|
Name |
Accession |
Description |
Interval |
E-value |
| Mcp5_PH |
pfam12814 |
Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal ... |
1492-1611 |
1.56e-65 |
|
Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal proteins is necessary for the cortical localization of the protein during meiosis, since the overall function of the protein is to anchor dynein at the cell cortex during the horsetail phase. During prophase I of fission yeast, horsetail nuclear movement occurs, and this starts when all the telomeres become bundled at the spindle pole body - SPB. Subsequent to this, the nucleus undergoes a dynamic oscillation, resulting in elongated nuclear morphology. Horsetail nuclear movement is thought to be predominantly due to the pulling of astral microtubules that link the SPB to cortical microtubule-attachment sites at the opposite end of the cell; the pulling force is believed to be provided by cytoplasmic dynein and dynactin.
Pssm-ID: 403884 Cd Length: 119 Bit Score: 217.20 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1492 RMIQAITQTMIGEYLWKYTRKTgREGLSENRHRRFFWIHPYTRTLYWSDRDPQSAGKTEMKGKSVAIESVREVEDNNPLP 1571
Cdd:pfam12814 1 SVIDAITQTMIGEYLYKYTRRR-RFKGSERRHKRYFWIHPYTRTLYWSSTNPTSAKASEGKSKSVKIESVTSVEDDNPLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2123157371 1572 PGLHQKSLIIGTPGRSIKFTAPTGQRHETWFNALNYLCQR 1611
Cdd:pfam12814 80 PGLHNKSIVITTPDREIKLTAPTRERHNIWYNALSYLLHR 119
|
|
| PH_PLC_plant-like |
cd13365 |
Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain; PLC-gamma (PLCgamma) was the ... |
1491-1608 |
2.37e-42 |
|
Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain; PLC-gamma (PLCgamma) was the second class of PLC discovered. PLC-gamma consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves internal to which is a PH domain split by two SH2 domains and a single SH3 domain, and a C-terminal C2 domain. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). This cd contains PLC members from fungi and plants. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270171 Cd Length: 115 Bit Score: 150.90 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1491 PRMIQAITQTMIGEYLWKYTRKtgreglsENRHRRFFWIHPYTRTLYWSDRDPQSAGKTEMKGKSVAIESVREVEDNNPL 1570
Cdd:cd13365 1 RDVIEAITQLKIGSYLLKYGRR-------GKPHFRYFWLSPDELTLYWSSPKKGSEKRVRLSSVSRIIPGQRTVVFKRPP 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2123157371 1571 PPGLHQKSLIIGTPG--RSIKFTAPTGQRHETWFNALNYL 1608
Cdd:cd13365 74 PPGLEEHSFSIIYADgeRSLDLTCKDRQEFDTWFTGLRYL 113
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1038-1440 |
6.95e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.04 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1038 SHATEPIPPHRqslhlselSSWSYEPKAPAPLALQKSTLSSQSTEPLEAKKP--LPKLSSITSQSSVPVQPKMQALSVSS 1115
Cdd:PHA03247 2621 THAPDPPPPSP--------SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPQRPRRRAARPTV 2692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1116 TVSAQVSEPvdPPKPATPTMSMHSALATEPIAPRQQVLRQANietqqtePMEPSVIVPSQYGVSNVTTLHDAHPESPTLP 1195
Cdd:PHA03247 2693 GSLTSLADP--PPPPPTPEPAPHALVSATPLPPGPAAARQAS-------PALPAAPAPPAVPAGPATPGGPARPARPPTT 2763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1196 --PHLPSPSRSPTRPATAQRLPPPKLALSFVSSQDTEPRDSSRPATAHRSLPPVLSTSATSVEHDEENTQAIEPSKSSFS 1273
Cdd:PHA03247 2764 agPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1274 DNIVSRGADRDSRTPLAPISSNLAPRSARPQMSDGGTqtmvsaeqidklllARNQRYSAIFTPSSVEKVASPPPSPSRRH 1353
Cdd:PHA03247 2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR--------------PPVRRLARPAVSRSTESFALPPDQPERPP 2909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1354 SNEGRTPRRPGSSGSIRSRAASPPPLP-------ADHREVIAAAAKSLPPPSPTVGAMGPPVMPASAYKKRPTTPSIRTN 1426
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPprpqpplAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP 2989
|
410
....*....|....
gi 2123157371 1427 SATLTPRAGGTTPR 1440
Cdd:PHA03247 2990 ASSTPPLTGHSLSR 3003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-369 |
1.52e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVE----QQQQESDMGPELRQRLAELEKEFNEVGRETARA 126
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleaEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 127 FLPKSRVPSGEAD------------SAIGQSVYSSEAQHSPTKVSVpsRKQRNQQPSRINDIALATEISTSLLSQLKELQ 194
Cdd:TIGR02168 774 EEELAEAEAEIEEleaqieqlkeelKALREALDELRAELTLLNEEA--ANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 195 AVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEvltkaaaDRENRLNHSLNLLRTEK 274
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE-------SKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 275 STLEREFEDLKQQF----TKLS-------DDHINKTKQTETELTSLRRNVAMTETEKNAL---------------QRKvE 328
Cdd:TIGR02168 925 AQLELRLEGLEVRIdnlqERLSeeysltlEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieeyeelkERY-D 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2123157371 329 ELSNQNQELAKAVAYRMKVDEQIaledtspDDGTEERETQT 369
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEEAIEEI-------DREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-340 |
1.10e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAH-LSETTRRLQETShLGNALVQQRRELEEKLHEVEQQQQESDmgpELRQRLAELEKEFNEVgretaraflp 129
Cdd:TIGR02168 207 RQAEKAERYKeLKAELRELELAL-LVLRLEELREELEELQEELKEAEEELE---ELTAELQELEEKLEEL---------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 130 KSRVPSGEADSAIGQSVY--SSEAQHsptKVSVPSRKQRNQQPSRINDIALATEISTSLLSQLKELQAVLLERDDALKaa 207
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELyaLANEIS---RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE-- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 208 dldrsQLEIEVEGLSQRLrvvDESESRLKDvnwsLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQ 287
Cdd:TIGR02168 348 -----ELKEELESLEAEL---EELEAELEE----LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2123157371 288 FTKLSDD-HINKTKQTETELTSLRRNVAMTETEKNALQ----RKVEELSNQNQELAKA 340
Cdd:TIGR02168 416 RERLQQEiEELLKKLEEAELKELQAELEELEEELEELQeeleRLEEALEELREELEEA 473
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1042-1450 |
1.13e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.80 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1042 EPIPPHRQS-LH-LSELSSW-SYEPKAPAPLALQKSTLSSQSTEPLEAKKPL-PKLSSITSQSSVPVQPkmqalsvsSTV 1117
Cdd:PHA03247 2527 EPVHPRMLTwIRgLEELASDdAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSePAVTSRARRPDAPPQS--------ARP 2598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1118 SAQVSEPVDPPKPATPTMSMHSALATEPIAPRQQvlrqanieTQQTEPMEPsvivpsqygvsnvttlHDAHPESPTLPPH 1197
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS--------PAANEPDPH----------------PPPTVPPPERPRD 2654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1198 LPSPSR-SPTRPATAQRLPPPKLAlsfvssqdtEPRDSSRPATAhrslPPVLSTSATSVEHDEENTQAIEPSKSSFSDNI 1276
Cdd:PHA03247 2655 DPAPGRvSRPRRARRLGRAAQASS---------PPQRPRRRAAR----PTVGSLTSLADPPPPPPTPEPAPHALVSATPL 2721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1277 VSRGADRDSRTPLAPISSnLAPRSARPQMSDGGTqtmvsaeqidklllARNQRYSAIFTPSSVEKVASPPPSPSRRhsne 1356
Cdd:PHA03247 2722 PPGPAAARQASPALPAAP-APPAVPAGPATPGGP--------------ARPARPPTTAGPPAPAPPAAPAAGPPRR---- 2782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1357 grTPRRPGSSGSIRSRAASPPPLPADHREVIAAAAKSLPPPSPTVGAMGPPVMPASAYKKRPTTPsirtnSATLTPRAGG 1436
Cdd:PHA03247 2783 --LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP-----PPPSLPLGGS 2855
|
410
....*....|....*..
gi 2123157371 1437 TTPR---ARRQSARSGA 1450
Cdd:PHA03247 2856 VAPGgdvRRRPPSRSPA 2872
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-440 |
3.82e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 177 ALATEISTsLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKD----VNWSLETQVRESEVL 252
Cdd:TIGR02168 257 ELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELESKLDEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 253 TKAAADRENRLNH---SLNLLRTEKSTLEREFEDLKQQFTKLsddhinktkqtETELTSLRRNVAMTETEKNALQRKVEE 329
Cdd:TIGR02168 336 AEELAELEEKLEElkeELESLEAELEELEAELEELESRLEEL-----------EEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 330 LSNQNQELAKAVAyrmKVDEQIALEDTSPDDGT-EERETQTPEHSPPPSPSKATPRHGMLESETLKHSLQHAHRMIQQLK 408
Cdd:TIGR02168 405 LEARLERLEDRRE---RLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270
....*....|....*....|....*....|..
gi 2123157371 409 NNIHREKTEKIELKRMLQDARDELETNRGALN 440
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-372 |
4.23e-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: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQesdmgpELRQRLAELEKEFNEVGRETARAflpk 130
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE------ELEAELAELEAELEELRLELEEL---- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 131 srvpsGEADSAIGQSVYSSEAqhsptkvsvpsRKQRNQQpsrinDIALATEISTSLLSQLKELQAVLLERDDALKAADLD 210
Cdd:COG1196 280 -----ELELEEAQAEEYELLA-----------ELARLEQ-----DIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 211 RSQLEIEVEGLSQRLRvvdESESRLKDVNwslETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREfEDLKQQFTK 290
Cdd:COG1196 339 LEELEEELEEAEEELE---EAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 291 LSDDHINKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEERETQTP 370
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
..
gi 2123157371 371 EH 372
Cdd:COG1196 492 RL 493
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
52-434 |
1.04e-08 |
|
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: 60.42 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 52 QAKRALQAHLSETTRRLQETSHLGNALVQQrreLEEKLHEVEQQQQesdmgpelrqRLAELEKEFNEVgretaraflpKS 131
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNK----------KIKELEKQLNQL----------KS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 132 RVpsgeadsaigqSVYSSEAQHSPTKvsvPSRKQRNQQPSRINDIAlaTEIS--TSLLSQLKElQAVLLERDdaLKAADL 209
Cdd:TIGR04523 296 EI-----------SDLNNQKEQDWNK---ELKSELKNQEKKLEEIQ--NQISqnNKIISQLNE-QISQLKKE--LTNSES 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 210 DRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFT 289
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 290 KLSDdhinktkqtetELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKavayrmkvdeQIALEDTSPDDGTEERETQT 369
Cdd:TIGR04523 437 KNNS-----------EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR----------SINKIKQNLEQKQKELKSKE 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2123157371 370 PEHSpppspskatprhgMLESET--LKHSLQHAHRMIQQLKNNIHREKTEKIELKRMLQDARDELET 434
Cdd:TIGR04523 496 KELK-------------KLNEEKkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-466 |
3.89e-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: 58.54 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 186 LLSQLKELQAvllERDDALKAADLDRSQLEIEVeglSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENRLNH 265
Cdd:TIGR02169 196 KRQQLERLRR---EREKAERYQALLKEKREYEG---YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 266 SLNLLRTEKSTLEREFEDLKQQF-TKLSDDHIN------KTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELA 338
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVkEKIGELEAEiaslerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 339 KAVA-----YRMKVDEQIALEDTSPDDGTEERETQTPEHSPPPSPSKATPRHGMLESET--LKHSLQHAHRMIQQLKNNI 411
Cdd:TIGR02169 350 KRRDklteeYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2123157371 412 HREKTEKIELKRMLQDARDELETNRGALNgpgSAGKRRSKTDKDLFKKPARPDRL 466
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLE---QLAADLSKYEQELYDLKEEYDRV 481
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1184-1449 |
5.57e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 58.26 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1184 LHDAHPESPTLPPHLPSPSRSPTRPATAQRlPPPKLALSFVSSQDTEPRDSSRPATAHRSLPPVLSTSATSVEHDEENTQ 1263
Cdd:PHA03307 138 LRPVGSPGPPPAASPPAAGASPAAVASDAA-SSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISAS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1264 AIEPSKSSFSDNIVSRGADRDSRTPLAPISSNLAPRSARPqmsDGGTQTMVSAEQIDKLLLARNQRysaiFTPSSVEKVA 1343
Cdd:PHA03307 217 ASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP---LPRPAPITLPTRIWEASGWNGPS----SRPGPASSSS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1344 S-----PPPSPSRRHSNEGRTPRRPGSSGSIRSRAASPPPLPADHREVIAAAAKSLPPPSPTVGAMGPPVMPASAYKKRP 1418
Cdd:PHA03307 290 SprersPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP 369
|
250 260 270
....*....|....*....|....*....|.
gi 2123157371 1419 ttPSIRTNSATLTPRAGGTTPRARRQSARSG 1449
Cdd:PHA03307 370 --RPSRAPSSPAASAGRPTRRRARAAVAGRA 398
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
163-329 |
1.06e-07 |
|
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: 54.93 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 163 RKQRNQQPSRINDialateistsLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLrvvDESESRLKDVnwsl 242
Cdd:COG1579 23 EHRLKELPAELAE----------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 243 eTQVRESEVLTK---AAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDDHINKTKQTETELTSLRRNVAMTETE 319
Cdd:COG1579 86 -RNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|
gi 2123157371 320 KNALQRKVEE 329
Cdd:COG1579 165 REELAAKIPP 174
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
975-1375 |
4.87e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 975 PDGHESRTQDQPRHTPLQMSNVSAHSTEPTASRPQPSTFSGMSTQATEPLSARRALSQFSQLSShATEPIPPHRQSLHLS 1054
Cdd:PHA03247 2593 PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP-APGRVSRPRRARRLG 2671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1055 ELSSWSYEPKAPAPLALQKS--TLSSQSTEPLEAKKPLPKLSSITSQSSVPVQPKMQALSVSSTVSAQVSEPV------- 1125
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVpagpatp 2751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1126 ----DPPKPATPTMSMHSALATEPIAPRQQVL-RQANIETQQTEPMEPSVIVPSQYGVSNVTTLHDAHPESPTLPPHLPS 1200
Cdd:PHA03247 2752 ggpaRPARPPTTAGPPAPAPPAAPAAGPPRRLtRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1201 PSRSPTRPATAQRLPPPKLAL--SFVSSQDTEPRDSSRPATAH---RSLPPVLSTSATSVEHDEEnTQAIEPSKSSFSDN 1275
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLggSVAPGGDVRRRPPSRSPAAKpaaPARPPVRRLARPAVSRSTE-SFALPPDQPERPPQ 2910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1276 IVSRGADRDSRTPLAPISSNLAPRS-ARPQ---------MSDGGTQTMVSAEQIDKLLLARnqrysaiftpSSVEKVASP 1345
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPPPPpPRPQpplapttdpAGAGEPSGAVPQPWLGALVPGR----------VAVPRFRVP 2980
|
410 420 430
....*....|....*....|....*....|
gi 2123157371 1346 PPSPSRRHSNEGRTPRRPGSSGSIRSRAAS 1375
Cdd:PHA03247 2981 QPAPSREAPASSTPPLTGHSLSRVSSWASS 3010
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
61-371 |
8.56e-07 |
|
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: 53.81 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 61 LSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESDMGPELRQRL--AELEKEFNEVGRETARAFLP-KSRVPSGE 137
Cdd:COG5185 270 LGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLaaAEAEQELEESKRETETGIQNlTAEIEQGQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 138 ADSAIGQSVYSSEAQHSPTKVSVPSRKQRNQQpsrindialateISTSLLSQLKELQAVLlerddalkaadldRSQLEIE 217
Cdd:COG5185 350 ESLTENLEAIKEEIENIVGEVELSKSSEELDS------------FKDTIESTKESLDEIP-------------QNQRGYA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 218 VEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKaaadrenrlnhSLNLLRTEKSTLEREFEDLKQQFTKLSDDHIN 297
Cdd:COG5185 405 QEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSK-----------LLNELISELNKVMREADEESQSRLEEAYDEIN 473
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123157371 298 KTKQTETELTSLRRNvaMTETEKNALQRKVEELSNQ-NQELAKAvayRMKVDEQIALEDTSPDDGTEERETQTPE 371
Cdd:COG5185 474 RSVRSKKEDLNEELT--QIESRVSTLKATLEKLRAKlERQLEGV---RSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-440 |
9.89e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 52 QAKRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESDMGpELRQRLAELEKEFnevgrETARAFLPKS 131
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEEL-----ERLEEALEEL 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 132 RVPSGEADSAIgQSVYSSEAQHSPTKVSVPSRKQRNQQPSR-INDIALATEISTSLLSQLKE------------------ 192
Cdd:TIGR02168 467 REELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEgVKALLKNQSGLSGILGVLSElisvdegyeaaieaalgg 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 193 -LQAVLLERDDALKAA-----------------------DLDRSQLEI--EVEGLSQRLRVVDESESRLKDVNWSLETQV 246
Cdd:TIGR02168 546 rLQAVVVENLNAAKKAiaflkqnelgrvtflpldsikgtEIQGNDREIlkNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 247 RESEVLTKAAADReNRLNHSLNLL------------------RTEKSTLER--EFEDLKQQFTKLSDDHINKTKQ---TE 303
Cdd:TIGR02168 626 LVVDDLDNALELA-KKLRPGYRIVtldgdlvrpggvitggsaKTNSSILERrrEIEELEEKIEELEEKIAELEKAlaeLR 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 304 TELTSLRRNVAMTETEKNALQRKV------------------EELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEER 365
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQIsalrkdlarleaeveqleERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123157371 366 ETQTPEHSPPPSPSKA-TPRHGMLESE--TLKHSLQHAHRMIQQLKNNIHREKTEKIELKRMLQDARDELETNRGALN 440
Cdd:TIGR02168 785 EELEAQIEQLKEELKAlREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
172-441 |
1.02e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 172 RINDIALATEISTSLLSQ-----LKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQV 246
Cdd:COG4372 14 SLFGLRPKTGILIAALSEqlrkaLFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 247 RESEVLT---KAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDDHINKTKQT---ETELTSLRRNVAMTETEK 320
Cdd:COG4372 94 AELAQAQeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELkelEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 321 NAL--QRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEERE-TQTPEHSPPPSPSKATPRHGMLESETLKHSL 397
Cdd:COG4372 174 QALseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLeAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2123157371 398 QHAHRMIQQLKNNIHREKTEKIELKRMLQDARDELETNRGALNG 441
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-355 |
1.39e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 56 ALQAHLSETTRRLQETSHLGNALVQQ----RRELEEKLHEVEQQQQESDmgpELRQRLAELEKEFNEvgREtaraflpks 131
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEeeklKERLEELEEDLSSLEQEIE---NVKSELKELEARIEE--LE--------- 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 132 rvpsgEADSAIGQSVYSSEAQHSPTKVsvpsrKQRNQQPSRINDialateistsllsQLKELQAVLLERDDALKAADLDR 211
Cdd:TIGR02169 772 -----EDLHKLEEALNDLEARLSHSRI-----PEIQAELSKLEE-------------EVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 212 SQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKL 291
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123157371 292 SDDhINKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQI-ALED 355
Cdd:TIGR02169 909 EAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIrALEP 972
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-437 |
1.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESDmgpELRQRLAELEKEFNEVGR-----ETAR 125
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE---ELKKKLKELEKRLEELEErhelyEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 126 AFLP-----KSRVPSGEADSAIGQSVYSSEAQHSPTKVSVPSRKQRNQQPSRINDIALAT-------------------- 180
Cdd:PRK03918 369 AKKEelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltee 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 181 ---EISTSLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLR---VVD---ESESRLKDVNWS-LETQVRESE 250
Cdd:PRK03918 449 hrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkeLAEqlkELEEKLKKYNLEeLEKKAEEYE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 251 VLT-------------KAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDDHINKTKQTETELTSL-RRNVAMT 316
Cdd:PRK03918 529 KLKekliklkgeikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 317 ETEKNaLQRKVEELSNQNQELAKAVAYRMKVDEQIA-----LEDTSPDDGTEERETQTPEHSPPPSpskatpRHGMLES- 390
Cdd:PRK03918 609 DAEKE-LEREEKELKKLEEELDKAFEELAETEKRLEelrkeLEELEKKYSEEEYEELREEYLELSR------ELAGLRAe 681
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2123157371 391 -ETLKHSLQHAHRMIQQLKNNIH--REKTEKIELkrmLQDARDELETNRG 437
Cdd:PRK03918 682 lEELEKRREEIKKTLEKLKEELEerEKAKKELEK---LEKALERVEELRE 728
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-341 |
2.63e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 54 KRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESdmgpelRQRLAELEKEFNEVGRETARAflpksrv 133
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA------SRKIGEIEKEIEQLEQEEEKL------- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 134 psgeadsaigqsvySSEAQHSPTKVSVPSRKQRNQQpsrindialateistsllSQLKELQAVLLERDDALkaadldrSQ 213
Cdd:TIGR02169 736 --------------KERLEELEEDLSSLEQEIENVK------------------SELKELEARIEELEEDL-------HK 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 214 LEIEVEGLSQRLrvvdeSESRLKDVNW---SLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQ--- 287
Cdd:TIGR02169 777 LEEALNDLEARL-----SHSRIPEIQAelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiks 851
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2123157371 288 FTKLSDDHINKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAV 341
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-434 |
2.93e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 80 QQRRELEEKLHEVEQQQQESD--MGpELRQRLAELEKEfnevgRETARAFLpksrvpsgeadsaigqsVYSSEAQHspTK 157
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEdiLG-ELERQLEPLERQ-----AEKAERYR-----------------ELKEELKE--LE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 158 VSVPSRKQRNQQpsriNDIALATEISTSLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLkd 237
Cdd:COG1196 227 AELLLLKLRELE----AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 238 vnwslETQVRESEVLTKAAADRENRLnhslnllRTEKSTLEREFEDLKQQFTKLSDDHINKTK----------QTETELT 307
Cdd:COG1196 301 -----EQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEeleeaeaelaEAEEALL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 308 SLRRNVAMTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEERETQTPEHSPPPSPSKATPRHGM 387
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2123157371 388 LESETLKHSLQHAHRMIQQLKNNIHREKTEKIELKRMLQDARDELET 434
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
186-336 |
3.19e-06 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 48.45 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 186 LLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLsqrlrvvdesESRLKDVNWSLEtqvrESEvltKAAADRENrLNH 265
Cdd:pfam12718 19 LEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKL----------EEQLKEAKEKAE----ESE---KLKTNNEN-LTR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123157371 266 SLNLLRTEkstLEREFEDLKQQFTKLsddhinktKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQE 336
Cdd:pfam12718 81 KIQLLEEE---LEESDKRLKETTEKL--------RETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-440 |
4.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 172 RINDIAlaTEIStsllSQLKELQAvllERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDvnwSLETQVRESEV 251
Cdd:COG1196 190 RLEDIL--GELE----RQLEPLER---QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA---ELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 252 LTKAAADRENRLNHslnlLRTEKSTLEREFEDLKQQFTKLsddhinkTKQTETELTSLRRNVAMTETEKNALQRKVEELS 331
Cdd:COG1196 258 LEAELAELEAELEE----LRLELEELELELEEAQAEEYEL-------LAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 332 NQNQELAKAVAyrmkvdEQIALEDTSPDDGTEERETQTPEHSPPPSPSKAtpRHGMLESETLKHSLQHAHRMIQQLKNNI 411
Cdd:COG1196 327 ELEEELEELEE------ELEELEEELEEAEEELEEAEAELAEAEEALLEA--EAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260
....*....|....*....|....*....
gi 2123157371 412 HREKTEKIELKRMLQDARDELETNRGALN 440
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-372 |
5.74e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 69 QETSHLGNALVQQRRELEEKLHEVEQQQQESDmgpELRQRLAELEKEFNEVGREtarafLPKSRVPSGEADSAIG--QSV 146
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESK-----IQNQEKLNQQKDEQIKklQQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 147 YSS-EAQHSPTKvsvpsrKQRNQQPSRINDIalaTEISTSLLSQLKELqavllerddalkaaDLDRSQLEIEVEGLSqrl 225
Cdd:TIGR04523 421 KELlEKEIERLK------ETIIKNNSEIKDL---TNQDSVKELIIKNL--------------DNTRESLETQLKVLS--- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 226 RVVDESESRLKDVNWSLETQVRESEVLTKAAADRENR----------LNHSLNLLRTEKSTLEREFEDLKQQFtkLSDDH 295
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKvkdltkkissLKEKIEKLESEKKEKESKISDLEDEL--NKDDF 552
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2123157371 296 INKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAvayRMKVDEQIALEDTSPDDGTEERETQTPEH 372
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE---KKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
77-352 |
8.82e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 77 ALVQQRRELEEKLHEVEQQQQ--ESDMGPELRQRLAELEKEFNEVGRETARAFLpksrvpsgEADSAIGqsvyssEAQHS 154
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKKGaePSRLYSLYEKEIEDLRRQLDTLTVERARLQL--------ELDNLRL------AAEDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 155 PTKvsvpsrkqrnqqpsrindiaLATEIStslLSQLKELQAVLLERDdaLKAADLDRSQLEIEVEGLSQR---LRVVDES 231
Cdd:pfam00038 88 RQK--------------------YEDELN---LRTSAENDLVGLRKD--LDEATLARVDLEAKIESLKEElafLKKNHEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 232 ESRlkdvnwSLETQVRESEVLTKAAADRENRLNHSLNLLRT------EKSTLERE------FEDLKQQFTKLSDDhinkT 299
Cdd:pfam00038 143 EVR------ELQAQVSDTQVNVEMDAARKLDLTSALAEIRAqyeeiaAKNREEAEewyqskLEELQQAAARNGDA----L 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123157371 300 KQTETELTSLRRNVAMTETE-------KNALQRKVEELSNQNQ-ELAKAVAYRMKVDEQIA 352
Cdd:pfam00038 213 RSAKEEITELRRTIQSLEIElqslkkqKASLERQLAETEERYElQLADYQELISELEAELQ 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-433 |
1.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 52 QAKRALQAHLSETTRRLQEtshlgnaLVQQRRELEEKLHEVEQQQQESDMGPELRQRLAELEKEFNEVGRETARaflpks 131
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEE-------LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 132 rvpsgeadsaigqsvYSSEAQHSPTKVsvpsrKQRNQQPSRINDIalaTEISTSLLSQLKELQAVLLERDDALkaadldr 211
Cdd:PRK03918 319 ---------------LEEEINGIEERI-----KELEEKEERLEEL---KKKLKELEKRLEELEERHELYEEAK------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 212 sQLEIEVEGLSQRL--RVVDESESRLKDV-NWSLETQVRESEVLTKAAA--DRENRLNHSLNLLRTEKSTL--------E 278
Cdd:PRK03918 369 -AKKEELERLKKRLtgLTPEKLEKELEELeKAKEEIEEEISKITARIGElkKEIKELKKAIEELKKAKGKCpvcgreltE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 279 REFEDLKQQFTKLSDDHINKTKQTETELTSLRRNVamteteknalqRKVEELSNQNQELAKavaYRMKVDEQIALEDTSP 358
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL-----------RELEKVLKKESELIK---LKELAEQLKELEEKLK 513
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123157371 359 DDGTEERETQTPEHspppspskatprhgmlesETLKHSLQHAHRMIQQLKNNIHRE---KTEKIELKRMLQDARDELE 433
Cdd:PRK03918 514 KYNLEELEKKAEEY------------------EKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELA 573
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
46-371 |
1.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 46 LNGSPAQAKRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESdMGPELRQRLAELEKEFNEVGR---- 121
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLLLIAAAllal 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 122 ETARAFLPKSRVPSGEADSAIGQSVYSSEAQHSPTKVSVPSRKQRNQQPSRINDIA----------------LATEISTS 185
Cdd:COG4717 262 LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEeeeleellaalglppdLSPEELLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 186 LLSQLKELQAVLLERDDAlkAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWslETQVRESEVLTKAAADRENRLNH 265
Cdd:COG4717 342 LLDRIEELQELLREAEEL--EEELQLEELEQEIAALLAEAGVEDEEELRAALEQA--EEYQELKEELEELEEQLEELLGE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 266 SLNLLR-TEKSTLEREFEDLKQQFTKLSDDHinktKQTETELTSLRR--NVAMTETEKNALQRKVEELSNQNQELAKAVA 342
Cdd:COG4717 418 LEELLEaLDEEELEEELEELEEELEELEEEL----EELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
330 340
....*....|....*....|....*....
gi 2123157371 343 YRMKVDEqiALEDTSpddgTEERETQTPE 371
Cdd:COG4717 494 ALKLALE--LLEEAR----EEYREERLPP 516
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
186-351 |
2.00e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 186 LLSQLKELQAVLLErddalkaadldrsqLEIEVEGLSQRLrvvDESESRLKDvnwsLETQVRESEVLTKAAADRENRLNH 265
Cdd:COG1579 22 LEHRLKELPAELAE--------------LEDELAALEARL---EAAKTELED----LEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 266 SLNLLRTEK--STLEREFEDLKQQFTKLSDDHINKTKQTET---ELTSLRRNVAMTETEKNALQRKVEE-LSNQNQELAK 339
Cdd:COG1579 81 QLGNVRNNKeyEALQKEIESLKRRISDLEDEILELMERIEEleeELAELEAELAELEAELEEKKAELDEeLAELEAELEE 160
|
170
....*....|..
gi 2123157371 340 AVAYRMKVDEQI 351
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
51-350 |
2.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETT----RRLQET----SHLGNALVQQRREL---EEKLHEVEQQQQESDMGPELRQRLAELEKEFNEV 119
Cdd:COG4717 173 AELQEELEELLEQLSlateEELQDLaeelEELQQRLAELEEELeeaQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 120 GRETARAFLpksrvpSGEADSAIGQSVYSSEAQHS----PTKVSVPSRKQRNQQPSRINDIAlateistsLLSQLKELQA 195
Cdd:COG4717 253 LIAAALLAL------LGLGGSLLSLILTIAGVLFLvlglLALLFLLLAREKASLGKEAEELQ--------ALPALEELEE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 196 vlLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRE---SEVLTKAAADRENRLNHSLNLLRt 272
Cdd:COG4717 319 --EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEqeiAALLAEAGVEDEEELRAALEQAE- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 273 EKSTLEREFEDLKQQFTKLSDDHINKTKQT-----ETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVAYRMKV 347
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
...
gi 2123157371 348 DEQ 350
Cdd:COG4717 476 QEL 478
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
45-331 |
2.65e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 45 YLNGSPAQAKRALQAHLSE-----TTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQE----------SDMGPELRQRL 109
Cdd:COG3206 142 YTSPDPELAAAVANALAEAyleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 110 AELEKEFNEVGRETARAflpKSRVPSGEADSAIGQSVYSSEAQHSptkvSVPSRKQRNQQpsrindialateistsLLSQ 189
Cdd:COG3206 222 SELESQLAEARAELAEA---EARLAALRAQLGSGPDALPELLQSP----VIQQLRAQLAE----------------LEAE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 190 LKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVvdesesrlkdvnwSLETQVREsevltkaaadrenrlnhslnl 269
Cdd:COG3206 279 LAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA-------------SLEAELEA--------------------- 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2123157371 270 LRTEKSTLEREFEDLKQQFTKLSddhinktkQTETELTSLRRNVAMTETEKNALQRKVEELS 331
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELP--------ELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
733-1139 |
3.75e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 48.95 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 733 STIQSRATEPQVPRPASLHFSALSAENTIPQAAPRPDLRV--SSVSAQETLPKASLQPALTVSTVSGHSTQPEAPRVAPL 810
Cdd:PRK14949 381 TPSALAAAVQAPHANEPQFVNAAPAEKKTALTEQTTAQQQvqAANAEAVAEADASAEPADTVEQALDDESELLAALNAEQ 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 811 TFSSLSAHESVPEPAPAARLGVSSVSSQNtlPEAARSVPLDMSSismhhTEPQHAATPALSMSSLSMHQTE---PQHLAV 887
Cdd:PRK14949 461 AVILSQAQSQGFEASSSLDADNSAVPEQI--DSTAEQSVVNPSV-----TDTQVDDTSASNNSAADNTVDDnysAEDTLE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 888 PAMGMSGLVSNETQPLAPTQDNSRALSMGVSGIVHQSSEPREGNTGRALASGALLVSGIHSQSTEPSDLGSS-------- 959
Cdd:PRK14949 534 SNGLDEGDYAQDSAPLDAYQDDYVAFSSESYNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAASladddild 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 960 AVTQRNPQQLD--SAIQP---DGHESRTQDQPRhTPLQMSNVSAHSTEPTASRPQPSTFSGMSTQATEPLSARRALSQFS 1034
Cdd:PRK14949 614 AVLAARDSLLSdlDALSPkegDGKKSSADRKPK-TPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAAL 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1035 QLSSHATEPI-------PPhrqslhlselssWSyEPKAPAPLALQKSTLSSQSTEPLEAKKPLPKLSSITSQSSVPVQPK 1107
Cdd:PRK14949 693 ASGSAPAPPPvpdpydrPP------------WE-EAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQ 759
|
410 420 430
....*....|....*....|....*....|...
gi 2123157371 1108 MQALSVSST-VSAQVSEPVDPPKPATPTMSMHS 1139
Cdd:PRK14949 760 AEAQSPASTtALTQTSSEVQDTELNLVLLSSGS 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-434 |
4.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 177 ALATEIST--SLLSQLKELQAVLLERDDALKA------ADLDRSQLEIEVEGLSQRLRVVDESESRLKdvnwSLETQVRE 248
Cdd:COG4913 621 ELEEELAEaeERLEALEAELDALQERREALQRlaeyswDEIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 249 SEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDDhinKTKQTETELTSLRRNVAMTETEK-------N 321
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL---ARLELRALLEERFAAALGDAVERelrenleE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 322 ALQRKVEELSNQNQELAKAV-AYRMKVDEQIALEDTSPDDGTEEREtqtpehspppspskatpRHGMLESETLKhslQHA 400
Cdd:COG4913 774 RIDALRARLNRAEEELERAMrAFNREWPAETADLDADLESLPEYLA-----------------LLDRLEEDGLP---EYE 833
|
250 260 270
....*....|....*....|....*....|....*
gi 2123157371 401 HRMIQQLKNNIHREKTE-KIELKRMLQDARDELET 434
Cdd:COG4913 834 ERFKELLNENSIEFVADlLSKLRRAIREIKERIDP 868
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
65-359 |
5.74e-05 |
|
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: 48.25 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 65 TRRLQETSHLGNALvqqrrELEEKLHEVEQQqqesdmgpELRQRLAELEKEFNEVGRETAR--AFLPKSRvpsgeadsai 142
Cdd:pfam01576 323 SKREQEVTELKKAL-----EEETRSHEAQLQ--------EMRQKHTQALEELTEQLEQAKRnkANLEKAK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 143 gQSVYSSEAQHSPTKVSVPSRKQRNQQPSRindialateistSLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLS 222
Cdd:pfam01576 380 -QALESENAELQAELRTLQQAKQDSEHKRK------------KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 223 QRLRVVDESESRL-KDVNwSLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFED-------LKQQFTKLSDD 294
Cdd:pfam01576 447 SLLNEAEGKNIKLsKDVS-SLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEeeeakrnVERQLSTLQAQ 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123157371 295 HINKTKQTETELTSLRrnvAMTETEKNaLQRKVEELSNQNQElaKAVAY----RMKVDEQIALEDTSPD 359
Cdd:pfam01576 526 LSDMKKKLEEDAGTLE---ALEEGKKR-LQRELEALTQQLEE--KAAAYdkleKTKNRLQQELDDLLVD 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
189-340 |
7.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 189 QLKELQAVLLERDDALKAADL--DRSQLEIEVEGLSQRLrvvDESESRLKDvnwsLETQVRESEVLTKAAADRENRLNHS 266
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLyqELEALEAELAELPERL---EELEERLEE----LRELEEELEELEAELAELQEELEEL 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2123157371 267 LNLLRTEKstlEREFEDLKQQFTKLSddhiNKTKQTETELTSLRRnvamtetEKNALQRKVEELSNQNQELAKA 340
Cdd:COG4717 183 LEQLSLAT---EEELQDLAEELEELQ----QRLAELEEELEEAQE-------ELEELEEELEQLENELEAAALE 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
51-340 |
8.90e-05 |
|
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: 47.48 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESDMGpelRQRLaELEK----------EFNEVG 120
Cdd:pfam01576 67 AARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAA---RQKL-QLEKvtteakikklEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 121 RETARAFLPKSRVPSGEADSAigqsvYSSEAQHSPTKVSVPSrKQRNQQPSRINDI-------------------ALATE 181
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISE-----FTSNLAEEEEKAKSLS-KLKNKHEAMISDLeerlkkeekgrqelekakrKLEGE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 182 IST------SLLSQLKELQAVLLERDDALKAAdLDRsqLEIEVEGLSQRLRVVDESESRLKDVNWSLEtqvreSEVLTKA 255
Cdd:pfam01576 217 STDlqeqiaELQAQIAELRAQLAKKEEELQAA-LAR--LEEETAQKNNALKKIRELEAQISELQEDLE-----SERAARN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 256 AADRENR-LNHSLNLLRTE--------------KSTLEREFEDLK-----------QQFTKLSDDHINKTKQTETELTSL 309
Cdd:pfam01576 289 KAEKQRRdLGEELEALKTEledtldttaaqqelRSKREQEVTELKkaleeetrsheAQLQEMRQKHTQALEELTEQLEQA 368
|
330 340 350
....*....|....*....|....*....|.
gi 2123157371 310 RRNVAMTETEKNALQRKVEELSNQNQELAKA 340
Cdd:pfam01576 369 KRNKANLEKAKQALESENAELQAELRTLQQA 399
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
242-351 |
9.83e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.55 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 242 LETQVRESEVLTKaaadRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSD------DHI-NKTKQTETELTSLRRNVA 314
Cdd:smart00787 153 LEGLKEDYKLLMK----ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptelDRAkEKLKKLLQEIMIKVKKLE 228
|
90 100 110
....*....|....*....|....*....|....*..
gi 2123157371 315 MTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQI 351
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
87-449 |
1.01e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 87 EKLHEVEQQQQESD-MGPELRQRLAELEKEfnevgRETARAFLPKSRVPSGEADSAIGQSVYSSEAQHSPTKVSVPS-RK 164
Cdd:TIGR02169 177 EELEEVEENIERLDlIIDEKRQQLERLRRE-----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASlEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 165 QRNQQPSRINDIALATEISTSLLSQL-KELQAVLLERDDALKAadlDRSQLEIEVEGLSqrlRVVDESESRLKDvnwsLE 243
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKE---KIGELEAEIASLE---RSIAEKERELED----AE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 244 TQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDD--HINKT-KQTETELTSLRRNVAMTETEK 320
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleEVDKEfAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 321 NALQRKVEELSNQNQELAKAVAyRMKVD-----EQIALEDTSPDDGTEERETQTPehspppspskatprhgmlESETLKH 395
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELA-DLNAAiagieAKINELEEEKEDKALEIKKQEW------------------KLEQLAA 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2123157371 396 SLQHAHRMIQQLKNNIHREKTEKIELKRMLqdarDELETNRGALnGPGSAGKRR 449
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQREL----AEAEAQARAS-EERVRGGRA 511
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
185-459 |
1.16e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 185 SLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETqvresEVLTKaaaDRENRLn 264
Cdd:COG1340 68 ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQT-----EVLSP---EEEKEL- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 265 hslnllrTEK-STLEREFEDLKQQFTKLsddhiNKTKQTETELTSLRRnvamtetEKNALQRKVEELSNQNQEL-AKAVA 342
Cdd:COG1340 139 -------VEKiKELEKELEKAKKALEKN-----EKLKELRAELKELRK-------EAEEIHKKIKELAEEAQELhEEMIE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 343 YRMKVDEQialedtspddgTEERETqtpehspppspskatprhgmlesetlkhslqhAHRMIQQLKNNIHREKTEKIELK 422
Cdd:COG1340 200 LYKEADEL-----------RKEADE--------------------------------LHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 2123157371 423 RMLQDARDELETNRGALNgpgsaGKRRSKTDKDLFKK 459
Cdd:COG1340 237 KELRELRKELKKLRKKQR-----ALKREKEKEELEEK 268
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
47-433 |
1.24e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 47 NGSPAQAKR-ALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESDMGPELRQRLAE----LEKEFNEVGR 121
Cdd:TIGR00618 188 KKKSLHGKAeLLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqlkKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 122 --ETARAFLPKSRVPSGEADSAIGQSVYSSEAQHSptkvsvpsrKQRNQQPSRINdialateisTSLLSQLKELQAVLLE 199
Cdd:TIGR00618 268 riEELRAQEAVLEETQERINRARKAAPLAAHIKAV---------TQIEQQAQRIH---------TELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 200 RDDALKAADLDRSQLEIEVEGLSQ--RLRVVDESESRLKDVnwsLETQVRESEVLTKAAADRENrLNHSLNLLRTEKSTL 277
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREI---SCQQHTLTQHIHTLQQQKTT-LTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 278 ERE-----FEDLKQQFTKLSDDHINKTKQTETELTSLRR----NVAMTETEKNALQRKV-------EELSNQNQELAKAV 341
Cdd:TIGR00618 406 QREqatidTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaaitCTAQCEKLEKIHLQESaqslkerEQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 342 AYRMKVDEQIALEDTSPDDGTEERETQTPEHSPPPSPSKATPR----------HGMLESETLKHSLQHAHRMIQQLKNNI 411
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmqrgeqtyaQLETSEEDVYHQLTSERKQRASLKEQM 565
|
410 420
....*....|....*....|..
gi 2123157371 412 HREKTEKIELKRMLQDARDELE 433
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIP 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-341 |
1.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 185 SLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKaAADRENRLN 264
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 265 HSLNLLRTEKSTLER-----------------EFEDLKQQFTKLSDDH--INKTKQTETELTSLRRNVAMTETEKnaLQR 325
Cdd:PRK03918 314 KRLSRLEEEINGIEErikeleekeerleelkkKLKELEKRLEELEERHelYEEAKAKKEELERLKKRLTGLTPEK--LEK 391
|
170
....*....|....*.
gi 2123157371 326 KVEELSNQNQELAKAV 341
Cdd:PRK03918 392 ELEELEKAKEEIEEEI 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
181-422 |
1.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 181 EISTSLLSQLKELQAV--LLERDDALK----AADLDRSQLEIEVEGLSQRLR----VVDESESRLKDvnwsLETQVRESE 250
Cdd:PRK03918 211 EISSELPELREELEKLekEVKELEELKeeieELEKELESLEGSKRKLEEKIReleeRIEELKKEIEE----LEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 251 VLtKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQftklsddhINKTKQTETELTSLRRNVAMTETEKNALQRKVEEL 330
Cdd:PRK03918 287 EL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE--------INGIEERIKELEEKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 331 SNQNQELAKAvayRMKVDEQIALEdtspddgtEERETQTPEHSPPpspskatprhgMLES-----ETLKHSLQHAHRMIQ 405
Cdd:PRK03918 358 EERHELYEEA---KAKKEELERLK--------KRLTGLTPEKLEK-----------ELEElekakEEIEEEISKITARIG 415
|
250
....*....|....*..
gi 2123157371 406 QLKNNIHREKTEKIELK 422
Cdd:PRK03918 416 ELKKEIKELKKAIEELK 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
78-353 |
1.51e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 78 LVQQRRELEEKLHEVEQQQQESDmgpelrQRLAELEKEFNEVGRETARafLPKSRVPSGEADSAIGQSVYSSE------- 150
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKD------EQIKKLQQEKELLEKEIER--LKETIIKNNSEIKDLTNQDSVKEliiknld 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 151 --AQHSPTKVSVPSR----------------KQRNQQPSRINDIA---------LATEIStSLLSQLKELQAVLLERDDA 203
Cdd:TIGR04523 461 ntRESLETQLKVLSRsinkikqnleqkqkelKSKEKELKKLNEEKkeleekvkdLTKKIS-SLKEKIEKLESEKKEKESK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 204 LKA---------ADLDRSQLEIEVEGLSQRLrvvdeseSRLKDVNWSLETQVRESEVLTKAAADRENRLNHSLNLLRTEK 274
Cdd:TIGR04523 540 ISDledelnkddFELKKENLEKEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 275 STLEREFEDLKQQFTKLSD--DHINKTKQTETELTSlrrnvAMTETEKNALQRKvEELSNQNQELAKavayrmKVDEQIA 352
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSiiKNIKSKKNKLKQEVK-----QIKETIKEIRNKW-PEIIKKIKESKT------KIDDIIE 680
|
.
gi 2123157371 353 L 353
Cdd:TIGR04523 681 L 681
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-439 |
1.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 244 TQVRESEVLTKAAADRE---NRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSD-----DHINKTKQTETELTSLrrnvam 315
Cdd:COG4717 71 KELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKllqllPLYQELEALEAELAEL------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 316 tETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEERETQTPEhspppspskatpRHGMLESEtlkh 395
Cdd:COG4717 145 -PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE------------ELEELQQR---- 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2123157371 396 sLQHAHRMIQQLKNNIH--REKTEKIELKRMLQDARDELETNRGAL 439
Cdd:COG4717 208 -LAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARLLL 252
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
717-1267 |
1.74e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 717 DSGMMTEPVPRQAVGLSTIQSRATEPQVPRPaslhfsalsAENTIPQAAPRPDlrvssVSAQETLPKASLQPaltvstvS 796
Cdd:PHA03247 2547 DAGDPPPPLPPAAPPAAPDRSVPPPRPAPRP---------SEPAVTSRARRPD-----APPQSARPRAPVDD-------R 2605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 797 GHSTQPEAPRVAPltfsslSAHESVPEPAPAARLGVSSVSSQNTLPEAARSVPLDMSSISmHHTEPQHAATPALSMSSLS 876
Cdd:PHA03247 2606 GDPRGPAPPSPLP------PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASS 2678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 877 MHQTEPQHLAVPAMGMsglVSNETQPLAPTQDNSRALSMGVSGIvhqsSEPREGNTGRALASGALLVSGIHSQSTEPSDL 956
Cdd:PHA03247 2679 PPQRPRRRAARPTVGS---LTSLADPPPPPPTPEPAPHALVSAT----PLPPGPAAARQASPALPAAPAPPAVPAGPATP 2751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 957 GSSAVTQRnPQQLDSAIQPDGHESRTQDQPRHTPLQMSNVSAHSTE--PTASRPQPSTFSGMSTQATEPLSARRALSQFS 1034
Cdd:PHA03247 2752 GGPARPAR-PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESREslPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1035 QLSSHATEPIPPHRQSLHLSELSSWSyepkapAPLALQKSTLSSQSTEPLEAKKPLPKLSSItSQSSVPVQPKMQALSvs 1114
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPPPSLPLGGSV------APGGDVRRRPPSRSPAAKPAAPARPPVRRL-ARPAVSRSTESFALP-- 2901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1115 stvsaqVSEPVDPPKPATPTMSMHSALATEPIAPRQQVLRQANIETQQTEPMEPSVIVPSQYGVSNVTTLHDAHPESPTl 1194
Cdd:PHA03247 2902 ------PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV- 2974
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1195 pPHLPSPSRSPTRPATAQRLPPPK-LALSFVSS--------QDTEPRDSSRPATAHRSLPPVLSTSATSVEHDEE--NTQ 1263
Cdd:PHA03247 2975 -PRFRVPQPAPSREAPASSTPPLTgHSLSRVSSwasslalhEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSErsDLE 3053
|
....
gi 2123157371 1264 AIEP 1267
Cdd:PHA03247 3054 ALDP 3057
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
745-1069 |
1.81e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 745 PRPASLHFSALSAENTIPQAAPRPDLRVSSVSAQ-ETLPKASLQPALTVSTVSGHSTQPEAPRVAPLTFSSLSAHEsvpe 823
Cdd:PHA03307 128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAAS---- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 824 PAPAARLGVSSVSSQNTLPEAARS--VPLDMSSISMHHTEPQHAATPALSMSSLSMHQTepqhLAVPAMGMSGLVSNETQ 901
Cdd:PHA03307 204 PRPPRRSSPISASASSPAPAPGRSaaDDAGASSSDSSSSESSGCGWGPENECPLPRPAP----ITLPTRIWEASGWNGPS 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 902 PLAPTQDNSralsmgvSGIVHQSSEPREGNTG-RALASGALLVSgiHSQSTEPSDLGSSAVTQRNPQQLDSAIQPDGHES 980
Cdd:PHA03307 280 SRPGPASSS-------SSPRERSPSPSPSSPGsGPAPSSPRASS--SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 981 RTQDQPrhtplqmSNVSAHSTEPTASRPQPSTFSGMSTQATEPLSARRALSQFSQLSSHATEPIPPHRQSLHLSELSSWS 1060
Cdd:PHA03307 351 PSPSRP-------PPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAAS 423
|
....*....
gi 2123157371 1061 YEPKAPAPL 1069
Cdd:PHA03307 424 GAFYARYPL 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-350 |
2.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETTRRLQETSHLGNALvqqrRELEEKLHEVEQQQQE-SDMGPELRQRLAELEKEFNEVGRETARaflp 129
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELETLEAEI----EDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGL---- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 130 ksrvpsGEAD-SAIGQSVYSSEAQHSPTKVSVpsRKQRNQQPSRINDIALATEISTSLLSQLKELQAVLLERDDALKAAD 208
Cdd:PRK02224 305 ------DDADaEAVEARREELEDRDEELRDRL--EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 209 LDRSQLEIEVEGLSQRLRVV-----------DESESRLKDVnwsLETQVRESEVLTKAAADR---ENRLNHSLNLL---- 270
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELrerfgdapvdlGNAEDFLEEL---REERDELREREAELEATLrtaRERVEEAEALLeagk 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 271 --------------------RTEKSTLEREFEDLKQQFTKLSDDH--INKTKQTETELTSLRRN-------VAMTETEKN 321
Cdd:PRK02224 454 cpecgqpvegsphvetieedRERVEELEAELEDLEEEVEEVEERLerAEDLVEAEDRIERLEERredleelIAERRETIE 533
|
330 340 350
....*....|....*....|....*....|
gi 2123157371 322 ALQRKVEELSNQNQEL-AKAVAYRMKVDEQ 350
Cdd:PRK02224 534 EKRERAEELRERAAELeAEAEEKREAAAEA 563
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
1500-1609 |
2.14e-04 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 42.16 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1500 TMIGEYLWKYTRKTGReglseNRHRRFFWIHPyTRTLYWSDRDPQSAGKTEmkgKSVAIESVREVED-NNPLPPGLHQKS 1578
Cdd:pfam00169 1 VVKEGWLLKKGGGKKK-----SWKKRYFVLFD-GSLLYYKDDKSGKSKEPK---GSISLSGCEVVEVvASDSPKRKFCFE 71
|
90 100 110
....*....|....*....|....*....|...
gi 2123157371 1579 LIIG--TPGRSIKFTAPTGQRHETWFNALNYLC 1609
Cdd:pfam00169 72 LRTGerTGKRTYLLQAESEEERKDWIKAIQSAI 104
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
55-342 |
2.20e-04 |
|
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: 46.32 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 55 RALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQ---QQQESDMGPELRQRLAELEKEfnEVGRETARAFLPKS 131
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAellQLQEDLAASERARRQAQQERD--ELADEIASGASGKS 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 132 RVPSGEA--DSAIGQSVYSSEAQHSPTKVSVPSRKQRNQQPSRINdIALATEISTS---------LLSQLKELQAVLLER 200
Cdd:pfam01576 879 ALQDEKRrlEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLT-TELAAERSTSqksesarqqLERQNKELKAKLQEM 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 201 DDALKaadldrSQLEIEVEGLSQRLRVVDEsesrlkdvnwSLETQVRESEVLTKAAADRENRLNHSLNLLRTEKstleRE 280
Cdd:pfam01576 958 EGTVK------SKFKSSIAALEAKIAQLEE----------QLEQESRERQAANKLVRRTEKKLKEVLLQVEDER----RH 1017
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2123157371 281 FEDLKQQFTKLSddhiNKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVA 342
Cdd:pfam01576 1018 ADQYKDQAEKGN----SRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVS 1075
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
622-1133 |
2.68e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 622 RSKASGSRVGTPKGSLDFHASSPAVESPASFASNSRENTPAQGKSLFAELNDLSGDEDGSSVGEGTPSRSSVVYSR---- 697
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRaaqa 2676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 698 ESSPEHLKRQA--ETVKSVMV-----DSGMMTEPVPRqavglstiqsrATEPQVPRPASLHFSALSAENTIPQAAPRPDL 770
Cdd:PHA03247 2677 SSPPQRPRRRAarPTVGSLTSladppPPPPTPEPAPH-----------ALVSATPLPPGPAAARQASPALPAAPAPPAVP 2745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 771 RVSSVSAQETLPKASLQPALTVSTV--SGHSTQPEAPRVAPLTFSSLSAHESVPEPAPAARLGVSSVSSQNTLPEAARSV 848
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAppAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 849 PLDMSSISMHHTEPqhAATPALSMSSLSMHQTEPQHLAVPAMGMSGlvSNETQPLAPTQDNSRALSMGVsgiVHQSSEPR 928
Cdd:PHA03247 2826 GPLPPPTSAQPTAP--PPPPGPPPPSLPLGGSVAPGGDVRRRPPSR--SPAAKPAAPARPPVRRLARPA---VSRSTESF 2898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 929 egntgralasgALLVSGIHSQSTEPSdlgssavtQRNPQQLDSAIQPDGHESRTQDQPR-HTPLQMSNVSAHSTEPTASR 1007
Cdd:PHA03247 2899 -----------ALPPDQPERPPQPQA--------PPPPQPQPQPPPPPQPQPPPPPPPRpQPPLAPTTDPAGAGEPSGAV 2959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1008 PQPSTFSGMSTQATEPlsaRRALSQfSQLSSHATEPIPPHRQSLHLSELSSWS-----YEPKAPAPLALQKSTLSSQSTE 1082
Cdd:PHA03247 2960 PQPWLGALVPGRVAVP---RFRVPQ-PAPSREAPASSTPPLTGHSLSRVSSWAsslalHEETDPPPVSLKQTLWPPDDTE 3035
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2123157371 1083 PLEAKKPLPKLSSITSQSSVPVQPkmqalsvsstvSAQVSEPVDPPKPATP 1133
Cdd:PHA03247 3036 DSDADSLFDSDSERSDLEALDPLP-----------PEPHDPFAHEPDPATP 3075
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
164-337 |
2.71e-04 |
|
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: 45.78 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 164 KQRNQQPSRindiaLATEIStSLLSQLKElqavllerDDALKAADLDR-SQLEIEVEGLSQRLRVVDESESRLKDVNWSL 242
Cdd:TIGR04523 113 KNDKEQKNK-----LEVELN-KLEKQKKE--------NKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELENELNLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 243 ETQVRESEVLTKAAADRENRLNHSLNLLRTEKS---TLEREFEDLKQQFTKLSDDHINKTK---QTETELTSLRRNVAMT 316
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDNIEKKQQeinEKTTEISNTQTQLNQL 258
|
170 180
....*....|....*....|....*
gi 2123157371 317 ETE----KNALQRKVEELSNQNQEL 337
Cdd:TIGR04523 259 KDEqnkiKKQLSEKQKELEQNNKKI 283
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
51-262 |
2.78e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAHLSETTRRLQETShlgnalvQQRRELEEKLHEVEQQQQesdmgpELRQRLAELEKEFNEV-------GRET 123
Cdd:COG4942 54 LKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEIA------ELRAELEAQKEELAELlralyrlGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 124 ARAFLPKSRVPsgeADSAIGQSVYSSEAQHsptkvsvpSRKQRNQQPSRINDIALATEISTSLLSQLKELQAVLLERDDA 203
Cdd:COG4942 121 PLALLLSPEDF---LDAVRRLQYLKYLAPA--------RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2123157371 204 LKAADLDR----SQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENR 262
Cdd:COG4942 190 LEALKAERqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1123-1450 |
3.44e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1123 EPVDPPKPATPTMSMHS-ALATEPIAPRQQVLRQANIETQQTEPMEPSVIVPSqygvsnvttlhDAHPESP--TLPPHLP 1199
Cdd:PHA03247 2505 DPDAPPAPSRLAPAILPdEPVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPP-----------AAPPAAPdrSVPPPRP 2573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1200 SPSrsPTRPATAQR-----LPP----PKLALSFVSSQDTEPRDSSRPATAHRSLPPVLSTSATSVEHDEENTQAIEPSKS 1270
Cdd:PHA03247 2574 APR--PSEPAVTSRarrpdAPPqsarPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER 2651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1271 SFSDNIVSRGA-DRDSRTPLAPISSNLAPRSARPQMSDGGTQTMVSaeqidkllLARnqrysaiftPSSVEKVASPPPSP 1349
Cdd:PHA03247 2652 PRDDPAPGRVSrPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS--------LAD---------PPPPPPTPEPAPHA 2714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1350 SrrhsnegrTPRRPGSSGSIRSRAASPPPlpadhreviaaAAKSLPPPSPTvgamGPPVMPASAYKKRPTTPSIRTNSAT 1429
Cdd:PHA03247 2715 L--------VSATPLPPGPAAARQASPAL-----------PAAPAPPAVPA----GPATPGGPARPARPPTTAGPPAPAP 2771
|
330 340
....*....|....*....|.
gi 2123157371 1430 LTPRAGGTTPRARRQSARSGA 1450
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLS 2792
|
|
| PH_PLC_ELMO1 |
cd01248 |
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ... |
1506-1608 |
3.84e-04 |
|
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269952 Cd Length: 108 Bit Score: 41.54 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1506 LWKYtrktgREGLSenRHRRFFWIHPYTRTLYWSDRdpqsagKTEMKGKSVAIESVREV-----------EDNNPLPPGL 1574
Cdd:cd01248 7 LLKY-----REGSK--PKERTFYLDPDGTRITWESS------KKKSEKKSIDISDIKEIrpgkdtdgfkrKKKSNKPKEE 73
|
90 100 110
....*....|....*....|....*....|....
gi 2123157371 1575 HQKSLIIGTPGRSIKFTAPTGQRHETWFNALNYL 1608
Cdd:cd01248 74 RCFSIIYGSNNKTLDLVAPSEDEANLWVEGLRAL 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-436 |
4.15e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 255 AAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDDhinkTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQN 334
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 335 QELAK-------------AVAYRMKVDEQIALEdTSPDDGTE-ERETQTPEHSPPPSPSKAtprhgmlesETLKHSLQHa 400
Cdd:COG4942 93 AELRAeleaqkeelaellRALYRLGRQPPLALL-LSPEDFLDaVRRLQYLKYLAPARREQA---------EELRADLAE- 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2123157371 401 hrmIQQLKNNIHREKTEKIELKRMLQDARDELETNR 436
Cdd:COG4942 162 ---LAALRAELEAERAELEALLAELEEERAALEALK 194
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
69-369 |
4.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 69 QETSHLGNALVQQRRELEEKLHEVEQQQQEsdmgpeLRQRLAELEKEFNEVGRETARAflpksrvpsgeadsaigqsvys 148
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQ------LREELEQAREELEQLEEELEQA---------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 149 seaqhsptkvsvpsRKQRNQQPSRINDIAlateistsllSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVV 228
Cdd:COG4372 72 --------------RSELEQLEEELEELN----------EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 229 DESESRLKDvnwsletqvrESEVLTKAAADRENRLNHslnlLRTEKSTLEREFEDLKQQFTKLSDDHINKTKQtetELTS 308
Cdd:COG4372 128 EQQRKQLEA----------QIAELQSEIAEREEELKE----LEEQLESLQEELAALEQELQALSEAEAEQALD---ELLK 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123157371 309 LRRNVAMTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEERETQT 369
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
77-301 |
5.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 77 ALVQQRRELEEKLHEVEQQQQESDmgpELRQRLAELEKEFNEVGRETARAflpksrvpsgeadsaigqsvysseaqhspt 156
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELE---ELEEELEELEAELEELREELEKL------------------------------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 157 kvsvpsRKQRNQQPsrindialateistsLLSQLKELQAVLL---ERDDALKAADLDRSQLEIEVEGLSQRLRVVDESES 233
Cdd:COG4717 122 ------EKLLQLLP---------------LYQELEALEAELAelpERLEELEERLEELRELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123157371 234 RLKDvNWSLETQVRESEvltkaAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSDDHINKTKQ 301
Cdd:COG4717 181 ELLE-QLSLATEEELQD-----LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
177-352 |
5.67e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 177 ALATEISTSLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRL----RVVDESESRLKDVNWSLETQVRESEVL 252
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalaRRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 253 TKAAADRENRLNHSLN-------------LLRTEKST-LEREFEDLKQqftkLSDDHINKTKQTETELTSLRRNVAMTET 318
Cdd:COG4942 96 RAELEAQKEELAELLRalyrlgrqpplalLLSPEDFLdAVRRLQYLKY----LAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190
....*....|....*....|....*....|....
gi 2123157371 319 EKNALQRKVEELSNQNQELAKAVAYRMKVDEQIA 352
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
51-257 |
6.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 51 AQAKRALQAhLSETTRRLQETShlgNALVQQRRELEEKLHEVEQQQQESDMGPELRQ-RLAELEKEFNEVGRETARAFLP 129
Cdd:COG4372 97 AQAQEELES-LQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQEELAALEQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 130 KSRVPSGEADSAIGQSVYSSEAQHSPTKVSVPSRKQRNQQPSRINDIALATEISTSLLSQLKELQAVLLERDDALKAADL 209
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2123157371 210 DRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAA 257
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1010-1408 |
7.43e-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: 44.76 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1010 PSTFSGMSTQATEPLSARRALSQFSQ--LSSHATEPIPPHRQSLHLSELSSWSYEPKAPApLALQKSTLSSQStePLEAK 1087
Cdd:pfam03154 146 PSIPSPQDNESDSDSSAQQQILQTQPpvLQAQSGAASPPSPPPPGTTQAATAGPTPSAPS-VPPQGSPATSQP--PNQTQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1088 KPLPKLSSItsQSSVPVQPKmqalSVSSTVSAQVSEPVDPPKPATPTMSMHSALATEPIAPRQQVLRQANIETQQTEPME 1167
Cdd:pfam03154 223 STAAPHTLI--QQTPTLHPQ----RLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1168 PSVIVP----SQYGVSNVTTLHDAHPESPTLPPhlPSPSRSPTRPATAQRLPPPKLALSFVSSQDTEPRDSSRPATAHRS 1243
Cdd:pfam03154 297 PFPLTPqssqSQVPPGPSPAAPGQSQQRIHTPP--SQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKH 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1244 lPPVLSTsatsvehdeentqaiePSKSSFSDNIVSRGADRdsrtPLAPISSNLAPRSARPQMSDGGTQTMVSAEQIDKLL 1323
Cdd:pfam03154 375 -PPHLSG----------------PSPFQMNSNLPPPPALK----PLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPV 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1324 LARNQRYSAIF----TPSSVEKVASPPPSPSRRHSNEGRTPRRPGSSgsirSRAASPPPLPADHREVIAAAAKSLPPPSp 1399
Cdd:pfam03154 434 LTQSQSLPPPAashpPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSG----PPTSTSSAMPGIQPPSSASVSSSGPVPA- 508
|
....*....
gi 2123157371 1400 TVGAMGPPV 1408
Cdd:pfam03154 509 AVSCPLPPV 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-435 |
7.49e-04 |
|
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: 44.63 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 163 RKQRNQQPSRINDIALATEISTSLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDvnwSL 242
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK---QL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 243 ETQVRESEVLTKAAADRENRLNhslnllrteksTLEREFEDLKQQ----FTKLSDDHI----NKTKQTETELTSLRRNVA 314
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLN-----------QLKSEISDLNNQkeqdWNKELKSELknqeKKLEEIQNQISQNNKIIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 315 MTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEERETQTPEhspppspskatprhgmLESEtlk 394
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND----------------LESK--- 399
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2123157371 395 hsLQHAHRMIQQLKNNIHREKTEKIELKRMLQDARDELETN 435
Cdd:TIGR04523 400 --IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1327-1434 |
7.84e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1327 NQRYSAIFT---------PSSVEKVAS--------PPPSPSRRHSNEGRTP--RRPGSSGSIRSRAASPPPLPADHREVI 1387
Cdd:PHA03247 344 RQHYPLGFPkrrrptwtpPSSLEDLSAgrhhpkraSLPTRKRRSARHAATPfaRGPGGDDQTRPAAPVPASVPTPAPTPV 423
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1388 AAAA---KSLPPPSPTVGAMGPPVMPASAYKKRPTTPSIRTNSATLTPRA 1434
Cdd:PHA03247 424 PASApppPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRKA 473
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1124-1397 |
8.72e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.46 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1124 PVDPPKPATPTMSMHSALATEPIAPRQQVLRQANIETQQTEPMEPSVIVPSQYGVSNVTTlhDAHPESPTLPPHLPSPSR 1203
Cdd:PRK07003 381 PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGD--DAADGDAPVPAKANARAS 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1204 SPTRPATAQRLPPPKLALSFVSSQDTEPrdssrPATAHRSLPPVLSTSATSVEHDEENTQAIepskssfsdniVSRGADR 1283
Cdd:PRK07003 459 ADSRCDERDAQPPADSGSASAPASDAPP-----DAAFEPAPRAAAPSAATPAAVPDARAPAA-----------ASREDAP 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1284 DSRTPLAPISSNLAPRSARPQMSDGGTQTMVSAEQIDKLLLARNQRYSAIFTPSSVEKVASPPPSPSRRHSNEGRTPRRP 1363
Cdd:PRK07003 523 AAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRAR 602
|
250 260 270
....*....|....*....|....*....|....
gi 2123157371 1364 GSSGSIRSRAASPPPLPADHReviaaaakSLPPP 1397
Cdd:PRK07003 603 AATGDAPPNGAARAEQAAESR--------GAPPP 628
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-333 |
9.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 189 QLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVV----DESESRLKDvnwSLETQVRESEVLTKAAADRENRLN 264
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqiRGNGGDRLE---QLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123157371 265 HSLNLLRTEKSTLEREFEDLKQQFTKLSDDHINKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQ 333
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
57-339 |
1.01e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 57 LQAHLSETTRRL--QETSHlgnalVQQRRELEEKLHEVEQQ-QQESDMGPELRQRLAELEKefnevgRETARAflpksrv 133
Cdd:pfam05557 7 SKARLSQLQNEKkqMELEH-----KRARIELEKKASALKRQlDRESDRNQELQKRIRLLEK------REAEAE------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 134 psgEADSAigqsvySSEAQHSPTKVSVPSRKQRNQQPSRINDialATEISTSLLSQLKELQAVLlerddalKAADLDRSQ 213
Cdd:pfam05557 69 ---EALRE------QAELNRLKKKYLEALNKKLNEKESQLAD---AREVISCLKNELSELRRQI-------QRAELELQS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 214 LEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENRL---NHSLNLLRTEKSTLER--EFEDLKQQF 288
Cdd:pfam05557 130 TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIqsqEQDSEIVKNSKSELARipELEKELERL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2123157371 289 tklsDDHINKtkqteteLTSLRRNVAMTETEKNALQRKVEELSNQNQELAK 339
Cdd:pfam05557 210 ----REHNKH-------LNENIENKLLLKEEVEDLKRKLEREEKYREEAAT 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-339 |
1.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 163 RKQRNQQPSRINDIALATE-ISTSLLSQLKELQAVLLErddaLKAADLDRSQLEIEVEGLSQRLRVVDESESR---LKDV 238
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTEnIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVKELEELKEEieeLEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 239 NWSLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLErEFEDLKQQFTKLS---DDHINKTKQTETELTSLRRnvam 315
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSefyEEYLDELREIEKRLSRLEE---- 321
|
170 180
....*....|....*....|....
gi 2123157371 316 tetEKNALQRKVEELSNQNQELAK 339
Cdd:PRK03918 322 ---EINGIEERIKELEEKEERLEE 342
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-290 |
1.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 104 ELRQRLAELEKEFNEVGRETARAflpksrvpSGEADSAIGQ-SVYSSEAQHSPTKVSVPS-RKQRNQQPSRINDIALATE 181
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEAL--------EAELDALQERrEALQRLAEYSWDEIDVASaEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 182 ISTSLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRL-----RVVDESESRLKDVNWSLETQVREsEVLTKAA 256
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqdRLEAAEDLARLELRALLEERFAA-ALGDAVE 764
|
170 180 190
....*....|....*....|....*....|....
gi 2123157371 257 ADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTK 290
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
78-456 |
1.40e-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: 43.88 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 78 LVQQRRELEEKLHEV-EQQQQESDMGpELRQRLAELEKEfnevgretaRAFLPKSrvpSGEADSAIGQSVYSSEAQHSPT 156
Cdd:TIGR00606 617 KEEQLSSYEDKLFDVcGSQDEESDLE-RLKEEIEKSSKQ---------RAMLAGA---TAVYSQFITQLTDENQSCCPVC 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 157 KVSVPSRKQRNQQPSRI-NDIALATEISTSLLSQLKELQAvllERDDALKAADLDRSQLEI---EVEGLSQRLRVV---- 228
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLqSKLRLAPDKLKSTESELKKKEK---RRDEMLGLAPGRQSIIDLkekEIPELRNKLQKVnrdi 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 229 -------DESESRLKDVNWSLE------TQVRESEVLTKAAADRENR------------LNHSLNLLRTEKSTLEREFED 283
Cdd:TIGR00606 761 qrlkndiEEQETLLGTIMPEEEsakvclTDVTIMERFQMELKDVERKiaqqaaklqgsdLDRTVQQVNQEKQEKQHELDT 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 284 LKQQ---FTKLSDD---HINKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVayRMKVDEQIALEDTS 357
Cdd:TIGR00606 841 VVSKielNRKLIQDqqeQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREI--KDAKEQDSPLETFL 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 358 PDDGTEERETQTPEHSPPpspskatpRHGMLESETLKHSLQHAHRMIQQLKNNIHREKtekielKRMLQDARDELETNRG 437
Cdd:TIGR00606 919 EKDQQEKEELISSKETSN--------KKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYLKQKETELNTVNA 984
|
410
....*....|....*....
gi 2123157371 438 ALNgpgSAGKRRSKTDKDL 456
Cdd:TIGR00606 985 QLE---ECEKHQEKINEDM 1000
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
26-330 |
1.41e-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: 43.67 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 26 AHDAQRQRYAAFDN--SQFSLYLNGSPAQAKRALQAHLS--ETTRRL-----QETSHLGNALVQQRRELEEKLHEVEQQQ 96
Cdd:pfam12128 612 ALQSAREKQAAAEEqlVQANGELEKASREETFARTALKNarLDLRRLfdekqSEKDKKNKALAERKDSANERLNSLEAQL 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 97 QESDMgpELRQRLAELEKEFnevgRETARAFLPKSRVPSGEADSAIGQSVYSSEAQHSptkvsvpSRKQRnqqpsrindi 176
Cdd:pfam12128 692 KQLDK--KHQAWLEEQKEQK----REARTEKQAYWQVVEGALDAQLALLKAAIAARRS-------GAKAE---------- 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 177 alateistslLSQLKElqavllERDDALKAADLDrsqlEIEVEGLSQRLRvvdESESRLKDVnwsletQVRESEVLTKAA 256
Cdd:pfam12128 749 ----------LKALET------WYKRDLASLGVD----PDVIAKLKREIR---TLERKIERI------AVRRQEVLRYFD 799
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2123157371 257 ADRENRLNHSLNLlRTEKSTLEREFEDLKQQFTKLSDDHINKTKQTETELTSLRR-NVAMTE--TEKNALQRKVEEL 330
Cdd:pfam12128 800 WYQETWLQRRPRL-ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKqQVRLSEnlRGLRCEMSKLATL 875
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
699-863 |
2.11e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.99 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 699 SSPEHLKRQAETVKSVMVDSGMMTEPVPRQAVGLSTIQSRATEPQVPRPASLHfsaLSAENTIPQAAPRPDLRVSSVSAQ 778
Cdd:PLN03209 389 TPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPY---ARYEDLKPPTSPSPTAPTGVSPSV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 779 ETLPKASLQPALTVSTVSGHSTQPEAPRVAPLTFSSLSAHESVP-EPAPAARLGVSSVSSQNTLPEAARSVPLDMSSISM 857
Cdd:PLN03209 466 SSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPtSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQ 545
|
....*.
gi 2123157371 858 HHTEPQ 863
Cdd:PLN03209 546 HHAQPK 551
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1186-1445 |
2.36e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1186 DAHPESPTLPPHlPSPSRSPTRPaTAQRLPPPKLA----LSFVSSQDT-EPRD----SSRPATAHRSLPPvlSTSATSVE 1256
Cdd:PHA03247 2503 PPDPDAPPAPSR-LAPAILPDEP-VGEPVHPRMLTwirgLEELASDDAgDPPPplppAAPPAAPDRSVPP--PRPAPRPS 2578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1257 HDEENTQAIEPSKSSFSDNIVSRGADRDS-RTPLAPISSNLAPRSARPQMSDGGTQTMVSAEQIDKLLLARNQRYSAIFT 1335
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDpRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP 2658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1336 PSSVEKVASPPPSPSRRHSNEGRTPRRPGSSGSIRSRA--ASPPPLPADHReviaaaakslPPPSPTVGAMGPPVMPASA 1413
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTslADPPPPPPTPE----------PAPHALVSATPLPPGPAAA 2728
|
250 260 270
....*....|....*....|....*....|....
gi 2123157371 1414 YKKRPTTPSIRTNSATLTPRA--GGTTPRARRQS 1445
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAGPAtpGGPARPARPPT 2762
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
77-342 |
2.47e-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: 42.44 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 77 ALVQQRRELEEKLHEVEQQQQEsdmgpeLRQRLAELEKEFNEVGRETAraflpksrvpsgEADSAIGQSVysseaqhspT 156
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAE------LEKELAALKKEEKALLKQLA------------ALERRIAALA---------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 157 KVSVpSRKQRNQQPSRINDiaLATEISTsLLSQLKELQAVLLERDDAL-KAADLDRSQLEIEVEGLSQRLRVVDesesRL 235
Cdd:COG4942 70 RIRA-LEQELAALEAELAE--LEKEIAE-LRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQ----YL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 236 KDVNWSLETQVREsevltkaaadrenrLNHSLNLLRTEKSTLEREFEDLKQQFTKLSddhiNKTKQTETELTSLRRNVAM 315
Cdd:COG4942 142 KYLAPARREQAEE--------------LRADLAELAALRAELEAERAELEALLAELE----EERAALEALKAERQKLLAR 203
|
250 260
....*....|....*....|....*..
gi 2123157371 316 TETEKNALQRKVEELSNQNQELAKAVA 342
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-342 |
2.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 189 QLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVvdesESRLKDVNWsletqvreSEVLTKAAADRENRLNHSLN 268
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREA----LQRLAEYSW--------DEIDVASAEREIAELEAELE 678
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2123157371 269 LLRTEKS---TLEREFEDLKQQFtklsddhinktKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVA 342
Cdd:COG4913 679 RLDASSDdlaALEEQLEELEAEL-----------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
56-337 |
3.01e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 56 ALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQE-SDMGPELRQRLAELeKEFNEVGRETARAfLPKSRVP 134
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaATLELEKEKLEQEL-QSWVKLAQDTGLN-LRSPEDL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 135 SGE------ADSAIGQSVYSSEAQhsptkvsvpSRKQRNQQPSrindiaLATEIStSLLSQLKELQAVLlERDDALKaad 208
Cdd:pfam05557 282 SRRieqlqqREIVLKEENSSLTSS---------ARQLEKARRE------LEQELA-QYLKKIEDLNKKL-KRHKALV--- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 209 lDRSQ-----LEIEVEGLSQRLRVVDeseSRLKDVNWSLETQVRESEvltkaAADRENRLNHSLNLLRTEKSTLEREFED 283
Cdd:pfam05557 342 -RRLQrrvllLTKERDGYRAILESYD---KELTMSNYSPQLLERIEE-----AEDMTQKMQAHNEEMEAQLSVAEEELGG 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2123157371 284 LKQQFTKLsddhinktkqtETELTSLRRNVAM-----TETEKNALQRKVEELSNQNQEL 337
Cdd:pfam05557 413 YKQQAQTL-----------ERELQALRQQESLadpsySKEEVDSLRRKLETLELERQRL 460
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
191-317 |
3.23e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 42.00 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 191 KELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENRLNHSLN-L 269
Cdd:COG5414 259 KEKQGAEEEGEEGMSEEDLDVGAAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEIGEEKEEDDENEENERHTeL 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2123157371 270 LRTEKSTLEREFEDLKQQFTK-----LSDDHINKTKQTETELTSLRRNVAMTE 317
Cdd:COG5414 339 LADELNELEKGIEEKRRQMESatnpiLQKRFESQLNVLLKELELKRKQLEMEE 391
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
38-333 |
3.35e-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: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 38 DNSQFSLYL----NGSPAQAKRALQAHLS---ETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQESDMGPE------ 104
Cdd:TIGR00606 284 DNSELELKMekvfQGTDEQLNDLYHNHQRtvrEKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqehi 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 105 -----LRQRLA-ELEKEFNEVG----RETARAFLPKSRVPSGEADSAigqSVYSSEAQHSPTKVSVPSRKQRNQQPSRIN 174
Cdd:TIGR00606 364 rardsLIQSLAtRLELDGFERGpfseRQIKNFHTLVIERQEDEAKTA---AQLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 175 DIALATEISTSLLSQLK----ELQAV------LLERDDALKAADLDRSQLE---------IEVEGLSQRLRVVDESESRL 235
Cdd:TIGR00606 441 TIELKKEILEKKQEELKfvikELQQLegssdrILELDQELRKAERELSKAEknsltetlkKEVKSLQNEKADLDRKLRKL 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 236 KDVNWSLE---TQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDlKQQFTKLSDDHINKTKQTETELTSLRRN 312
Cdd:TIGR00606 521 DQEMEQLNhhtTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKE 599
|
330 340
....*....|....*....|.
gi 2123157371 313 VAMTETEKNALQRKVEELSNQ 333
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQ 620
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
1505-1610 |
4.04e-03 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 38.68 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1505 YLWKYTRKTGReglseNRHRRFFWIHPytRTLYWSDrDPQSAGKTEMKGK-SVAIESVREVEDNNPLPpglHQKSLIIGT 1583
Cdd:smart00233 6 WLYKKSGGGKK-----SWKKRYFVLFN--STLLYYK-SKKDKKSYKPKGSiDLSGCTVREAPDPDSSK---KPHCFEIKT 74
|
90 100
....*....|....*....|....*...
gi 2123157371 1584 P-GRSIKFTAPTGQRHETWFNALNYLCQ 1610
Cdd:smart00233 75 SdRKTLLLQAESEEEREKWVEALRKAIA 102
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1191-1446 |
4.40e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.14 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1191 SPTLPPHLPSPSRSPTRPATAQ----RLPPPKLALSFVSSQDTEPRDSSRP-ATAHRSLPPVLSTSATSVEHDEENTQAI 1265
Cdd:PRK07003 373 PARVAGAVPAPGARAAAAVGASavpaVTAVTGAAGAALAPKAAAAAAATRAeAPPAAPAPPATADRGDDAADGDAPVPAK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1266 EPSKSSfsdnIVSRGADRDSRTPLAPISSNLAPRSARPQMSDGGTQTMVSAEQIDKLLLARNQRYSAIFTPSSVEKVASP 1345
Cdd:PRK07003 453 ANARAS----ADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPP 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1346 PPSPSRRHSNEGRTPRRPGSSG--------------SIRSRAASPPPLPAdhreviAAAAKSLPPPSPtvgamgppvmpa 1411
Cdd:PRK07003 529 APEARPPTPAAAAPAARAGGAAaaldvlrnagmrvsSDRGARAAAAAKPA------AAPAAAPKPAAP------------ 590
|
250 260 270
....*....|....*....|....*....|....*
gi 2123157371 1412 saykkRPTTPsirtnsaTLTPRAGGTTPRARRQSA 1446
Cdd:PRK07003 591 -----RVAVQ-------VPTPRARAATGDAPPNGA 613
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
56-346 |
4.54e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 56 ALQAHLSETTRRLQETSHLGNALVQQRRELEEKLHEVEQQQQ-----------ESDMGPELRQRLAE--------LEKEF 116
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINhynekksrLEEKI 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 117 NEVGRETA-----RAFLPK--SRVPSGEADSAIGQSVYSSEAQHSPTKVSVpsrkqrnqqpsRINDIALATEISTSLLSQ 189
Cdd:PRK01156 486 REIEIEVKdidekIVDLKKrkEYLESEEINKSINEYNKIESARADLEDIKI-----------KINELKDKHDKYEEIKNR 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 190 LKELQAVLLE--RDDALKAA------DLD--RSQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEvltkaaaDR 259
Cdd:PRK01156 555 YKSLKLEDLDskRTSWLNALavisliDIEtnRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE-------NE 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 260 ENRLNHSLNLLRTEK---STLEREFEDLKQQFTKLsdDHINKTK--------QTETELTSLRRNVAMTETEKNALQRKVE 328
Cdd:PRK01156 628 ANNLNNKYNEIQENKiliEKLRGKIDNYKKQIAEI--DSIIPDLkeitsrinDIEDNLKKSRKALDDAKANRARLESTIE 705
|
330
....*....|....*...
gi 2123157371 329 ELSNQNQELAKAVAYRMK 346
Cdd:PRK01156 706 ILRTRINELSDRINDINE 723
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
179-337 |
4.75e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 179 ATEIST--SLLSQLKELQAVLLERDDALKAADLDRSQLEIEVEGLSQRLRVVDESESRLKDvnwSLETqvresevLTKAa 256
Cdd:PRK04778 344 ESELESvrQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSE---MLQG-------LRKD- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 257 adrENRLNHSLNLLRTEKSTLEREFE---------DLKQQFTKLSDdhinKTKQTETELTSLRRNVamtetekNALQRKV 327
Cdd:PRK04778 413 ---ELEAREKLERYRNKLHEIKRYLEksnlpglpeDYLEMFFEVSD----EIEALAEELEEKPINM-------EAVNRLL 478
|
170
....*....|
gi 2123157371 328 EELSNQNQEL 337
Cdd:PRK04778 479 EEATEDVETL 488
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
738-1227 |
4.77e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 738 RATEPQVPRPASLHFSALSAENTIPQAAPRPDLRVSSVSAQETLPKASLQPAltvstvsghSTQPEAPRVAPlTFSSLSA 817
Cdd:PHA03247 2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---------VPPPERPRDDP-APGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 818 HESVPEPAPAARlgvSSVSSQNTLPEAARSVPLDMSSISMHH---TEPQHAATPALSMSSLSMhqtepqhlaVPAMGMSG 894
Cdd:PHA03247 2664 PRRARRLGRAAQ---ASSPPQRPRRRAARPTVGSLTSLADPPpppPTPEPAPHALVSATPLPP---------GPAAARQA 2731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 895 LVSNETQPLAPTQDNSRALSMGVSgivhQSSEPREGNTGRALASGALLVSGIHSQSTEPSDLGSSAVTQRNPQQLDSAIQ 974
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGPA----RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 975 PDGHESRTQDQPRH----TPLQMSNVSAHSTEPTASRPQPSTF-------------------SGMSTQATEPLSARRALS 1031
Cdd:PHA03247 2808 PAAVLAPAAALPPAaspaGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvrrrppsrSPAAKPAAPARPPVRRLA 2887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1032 QFSQLSSHATEPIPPHRQSLHLSELSSWSYEPKAPAPLALQKSTLSSQSTEPLEAKKPLPKLSSITSQSSVPVQPKMQAL 1111
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 1112 -----SVSSTVSAQVSEPVDPPKPATPTMSMHS-----------ALATEPiAPRQQVLRQANIETQQTEPMEPSVIVPSQ 1175
Cdd:PHA03247 2968 vpgrvAVPRFRVPQPAPSREAPASSTPPLTGHSlsrvsswasslALHEET-DPPPVSLKQTLWPPDDTEDSDADSLFDSD 3046
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2123157371 1176 YGVSNVTTLhDAHPESPTLPPHLPSPSRSP---TRPATAQRLPPPKLALSFVSSQ 1227
Cdd:PHA03247 3047 SERSDLEAL-DPLPPEPHDPFAHEPDPATPeagARESPSSQFGPPPLSANAALSR 3100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-312 |
5.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 188 SQLKELQAVLLERDDALKAADLDR-SQLEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEvltKAAADRENRLNHS 266
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASA---EEFAALRAEAAAL 392
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2123157371 267 LNLLRTEKSTLEREFEDLKQQFTKLSDDHinktKQTETELTSLRRN 312
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERR 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
54-365 |
5.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 54 KRALQAHLSETTRRLQETShlgNALVQQRRELEEKLHEVEQQQQESDmgpELRQRLAELEKEFNEVgrETARAFLPKSRV 133
Cdd:COG4372 61 LEQLEEELEQARSELEQLE---EELEELNEQLQAAQAELAQAQEELE---SLQEEAEELQEELEEL--QKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 134 PSGEADSAIGQSVYSSEAQhsptkvsvpsRKQRNQQPSRINDIALATEISTSLLSQLKELQAVLLERDDALKAADLDRSQ 213
Cdd:COG4372 133 QLEAQIAELQSEIAEREEE----------LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 214 LEIEVEGLSQRLRVVDESESRLKDVNWSLETQVRESEVLTKAAADRENRLNHSLNLLRTEKSTLEREFEDLKQQFTKLSD 293
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2123157371 294 DHINK-TKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAVAYRMKVDEQIALEDTSPDDGTEER 365
Cdd:COG4372 283 LELEAlEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
286-341 |
5.95e-03 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 41.35 E-value: 5.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123157371 286 QQFTKLSDDHI-----NKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQELAKAV 341
Cdd:PRK13729 60 TTFDDKVRQHAttemqVTAAQMQKQYEEIRRELDVLNKQRGDDQRRIEKLGQDNAALAEQV 120
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
211-337 |
6.91e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 211 RSQLEIEVEGLSQRLRVVDESESRLKDvnwSLETQVR---------ESEvLTKAAADREnrlnhSLNLLRTEKSTLEREF 281
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQE---DLEKQAEiareaqqnyERE-LVLHAEDIK-----ALQALREELNELKAEI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2123157371 282 EDLKQQFTKLSDDHINKTKQTETELTSLrrnvamtETEKNALQRKVEELSNQNQEL 337
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKEL-------EKELSELEKRIEDLNEQNKLL 122
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
200-352 |
9.60e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 200 RDDALKAAdldrsqleieVEgLSQR-----------LRVVDESESRLK----------DvnwSLETQVRESEVlTKAAAD 258
Cdd:COG0542 367 TDEALVAA----------VR-LSDRyitdrflpdkaIDLIDEAAARVRmeidskpeelD---ELERRLEQLEI-EKEALK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123157371 259 RENRLNH--SLNLLRTEKSTLEREFEDLKQQFtklsddhiNKTKQTETELTSLRRNVAMTETEKNALQRKVEELSNQNQE 336
Cdd:COG0542 432 KEQDEASfeRLAELRDELAELEEELEALKARW--------EAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAE 503
|
170
....*....|....*..
gi 2123157371 337 LAKAVayRMKVDEQ-IA 352
Cdd:COG0542 504 LAPLL--REEVTEEdIA 518
|
|
| |
