|
Name |
Accession |
Description |
Interval |
E-value |
| MRVI1 |
pfam05781 |
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the ... |
1028-1512 |
9.26e-82 |
|
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the lymphoid-restricted membrane protein (JAW1) and the IP3 receptor associated cGMP kinase substrates A and B (IRAGA and IRAGB). The function of MRVI1 is unknown although mutations in the Mrvi1 gene induces myeloid leukaemia by altering the expression of a gene important for myeloid cell growth and/or differentiation so it has been speculated that Mrvi1 is a tumour suppressor gene. IRAG is very similar in sequence to MRVI1 and is an essential NO/cGKI-dependent regulator of IP3-induced calcium release. Activation of cGKI decreases IP3-stimulated elevations in intracellular calcium, induces smooth muscle relaxation and contributes to the antiproliferative and pro-apoptotic effects of NO/cGMP. Jaw1 is a member of a class of proteins with COOH-terminal hydrophobic membrane anchors and is structurally similar to proteins involved in vesicle targeting and fusion. This suggests that the function and/or the structure of the ER in lymphocytes may be modified by lymphoid-restricted resident ER proteins.
Pssm-ID: 461738 Cd Length: 521 Bit Score: 279.09 E-value: 9.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1028 TSSSPHSGSPVTHASQSGSGVGSvtsdPCQS---ADSAAKKDSLPLGGKKKRELERESSMEVI---EERKVQEDQSESSV 1101
Cdd:pfam05781 59 TVTSSDSRSPILRMASWDLDCKE----LCEKeeeKRFASKAGEKQGKSPAFKDIQIQVSEEHIlmrNKNLVGLEAPEESE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1102 TTDKGSDMSGSSGTAIAD------------KNSSLSPNDKEIEADFQRLALGFKCDMFTLEKRLRLEERSRDLAEENVRK 1169
Cdd:pfam05781 135 TAEQERKESAAGEDVMSSipdvlvkkvnfhQSLNTSANEKEVEAEFLRLSLAFKCDWFTLEKRVKLEERSRDLAEENLKK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1170 EISSCQGLLQALTPLCEDDNQSMEIIQRLQKNLEILIQSMSRVSSRSEMLGAIHQESRIGKAVEVMIQHVENLRRMYTKE 1249
Cdd:pfam05781 215 EITNCLKLLESLTPLCEHDNQAQEIYKKLEKSIAVLSQCAARVASRAEMLGAINQESRVSKAVEVMIQHVENLKRMYAKE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1250 HAELLELREALMQNERSFGSQTErgKDDFRGKKQPTQY--YKSSTRRVSIAAIPRSGGgnmQFDMSKTQDcsetETERLT 1327
Cdd:pfam05781 295 HAELEELKQLLLQNSRSFNPLED--EDDCQIKKRSMSLnsKPSSLRRVSIASLPRNIG---NSGMASGME----NNDRLS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1328 RRSP-WNV--GGKSSARPPLKRFVSSAAWVETEEPSLLMKgtAYDNtdcqvEDEQKEEPVAERRRSSLSELGSKltslil 1404
Cdd:pfam05781 366 RRSSsWRIlgNKQSEHRPSLHRFISTYSWSDAEEESCEVK--AKDE-----EEPYGEEGVEKTRKPSLSEKKNN------ 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1405 PLKTSQDELFVMLptpspsptstdpgmAQSLSHSLTSSREAaaarsGRGLWLWLAMVVVLAGLLALLASLVMQPAVDAAP 1484
Cdd:pfam05781 433 PSKWDVSSIYETL--------------ASWLTNLYPSLRKA-----NKVLWLSVAAIVLFAALMSFLTGQFFQSCVEAAP 493
|
490 500
....*....|....*....|....*...
gi 1838139839 1485 VGTGDSWMTIQQLLWPYTGLRHNGQPPV 1512
Cdd:pfam05781 494 TQEGDSWCSLEHILWPFTGLQHEGPPPV 521
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
362-551 |
3.48e-47 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 167.66 E-value: 3.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 362 ETSELVCCVADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREE 441
Cdd:pfam14662 2 ETSDLLTCVEDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 442 GRARASAHSKRVDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLID 521
Cdd:pfam14662 82 ARRSLLAQNKQLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIE 161
|
170 180 190
....*....|....*....|....*....|
gi 1838139839 522 ELKSTVEEYSSITELLRSHKSKLESQMQMM 551
Cdd:pfam14662 162 ELKSTVEEYSSIEEELRAEKSRLESQLPDM 191
|
|
| EF-hand_9 |
pfam14658 |
EF-hand domain; |
243-308 |
5.59e-14 |
|
EF-hand domain;
Pssm-ID: 405361 Cd Length: 66 Bit Score: 67.84 E-value: 5.59e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 243 DTIFYACDTQRRGKVYVSHIVDFLRHTTSRNSGDSGLEDLCNMLDPEHKDISIDLVTYHAVMKEWI 308
Cdd:pfam14658 1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDALVDLDTFLRVMRDWI 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
330-745 |
1.58e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 330 LRDSLSAKRSMLFNITSgSLEAFggeASRAEFETSELVCCVADLQMSNQKLEEEVRKMKLVVE-SMEDSNQKLAEENEEL 408
Cdd:pfam15921 283 LTEKASSARSQANSIQS-QLEII---QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 409 HNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHSKRV-DRENQSLIaSIASLQEENFRVTMETEELQrriAE 487
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwDRDTGNSI-TIDHLRRELDDRNMEVQRLE---AL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 488 LRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEEYSSITELLRSHKSKLESqmqmmqpdmsgaglslsvafr 567
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES--------------------- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 568 lNQSSSGSLQTELALAQSPLEAhygvdllstTMSCVSPLDMTLDREVLLMLQGPNPEQMAREFKNLLNKLKRNFREEtNS 647
Cdd:pfam15921 494 -SERTVSDLTASLQEKERAIEA---------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEK-DK 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 648 VLSTTRGLLDNCAQPAGDQD---AVLQKVQAELDAKREDWALSLDQ---LAQYTDSLEKELMKMASNMRRSRTEILHL-S 720
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGrtaGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLELEKVKLVNAgS 642
|
410 420
....*....|....*....|....*
gi 1838139839 721 VRVQEQENQKHQLCEELEQIKTPQD 745
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRN 667
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-549 |
1.26e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 324 QEDSVKLRDSLSAKRSMLFNITSGSLEAFGgEASRAEFETSELVccvADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAE 403
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIE---KEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 404 ENEELhnqATVNQQLAQKEKMLN---EEVEEMKATLNcrEEGRARASAHSKRVDRENQSLIASIASLQEENFRVTMETE- 479
Cdd:TIGR02169 756 VKSEL---KELEARIEELEEDLHkleEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEy 830
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 480 ------ELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEEYSSITELLRSHKSKLESQMQ 549
Cdd:TIGR02169 831 lekeiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
378-530 |
2.17e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 378 QKLEEEVRKMKLVVEsmedsnqKLAEENEELHNQatvnqqLAQKEkmlnEEVEEMKATLN-CREEGRARAsahskRVDRE 456
Cdd:COG2433 409 TEEEEEIRRLEEQVE-------RLEAEVEELEAE------LEEKD----ERIERLERELSeARSEERREI-----RKDRE 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838139839 457 NQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLqvqiHSfdavvGEKEAVIVEKSRLIDELKSTVEEY 530
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRKLERLKELWKLE----HS-----GELVPVKVVEKFTKEAIRRLEEEY 531
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
849-955 |
2.29e-05 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 48.48 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 849 EHDLDVQSMQEQEAVPLSAHSQAVGIRNPeADAPPDLSHSKNNNGEALVTEESPSCDPAQNQSSSPEQePTVPPSNTPPT 928
Cdd:PRK10856 148 DQSSAELSQNSGQSVPLDTSTTTDPATTP-APAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQ-ANVDTAATPAP 225
|
90 100
....*....|....*....|....*..
gi 1838139839 929 EVPTDSTTPGPAETITQTESTQPTSED 955
Cdd:PRK10856 226 AAPATPDGAAPLPTDQAGVSTPAADPN 252
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
752-1069 |
6.52e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 752 QTPAPEEEPGDDLDWDEQFALQDfLKNELAERNCKEQGGRTERGEKEDAEErwtVVDTAGEGEVRDTSTPVSALSGRTlP 831
Cdd:PHA03307 23 RPPATPGDAADDLLSGSQGQLVS-DSAELAAVTVVAGAAACDRFEPPTGPP---PGPGTEAPANESRSTPTWSLSTLA-P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 832 RNGAAEEShdyaactesehdlDVQSMQEQEAVPLSAHSQAVGIRNPEADAPPDL----SHSKNNNGEALVTEESPSCDPA 907
Cdd:PHA03307 98 ASPAREGS-------------PTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLrpvgSPGPPPAASPPAAGASPAAVAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 908 --------QNQSSSPEQEPT--VPPSNTPPTEVPTDSTTPGPAETITQTESTQPTSEDHREEEKEGEADPSTGDMSHTKS 977
Cdd:PHA03307 165 daassrqaALPLSSPEETARapSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 978 PSQDQSADGSAAEDSTCLLPVLVEEEESVQDGTAEVVPTVSASM----EETDRFTSSSPHSGSPVTHASQSGSGVGSVTS 1053
Cdd:PHA03307 245 SGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSssprERSPSPSPSSPGSGPAPSSPRASSSSSSSRES 324
|
330
....*....|....*.
gi 1838139839 1054 DPCQSADSAAKKDSLP 1069
Cdd:PHA03307 325 SSSSTSSSSESSRGAA 340
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
372-745 |
2.34e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 372 DLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQAT-VNQQLAQKEKmLNEEVEEMKATLNCREEgrarasahs 450
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdLESKIQNQEK-LNQQKDEQIKKLQQEKE--------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 451 kRVDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRlidELKSTVEEY 530
Cdd:TIGR04523 423 -LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEKEL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 531 SSITEllrsHKSKLESQMQMMQPdmsgaglslsvafrlNQSSSGSLQTELALAQSPLEahygvDLLSTTMSCVSPLDMTL 610
Cdd:TIGR04523 499 KKLNE----EKKELEEKVKDLTK---------------KISSLKEKIEKLESEKKEKE-----SKISDLEDELNKDDFEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 611 DREVLlmlqgpnpEQMAREFKNLLNKLKrnfrEETNSVLSTTRGLldncaqpagdqDAVLQKVQAELDAKREdwalsldQ 690
Cdd:TIGR04523 555 KKENL--------EKEIDEKNKEIEELK----QTQKSLKKKQEEK-----------QELIDQKEKEKKDLIK-------E 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838139839 691 LAQYT---DSLEKELMKMASNMRRSRTEILHLsvrvqeqENQKHQLCEELEQIKTPQD 745
Cdd:TIGR04523 605 IEEKEkkiSSLEKELEKAKKENEKLSSIIKNI-------KSKKNKLKQEVKQIKETIK 655
|
|
| rad2 |
TIGR00600 |
DNA excision repair protein (rad2); All proteins in this family for which functions are known ... |
851-1095 |
3.26e-03 |
|
DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. 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: 273166 [Multi-domain] Cd Length: 1034 Bit Score: 42.19 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 851 DLDVQSMQEQEAVPLSAHSQAVGIRNPEADAPPDLSHSKN---NNGEALVTEESPSCDPAQNQSSSPEQEPTVPPSNTPp 927
Cdd:TIGR00600 509 DRKSELSIERTVKPVSSEFGLPSQREDKLAIPTEGTQNLQgisDHPEQFEFQNELSPLETKNNESNLSSDAETEGSPNP- 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 928 tEVPTDSTTPGPAETITQTESTQPTSEDHREEEKEgeadpstgdmSHTKSPSQDQSADGSAAEDSTCLLPVLVEEEESVQ 1007
Cdd:TIGR00600 588 -EMPSWSSVTVPSEALDNYETTNPSNAKEVRNFAE----------TGIQTTNVGESADLLLISNPMEVEPMESEKEESES 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1008 DGTAEVVPTVSaSMEETDRFTSSSPhsgspvTHASQSGSgvgsvtSDPCQSADSAAKKDSLPLggkKKRELERESSMEVI 1087
Cdd:TIGR00600 657 DGSFIEVDSVS-STLELQVPSKSQP------TDESEENA------ENKVASIEGEHRKEIEDL---LFDESEEDNIVGMI 720
|
....*...
gi 1838139839 1088 EERKVQED 1095
Cdd:TIGR00600 721 EEEKDADD 728
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-546 |
5.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 379 KLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRA---RASAHSKRV-D 454
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKRLtG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 455 RENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVG------------EKEAVIVEKSRLIDE 522
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKR 463
|
170 180
....*....|....*....|....
gi 1838139839 523 LKSTVEEYSSITELLRSHKSKLES 546
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEK 487
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MRVI1 |
pfam05781 |
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the ... |
1028-1512 |
9.26e-82 |
|
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the lymphoid-restricted membrane protein (JAW1) and the IP3 receptor associated cGMP kinase substrates A and B (IRAGA and IRAGB). The function of MRVI1 is unknown although mutations in the Mrvi1 gene induces myeloid leukaemia by altering the expression of a gene important for myeloid cell growth and/or differentiation so it has been speculated that Mrvi1 is a tumour suppressor gene. IRAG is very similar in sequence to MRVI1 and is an essential NO/cGKI-dependent regulator of IP3-induced calcium release. Activation of cGKI decreases IP3-stimulated elevations in intracellular calcium, induces smooth muscle relaxation and contributes to the antiproliferative and pro-apoptotic effects of NO/cGMP. Jaw1 is a member of a class of proteins with COOH-terminal hydrophobic membrane anchors and is structurally similar to proteins involved in vesicle targeting and fusion. This suggests that the function and/or the structure of the ER in lymphocytes may be modified by lymphoid-restricted resident ER proteins.
Pssm-ID: 461738 Cd Length: 521 Bit Score: 279.09 E-value: 9.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1028 TSSSPHSGSPVTHASQSGSGVGSvtsdPCQS---ADSAAKKDSLPLGGKKKRELERESSMEVI---EERKVQEDQSESSV 1101
Cdd:pfam05781 59 TVTSSDSRSPILRMASWDLDCKE----LCEKeeeKRFASKAGEKQGKSPAFKDIQIQVSEEHIlmrNKNLVGLEAPEESE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1102 TTDKGSDMSGSSGTAIAD------------KNSSLSPNDKEIEADFQRLALGFKCDMFTLEKRLRLEERSRDLAEENVRK 1169
Cdd:pfam05781 135 TAEQERKESAAGEDVMSSipdvlvkkvnfhQSLNTSANEKEVEAEFLRLSLAFKCDWFTLEKRVKLEERSRDLAEENLKK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1170 EISSCQGLLQALTPLCEDDNQSMEIIQRLQKNLEILIQSMSRVSSRSEMLGAIHQESRIGKAVEVMIQHVENLRRMYTKE 1249
Cdd:pfam05781 215 EITNCLKLLESLTPLCEHDNQAQEIYKKLEKSIAVLSQCAARVASRAEMLGAINQESRVSKAVEVMIQHVENLKRMYAKE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1250 HAELLELREALMQNERSFGSQTErgKDDFRGKKQPTQY--YKSSTRRVSIAAIPRSGGgnmQFDMSKTQDcsetETERLT 1327
Cdd:pfam05781 295 HAELEELKQLLLQNSRSFNPLED--EDDCQIKKRSMSLnsKPSSLRRVSIASLPRNIG---NSGMASGME----NNDRLS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1328 RRSP-WNV--GGKSSARPPLKRFVSSAAWVETEEPSLLMKgtAYDNtdcqvEDEQKEEPVAERRRSSLSELGSKltslil 1404
Cdd:pfam05781 366 RRSSsWRIlgNKQSEHRPSLHRFISTYSWSDAEEESCEVK--AKDE-----EEPYGEEGVEKTRKPSLSEKKNN------ 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1405 PLKTSQDELFVMLptpspsptstdpgmAQSLSHSLTSSREAaaarsGRGLWLWLAMVVVLAGLLALLASLVMQPAVDAAP 1484
Cdd:pfam05781 433 PSKWDVSSIYETL--------------ASWLTNLYPSLRKA-----NKVLWLSVAAIVLFAALMSFLTGQFFQSCVEAAP 493
|
490 500
....*....|....*....|....*...
gi 1838139839 1485 VGTGDSWMTIQQLLWPYTGLRHNGQPPV 1512
Cdd:pfam05781 494 TQEGDSWCSLEHILWPFTGLQHEGPPPV 521
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
362-551 |
3.48e-47 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 167.66 E-value: 3.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 362 ETSELVCCVADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREE 441
Cdd:pfam14662 2 ETSDLLTCVEDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 442 GRARASAHSKRVDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLID 521
Cdd:pfam14662 82 ARRSLLAQNKQLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIE 161
|
170 180 190
....*....|....*....|....*....|
gi 1838139839 522 ELKSTVEEYSSITELLRSHKSKLESQMQMM 551
Cdd:pfam14662 162 ELKSTVEEYSSIEEELRAEKSRLESQLPDM 191
|
|
| EF-hand_9 |
pfam14658 |
EF-hand domain; |
243-308 |
5.59e-14 |
|
EF-hand domain;
Pssm-ID: 405361 Cd Length: 66 Bit Score: 67.84 E-value: 5.59e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 243 DTIFYACDTQRRGKVYVSHIVDFLRHTTSRNSGDSGLEDLCNMLDPEHKDISIDLVTYHAVMKEWI 308
Cdd:pfam14658 1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDALVDLDTFLRVMRDWI 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
330-745 |
1.58e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 330 LRDSLSAKRSMLFNITSgSLEAFggeASRAEFETSELVCCVADLQMSNQKLEEEVRKMKLVVE-SMEDSNQKLAEENEEL 408
Cdd:pfam15921 283 LTEKASSARSQANSIQS-QLEII---QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 409 HNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHSKRV-DRENQSLIaSIASLQEENFRVTMETEELQrriAE 487
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwDRDTGNSI-TIDHLRRELDDRNMEVQRLE---AL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 488 LRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEEYSSITELLRSHKSKLESqmqmmqpdmsgaglslsvafr 567
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES--------------------- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 568 lNQSSSGSLQTELALAQSPLEAhygvdllstTMSCVSPLDMTLDREVLLMLQGPNPEQMAREFKNLLNKLKRNFREEtNS 647
Cdd:pfam15921 494 -SERTVSDLTASLQEKERAIEA---------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEK-DK 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 648 VLSTTRGLLDNCAQPAGDQD---AVLQKVQAELDAKREDWALSLDQ---LAQYTDSLEKELMKMASNMRRSRTEILHL-S 720
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGrtaGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLELEKVKLVNAgS 642
|
410 420
....*....|....*....|....*
gi 1838139839 721 VRVQEQENQKHQLCEELEQIKTPQD 745
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRN 667
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
372-1105 |
2.28e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 372 DLQMSNQKLEEEVRKMKLVVE-SMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHS 450
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 451 KRVDRENQSLIASIASLQEENFRVTMETEELQRRIAE---LRNINTD-----------------LQVQIHSFDAVVGE-- 508
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQhg 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 509 --KEAVIVEKSRLIDELKSTVEEYSSITELlrshKSKLESQMQMMQPDMSGAGLSlsvAFRLNQSSSGSLQTELALAQSP 586
Cdd:pfam15921 583 rtAGAMQVEKAQLEKEINDRRLELQEFKIL----KDKKDAKIRELEARVSDLELE---KVKLVNAGSERLRAVKDIKQER 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 587 LEahygvdLLSTTMSCVSPLD-MTLDREVLlmlqGPNPEQMAREFKNLLNKLKRNFReETNSVLSTTRGLLDNCAQPAGD 665
Cdd:pfam15921 656 DQ------LLNEVKTSRNELNsLSEDYEVL----KRNFRNKSEEMETTTNKLKMQLK-SAQSELEQTRNTLKSMEGSDGH 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 666 QDAVLQKVQAELDAKREDwalsldqlaqyTDSLEKELMKMASNMRRSRTEILHLsvrvqeqENQKHQLCEELEQIKTPQD 745
Cdd:pfam15921 725 AMKVAMGMQKQITAKRGQ-----------IDALQSKIQFLEEAMTNANKEKHFL-------KEEKNKLSQELSTVATEKN 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 746 SRAASCQTPAPEEEPGDDLDWDEQFALQdflKNELAERNCKEQggrTERGEKEDA----EERWTVVDTAGEGEVRDTSTP 821
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMEVALD---KASLQFAECQDI---IQRQEQESVrlklQHTLDVKELQGPGYTSNSSMK 860
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 822 VSALSGRTLPRNGAAEESHDYAACTESEHDLDVQSMQEQEAVPLSAHSQAvgIRNPEADAPPDLSHSKNNNGEALVTEES 901
Cdd:pfam15921 861 PRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQE--LRSVINEEPTVQLSKAEDKGRAPSLGAL 938
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 902 PSCDPAQNQSSSPEQEPTVPPSNTPPTEvptdsttpgpAETITQTESTQPTSEDHREEEkegeaDPSTG-DMSHTKSPSQ 980
Cdd:pfam15921 939 DDRVRDCIIESSLRSDICHSSSNSLQTE----------GSKSSETCSREPVLLHAGELE-----DPSSCfTFPSTASPSV 1003
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 981 DQSAdgsaaedstcllpvlveeeesvqdgtaevvptvsasmeetDRFTSSSPHSgSPVtHASQSGSGVGSVTS------- 1053
Cdd:pfam15921 1004 KNSA----------------------------------------SRSFHSSPKK-SPV-HSLLTSSAEGSIGSssqyrsa 1041
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1838139839 1054 DPCQSADSAAKKDSLPL--GGKKKRELE-RESSMEVIEERKVQEDQSESSVTTDK 1105
Cdd:pfam15921 1042 KTIHSPDSVKDSQSLPIetTGKTCRKLQnRLESLQTLVEDLQLKNQAMSSMIRNQ 1096
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-549 |
1.26e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 324 QEDSVKLRDSLSAKRSMLFNITSGSLEAFGgEASRAEFETSELVccvADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAE 403
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIE---KEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 404 ENEELhnqATVNQQLAQKEKMLN---EEVEEMKATLNcrEEGRARASAHSKRVDRENQSLIASIASLQEENFRVTMETE- 479
Cdd:TIGR02169 756 VKSEL---KELEARIEELEEDLHkleEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEy 830
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 480 ------ELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEEYSSITELLRSHKSKLESQMQ 549
Cdd:TIGR02169 831 lekeiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-546 |
3.40e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 321 EVSQEDSVKLRDSLSaKRSMLFNITSGSLEAFGGEASRAEfetselvccvADLQMSNQKLEEEVRKMKLVVESMEDSNQK 400
Cdd:TIGR02168 263 QELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLE----------QQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 401 LAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHSKRVDRENQSLIASIASLQEENFRVTMETEE 480
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838139839 481 LQRRIAELRNINTDLQVQIHS--FDAVVGEKEAVIVEKSRLIDELKSTVEEYSSITELLRSHKSKLES 546
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
373-739 |
5.43e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 373 LQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVE-EMKATLNCREEGRARASAHSK 451
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 452 RvdRENQSLI-----ASIASLQE----ENFR----------VTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAV 512
Cdd:pfam05483 343 A--KAAHSFVvtefeATTCSLEEllrtEQQRleknedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 513 IVEK---SRLIDELKSTVEEYSSITELLRSHKSKLESQMQMmqpdmsgagLSLSVAFRLNQSSsgSLQTEL---ALAQSP 586
Cdd:pfam05483 421 LDEKkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA---------IKTSEEHYLKEVE--DLKTELekeKLKNIE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 587 LEAHYGVDLLSTTMSCVSPLDMTLD---REVLLMLQGPNPEQMAREFKNLLNKlKRNFREEtnsvlsttrglldncaqpa 663
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLElkkHQEDIINCKKQEERMLKQIENLEEK-EMNLRDE------------------- 549
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 664 gdqdavLQKVQAELDAKREDWALSLDQLAQYTDSLEKELMKMASNMRRSRTEILHLsvrvQEQENQKHQLCEELEQ 739
Cdd:pfam05483 550 ------LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL----KKQIENKNKNIEELHQ 615
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-549 |
1.91e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 370 VADLQMSNQKLEEEVRKMKLVVESMEdsnQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAH 449
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 450 SKRVDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEE 529
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180
....*....|....*....|
gi 1838139839 530 YSSITELLRSHKSKLESQMQ 549
Cdd:TIGR02168 857 LAAEIEELEELIEELESELE 876
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
378-530 |
2.17e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 378 QKLEEEVRKMKLVVEsmedsnqKLAEENEELHNQatvnqqLAQKEkmlnEEVEEMKATLN-CREEGRARAsahskRVDRE 456
Cdd:COG2433 409 TEEEEEIRRLEEQVE-------RLEAEVEELEAE------LEEKD----ERIERLERELSeARSEERREI-----RKDRE 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838139839 457 NQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLqvqiHSfdavvGEKEAVIVEKSRLIDELKSTVEEY 530
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRKLERLKELWKLE----HS-----GELVPVKVVEKFTKEAIRRLEEEY 531
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
849-955 |
2.29e-05 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 48.48 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 849 EHDLDVQSMQEQEAVPLSAHSQAVGIRNPeADAPPDLSHSKNNNGEALVTEESPSCDPAQNQSSSPEQePTVPPSNTPPT 928
Cdd:PRK10856 148 DQSSAELSQNSGQSVPLDTSTTTDPATTP-APAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQ-ANVDTAATPAP 225
|
90 100
....*....|....*....|....*..
gi 1838139839 929 EVPTDSTTPGPAETITQTESTQPTSED 955
Cdd:PRK10856 226 AAPATPDGAAPLPTDQAGVSTPAADPN 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-742 |
4.95e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 373 LQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQA--TVNQQLAQ---KEKMLNE---EVEEMKATLNCREEgrA 444
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLqnTVHELEAAkclKEDMLEDsntQIEQLRKMMLSHEG--V 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 445 RASAHSKRVDRENqsliASIASLQEENFRVTMEteelqrriaeLRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELK 524
Cdd:pfam15921 186 LQEIRSILVDFEE----ASGKKIYEHDSMSTMH----------FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 525 StvEEYSSITELLRSHKSKLESQMQMMQPDMSGAGLSLSVAfrlnQSSSGSLQTELALAQSPLEAHYGVDL--LSTTMSC 602
Cdd:pfam15921 252 S--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSA----RSQANSIQSQLEIIQEQARNQNSMYMrqLSDLEST 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 603 VSPLDMTLdrevllmlqgpnpEQMAREFKNLLNKLKRNFrEETNSVLSTTRGLLDNCAQPAGDQDAVLQKVQAELDAKRE 682
Cdd:pfam15921 326 VSQLRSEL-------------REAKRMYEDKIEELEKQL-VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 683 DWALSLDQLAQY----------TDSLEKELMKmaSNMRRSRTEILHLSVRVQEQENQKHQLC------EELEQIKT 742
Cdd:pfam15921 392 ELSLEKEQNKRLwdrdtgnsitIDHLRRELDD--RNMEVQRLEALLKAMKSECQGQMERQMAaiqgknESLEKVSS 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-549 |
1.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 371 ADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELhnqatvnQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHS 450
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELEL-------EEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 451 KRVDRENQSLIASIASLQEenfrvtmETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEEY 530
Cdd:COG1196 319 EELEEELAELEEELEELEE-------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170
....*....|....*....
gi 1838139839 531 SSITELLRSHKSKLESQMQ 549
Cdd:COG1196 392 LRAAAELAAQLEELEEAEE 410
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
643-1012 |
1.62e-04 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 46.42 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 643 EETNSVLSTTRGLLDN-CAQPAGDQDAVLQKVQAELDAKREDWALSLDQLAQYTDSLEKElMKMASNMRRSRTEilHLSV 721
Cdd:pfam20435 223 EKTNFKLSQDKGSNDDpLIKPRHNSDSIETDSESPENATRRPVTRSLLQRRVGAKGVQKK-TKAGANLGRKCTE--QVNS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 722 RVQEQENQKHQLCEELEQIKTPQDSRAASCQTPA----PEEEPGDDLDWDeqfalqdflKNELAERNCKEQGGRTERGEK 797
Cdd:pfam20435 300 VFSFEEGLRGKIGTAVNSSVMPKKQRGRRKNTVVkcrkAHSRKKDEADWS---------RKEASKSNTPPRSESTETGKR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 798 EDAEERwtvvdtagEGEVRDTStpvsalsgrtlPRNGAAEESHDYaacteSEHDLDVQSMQEQEAVPLSAHSQAVGIRNP 877
Cdd:pfam20435 371 SSSSDK--------KGSSHDLH-----------PQSKARKQKPDI-----STREGDFHPSPEAEAAALPEMSQGLSKNGD 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 878 EADAPPDLSHSKNNNGE-----------ALVTEESPSCDPAQNQSSSPEQEPTVPPSNTPPTEVPTDSTTPGPAETITQT 946
Cdd:pfam20435 427 KHERPSNIFREKSVEPEnefqsptfgykAPISSPSPCCSPEASPLQPRNISPTLDETETPIFSFGTKKTSQGTTGQASDT 506
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838139839 947 ESTQPTS-EDHREEEKEGEADPSTGDMSHTKSPSQDQSADGSAAEDSTCLLPVLVEEEESVQDGTAE 1012
Cdd:pfam20435 507 EKRLPDFlEKKRDYSFRRESSPEPNEDLVLSDPSSDERDSDGSREDSPVLGHNISPEERETANWTNE 573
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
379-552 |
3.33e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 379 KLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHSKRVDRENQ 458
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 459 SLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVE-KSRLIDELKSTVEEYSSITELL 537
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEaEAELAEAEEALLEAEAELAEAE 378
|
170
....*....|....*
gi 1838139839 538 RSHKSKLESQMQMMQ 552
Cdd:COG1196 379 EELEELAEELLEALR 393
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
379-716 |
3.48e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 379 KLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATvnqQLAQKEKMLNEEVEEMKATLNCREEGRARASAHSKRVDRENQ 458
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 459 SLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRLIDELKSTVEEYSSITELLR 538
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 539 SHKSKLESQMQMMQPDMSGAGLSLSvafrlnqsssgSLQTELALAQSPLEAHYgvDLLSTtmscvspldmtldREVLLML 618
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIE-----------ELEELIEELESELEALL--NERAS-------------LEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 619 QGPNPEQMAREFKNLLNKLKRNfreetnsvlsttRGLLDNCAQPAGDQDAVLQKVQAELDAK----REDWALSLDQLAQY 694
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSEL------------RRELEELREKLAQLELRLEGLEVRIDNLqerlSEEYSLTLEEAEAL 959
|
330 340
....*....|....*....|..
gi 1838139839 695 TDSLEKELMKMASNMRRSRTEI 716
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
377-552 |
4.00e-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: 45.01 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 377 NQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNcreegraRASAHSKRVDRE 456
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-------KLESEKKEKESK 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 457 NQSLIASIASLQEENFRVTMETE--ELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVE-----------KSRLIDEL 523
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEKEidEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlikeieekekkISSLEKEL 619
|
170 180 190
....*....|....*....|....*....|..
gi 1838139839 524 KSTVEEYSSITEL---LRSHKSKLESQMQMMQ 552
Cdd:TIGR04523 620 EKAKKENEKLSSIiknIKSKKNKLKQEVKQIK 651
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
898-987 |
6.02e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 44.18 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 898 TEESPSCDPAQnQSSSPEQEPT---VPPSNTPPTEVPTD-STTPGPAETITQTESTQP-------TSEDHREEEKEGEAD 966
Cdd:PHA03291 180 GSADGSCDPAL-PLSAPRLGPAdvfVPATPRPTPRTTASpETTPTPSTTTSPPSTTIPapsttiaAPQAGTTPEAEGTPA 258
|
90 100
....*....|....*....|.
gi 1838139839 967 PSTGDMSHTKSPSQDQSADGS 987
Cdd:PHA03291 259 PPTPGGGEAPPANATPAPEAS 279
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
752-1069 |
6.52e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 752 QTPAPEEEPGDDLDWDEQFALQDfLKNELAERNCKEQGGRTERGEKEDAEErwtVVDTAGEGEVRDTSTPVSALSGRTlP 831
Cdd:PHA03307 23 RPPATPGDAADDLLSGSQGQLVS-DSAELAAVTVVAGAAACDRFEPPTGPP---PGPGTEAPANESRSTPTWSLSTLA-P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 832 RNGAAEEShdyaactesehdlDVQSMQEQEAVPLSAHSQAVGIRNPEADAPPDL----SHSKNNNGEALVTEESPSCDPA 907
Cdd:PHA03307 98 ASPAREGS-------------PTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLrpvgSPGPPPAASPPAAGASPAAVAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 908 --------QNQSSSPEQEPT--VPPSNTPPTEVPTDSTTPGPAETITQTESTQPTSEDHREEEKEGEADPSTGDMSHTKS 977
Cdd:PHA03307 165 daassrqaALPLSSPEETARapSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 978 PSQDQSADGSAAEDSTCLLPVLVEEEESVQDGTAEVVPTVSASM----EETDRFTSSSPHSGSPVTHASQSGSGVGSVTS 1053
Cdd:PHA03307 245 SGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSssprERSPSPSPSSPGSGPAPSSPRASSSSSSSRES 324
|
330
....*....|....*.
gi 1838139839 1054 DPCQSADSAAKKDSLP 1069
Cdd:PHA03307 325 SSSSTSSSSESSRGAA 340
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
833-1128 |
1.05e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 833 NGAAEESHDYAACTESEHDLD---------VQSMQEQEAVPLSAHSQAVGIRNPEADAPPDLSHSKNNNGEALVTEESPS 903
Cdd:PHA03307 14 AAEGGEFFPRPPATPGDAADDllsgsqgqlVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 904 CD-PAQNQSSSPEQEPTVPPSNTPPTEVPTDST--TPGPAETITQTESTQPTSEDHREEEKEGEADPSTGdmSHTKSPSQ 980
Cdd:PHA03307 94 TLaPASPAREGSPTPPGPSSPDPPPPTPPPASPppSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA--SDAASSRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 981 DQSAdgsaaedstclLPVLVEEEESVQDGTAEVVPTVSASmeetdRFTSSSPHSGSPVTHASQSGSGVG--SVTSDPCQS 1058
Cdd:PHA03307 172 AALP-----------LSSPEETARAPSSPPAEPPPSTPPA-----AASPRPPRRSSPISASASSPAPAPgrSAADDAGAS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1059 ADSAAKKDSLPLGGKKKRELERESSMEVIEERKVQEDQSESSVTTDKGsdmSGSSGTAIADKNSSLSPND 1128
Cdd:PHA03307 236 SSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPG---PASSSSSPRERSPSPSPSS 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
376-547 |
1.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 376 SNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNqatVNQQLAQKEKML---NEEVEEMKATLNCREEGRARASAHSKR 452
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELEQARSELeqlEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 453 VDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIvEKSRLIDELKSTVEEYSS 532
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQELQALSEAEAEQA 184
|
170
....*....|....*
gi 1838139839 533 ITELLRSHKSKLESQ 547
Cdd:COG4372 185 LDELLKEANRNAEKE 199
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
380-502 |
1.57e-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: 40.31 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 380 LEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLN----EEVEEMKATLNcreEGRARASAHSKRVDR 455
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHaediKALQALREELN---ELKAEIAELKAEAES 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1838139839 456 ENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSF 502
Cdd:pfam07926 83 AKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLESL 129
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-549 |
2.27e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 371 ADLQMSNQKLEEEVRKMKlvvESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRARASAHS 450
Cdd:COG1196 312 RELEERLEELEEELAELE---EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 451 KRVDRENQSLIASIASLQEENfrvtmetEELQRRIAELRNINTDLQvqihsfDAVVGEKEAVIVEKSRLIDELKSTVEEY 530
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAE-------EALLERLERLEEELEELE------EALAELEEEEEEEEEALEEAAEEEAELE 455
|
170
....*....|....*....
gi 1838139839 531 SSITELLRSHKSKLESQMQ 549
Cdd:COG1196 456 EEEEALLELLAELLEEAAL 474
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
372-745 |
2.34e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 372 DLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQAT-VNQQLAQKEKmLNEEVEEMKATLNCREEgrarasahs 450
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdLESKIQNQEK-LNQQKDEQIKKLQQEKE--------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 451 kRVDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVEKSRlidELKSTVEEY 530
Cdd:TIGR04523 423 -LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEKEL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 531 SSITEllrsHKSKLESQMQMMQPdmsgaglslsvafrlNQSSSGSLQTELALAQSPLEahygvDLLSTTMSCVSPLDMTL 610
Cdd:TIGR04523 499 KKLNE----EKKELEEKVKDLTK---------------KISSLKEKIEKLESEKKEKE-----SKISDLEDELNKDDFEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 611 DREVLlmlqgpnpEQMAREFKNLLNKLKrnfrEETNSVLSTTRGLldncaqpagdqDAVLQKVQAELDAKREdwalsldQ 690
Cdd:TIGR04523 555 KKENL--------EKEIDEKNKEIEELK----QTQKSLKKKQEEK-----------QELIDQKEKEKKDLIK-------E 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838139839 691 LAQYT---DSLEKELMKMASNMRRSRTEILHLsvrvqeqENQKHQLCEELEQIKTPQD 745
Cdd:TIGR04523 605 IEEKEkkiSSLEKELEKAKKENEKLSSIIKNI-------KSKKNKLKQEVKQIKETIK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-490 |
2.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 324 QEDSVKLRDSLSAKRSMLfNITSGSLEAFGGEASRAEFETSELVCCVADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAE 403
Cdd:TIGR02168 788 EAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 404 ENEELHNQATV--NQQLAQKEKM--LNEEVEEMKATLNCREE--GRARASAHSKR-----VDRENQSLIASIASLQE--- 469
Cdd:TIGR02168 867 LIEELESELEAllNERASLEEALalLRSELEELSEELRELESkrSELRRELEELReklaqLELRLEGLEVRIDNLQErls 946
|
170 180 190
....*....|....*....|....*....|...
gi 1838139839 470 ENFRVTME------------TEELQRRIAELRN 490
Cdd:TIGR02168 947 EEYSLTLEeaealenkieddEEEARRRLKRLEN 979
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-546 |
3.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 349 LEAFGGEASRAEFETSELVCCVADLQMSNQKLEEEVRKMKlvvESMEDSNQKLAEENeelhnqatvnqqlAQKEKmLNEE 428
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---AEIEELEREIEEER-------------KRRDK-LTEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 429 VEEMKATlncREEGRARASAhskrVDRENQSLIASIASLQEENFRVTMETEELQR--------------RIAELRNINTD 494
Cdd:TIGR02169 359 YAELKEE---LEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKReldrlqeelqrlseELADLNAAIAG 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 495 LQVQIHSFDAVVGEKEAVIVEK----SRLIDELKSTVEEYSSITELLRSHKSKLES 546
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQewklEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| rad2 |
TIGR00600 |
DNA excision repair protein (rad2); All proteins in this family for which functions are known ... |
851-1095 |
3.26e-03 |
|
DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. 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: 273166 [Multi-domain] Cd Length: 1034 Bit Score: 42.19 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 851 DLDVQSMQEQEAVPLSAHSQAVGIRNPEADAPPDLSHSKN---NNGEALVTEESPSCDPAQNQSSSPEQEPTVPPSNTPp 927
Cdd:TIGR00600 509 DRKSELSIERTVKPVSSEFGLPSQREDKLAIPTEGTQNLQgisDHPEQFEFQNELSPLETKNNESNLSSDAETEGSPNP- 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 928 tEVPTDSTTPGPAETITQTESTQPTSEDHREEEKEgeadpstgdmSHTKSPSQDQSADGSAAEDSTCLLPVLVEEEESVQ 1007
Cdd:TIGR00600 588 -EMPSWSSVTVPSEALDNYETTNPSNAKEVRNFAE----------TGIQTTNVGESADLLLISNPMEVEPMESEKEESES 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 1008 DGTAEVVPTVSaSMEETDRFTSSSPhsgspvTHASQSGSgvgsvtSDPCQSADSAAKKDSLPLggkKKRELERESSMEVI 1087
Cdd:TIGR00600 657 DGSFIEVDSVS-STLELQVPSKSQP------TDESEENA------ENKVASIEGEHRKEIEDL---LFDESEEDNIVGMI 720
|
....*...
gi 1838139839 1088 EERKVQED 1095
Cdd:TIGR00600 721 EEEKDADD 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-561 |
3.87e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 371 ADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREE---GRARAS 447
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 448 AHSKRVDRE----------------------NQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAV 505
Cdd:COG4942 114 YRLGRQPPLalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838139839 506 VGEKEAVIVEKSRLIDELKSTVEEYSSITELLRSHKSKLESQMQMMQPDMSGAGLS 561
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
360-560 |
4.24e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 360 EFETSELVCCVADLQMSNQKLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQ----LAQKEKMLNEEVEEMKAT 435
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArireLEEDIKTLTQRVLERETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 436 LNCREEGRARASAHSKRVDRENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVGEKEAVIVE 515
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838139839 516 KSRLIDELKSTVEEYSS---ITELLRSHKSKLESQMQMMQPDMSGAGL 560
Cdd:pfam07888 232 NEALLEELRSLQERLNAserKVEGLGEELSSMAAQRDRTQAELHQARL 279
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-546 |
5.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 379 KLEEEVRKMKLVVESMEDSNQKLAEENEELHNQATVNQQLAQKEKMLNEEVEEMKATLNCREEGRA---RASAHSKRV-D 454
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKRLtG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838139839 455 RENQSLIASIASLQEENFRVTMETEELQRRIAELRNINTDLQVQIHSFDAVVG------------EKEAVIVEKSRLIDE 522
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKR 463
|
170 180
....*....|....*....|....
gi 1838139839 523 LKSTVEEYSSITELLRSHKSKLES 546
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEK 487
|
|
| |
