERI 650
Cdd:TIGR02168 824 ERLESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*.
gi 590122003 651 LALEADMTKWEQKYLE 666
Cdd:TIGR02168 904 RELESKRSELRRELEE 919
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
441-659 |
1.67e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 441 LQKVETEIQRVSEAYENlVKS--SSKREALEKamrnkLEGEIRRMHDfnRDLRDRLETANKQLAE-----KEYEGSED-- 511
Cdd:PRK02224 161 LGKLEEYRERASDARLG-VERvlSDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 512 --TRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQAL 589
Cdd:PRK02224 233 reTRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDD 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 590 VQLQAACEKREQLEHRlRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTK 659
Cdd:PRK02224 307 ADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
351-629 |
2.47e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 351 LSRHQQHLLSSQSHQGdHYRHAQASLTSAQQQPGeaysAMPRAQQSASyqpmpadpfAMVSRAQQMVEILSDENRNLRQE 430
Cdd:PRK04863 399 LADYQQALDVQQTRAI-QYQQAVQALERAKQLCG----LPDLTADNAE---------DWLEEFQAKEQEATEELLSLEQK 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 431 LD------GCYEKVARL-QKVETEIQRvSEAY----ENLVKSSSKREALEK--AMRNKLeGEIRRMHDFNRDLRDRLETA 497
Cdd:PRK04863 465 LSvaqaahSQFEQAYQLvRKIAGEVSR-SEAWdvarELLRRLREQRHLAEQlqQLRMRL-SELEQRLRQQQRAERLLAEF 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 498 NKQLaEKEYEGSEDtrktisqLFAKHKENQREKEKLEAELATARSTNEDQRRHIE----------IRDQALSNAQAKVVK 567
Cdd:PRK04863 543 CKRL-GKNLDDEDE-------LEQLQEELEARLESLSESVSEARERRMALRQQLEqlqariqrlaARAPAWLAAQDALAR 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590122003 568 LEE----ELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLriQQRQGNSQPT 629
Cdd:PRK04863 615 LREqsgeEFEDSQ---DVTEYMQQLLERERELTVERDELAAR-KQALDEEIERL--SQPGGSEDPR 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
420-656 |
2.66e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 420 LSDENRNLRQELDGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 485
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 486 FNRDLRDRLETANK-QLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 564
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 565 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNASEYnaaa 638
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 590122003 639 lmelLREKEERILALEAD 656
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
420-617 |
5.00e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKS------------SSKREALEKAMRNKLE-----GEIRR 482
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesveelEERLKELEPFYNEYLElkdaeKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 483 MHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQLFAK-----HKENQREKEKLEAELATARSTNEDQRRHieiRDQA 557
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKR---REEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 558 LSNAQakvvKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:PRK03918 693 KKTLE----KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
421-623 |
8.61e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 421 SDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQ 500
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 501 LAEKEYEGSEDTR---KTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 577
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 590122003 578 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 623
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
440-623 |
8.75e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 440 RLQKVETEIQRVseayenlvkssskrealeKAMRNKLEGEIrrmhdfnRDLRDRLETANKQLAEKEyEGSEDTRKTISQL 519
Cdd:COG1579 11 DLQELDSELDRL------------------EHRLKELPAEL-------AELEDELAALEARLEAAK-TELEDLEKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 520 FAKHKENQREKEKLEAELATARSTNEdqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKR 599
Cdd:COG1579 65 ELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....
gi 590122003 600 EQLEHRLRTRLERELESLRIQQRQ 623
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE 160
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
418-658 |
1.49e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 418 EILSDENRNLRQELDGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRDRL 494
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 495 ETANKQL--AEKEYEGSEDTR---KTISQLFAKHKENQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 555
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 556 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRLRTRLER-ELESLRIQQRQGNS 626
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIAERRETiEEKRERAEELRERA 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 590122003 627 QPTNAS----EYNAAALMELLREKEERILALEADMT 658
Cdd:PRK02224 547 AELEAEaeekREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-564 |
2.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 422 DENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 488
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590122003 489 DLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAK 564
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
414-765 |
3.39e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 414 QQMVEILSDENRNLRQELDGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 482
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 483 MHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKE-------------KLEAELATARSTNEDQRR 549
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 550 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT 629
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 630 NASEYNAAALMELLREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 708
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 590122003 709 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 765
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-612 |
5.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklEGEIRRmhdfNRDLR 491
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAE----LEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 492 DRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATArstnEDQRRHIEIRDQALSNAQAKVVKLEEE 571
Cdd:COG4913 678 ERLDASSDDLAALE-EQLEELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 590122003 572 LKKKQVYVDKVEK-MQQALV-QLQAACEKREQLEHRLRTRLER 612
Cdd:COG4913 753 ERFAAALGDAVEReLRENLEeRIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-752 |
5.86e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 427 LRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKE 505
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 506 YEGSEDtRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 585
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 586 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnaseynAAALMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 665 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 744
Cdd:TIGR02168 424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497
|
....*...
gi 590122003 745 QQRSRKEP 752
Cdd:TIGR02168 498 QENLEGFS 505
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
445-552 |
7.85e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 445 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHK 524
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE 466
|
90 100 110
....*....|....*....|....*....|
gi 590122003 525 ENQREKE--KLEAELATARSTNEDQRRHIE 552
Cdd:COG2433 467 ISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
420-667 |
1.11e-04 |
|
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: 45.84 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRDR 493
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 494 LETANKQLAEKEYEGSEDTRKTISQLF------AKHKENQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 559
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 560 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 619
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 590122003 620 QQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKwEQKYLEE 667
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
464-762 |
1.25e-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: 45.73 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 464 KREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKT------ISQLFAKHKENQREKEKLEAEL 537
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllyLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 538 ATARSTNEDQRRHIEIRDQALSNA--QAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRL----- 610
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENkeEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKaekel 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 611 -ERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTV 689
Cdd:pfam02463 331 kKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 590122003 690 ISHSPNTSYDTALEariQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 762
Cdd:pfam02463 411 LELARQLEDLLKEE---KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
182-407 |
1.89e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.14 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 182 MSLATSGVKAHPPVTSAPLSP----PQPNDLYKNATSSSEFYKAQGP-PPSQHSLKG----MEHRGPPPEYPFKGVPSQS 252
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPlqpmTQPPPPSQVSPQPLPQPSLHGQmPPMPHSLQTgpshMQHPVPPQPFPLTPQSSQS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 253 VVCKSQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARAtqdisSLSLSARNSQPHSPTSSL-TAGASSLPLLQSPPS 331
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPA-----PLSMPHIKPPPTTPIPQLpNPQSHKHPPHLSGPS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 332 -----TRLPPGQHL-----VSNQGDHSAHLSRHQqhlLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRA--QQSASY 399
Cdd:pfam03154 383 pfqmnSNLPPPPALkplssLSTHHPPSAHPPPLQ---LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSglHQVPSQ 459
|
....*...
gi 590122003 400 QPMPADPF 407
Cdd:pfam03154 460 SPFPQHPF 467
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
413-654 |
2.03e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 413 AQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIR------RMHDF 486
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 487 N---RDLRDRLETANKQLAEKEYEGSEDTRKTIsqlfakhKENQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 563
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 564 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQ-QRQGNSQPTNASEYNAAALMEL 642
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAKlERQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|..
gi 590122003 643 LREKEERILALE 654
Cdd:COG5185 531 RARGYAHILALE 542
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
197-409 |
3.73e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 197 SAPLSPPQPNDLYKNATSSSEFYKAQGPPPSQHSLKG--------------MEHRGPPPEYPfkGVPSQSVVCKSQEPgh 262
Cdd:pfam03154 143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGaasppsppppgttqAATAGPTPSAP--SVPPQGSPATSQPP-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 263 fysehrlNQPGRTEGQLMRYQHPPEYGAARAtqdisslslsarnSQPHSPTSSLTAGA-----SSLPLLQSPPSTRLPPG 337
Cdd:pfam03154 219 -------NQTQSTAAPHTLIQQTPTLHPQRL-------------PSPHPPLQPMTQPPppsqvSPQPLPQPSLHGQMPPM 278
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 590122003 338 QHLVSNQGDHSAHLSRHQQHLLSSQSHQGD--HYRHAQASLTSAQQQPGEAYSAMPRAQQSASYQPMPADPFAM 409
Cdd:pfam03154 279 PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM 352
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
510-808 |
5.25e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 510 EDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 585
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 586 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQ 662
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 663 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 742
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590122003 743 VLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLAHSSTLTGAPIMEEKRDDKSWKGSLGKEKE 808
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
413-617 |
1.16e-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: 42.85 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 413 AQQMVEILSDENRNLRQEldgcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 491
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 492 DRLETANKQLAEKEYE------GSEDTRKTISQLFAKHKENQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 558
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 590122003 559 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 617
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
447-664 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 447 EIQRVSEAY-ENLVKSS--SKREALEKAmRNKLEGEIRRmhdfnrdLRDRLETANKQLAE--KEY------EGSEDTRKT 515
Cdd:COG3206 149 LAAAVANALaEAYLEQNleLRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfrQKNglvdlsEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 516 ISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIE--IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQL 592
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 590122003 593 QAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnASEYNAAALMelLREKEERILALEADMTKWEQKY 664
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
412-614 |
1.69e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREAL---------EKAMRNKLEGEIRR 482
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 483 MHDFNR-------DLRDRLETANKQLAEKEYEGSEDTRkTISQLFAKHKENQREKEKLEAELATARSTNEDqrrhIEIRD 555
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 590122003 556 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL 614
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-762 |
1.76e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 415 QMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRDR 493
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 494 LEtankqlaekEYEGSEDTRktisqlfakhkenqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 573
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 574 KKQVYVDKVEKMQQALVQlqaacEKREQLEHRLRtRLERELESLRIQQRQGNSQPTNA-SEYNaaALMELLREKEERILA 652
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVK-----EKIGELEAEIA-SLERSIAEKERELEDAEERLAKLeAEID--KLLAEIEELEREIEE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 653 LEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR- 726
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELAd 424
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 590122003 727 ----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 762
Cdd:TIGR02169 425 lnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
372-507 |
1.96e-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: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 372 AQASLTSAQQQPGEAYSAMPRAQQSASYQPMPADPFAMVSRAQQMVEILSDEN---RNLRQELDgcyekvARLQKVETEI 448
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIA------ALRAQLQQEA 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 590122003 449 QRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRdRLEtANKQLAEKEYE 507
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR-RLE-REVEVARELYE 368
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-649 |
2.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 439 ARLQKVETEIQRVSEAYENLvksssKREALEKAMRNKLEGEIRRMH---DFNRDLRDRLETANKQLAEKEYEGSEDTR-- 513
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKL-----RKELRELEKVLKKESELIKLKelaEQLKELEEKLKKYNLEELEKKAEEYEKLKek 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 514 ---------------KTISQLFAKHKENQREKEKLEAELA-------------------TARSTNEDQRRHIEIRD--QA 557
Cdd:PRK03918 534 liklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAellkeleelgfesveeleeRLKELEPFYNEYLELKDaeKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 558 LSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACEKREQLEHR----LRTRLERELESLRIQQRQGNSQptnaS 632
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKrLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKR----R 689
|
250
....*....|....*..
gi 590122003 633 EYNAAALMELLREKEER 649
Cdd:PRK03918 690 EEIKKTLEKLKEELEER 706
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
488-659 |
2.31e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 488 RDLRDRLETANKQLAEKEyegsedtrKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 567
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 568 LEEELKK-KQVYVDKVEKMQ----QALVQLQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQpTNASEYNA 636
Cdd:COG4942 95 LRAELEAqKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAAL-RAELEAER 173
|
170 180
....*....|....*....|...
gi 590122003 637 AALMELLREKEERILALEADMTK 659
Cdd:COG4942 174 AELEALLAELEEERAALEALKAE 196
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-600 |
2.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQ-RVSEAYENLVKSSSKR-EALEKAMRNkLEGEIRRMhdfnRD 489
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReELDELEAQIRGNGGDRlEQLEREIER-LERELEER----ER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 490 LRDRLETANKQLAEKEYEGSEDtrktisqlFAkhkENQREKEKLEAELATARSTNEDQRRHIEirdQALSNAQAKVVKLE 569
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEE--------FA---ALRAEAAALLEALEEELEALEEALAEAE---AALRDLRRELRELE 425
|
170 180 190
....*....|....*....|....*....|....
gi 590122003 570 EE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 600
Cdd:COG4913 426 AEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
410-694 |
3.10e-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: 41.26 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVE-------TEIQRVSEAY--------------ENLVKSSSKREaL 468
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 469 EKAMRNKLEGEIRRMHDF----------NRDLRDRLETANKQ-LAEKEYEGSEDTRKTISQLFAKHKENQREKEkleael 537
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 538 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 606
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 607 RTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 686
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 590122003 687 TTVISHSP 694
Cdd:pfam17380 595 TPITTIKP 602
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
511-667 |
4.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 511 DTRktISQLFAKHKENQREKEKLEAELATARSTnedqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALV 590
Cdd:COG1579 16 DSE--LDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590122003 591 QLQAAcekREQlehrlrTRLERELESLRIQQRQgnsqptnaSEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:COG1579 84 NVRNN---KEY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
582-757 |
4.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 582 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWE 661
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 662 QKyleenvmrhfaldaAATVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 741
Cdd:COG1579 80 EQ--------------LGNVRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170
....*....|....*.
gi 590122003 742 KVLQQRSRKEPSKTEQ 757
Cdd:COG1579 141 EEKKAELDEELAELEA 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-592 |
4.70e-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: 40.77 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 414 QQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDL 490
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 491 RDRLETANKQLAEKEYEGSEDTR-KTISQLfaKH-----KENQREKEKLEAELATARStneDQRRHIEIRDQALSNAQAK 564
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKnKEIEEL--KQtqkslKKKQEEKQELIDQKEKEKK---DLIKEIEEKEKKISSLEKE 618
|
170 180
....*....|....*....|....*...
gi 590122003 565 VVKLEEELKKKQVYVDKVEKMQQALVQL 592
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-571 |
5.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 410 VSRAQQMVEILSDENRNLRQELDGCYEKVA-----RLQKVETEIQRVSEAYENLvksSSKREALEKAMRN---KLEGEIR 481
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERELEER---ERRRARLEALLAAlglPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 482 RMHDFNRDLRDRLETANKQLAEkeyegsedTRKTISQLFAKHKENQREKEKLEAELA--TARSTNEDQRRHiEIRD---Q 556
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIAslERRKSNIPARLL-ALRDalaE 451
|
170 180
....*....|....*....|...
gi 590122003 557 ALSNAQAKV--------VKLEEE 571
Cdd:COG4913 452 ALGLDEAELpfvgelieVRPEEE 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
426-659 |
5.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 426 NLRQELDGCYEKVARLQKV----ETEIQRVSEayENLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRDRLETANKQL 501
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 502 aekeyegsEDTRKTISQLFAKHKENQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 575
Cdd:pfam15921 492 --------ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 576 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNSQptnaseynaaalmelLREKEERI 650
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 590122003 651 LALEADMTK 659
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-656 |
6.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 436 EKVARLQKVEtEIQRVSEAY---ENLVKSSSKREALEKAMRNKLEgeiRRMHDFNRDLRDRLETANKQLAEK----EYEG 508
Cdd:PTZ00121 1552 KKAEELKKAE-EKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAKKAEEAKikaeELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 509 SEDTRKTISQLFAKHKENQREKEKLEAELAT--------ARSTNEDQRRHIEIRdqalsNAQAKVVKLEEELKKKQVYVD 580
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 581 KVEKMQQALV-------QLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNSQPTNASEYNAAAlmELLREKEERI 650
Cdd:PTZ00121 1703 KAEELKKKEAeekkkaeELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA--EEIRKEKEAV 1780
|
....*.
gi 590122003 651 LALEAD 656
Cdd:PTZ00121 1781 IEEELD 1786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-599 |
6.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 358 LLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRAQQSAsyqpmpADPFAMVSRAQQMVEILSDENRNLRQELDGCYEK 437
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE------KALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 438 VARLQKVETEIQRVSEAYENLVKSSSKreALEKAMRNKLEGEIRRMHDFNRDLRDRleTANKQLAEKEYEGSEDTRKTIS 517
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 518 QLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACE 597
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 590122003 598 KR 599
Cdd:COG4942 241 ER 242
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
443-663 |
7.57e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.86 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 443 KVETEIQRVSEAYENLvkSSSKREALEKAMRNKLEGEIR------RMHDFNRDlRDR-----LETANKQLAEKEYE---- 507
Cdd:COG2268 98 KVNSDPEDIANAAERF--LGRDPEEIEELAEEKLEGALRavaaqmTVEELNED-REKfaekvQEVAGTDLAKNGLElesv 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 508 ---GSEDT--------RKTISQLFAKHKENQREKEKlEAELATARSTNE------DQRRHIEIRDQALSNAQAKVVKLEE 570
Cdd:COG2268 175 aitDLEDEnnyldalgRRKIAEIIRDARIAEAEAER-ETEIAIAQANREaeeaelEQEREIETARIAEAEAELAKKKAEE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 571 ELKkkqvyVDKVEKMQQALVQLQAAcEKREQLEHRLR-TRLERELEslrIQQrqgnsqptnaseynAAALMELLREKEER 649
Cdd:COG2268 254 RRE-----AETARAEAEAAYEIAEA-NAEREVQRQLEiAEREREIE---LQE--------------KEAEREEAELEADV 310
|
250
....*....|....
gi 590122003 650 ILALEADMTKWEQK 663
Cdd:COG2268 311 RKPAEAEKQAAEAE 324
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
436-617 |
8.47e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 38.49 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 436 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrdrletANKQLAEKEYEGSEDTRKT 515
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 516 ISQLFAKHKE-NQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 577
Cdd:cd07596 66 LSKLGKAAEElSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 590122003 578 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
425-749 |
9.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 425 RNLRQELDGCYEKVARLqkvETEIQRVSEAYENLvkssskREALekAMRNKLEGEIRRMHDfnRDLRDRLETANKQLAEk 504
Cdd:PRK04863 840 RQLNRRRVELERALADH---ESQEQQQRSQLEQA------KEGL--SALNRLLPRLNLLAD--ETLADRVEEIREQLDE- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 505 eyegSEDTRKTISQlfakhkeNQREKEKLEAELATARSTNED----QRRHIEIrDQALSNAQAKVVKLEEELKKKQVYvd 580
Cdd:PRK04863 906 ----AEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQfeqlKQDYQQA-QQTQRDAKQQAFALTEVVQRRAHF-- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 581 kveKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQRQGNSQptnASEYNA--AALMELLREKEERILALEADMT 658
Cdd:PRK04863 972 ---SYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQ---LAQYNQvlASLKSSYDAKRQMLQELKQELQ 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 659 KWEQKYLEENVMRhfaldaaatVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKD 738
Cdd:PRK04863 1045 DLGVPADSGAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
330
....*....|.
gi 590122003 739 AMIKVLQQRSR 749
Cdd:PRK04863 1116 AGWCAVLRLVK 1126
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-573 |
9.22e-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: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 489
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 490 LRDRLETANKQLAEKEyEGSEDTRKTISQLfakhKENQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVKLE 569
Cdd:TIGR02168 913 LRRELEELREKLAQLE-LRLEGLEVRIDNL----QERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKRLE 978
|
....
gi 590122003 570 EELK 573
Cdd:TIGR02168 979 NKIK 982
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
408-662 |
9.26e-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: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 408 AMVSRAQQMVEILSDEnrnLRQELDGCYEKVA----RLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRR 482
Cdd:pfam12128 315 AAVAKDRSELEALEDQ---HGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 483 MHDFNRDLRDRLETANKQLAEKE--YEGSEdtrktiSQLfakhkenqreKEKLEAELATARstneDQRRHIEIRDQALSN 560
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEddLQALE------SEL----------REQLEAGKLEFN----EEEYRLKSRLGELKL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590122003 561 AQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynaaaLM 640
Cdd:pfam12128 452 RLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LE 526
|
250 260
....*....|....*....|...
gi 590122003 641 ELLREKEERILA-LEADMTKWEQ 662
Cdd:pfam12128 527 LQLFPQAGTLLHfLRKEAPDWEQ 549
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