|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
83-1196 |
1.98e-179 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 559.59 E-value: 1.98e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 83 MITHIVNQNFKSYAgEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK-IRSKKLSVLIHnSDEHKDIQSCTVE 161
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIH-SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 162 VHFqkiidKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 241
Cdd:pfam02463 79 ITF-----DNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 242 GQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNH 321
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 322 VCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVR 401
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 402 EKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKEKE 481
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 482 KELQKLTQEETNFKSLVHDLFQKVE------------------------------------------------------- 506
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEdllkeekkeeleileeeeesielkqgklteekeelekqelkllkdelelkksedl 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 507 -----------------------EAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHALD 563
Cdd:pfam02463 474 lketqlvklqeqlelllsrqkleERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 564 YIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFdlvkvkdekirqafyfalrdtlvadNL 643
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA-------------------------QL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 644 DQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLE 723
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 724 ERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVE 803
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 804 AEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAE 883
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 884 LKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISK 963
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 964 ISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFR 1043
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1044 QAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSL 1123
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVAL 1088
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806949 1124 ALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNITKS 1196
Cdd:pfam02463 1089 ALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-1187 |
1.77e-109 |
|
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: 371.32 E-value: 1.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGY-RAQKIRSKKLSVLIHNSDEHKDIQSCTVEV 162
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLsSSKAMRAERLSDLISNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 163 HFQKIIDKEGDDYEVIpnsnfyVSRTACRDN-TSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFlILQGEVEQIAMMKPK 241
Cdd:TIGR02169 81 TFKNDDGKFPDELEVV------RRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 242 GQTEhdegmleYLEDIIGCGRLNEPIKVLCRRVEILnehrGEKLNRVKMVEKEK----DALEGEKNIAIEFLTLENE--- 314
Cdd:TIGR02169 154 ERRK-------IIDEIAGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKrqqlERLRREREKAERYQALLKEkre 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 315 ------IFRKKNHVCQyyIYELQKRIAEMETQKEKIHEDTKEINEKSNIL---------------SNEMKAKNKDVKDTE 373
Cdd:TIGR02169 223 yegyelLKEKEALERQ--KEAIERQLASLEEELEKLTEEISELEKRLEEIeqlleelnkkikdlgEEEQLRVKEKIGELE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 374 KKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQL---QKDKEKV-EEFKSIPAKSNNIINE-------- 441
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIeeeRKRRDKLtEEYAELKEELEDLRAEleevdkef 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 442 -----------------TTTRNNALEKEKEKEEKKLKEVMD--SLKQETQGLQKEKEKEKELQKLTQE-----ETNFKSL 497
Cdd:TIGR02169 381 aetrdelkdyrekleklKREINELKRELDRLQEELQRLSEElaDLNAAIAGIEAKINELEEEKEDKALeikkqEWKLEQL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 498 VHDL-------------FQKVEEAKSSLAMNRSRGKV-LDAIIQEKKSGR---------IPGIYGRLGDLGAIDEKYDVA 554
Cdd:TIGR02169 461 AADLskyeqelydlkeeYDRVEKELSKLQRELAEAEAqARASEERVRGGRaveevlkasIQGVHGTVAQLGSVGERYATA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 555 ISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFDLVKVkDEKIRQAFYFA 633
Cdd:TIGR02169 541 IEVAAGNrLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-DPKYEPAFKYV 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 634 LRDTLVADNLDQATRVAYQkdrrWRVVTLQGQIIEQSGTMTGGgSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAM 713
Cdd:TIGR02169 620 FGDTLVVEDIEAARRLMGK----YRMVTLEGELFEKSGAMTGG-SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQ 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 714 Q-IQEQKVQLEERVVKLRHSEREMRnTLEKftaSIQRLIEQEEYLNVQVKELEANVlatapDKKKQKLleENVSAFKTEY 792
Cdd:TIGR02169 695 SeLRRIENRLDELSQELSDASRKIG-EIEK---EIEQLEQEEEKLKERLEELEEDL-----SSLEQEI--ENVKSELKEL 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 793 DAV----AEKAGKVEAEVKRL-----HNTIVEINNHkLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSV 863
Cdd:TIGR02169 764 EARieelEEDLHKLEEALNDLearlsHSRIPEIQAE-LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 864 LRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHalqkdalSIKLKLEQI 943
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-------ELEAQIEKK 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 944 DGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEiSVLSPEDLEAiknpdsitnQIALLEARCHEMKP-NLGAIAEYKKKE 1022
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQA---------ELQRVEEEIRALEPvNMLAIQEYEEVL 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1023 ELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTlGGDAELELVDSLDPFSEGIMFSVRP 1102
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAKP 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1103 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1182
Cdd:TIGR02169 1065 KGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYAD 1144
|
....*
gi 578806949 1183 RLIGI 1187
Cdd:TIGR02169 1145 RAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-1187 |
1.34e-91 |
|
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: 320.85 E-value: 1.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 92 FKSYAgEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFqkiiD 169
Cdd:TIGR02168 10 FKSFA-DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEVELVF----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 170 KEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLL-------RSHGIdldhnrflILQGEVEQIAMMKP-- 240
Cdd:TIGR02168 85 NSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFldtglgkRSYSI--------IEQGKISEIIEAKPee 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 241 -----------------KGQTE----HDEGMLEYLEDIIG-CGRLNEPIK----------------------VLCRRVEI 276
Cdd:TIGR02168 157 rraifeeaagiskykerRKETErkleRTRENLDRLEDILNeLERQLKSLErqaekaerykelkaelrelelaLLVLRLEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 277 LNEHRGEKLNRVKMVEKEKDALEGEKN---IAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINE 353
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQeleEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 354 KSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPA 433
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 434 KSNNIINETTTRNNALEKEKEKEEKKLKEVMDSL----KQETQGLQKEKEKEKELQKLTQEETN-----FKSLVHDLFQK 504
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEealeeLREELEEAEQA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 505 VEEAKSSLAMNRSRGKVLDAIIQE------------KKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHA-LDYIVVDSID 571
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENlegfsegvkallKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrLQAVVVENLN 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 572 IAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPR----LFDLVKVkDEKIRQAFYFALRDTLVADNLDQAT 647
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvAKDLVKF-DPKLRKALSYLLGGVLVVDDLDNAL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 648 RVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVV 727
Cdd:TIGR02168 636 ELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 728 KLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlaTAPDKKKQKLLEENVSAFkTEYDAVAEKAGKVEAEVK 807
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL--TELEAEIEELEERLEEAE-EELAEAEAEIEELEAQIE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 808 RLhntiveinnhklkaqQDKLDKINKQLDEcasaitkAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSL 887
Cdd:TIGR02168 793 QL---------------KEELKALREALDE-------LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 888 EDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLH 967
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 968 PIE-----DNPIEEISVLSPEDLE-AIKNPDSITNQIALLEARCHEMKP--------NLGAIAEYKKKEELYLQRVAELD 1033
Cdd:TIGR02168 931 LEGlevriDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENkikelgpvNLAAIEEYEELKERYDFLTAQKE 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1034 KITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNL 1113
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLL 1090
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806949 1114 SGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1187
Cdd:TIGR02168 1091 SGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
82-241 |
7.50e-68 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 227.18 E-value: 7.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 82 LMITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVE 161
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 162 VHFQKIIDKEgddyevipnsnfyvsrtacrdntsvyhisgkkktfkdvgnLLRSHGIDLDHNRFLILQGEVEQIAMMkPK 241
Cdd:cd03274 81 VHFQEIIDKP----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM-PK 119
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1103-1197 |
1.14e-65 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 221.02 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1103 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1182
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 578806949 1183 RLIGIYKTYNITKSV 1197
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
84-1187 |
1.58e-57 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 216.34 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG---YRAqkIRSKKLSVLIHN-SDEHKDIQSCT 159
Cdd:COG1196 3 LKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKS--LRGGKMEDVIFAgSSSRKPLGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 160 VEVHF---QKIIDkeGDDYEVIpnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLD-HNrfLILQGEVEQI 235
Cdd:COG1196 80 VSLTFdnsDGTLP--IDYDEVT------ITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPEsYS--IIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 236 AMMKPkgqtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILNEHRG--EKLNRVK--MVEKEK--DALEGEKNIAIEFL 309
Cdd:COG1196 150 IEAKP-------EERRAIIEEAAGISKYKE------RKEEAERKLEAteENLERLEdiLGELERqlEPLERQAEKAERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 310 TLENEIFRKKNHVCQYYIYELQKRI-------------------------AEMETQKEKIHEDTKEINEKS---NILSNE 361
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELeeleaeleeleaeleeleaelaeleAELEELRLELEELELELEEAQaeeYELLAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 362 MKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFK------------ 429
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEealleaeaelae 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 430 ----------------------------------SIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQ 475
Cdd:COG1196 377 aeeeleelaeellealraaaelaaqleeleeaeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 476 KEKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSS----LAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKY 551
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 552 DVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVwAKKMTEIQTPENTPRLFDLVKVkDEKIRQAF 630
Cdd:COG1196 537 EAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-RAALAAALARGAIGAAVDLVAS-DLREADAR 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 631 YFALRDTLV-----ADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKvmKGRMGSSLVIEISEEEVNKMESQL 705
Cdd:COG1196 615 YYVLGDTLLgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR--ELLAALLEAEAELEELAERLAEEE 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 706 QNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEkftasiQRLIEQEEYLNVQVKELEANVLATAPDkkkqklleenv 785
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEE------QLEAEREELLEELLEEEELLEEEALEE----------- 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 786 safkteydavaekagkveaevkrlhntiveinnhklkaqqdkldkinkqldecasaitkaqvaiktadrnlqkaqdsvLR 865
Cdd:COG1196 756 ------------------------------------------------------------------------------LP 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 866 TEKEIKDTEKEVDDLTAELKSLEDkaaevVkNTNAAEEsLPEIQKEHRNLLQELkviqenehalqkdalsiklkleqidg 945
Cdd:COG1196 758 EPPDLEELERELERLEREIEALGP-----V-NLLAIEE-YEELEERYDFLSEQR-------------------------- 804
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 946 hiaehnskikywhkeiskislhpiednpieeisvlspEDLEaiknpdsitnqiallEARchemkpnlgaiaeykkkEELy 1025
Cdd:COG1196 805 -------------------------------------EDLE---------------EAR-----------------ETL- 814
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1026 LQRVAELDKITYERdsFRQAYEDLRKQrlnefmagfyiitnkLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKK 1105
Cdd:COG1196 815 EEAIEEIDRETRER--FLETFDAVNEN---------------FQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQPPGK 877
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1106 SWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLI 1185
Cdd:COG1196 878 KLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
|
..
gi 578806949 1186 GI 1187
Cdd:COG1196 958 GV 959
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
535-649 |
1.10e-32 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 123.11 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 535 PGIYGRLGDLGAIDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAV-----WAKKMTEIQT 608
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGrLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 578806949 609 PENTPRLFDLVKVkDEKIRQAFYFALRDTLVADNLDQATRV 649
Cdd:smart00968 81 PGFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1113-1195 |
1.69e-32 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 124.73 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1113 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKN-AQFIIISLRNNMFEISDRLIGIYKTY 1191
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 578806949 1192 NITK 1195
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
90-242 |
1.97e-31 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 123.84 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 90 QNFKSYAGEKILGPFhKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFQkii 168
Cdd:cd03275 7 ENFKSYKGRHVIGPF-DRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRaRVGKPDSNSAYVTAVYE--- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806949 169 dkegDDYEVIPnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKG 242
Cdd:cd03275 83 ----DDDGEEK-----TFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPPG 147
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1102-1189 |
1.24e-29 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 118.83 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1102 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEI 1180
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*....
gi 578806949 1181 SDRLIGIYK 1189
Cdd:cd03275 225 ADALVGVYR 233
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
534-650 |
7.35e-29 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 111.97 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 534 IPGIYGRLGDLGAIDEKYDVAISSCC-HALDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTpENT 612
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLK-GGA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 578806949 613 PRLFDLVKVKDEkIRQAFYFALRDTLVADNLDQATRVA 650
Cdd:pfam06470 80 GPLLDLVEYDDE-YRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1108-1187 |
9.93e-28 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 111.40 E-value: 9.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1108 KKIFN---LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRL 1184
Cdd:cd03278 106 KKVQRlslLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
...
gi 578806949 1185 IGI 1187
Cdd:cd03278 186 YGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
84-167 |
1.84e-27 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 110.09 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKILGPFHkRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHnSDEHKDIQSCTVEVH 163
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG-GGVKAGINSASVEIT 78
|
....
gi 578806949 164 FQKI 167
Cdd:cd03239 79 FDKS 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1110-1190 |
1.07e-23 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 98.97 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1110 IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEISDRLIGIY 1188
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
..
gi 578806949 1189 KT 1190
Cdd:cd03227 155 KV 156
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1107-1193 |
7.10e-17 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 81.58 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1107 WKK-IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLi 1185
Cdd:cd03273 160 WKEsLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL- 238
|
....*...
gi 578806949 1186 giYKTYNI 1193
Cdd:cd03273 239 --FRTRFV 244
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1108-1187 |
9.49e-17 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 81.15 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1108 KKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1187
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
84-164 |
2.28e-16 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 78.66 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHNSDEHKDIQS-CTVE 161
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGeQSAKSLRGEKMSDVIFAGSETRKPANfAEVT 79
|
...
gi 578806949 162 VHF 164
Cdd:cd03278 80 LTF 82
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
84-238 |
1.51e-15 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 77.72 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRA-QKIRSKKLSVLIHNSDEhKDIQSCTVEV 162
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQ-AGITKASVTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 163 HFqKIIDKEG-----DDYEVIPnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAM 237
Cdd:cd03273 82 VF-DNSDKSQspigfENYPEIT-----VTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLN 155
|
.
gi 578806949 238 M 238
Cdd:cd03273 156 M 156
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
86-170 |
7.58e-15 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 73.55 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 86 HIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKklsvlihnSDEHKDIQSCTVEVHFQ 165
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR--------SGVKAGCIVAAVSAELI 72
|
....*
gi 578806949 166 KIIDK 170
Cdd:cd03227 73 FTRLQ 77
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
84-245 |
6.92e-13 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 69.60 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIqSCTVEVH 163
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVM-SAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 164 FQKIidkegDDYEVIPNSNFYVSRT--ACRDNtsvYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 241
Cdd:cd03272 80 FDNS-----DNRFPIDKEEVRLRRTigLKKDE---YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQD 151
|
....
gi 578806949 242 GQTE 245
Cdd:cd03272 152 EQQE 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
774-954 |
1.21e-08 |
|
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: 56.86 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 774 DKKKQKLLEEnVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKtad 853
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 854 rNLQKAQDSVlRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQEnehALQKDA 933
Cdd:COG1579 77 -KYEEQLGNV-RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEEL 151
|
170 180
....*....|....*....|.
gi 578806949 934 LSIKLKLEQIDGHIAEHNSKI 954
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1110-1189 |
2.20e-08 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 54.56 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1110 IFNLSGGEKTLSSLALVFALhhyKPtPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFE-ISDRLIGI 1187
Cdd:cd00267 78 VPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
..
gi 578806949 1188 YK 1189
Cdd:cd00267 154 KD 155
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
688-1055 |
2.48e-08 |
|
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: 58.70 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 688 SLVIEISEEEVNKMESQLQNDSKKAMQiQEQKVQLEERVVKLRHSEREMRN--TLEKFTA--SIQRLIEQEEYLNVQVKE 763
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETLIASRQEER-QETSAELNQLLRTLDDQWKEKRDelNGELSAAdaAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 764 -LEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKI----------- 831
Cdd:pfam12128 334 fLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIreardrqlava 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 832 -----------NKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVD-------DLTAELKSLEDKAAE 893
Cdd:pfam12128 414 eddlqaleselREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDErierareEQEAANAEVERLQSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 894 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIklkleqidghIAEHNSKIKYWHKEISKI--------- 964
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL----------LHFLRKEAPDWEQSIGKVispellhrt 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 965 SLHPI--EDNPIEEISVLSPE-DLEAIKNPDSITNQIAlLEARCHEMKPNLGAIAE-YKKKEELYLQRVAELDKITYERD 1040
Cdd:pfam12128 564 DLDPEvwDGSVGGELNLYGVKlDLKRIDVPEWAASEEE-LRERLDKAEEALQSAREkQAAAEEQLVQANGELEKASREET 642
|
410
....*....|....*..
gi 578806949 1041 SFRQAYE--DLRKQRLN 1055
Cdd:pfam12128 643 FARTALKnaRLDLRRLF 659
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
83-178 |
5.17e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.63 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 83 MITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFgYRAQKIRSKKLSVLIHNSDEhkdiqSCTVEV 162
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYAL-YGKARSRSKLRSDLINVGSE-----EASVEL 73
|
90
....*....|....*.
gi 578806949 163 HFQkiidKEGDDYEVI 178
Cdd:COG0419 74 EFE----HGGKRYRIE 85
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
83-129 |
5.48e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.48 E-value: 5.48e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 578806949 83 MITHIVNQNFKSYAGEKI-LGPFHkrfsCIIGPNGSGKSNVIDSMLFV 129
Cdd:COG4637 1 MITRIRIKNFKSLRDLELpLGPLT----VLIGANGSGKSNLLDALRFL 44
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
703-949 |
9.14e-08 |
|
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: 56.29 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 703 SQLQNDSK-KAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKE-LEANVLATAPDKKKQKL 780
Cdd:pfam05557 12 SQLQNEKKqMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 781 LEENVSAFKTEYDAVAEKAGKVeAEVKRlhntIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKtadrNLQKAQ 860
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNEL-SELRR----QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 861 DSVLRTEKEIKDTEKEVddltaelkSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQE---LKVIQENEHALQKDALSIK 937
Cdd:pfam05557 163 SSLAEAEQRIKELEFEI--------QSQEQDSEIVKNSKSELARIPELEKELERLREHnkhLNENIENKLLLKEEVEDLK 234
|
250
....*....|..
gi 578806949 938 LKLEQIDGHIAE 949
Cdd:pfam05557 235 RKLEREEKYREE 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
695-1129 |
1.09e-07 |
|
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: 56.52 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKL---RHSEREMRNTLEKFTASIQRLIEQEEYLNVQVK-ELEANVLA 770
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAcEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 771 TAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRlhntivEINNHKLKAQQDKLDKINKQLdecaSAITKAQVAIK 850
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE------RVREHALSIRVLPKELLASRQ----LALQKMQSEKE 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 851 --TADRNLQKAQDSVLRTEKE-IKDTEKEVDDLTAELKSLEdkaAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEH 927
Cdd:TIGR00618 691 qlTYWKEMLAQCQTLLRELEThIEEYDREFNEIENASSSLG---SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 928 ALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEIsKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHE 1007
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL-KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1008 MKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVD 1087
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVN 926
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 578806949 1088 SLDPFSEGIMF------SVRPPKkswkkifNLSGGEKTLSSLALVFAL 1129
Cdd:TIGR00618 927 ARKYQGLALLVadaytgSVRPSA-------TLSGGETFLASLSLALAL 967
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
721-950 |
3.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 721 QLEERVVKLRhserEMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATApdKKKQKLLEENVSAFKTEYDAVAEKAG 800
Cdd:COG4913 239 RAHEALEDAR----EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 801 KVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDEcasaitkAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDL 880
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREIER-------LERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 881 TAELKSLEDKAAEVVKntnAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEH 950
Cdd:COG4913 386 RAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
780-1003 |
4.75e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 780 LLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKA 859
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE-ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 860 QDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 939
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806949 940 -LEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEA 1003
Cdd:COG4372 187 eLLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
695-906 |
8.25e-07 |
|
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: 52.84 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELE---ANVLAT 771
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 772 APDKKKQKLLEENVSAfktEYDAVAEKAGKVEAEVKRLHNTIVEinnhKLKAQQDKLDKINKQLDECASAITKAQVAIKT 851
Cdd:COG4942 113 LYRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAE----ELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578806949 852 ADRNLQKAQDS----VLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLP 906
Cdd:COG4942 186 ERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
695-955 |
9.61e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA-------- 766
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNtresletq 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 767 --------NVLATAPDKKKQKL----------------LEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLK 822
Cdd:TIGR04523 470 lkvlsrsiNKIKQNLEQKQKELkskekelkklneekkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 823 AQQD-KLDKINKQLDECASAITKaqvaIKTADRNLQKAQDSVlrtEKEIKDTEKEVDDLTAELKSLEDKAAEVvkntnaa 901
Cdd:TIGR04523 550 DDFElKKENLEKEIDEKNKEIEE----LKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKKISSL------- 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 578806949 902 EESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIK 955
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
691-911 |
5.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQvkeLEANVLA 770
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL---LGSESFS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 771 TAPDkkkqklleeNVSAFKTEYDAVAEKAGKVEAEVKrlhntiveinnhKLKAQQDKLDkinKQLDECASAITKAQVAIK 850
Cdd:COG3883 116 DFLD---------RLSALSKIADADADLLEELKADKA------------ELEAKKAELE---AKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806949 851 TADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKE 911
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-944 |
5.77e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 707 NDSKKAMQIQEQKVQLEERVvklrhseREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLatapdKKKQKLLEENVS 786
Cdd:COG4913 238 ERAHEALEDAREQIELLEPI-------RELAERYAAARERLAELEYLRAALRLWFAQRRLELL-----EAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 787 AFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRT 866
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806949 867 EKEIKDTekeVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALqKDALSIKLKLEQID 944
Cdd:COG4913 386 RAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAEALGLDEAE 459
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
691-964 |
5.79e-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: 50.79 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA--NV 768
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqiND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 769 LATAPDKKKQ--KLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINN--HKLKAQQDKLDKINKQLDECASAITK 844
Cdd:TIGR04523 396 LESKIQNQEKlnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 845 aqvAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQE 924
Cdd:TIGR04523 476 ---SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 578806949 925 NehalqkdalsikLKLEQIDGHIAEHNSKIKYWHKEISKI 964
Cdd:TIGR04523 553 E------------LKKENLEKEIDEKNKEIEELKQTQKSL 580
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-438 |
6.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 90 QNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSmLFVFGYRAQKIRSKKLSvlihNSDEHKDIQSCT-VEVHFqkii 168
Cdd:PRK03918 9 KNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEA-ILVGLYWGHGSKPKGLK----KDDFTRIGGSGTeIELKF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 169 DKEGDDYEVIPNSNFYVSRTACRDNTSVYHiSGKKKTFKDVGNLLRSHgidLDHNRFLILQGEVEQIammkpkgqTEHDE 248
Cdd:PRK03918 78 EKNGRKYRIVRSFNRGESYLKYLDGSEVLE-EGDSSVREWVERLIPYH---VFLNAIYIRQGEIDAI--------LESDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 249 GMLEYLEDIIGCGRLnepikvlcrrveilnEHRGEKLNRV-KMVEKEKDALEgekniaiEFLTLENEIfrkknhvcqyyi 327
Cdd:PRK03918 146 SREKVVRQILGLDDY---------------ENAYKNLGEViKEIKRRIERLE-------KFIKRTENI------------ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 328 yelQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDtekklnkitkfIEENKEKFTQLDLEDVQVREKLKHA 407
Cdd:PRK03918 192 ---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-----------LEELKEEIEELEKELESLEGSKRKL 257
|
330 340 350
....*....|....*....|....*....|.
gi 578806949 408 TSKAKKLEKQLQKDKEKVEEFKSIPAKSNNI 438
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
715-1070 |
9.46e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 715 IQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATapdkkkqkllEENVSAFKTEYDA 794
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA----------REAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 795 VAEKagkVEAEVKRLHNTIVEinnhkLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDsvLRTE------- 867
Cdd:PRK02224 389 LEEE---IEELRERFGDAPVD-----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA--LLEAgkcpecg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 868 ---------KEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAE-----ESLPEIQKEHRNLLQELkvIQENEHALQKDA 933
Cdd:PRK02224 459 qpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaEDRIERLEERREDLEEL--IAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 934 lsikLKLEQIDGHIAEHNSKIKYWHKEISKisLHPIEDNPIEEISVLS------PEDLEAIKNPDSITNQIALLEARCHE 1007
Cdd:PRK02224 537 ----ERAEELRERAAELEAEAEEKREAAAE--AEEEAEEAREEVAELNsklaelKERIESLERIRTLLAAIADAEDEIER 610
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806949 1008 MKPNLGAIAEYKKKEELYLQ----RVAELDKiTYERDSFRQAYEDlrKQRLNEFMAGfyiITNKLKE 1070
Cdd:PRK02224 611 LREKREALAELNDERRERLAekreRKRELEA-EFDEARIEEARED--KERAEEYLEQ---VEEKLDE 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
714-892 |
1.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 714 QIQEQKVQLEERVVKLRHSeREMRNTLEKFTASIQRLIEQEEYLNVQVKELEAnVLATAPDKKKQKLLEENVSAFKTEYD 793
Cdd:COG4717 72 ELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 794 avaekagKVEAEVKRLHNTIVEInnhklKAQQDKLDKINKQLDECASAIT-KAQVAIKTADRNLQKAQDSVLRTEKEIKD 872
Cdd:COG4717 150 -------ELEERLEELRELEEEL-----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|
gi 578806949 873 TEKEVDDLTAELKSLEDKAA 892
Cdd:COG4717 218 AQEELEELEEELEQLENELE 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
838-932 |
1.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 838 CASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQ 917
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|....*
gi 578806949 918 ELKVIQENEHALQKD 932
Cdd:COG4942 91 EIAELRAELEAQKEE 105
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
84-170 |
1.34e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.85 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRaqkiRSKKLSVL-IHNSDEHKDIqSCTVEV 162
Cdd:COG3593 3 LEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPS----SSRKFDEEdFYLGDDPDLP-EIEIEL 75
|
....*...
gi 578806949 163 HFQKIIDK 170
Cdd:COG3593 76 TFGSLLSR 83
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
748-930 |
1.38e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.36 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 748 QRLIEQEEYLNVQVKEL---EANVLATAPDKKKQKLLEEnVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKL-KA 823
Cdd:pfam07111 59 QALSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLE-AQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 824 QQDKLDKINKQLDECASAITKAQ----VAIKTADRNLQKAQDSvLRTE-----KEIKDTEKEVDDLTAEL-KSLEDKAAE 893
Cdd:pfam07111 138 SQRELEEIQRLHQEQLSSLTQAHeealSSLTSKAEGLEKSLNS-LETKrageaKQLAEAQKEAELLRKQLsKTQEELEAQ 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578806949 894 VVKNTN----AAEESLPEIQK-----EHRNLLQELKVIQENEHALQ 930
Cdd:pfam07111 217 VTLVESlrkyVGEQVPPEVHSqtwelERQELLDTMQHLQEDRADLQ 262
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
690-967 |
1.56e-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: 49.35 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 690 VIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRL---IEQEEYLNVQVKELEA 766
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELearVSDLELEKVKLVNAGS 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 767 NVLATAPDKKKQK--LLEEnVSAFKTEYDAVAEkagkvEAEVKRlhntiveiNNHKLKAQQDKL--DKINKQLDECASAI 842
Cdd:pfam15921 643 ERLRAVKDIKQERdqLLNE-VKTSRNELNSLSE-----DYEVLK--------RNFRNKSEEMETttNKLKMQLKSAQSEL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 843 TKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVK-------NTNAAEESLPEIQKEHRNL 915
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKekhflkeEKNKLSQELSTVATEKNKM 788
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 578806949 916 LQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLH 967
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1113-1189 |
1.62e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 47.21 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1113 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK---NAQFIIISLRNNMFEISDRLIGIYK 1189
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQDISGLASSDDVKVFR 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
715-926 |
3.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 715 IQEQKVQLEERVVKLRHSEREMRNTLEKFtasiQRLIEQEEYLNvQVKELEanvlatapdKKKQKLLEENVSAFKTEYDA 794
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKE----SELIKLKELAE-QLKELE---------EKLKKYNLEELEKKAEEYEK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 795 VAEKAGKVEAEVKRLHNTIVEIN--NHKLKAQQDKLDKINKQLDECASAITKAQV-AIKTADRNLQKAQdSVLRTEKEIK 871
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELE-PFYNEYLELK 608
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578806949 872 DTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEhrnlLQELKVIQENE 926
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE----LEELEKKYSEE 659
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
700-955 |
3.54e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 700 KMESQLQNdskkamqIQEQKVQLEERVVKLRHSE-REMRNTLEKFTASIQRLIEQ--------EEYLNVQVKELEANVla 770
Cdd:pfam06160 150 ELEKQLAE-------IEEEFSQFEELTESGDYLEaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEELKEGY-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 771 tapdkkkQKLLEENvsaFKTEYDAVAEKAGKVEaevKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIK 850
Cdd:pfam06160 221 -------REMEEEG---YALEHLNVDKEIQQLE---EQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 851 TADRNLQKAQDSVLRTEKEIKDTEKEVD-----------------DLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHR 913
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlnenelervrGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELE 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 578806949 914 NLLQELKVIQENE-------HALQKDALSIKLKLEQIDGHIAEHNSKIK 955
Cdd:pfam06160 368 EILEQLEEIEEEQeefkeslQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
820-919 |
3.57e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 820 KLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEvvkntn 899
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------ 94
|
90 100
....*....|....*....|
gi 578806949 900 aAEESLPEIQKEHRNLLQEL 919
Cdd:COG4942 95 -LRAELEAQKEELAELLRAL 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
751-932 |
3.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 751 IEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAgKVEAEVKRLHNTIVEinnhkLKAQQDKLDK 830
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS-WDEIDVASAEREIAE-----LEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 831 INKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVknTNAAEESLPEIQK 910
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALG 760
|
170 180
....*....|....*....|....*...
gi 578806949 911 E------HRNLLQELKVIQENEHALQKD 932
Cdd:COG4913 761 DaverelRENLEERIDALRARLNRAEEE 788
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
692-1114 |
3.87e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 692 EISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELeanvlat 771
Cdd:COG5022 929 LIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL------- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 772 apdkkkqklleenvSAFKTEYDAVAEKagkvEAEVKRLHNTIVEINNH-KLKAQQDKLDKINKQLDECASAITKAQVAIK 850
Cdd:COG5022 1002 --------------AELSKQYGALQES----TKQLKELPVEVAELQSAsKIISSESTELSILKPLQKLKGLLLLENNQLQ 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 851 TADRNLQKAQDSVLRTEKEIKDTEK-EVDDLTAELKSLEDKAAEVVKNTN------AAEESLPEIQKEHRNLLQELKVIQ 923
Cdd:COG5022 1064 ARYKALKLRRENSLLDDKQLYQLEStENLLKTINVKDLEVTNRNLVKPANvlqfivAQMIKLNLLQEISKFLSQLVNTLE 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 924 ENEHALQKDalsiKLKLEQIDGHIAEHNSKIKYWHKEISKISlhPIEDNPIEEISVLSPEDLEAIKNP-DSITNQIALLE 1002
Cdd:COG5022 1144 PVFQKLSVL----QLELDGLFWEANLEALPSPPPFAALSEKR--LYQSALYDEKSKLSSSEVNDLKNElIALFSKIFSGW 1217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1003 ARCHEMKPNLGAIAEYKKKEELYlqrvaeldKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAE 1082
Cdd:COG5022 1218 PRGDKLKKLISEGWVPTEYSTSL--------KGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSL 1289
|
410 420 430
....*....|....*....|....*....|..
gi 578806949 1083 LELVDSLDpFSEGIMfsvRPPKKSWKKIFNLS 1114
Cdd:COG5022 1290 LQYINVGL-FNALRT---KASSLRWKSATEVN 1317
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
764-942 |
4.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 764 LEANVLATAPDKKKQKllEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAIT 843
Cdd:COG3883 6 LAAPTPAFADPQIQAK--QKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 844 KAQVAIKTADRNLQKAQDSVLRTE--------------------------KEIKDTEKEVDDLTAELKSLEDKAAEVVKN 897
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDvllgsesfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578806949 898 TNAAEESLPEIQK---EHRNLLQELKViQENEHALQKDALSIKLKLEQ 942
Cdd:COG3883 163 KAELEAAKAELEAqqaEQEALLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
326-1035 |
5.97e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 326 YIYELQKRIAEMETQKEKIHEDTKEINE---KSNILSNEMKAK-------------NKDVKDTEKKLNKITKFIEENKek 389
Cdd:TIGR01612 1109 YADEINKIKDDIKNLDQKIDHHIKALEEikkKSENYIDEIKAQindledvadkaisNDDPEEIEKKIENIVTKIDKKK-- 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 390 ftqldledvQVREKLKHATSKAKKLEKqlqkDKEKVEEFKSIPAKSNNIIN----ETTTRNNALEKEKEKEEKKLKEVMD 465
Cdd:TIGR01612 1187 ---------NIYDEIKKLLNEIAEIEK----DKTSLEEVKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLD 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 466 SLKQETQglqkEKEKEKELQKLTQEETNFKSLVHDLFQK--VEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGD 543
Cdd:TIGR01612 1254 EIKEKSP----EIENEMGIEMDIKAEMETFNISHDDDKDhhIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 544 LGAIDEKYDVAISSCCHALDYI--------VVDSIDIAQECVNFLKRQNIGVATfiGLDKMAVWAKKMTE-IQTPENTPR 614
Cdd:TIGR01612 1330 NLLDAQKHNSDINLYLNEIANIynilklnkIKKIIDEVKEYTKEIEENNKNIKD--ELDKSEKLIKKIKDdINLEECKSK 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 615 LFDLVKVKD-----EKIRQAFYFALRDTlvaDNLDQATRVAYQKDRRwrvVTLQGQIIEQSGTMTGGGSKVMKGRMGSSL 689
Cdd:TIGR01612 1408 IESTLDDKDideciKKIKELKNHILSEE---SNIDTYFKNADENNEN---VLLLFKNIEMADNKSQHILKIKKDNATNDH 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 690 VIEISEEEVNKMESQLQNDS--KKAMQIQEQKV---QLEERVVKL--RHSEREMRNTLEKFTASIQRLIEQeeylnvqVK 762
Cdd:TIGR01612 1482 DFNINELKEHIDKSKGCKDEadKNAKAIEKNKElfeQYKKDVTELlnKYSALAIKNKFAKTKKDSEIIIKE-------IK 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 763 ELEANVLATApDKKKQKLLEENVSAFKTEYDAVA-EKAGK----VEAEVKRLHNTIVEINNHKLKAQQ--DKLDKINKQL 835
Cdd:TIGR01612 1555 DAHKKFILEA-EKSEQKIKEIKKEKFRIEDDAAKnDKSNKaaidIQLSLENFENKFLKISDIKKKINDclKETESIEKKI 1633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 836 DECASAITKAQVAIKTADRN-LQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTN-AAEESLPEIQKEHR 913
Cdd:TIGR01612 1634 SSFSIDSQDTELKENGDNLNsLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANK 1713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 914 NLLQELKVIQENEHALQKDALSIKlKLEQIDGH--IAEHNSKIKYWHKEIskISLHPIEDNPIEEISVlSPEDLEAIKNp 991
Cdd:TIGR01612 1714 EEIESIKELIEPTIENLISSFNTN-DLEGIDPNekLEEYNTEIGDIYEEF--IELYNIIAGCLETVSK-EPITYDEIKN- 1788
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 578806949 992 DSITNQIALLEarchemkpnlgaIAEYKKKEELYLQRVA--ELDKI 1035
Cdd:TIGR01612 1789 TRINAQNEFLK------------IIEIEKKSKSYLDDIEakEFDRI 1822
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
827-955 |
6.07e-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: 46.07 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 827 KLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEvvkntnaAEESLP 906
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-------YEEQLG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 578806949 907 EI--QKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIK 955
Cdd:COG1579 84 NVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
794-942 |
7.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 794 AVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDT 873
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 874 EKEVDDLTAELKSL---------EDKAAEVVKNTNAAE-----ESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 939
Cdd:COG4942 96 RAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
...
gi 578806949 940 LEQ 942
Cdd:COG4942 176 LEA 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1053 |
9.97e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 859 AQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKL 938
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 939 KLEQIDGHIAEHNSKIkYWHKEISKISLhpiednpieeisVLSPED-LEAIKNPDSITNQIALLEARCHEMKPNLGAIAE 1017
Cdd:COG4942 98 ELEAQKEELAELLRAL-YRLGRQPPLAL------------LLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 578806949 1018 ykKKEELYLQRvAELDKITYERDSFRQAYEDLRKQR 1053
Cdd:COG4942 165 --LRAELEAER-AELEALLAELEEERAALEALKAER 197
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
694-911 |
1.04e-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: 45.91 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 694 SEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA--NVLAT 771
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKeiAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 772 APDKKKQKLLEENVSAFKT---EYDAVAEKAGKVEAEVKRLhntivEINNHKLKAQQDKLDKINKQLDECASAITKAQVA 848
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgrqPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806949 849 IKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKE 911
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
839-1046 |
1.19e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 839 ASAITKAQVAIKTADRNLQKAQDSVLRT-EKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRN--- 914
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEElQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVkkk 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 915 LLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIkywhkeiskislhpiednpIEEISVLspEDLEAIKNPDS- 993
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPL-------------------IEEYRAL--KEAKSNKEDESq 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578806949 994 -ITNQIALLEARCHEMkpnlgaIAEYKKKEELYLQRVAELDKITyeRDSFRQAY 1046
Cdd:pfam05667 451 rKLEEIKELREKIKEV------AEEAKQKEELYKQLVAEYERLP--KDVSRSAY 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-961 |
1.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 658 RVVTLQGQIiEQSGTMtggGSKVMKGRMGSSLV--------IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERvvKL 729
Cdd:COG4913 575 RAITRAGQV-KGNGTR---HEKDDRRRIRSRYVlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQER--RE 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 730 RHSEREMRNTLEKFTASIQRLIEQeeyLNVQVKELEAN--VLATApdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVK 807
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAE---LEAELERLDASsdDLAAL--EEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 808 RLhntiveinnhklkaqQDKLDKINKQLDEcASAITKAQVAIKTADRNLQKAQDSVLRTEKEikDTEKEVDDLTAELKSL 887
Cdd:COG4913 724 QA---------------EEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 888 EDKAAEV-----------VKNTNAAEESLPEIQKEHRNLlqelkvIQENEHALQKDALsiKLKLEQIDGHIAEHNSKIKY 956
Cdd:COG4913 786 EEELERAmrafnrewpaeTADLDADLESLPEYLALLDRL------EEDGLPEYEERFK--ELLNENSIEFVADLLSKLRR 857
|
....*
gi 578806949 957 WHKEI 961
Cdd:COG4913 858 AIREI 862
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
691-946 |
1.39e-04 |
|
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: 46.19 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRliEQEEYLNVQVKELEANVLA 770
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR--EKERELVDCQRELEKLNKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 771 TAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRL----------HNTIVEI---NNHKLK--AQQDKLDKINKQL 835
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLatrleldgfeRGPFSERqikNFHTLVieRQEDEAKTAAQLC 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 836 DECAS-------AITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKntnaAEESLPEI 908
Cdd:TIGR00606 415 ADLQSkerlkqeQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK----AERELSKA 490
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 578806949 909 QKEH--RNLLQELKVIQENEHALQKDALSIKLKLEQIDGH 946
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
691-901 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLiEQEEYLNVQVKELEANVLA 770
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 771 TapdkkkqklleeNVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKlKAQQDKLDKINKQLDECASAITKAQVAIK 850
Cdd:COG4942 136 R------------RLQYLKYLAPARREQAEELRADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578806949 851 TADRNLQKAQdsvlrteKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA 901
Cdd:COG4942 203 RLEKELAELA-------AELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
820-1026 |
2.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 820 KLKAQQDKLDKINKQLDE-CASAITKAQVAIKTAD---RNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLED--KAAE 893
Cdd:COG4717 50 RLEKEADELFKPQGRKPElNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 894 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHalqkdalsiklKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNp 973
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLSLATEEELQDL- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578806949 974 IEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYL 1026
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
691-901 |
2.24e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLN-----VQVKELE 765
Cdd:pfam06008 42 IEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGendfaLPSSDLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 766 aNVLATApdkkkQKLLEE----NVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASA 841
Cdd:pfam06008 122 -RMLAEA-----QRMLGEirsrDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLREL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 842 ITKAQVAIKTADRNLQKAQdsvlRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA 901
Cdd:pfam06008 196 LREAAAKTRDANRLNLANQ----ANLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLL 251
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
695-944 |
2.34e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATapd 774
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 775 KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADR 854
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 855 NlQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDAL 934
Cdd:COG4372 215 E-LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250
....*....|
gi 578806949 935 SIKLKLEQID 944
Cdd:COG4372 294 ELKLLALLLN 303
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
84-125 |
2.53e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.76 E-value: 2.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 578806949 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDS 125
Cdd:COG1195 2 LKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEA 41
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
869-965 |
2.62e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 869 EIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA-EESLPEIQKEHRNL---LQELKVIQENEHALQKDALSIKLKLEQID 944
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELeeeLEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100
....*....|....*....|.
gi 578806949 945 GHIAEHNSKIKYWHKEISKIS 965
Cdd:COG0542 485 GKIPELEKELAELEEELAELA 505
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
616-961 |
2.93e-04 |
|
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: 45.10 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 616 FDLVKVKDEKIRQAFYFALR-DTLVADNLDQAtrvaYQK---DRRWRVVTLQGQIIEQSGTMTGggskvmkgrmgSSLVI 691
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKeDHEKIQHLEEE----YKKeinDKEKQVSLLLIQITEKENKMKD-----------LTFLL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 692 EISEEEVNKMESQLQNDSKKAMQIQEQK----VQLEERVVKLRHS---EREMRNTLEKFTASIQRLIEQEEYL------- 757
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSmstQKALEEDLQIATKTICQLTEEKEAQmeelnka 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 758 ----NVQVKELEANVLATAPD-KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINN-HKLKAQQDKLDKI 831
Cdd:pfam05483 344 kaahSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 832 NKQLDECASAITKAQVAI----KTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPE 907
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578806949 908 IQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEI 961
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-420 |
3.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 261 GRLNEPIKVLCRRVEILNEHR---GEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEM 337
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 338 ETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNK-------ITKfiEENKEKFTQLDLEDVQVREKLKHATSK 410
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTE--EHRKELLEEYTAELKRIEKELKEIEEK 474
|
170
....*....|
gi 578806949 411 AKKLEKQLQK 420
Cdd:PRK03918 475 ERKLRKELRE 484
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
90-258 |
3.74e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 42.87 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 90 QNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNS--DEHKDIQSCTVEVHFQKI 167
Cdd:pfam13476 4 ENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDirIGLEGKGKAYVEITFENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 168 IDKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDvgnllrSHGIDLDHNRFLILQGEvEQIAMMKPKGQTEHD 247
Cdd:pfam13476 82 DGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISE------LLKSDKIILPLLVFLGQ-EREEEFERKEKKERL 154
|
170
....*....|.
gi 578806949 248 EGMLEYLEDII 258
Cdd:pfam13476 155 EELEKALEEKE 165
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
104-238 |
5.68e-04 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 43.34 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 104 FHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK--IRSKKLSVLIH----NSDEHKdiqsctvevHFQKIIDKEGDDYEV 177
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVVEgvfdISDEEE---------AKALLLELGIEDDDD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806949 178 IpnsnfYVSRTACRDNTSVYHISGK---KKTFKDVGNLL------RSHGIDLDHNRFL-ILQGEVEQIAMM 238
Cdd:cd03241 90 L-----IIRREISRKGRSRYFINGQsvtLKLLRELGSLLvdihgqHDHQNLLNPERQLdLLDGGLDDVEFL 155
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
327-441 |
5.70e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.40 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 327 IYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDV------KDTEKKLN--KITKFIEENKEKFTQLDLEDV 398
Cdd:pfam09728 112 LKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFekllktKELEVQLAeaKLQQATEEEEKKAQEKEVAKA 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578806949 399 -QVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINE 441
Cdd:pfam09728 192 rELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTT 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-427 |
6.73e-04 |
|
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: 42.60 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 279 EHRGEKLN-RVKMVEKEKDALEGE-KNIAIEFLTLENEIFRKKNHVCQyyiyeLQKRIAEMETQKEKIHeDTKEINeksn 356
Cdd:COG1579 23 EHRLKELPaELAELEDELAALEARlEAAKTELEDLEKEIKRLELEIEE-----VEARIKKYEEQLGNVR-NNKEYE---- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806949 357 ILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEE 427
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
753-933 |
7.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 753 QEEYLNVQVKELEANVLATapdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKIN 832
Cdd:COG3883 17 QIQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 833 KQL----------------DECASAITKAQV--AIKTADRN-LQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAE 893
Cdd:COG3883 93 RALyrsggsvsyldvllgsESFSDFLDRLSAlsKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578806949 894 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDA 933
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
710-896 |
7.76e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 710 KKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANvlATAPDKKKQklleenvsaFK 789
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG--GVCPTCTQQ---------IS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 790 TEYDAVAEkagkveaevkrLHNTIVEINnHKLKAQQDKLDKINKQLDECASAITKA---QVAIKTADRNLQKAQDSVLRT 866
Cdd:PHA02562 296 EGPDRITK-----------IKDKLKELQ-HSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKV 363
|
170 180 190
....*....|....*....|....*....|
gi 578806949 867 EKEIKDTEKEVDDLTAELKSLEDKAAEVVK 896
Cdd:PHA02562 364 KAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
694-1075 |
9.78e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 694 SEEEVNKMESQL-----QNDSKKAMQIQeQKVQLEERVVKLRHSEREMRNTLEKFTASIQR--LIEQEEYLNVQVKELEA 766
Cdd:pfam15921 290 ARSQANSIQSQLeiiqeQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 767 NVLATAPDKKKQKLLEEnvsAFKTEYDAVAEKAGKVEAEVKRLHNTIV------EINNHKLKAQqdKLDKINKQL-DECA 839
Cdd:pfam15921 369 SQESGNLDDQLQKLLAD---LHKREKELSLEKEQNKRLWDRDTGNSITidhlrrELDDRNMEVQ--RLEALLKAMkSECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 840 SAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEEslpeiqKEhrnllqel 919
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE------KE-------- 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 920 KVIQENEHALQKDALSIKLKLEQIDgHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAI-----KNPDSI 994
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgRTAGAM 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 995 TNQIALLEARCHEMKPNLGAIAEYKKKEELYLQ----RVAELD----KITYERDSFRQAYEDLRKQR---LNEFMAGFYI 1063
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIReleaRVSDLElekvKLVNAGSERLRAVKDIKQERdqlLNEVKTSRNE 668
|
410
....*....|..
gi 578806949 1064 ItNKLKENYQML 1075
Cdd:pfam15921 669 L-NSLSEDYEVL 679
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
83-129 |
1.18e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.72 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 578806949 83 MITHIVNQNFKSYAGEKIL-----GPFHKRFSCIIGPNGSGKSNVIDSMLFV 129
Cdd:COG1106 1 MLISFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
691-926 |
1.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLA 770
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 771 TAPDkkkqklleenVSAFKTEYDAVAEKAGKVEAEVKRLHntiveinnhklkaqqDKLDKINKQLDECASAITKAQVAIK 850
Cdd:PRK02224 333 CRVA----------AQAHNEEAESLREDADDLEERAEELR---------------EEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806949 851 TadrnlqkaqdsvlrTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLlqeLKVIQENE 926
Cdd:PRK02224 388 E--------------LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA---RERVEEAE 446
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
740-1051 |
1.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 740 LEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVkrlhntiveinnh 819
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 820 klkaqqDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDL---TAELKSLEDKAAE--- 893
Cdd:PRK03918 224 ------EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekVKELKELKEKAEEyik 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 894 VVKNTNAAEESLPEIQKEHRNLLQELKVIQEnehaLQKDALSIKLKLEQIDGHIAE---HNSKIKYWHKEISKISLHPIE 970
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEE----RIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 971 DNPIE-EISVLSPEDLEAI-----KNPDSITNQIALLEARCHEMKPNLG----AIAEYKK----------------KEEL 1024
Cdd:PRK03918 374 LERLKkRLTGLTPEKLEKEleeleKAKEEIEEEISKITARIGELKKEIKelkkAIEELKKakgkcpvcgrelteehRKEL 453
|
330 340
....*....|....*....|....*..
gi 578806949 1025 YLQRVAELDKITYERDSFRQAYEDLRK 1051
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRK 480
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
83-154 |
1.48e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.91 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806949 83 MITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKD 154
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
803-955 |
1.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 803 EAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTA 882
Cdd:COG3883 15 DPQIQAKQKELSELQA-ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 883 EL----------------KSLED--KAAEVVKNTNAAEESLPEIQKEHRNLLQELKV-IQENEHALQKDALSIKLKLEQI 943
Cdd:COG3883 94 ALyrsggsvsyldvllgsESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAeLEAKLAELEALKAELEAAKAEL 173
|
170
....*....|..
gi 578806949 944 DGHIAEHNSKIK 955
Cdd:COG3883 174 EAQQAEQEALLA 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
695-1051 |
1.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSERE---MRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlAT 771
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 772 APDKKKQKLLEENVSAFKTEYDA----VAEKAGKVEAEVKRLHNTIVEINN---------HKLKAQQDKLDKINK--QLD 836
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDelreIEKRLSRLEEEINGIEERIKELEEkeerleelkKKLKELEKRLEELEErhELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 837 ECASAITKAQVAIKT--ADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNA---AEESLP----E 907
Cdd:PRK03918 365 EEAKAKKEELERLKKrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPvcgrE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 908 IQKEHR------------NLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHN--SKIKYWHKEISKISLHPIEDNP 973
Cdd:PRK03918 445 LTEEHRkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 974 IE-------------EISVLSpEDLEAIKnpdSITNQIALLEARCHEMKPNLGAIaeYKKKEELYLQRVAELDKITYERD 1040
Cdd:PRK03918 525 EEyeklkekliklkgEIKSLK-KELEKLE---ELKKKLAELEKKLDELEEELAEL--LKELEELGFESVEELEERLKELE 598
|
410
....*....|.
gi 578806949 1041 SFRQAYEDLRK 1051
Cdd:PRK03918 599 PFYNEYLELKD 609
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
704-896 |
1.84e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 704 QLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlatapDKKKQKLleE 783
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-----KKYEEQL--G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 784 NVSAFKtEYDAVaekagkveaevkrlhntiveinNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSV 863
Cdd:COG1579 84 NVRNNK-EYEAL----------------------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|...
gi 578806949 864 LRTEKEIkdtEKEVDDLTAELKSLEDKAAEVVK 896
Cdd:COG1579 141 EEKKAEL---DEELAELEAELEELEAEREELAA 170
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
695-963 |
2.36e-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: 42.13 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKEleanvlatapd 774
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK----------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 775 kkkqklleenvsAFKTEYDAVAEKAGKVEAEVKRLhntiveinnhkLKAQQDKLDKINKQLDECASAITKAQVAIKTAdr 854
Cdd:pfam12128 672 ------------ALAERKDSANERLNSLEAQLKQL-----------DKKHQAWLEEQKEQKREARTEKQAYWQVVEGA-- 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 855 nlQKAQDSVLRTEKEikdteKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHA------ 928
Cdd:pfam12128 727 --LDAQLALLKAAIA-----ARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfd 799
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578806949 929 -------LQKDALSIKL-----KLEQIDGHIAEHNSKIKYWHKEISK 963
Cdd:pfam12128 800 wyqetwlQRRPRLATQLsnierAISELQQQLARLIADTKLRRAKLEM 846
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-429 |
2.45e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 274 VEILNEHRgEKLNRVKM-VEKEKDALEGE-KNIAIEFLTL-----ENEIFRKKNHVcqyYIYELQKRIAEMETQK----E 342
Cdd:pfam01576 358 LEELTEQL-EQAKRNKAnLEKAKQALESEnAELQAELRTLqqakqDSEHKRKKLEG---QLQELQARLSESERQRaelaE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 343 KIHEDTKEINEKSNILsNEMKAKN----KDVKDTEKKLNKITKFI-EENKEKFT------QLDLEDVQVREKLKHATSKA 411
Cdd:pfam01576 434 KLSKLQSELESVSSLL-NEAEGKNiklsKDVSSLESQLQDTQELLqEETRQKLNlstrlrQLEDERNSLQEQLEEEEEAK 512
|
170
....*....|....*...
gi 578806949 412 KKLEKQLQKDKEKVEEFK 429
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMK 530
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
696-1002 |
2.55e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 696 EEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSE----------REMRNTLEKFTASIQRLIEQEEYLNVQVKELe 765
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniqknidkiKNKLLKLELLLSNLKKKIQKNKSLESQISEL- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 766 anvlatapdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKA 845
Cdd:TIGR04523 224 ---------KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK-QLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 846 QVAIKtaDRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQEN 925
Cdd:TIGR04523 294 KSEIS--DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 926 EHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEI----SKISLHPIEDNPIE-EISVLSPEDLEAIKNPDSITNQIAL 1000
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEKELLEkEIERLKETIIKNNSEIKDLTNQDSV 451
|
..
gi 578806949 1001 LE 1002
Cdd:TIGR04523 452 KE 453
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
820-892 |
2.63e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.64 E-value: 2.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806949 820 KLKAQQDKLDKINKQLDECASAITKAQ-VAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAA 892
Cdd:TIGR04320 283 ALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
622-808 |
3.24e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 622 KDEKIRQafyfalrdtlvadNLDQATRVAYQKDRRWRvvtlqgQIIEQSGTMTGGGSKVMKGRMGSSLVIEisEEEVNKM 701
Cdd:pfam17380 390 KNERVRQ-------------ELEAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 702 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNtlekftasiQRLIEQEEYLNVQvKELEANVLATAPDKKKQKLL 781
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD---------RKRAEEQRRKILE-KELEERKQAMIEEERKRKLL 518
|
170 180
....*....|....*....|....*..
gi 578806949 782 EENVSAFKTeydAVAEKAGKVEAEVKR 808
Cdd:pfam17380 519 EKEMEERQK---AIYEEERRREAEEER 542
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
734-931 |
3.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 734 REMRNTLEKFTASIQRL-IEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAeVKRLHNT 812
Cdd:COG4717 52 EKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 813 IVEIN--NHKLKAQQDKLDKINKQLDEcasaITKAQVAIKTADRNLQKAQDSVLRTEKEIK-DTEKEVDDLTAELKSLED 889
Cdd:COG4717 131 YQELEalEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578806949 890 KAAEvvkntnaAEESLPEIQKEHRNLLQELKVIQENEHALQK 931
Cdd:COG4717 207 RLAE-------LEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
691-920 |
3.36e-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: 41.96 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 691 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEK---FTASIQRLIEQEEYLNVQVKELEAN 767
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQ 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 768 VLATAPDKKK-QKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLH-------NTIVEINNHKLKAQQDKLDKINKQLDECA 839
Cdd:TIGR00606 911 DSPLETFLEKdQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdieNKIQDGKDDYLKQKETELNTVNAQLEECE 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 840 SAITKAQVAIKTADRNL--QKAQDSVLRTEKEIKDTEKEVDDLTAELKSL-----EDKAAEVVKNTNAAEESLPEIQKEH 912
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
....*...
gi 578806949 913 RNLLQELK 920
Cdd:TIGR00606 1071 VLALGRQK 1078
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
692-935 |
3.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 692 EISEEEVNKMESQLQN-------DSKKAMQIQeQKVQLEERVVKLRHSereMRNTLEKFTASIQRLIEQEEYLNVQVKEL 764
Cdd:PRK04863 386 EAAEEEVDELKSQLADyqqaldvQQTRAIQYQ-QAVQALERAKQLCGL---PDLTADNAEDWLEEFQAKEQEATEELLSL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 765 EanvlatapdkkkQKLleeNVS-AFKTEYDAVAEKAGKVEAEVKRL--HNTIVE-INNH-KLKAQQDKLDKINKQLDECA 839
Cdd:PRK04863 462 E------------QKL---SVAqAAHSQFEQAYQLVRKIAGEVSRSeaWDVARElLRRLrEQRHLAEQLQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 840 SAITKAQVAIKTADRNLQKAQDSVLRTEkeikDTEKEVDDLTAELKSLEDKAAEVVkntnAAEESLPEIQKEHRNLLQEL 919
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDED----ELEQLQEELEARLESLSESVSEAR----ERRMALRQQLEQLQARIQRL 598
|
250
....*....|....*.
gi 578806949 920 KVIQENEHALQkDALS 935
Cdd:PRK04863 599 AARAPAWLAAQ-DALA 613
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
695-920 |
4.24e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 695 EEEVNKMESQLQNDSKKAMQiqeqkvQLEERVVKLRHSEReMRNTLEKftaSIQRLIEQEEYLNVQVKELEANVLATAPD 774
Cdd:pfam01576 337 EEETRSHEAQLQEMRQKHTQ------ALEELTEQLEQAKR-NKANLEK---AKQALESENAELQAELRTLQQAKQDSEHK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 775 KKK--QKLLEENVSAFKTEY--DAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDkLDKINKQL---DECASAITKAQV 847
Cdd:pfam01576 407 RKKleGQLQELQARLSESERqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD-VSSLESQLqdtQELLQEETRQKL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806949 848 AIKTADRNLQKAQDSV---LRTEKEIKDT-EKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELK 920
Cdd:pfam01576 486 NLSTRLRQLEDERNSLqeqLEEEEEAKRNvERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
263-446 |
4.44e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 263 LNEPIKVLCRRVEILNEHrgeklnrvKMVEKEKDALEGEKNIAIEFL-TLENEIFRKKNHVC------QYYIYELQKRIA 335
Cdd:pfam05483 407 LEELKKILAEDEKLLDEK--------KQFEKIAEELKGKEQELIFLLqAREKEIHDLEIQLTaiktseEHYLKEVEDLKT 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 336 EMETQKEKIHE----------DTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLK 405
Cdd:pfam05483 479 ELEKEKLKNIEltahcdklllENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578806949 406 HATSKAK-KLEKQLQKDK-------EKVEEFKSIPAKSNNIINETTTRN 446
Cdd:pfam05483 559 QKGDEVKcKLDKSEENARsieyevlKKEKQMKILENKCNNLKKQIENKN 607
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
700-1017 |
4.72e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 700 KMESQLQNDSKKAMQIQEQKVQLEervvKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQK 779
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEIN----SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 780 LLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEIN--NHKLKAQQDKLDKINKQLDECASaitkaqvaikTADRNLQ 857
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNryESEIKTAESDLSMELEKNNYYKE----------LEERHMK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 858 KAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKnTNAAEESLPEIQKEHRNLLQELKVIQEnehaLQKDALSIK 937
Cdd:PRK01156 285 IINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK-YHAIIKKLSVLQKDYNDYIKKKSRYDD----LNNQILELE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 938 LKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNP-----DSITNQIALLEARCHEMKPNL 1012
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEinvklQDISSKVSSLNQRIRALRENL 439
|
....*
gi 578806949 1013 GAIAE 1017
Cdd:PRK01156 440 DELSR 444
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
108-140 |
5.61e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 5.61e-03
10 20 30
....*....|....*....|....*....|...
gi 578806949 108 FSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSK 140
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLT 33
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
84-128 |
5.84e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 39.97 E-value: 5.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 578806949 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLF 128
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
692-1148 |
6.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 692 EISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTAS------IQRLIEQEEYLNVqVKELE 765
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTEEHRKEL-LEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 766 ANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEA------EVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECA 839
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 840 SAItkaqvaiKTADRNLQKAQDsvlrTEKEIKDTEKEVDDLTAELKSLEDKAAEV-VKNTNAAEESLPEIQKEHRNLLqE 918
Cdd:PRK03918 539 GEI-------KSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPFYNEYL-E 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 919 LKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISkislhpiednpiEEISVLSPEDLEAIKNP-DSITNQ 997
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE------------ELEKKYSEEEYEELREEyLELSRE 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 998 IALLEARCHEMKPNLGAIAEYKKKEElylQRVAELDKITYERDSFRQAYEDLrkQRLNEfmagfyiitnKLKENYQMLTL 1077
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLK---EELEEREKAKKELEKLEKALERV--EELRE----------KVKKYKALLKE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1078 GGDAELELVDS--LDPFSEGIMFSVRPPKKSWKKIFN------------LSGGEKTLSSLALVFALHHYK--PTPLYFMD 1141
Cdd:PRK03918 740 RALSKVGEIASeiFEELTEGKYSGVRVKAEENKVKLFvvyqgkerpltfLSGGERIALGLAFRLALSLYLagNIPLLILD 819
|
....*..
gi 578806949 1142 EIDAALD 1148
Cdd:PRK03918 820 EPTPFLD 826
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
692-1189 |
6.80e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 692 EISEEEVNKMESQLQndsKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKF--------------TASIQRLI----EQ 753
Cdd:PRK01156 401 EIDPDAIKKELNEIN---VKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIInhynEK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 754 EEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKT-EYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQdkldkin 832
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEE------- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 833 kqLDECASAITKAQVAIKTADRNLQKAQDSVLrtekEIKDTEKEVDDLTAELKSLEDKAAEVVKN----TNAAEESLPEI 908
Cdd:PRK01156 551 --IKNRYKSLKLEDLDSKRTSWLNALAVISLI----DIETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 909 QKEHRNLLQELKVIQENEHALQKdalsIKLKLEQIDGHIAEHNSKIKYWHKEISKISlhPIEDNpieeISVLSPEDLEAI 988
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEK----LRGKIDNYKKQIAEIDSIIPDLKEITSRIN--DIEDN----LKKSRKALDDAK 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 989 KNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKItyeRDSF-RQAYEDLRKQRLNEFMagfyiiTNK 1067
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRL---REAFdKSGVPAMIRKSASQAM------TSL 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1068 LKENYQMLTLggdaelelvdSLDPFSEGIMFSVRPPKKSW-KKIFNLSGGEKTLSSLALVFALHHY--KPTPLYFMDEID 1144
Cdd:PRK01156 766 TRKYLFEFNL----------DFDDIDVDQDFNITVSRGGMvEGIDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPT 835
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 578806949 1145 AALDFKNVS----IVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYK 1189
Cdd:PRK01156 836 AFLDEDRRTnlkdIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKK 884
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
329-417 |
7.23e-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: 40.13 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 329 ELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHAT 408
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
....*....
gi 578806949 409 SKAKKLEKQ 417
Cdd:COG4942 111 RALYRLGRQ 119
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-444 |
7.32e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 277 LNEHRGEKLNRVKMVEKEKDAL-EGEKNIAIEFLTLENEIFRKKNHVCQYyiyELQKRIAEMETQKEKIHEDTKEINEKS 355
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLkEKIEKLESEKKEKESKISDLEDELNKD---DFELKKENLEKEIDEKNKEIEELKQTQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 356 NILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVE----EFKSI 431
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKqikeTIKEI 657
|
170
....*....|...
gi 578806949 432 PAKSNNIINETTT 444
Cdd:TIGR04523 658 RNKWPEIIKKIKE 670
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
84-166 |
7.46e-03 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 40.03 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQkiRSKKLSVLIHNSDEHkdiqsCTVEVH 163
Cdd:TIGR00611 3 LSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSH--RTSRDKPLIRFGAEA-----FVIEGR 73
|
...
gi 578806949 164 FQK 166
Cdd:TIGR00611 74 VSK 76
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
818-1195 |
7.80e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 818 NHKLKAQQDKLDKINKQLDEcasAITKAQVAIktaDRNLQKAQD---SVLRTEKEIKDTEKEVDDLTAELKSLEDKAA-- 892
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGE---NIARKQNKY---DELVEEAKTikaEIEELTDELLNLVMDIEDPSAALNKLNTAAAki 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 893 ----------------------------EVVKNTNAAEESLPEIQKEHRNLL---QELKVIQENEHALQKDALSIKLKLE 941
Cdd:PHA02562 268 kskieqfqkvikmyekggvcptctqqisEGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 942 QIDGHIAEHNSKIKYWHKEISKISLHPIEDNpiEEISVLSpEDLEAIKNPDSitnqiallearchemkpnlgaiaeYKKK 1021
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNA--EELAKLQ-DELDKIVKTKS------------------------ELVK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1022 EELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMagfyiitnKLKENYQMLTLggDAElelvdsldpFSEGImfsvr 1101
Cdd:PHA02562 401 EKYHRGIVTDLLKDSGIKASIIKKYIPYFNKQINHYL--------QIMEADYNFTL--DEE---------FNETI----- 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 1102 ppKKSWKKIF---NLSGGEKTLSSLALVFA------LHHYKPTPLYFMDEI-DAALDFKNVSIVaFYIYEQTKNAQFIII 1171
Cdd:PHA02562 457 --KSRGREDFsyaSFSQGEKARIDLALLFTwrdvasKVSGVDTNLLILDEVfDGALDAEGTKAL-LSILDSLKDTNVFVI 533
|
410 420
....*....|....*....|....
gi 578806949 1172 SLRNNMFEISDRLIGIYKTYNITK 1195
Cdd:PHA02562 534 SHKDHDPQKFDRHLKMEKVGRFSV 557
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
692-965 |
9.85e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 692 EISEEEVNKMESQL-----QNDSKKAMQIQEQKVQLEErvvKLRHSEREMRNTLEKftasIQRLIEQEEYLNVQVKELea 766
Cdd:pfam06160 56 DIVTKSLPDIEELLfeaeeLNDKYRFKKAKKALDEIEE---LLDDIEEDIKQILEE----LDELLESEEKNREEVEEL-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 767 nvlatapdKKK----QKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTI-----VEINNHKLKAQQDkLDKINKQLDE 837
Cdd:pfam06160 127 --------KDKyrelRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELTesgdyLEAREVLEKLEEE-TDALEELMED 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 838 CASAITKAQVAIKTADRNLQ------KAQDSVLRT---EKEIKDTEKEVDDLTAELKSLEDKAAE--------------- 893
Cdd:pfam06160 198 IPPLYEELKTELPDQLEELKegyremEEEGYALEHlnvDKEIQQLEEQLEENLALLENLELDEAEealeeieeridqlyd 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806949 894 -----------VVKNTNAAEESLPEIQKEHRNLLQELK------VIQENE----HALQKDALSIKLKLEQIDGHIAEHN- 951
Cdd:pfam06160 278 llekevdakkyVEKNLPEIEDYLEHAEEQNKELKEELErvqqsyTLNENElervRGLEKQLEELEKRYDEIVERLEEKEv 357
|
330 340
....*....|....*....|
gi 578806949 952 ------SKIKYWHKEISKIS 965
Cdd:pfam06160 358 ayselqEELEEILEQLEEIE 377
|
|
| |
