|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
99-248 |
8.56e-42 |
|
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: 151.98 E-value: 8.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 99 VISMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSIQKLIKNGEVSATISITLSNSGL 178
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTLKNQGL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 179 rpfkadifgphltvvrqirhssstydlqDArgksvskkvsdirrmllcfginveNPIFVLNQEAAREFLK 248
Cdd:cd03276 81 ----------------------------DA------------------------NPLCVLSQDMARSFLT 98
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1027-1122 |
6.61e-36 |
|
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: 135.03 E-value: 6.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 1027 PSGNETSNTRSLSGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFTDEVNRKFITEILIGEGLEWLSRQYCFLTPQDTKV 1106
Cdd:cd03276 99 SNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISG 178
|
90
....*....|....*..
gi 7301120 1107 EASN-LITVHKLEAPER 1122
Cdd:cd03276 179 LASSdDVKVFRMKDPRG 195
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-1076 |
8.09e-24 |
|
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: 108.99 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 115 IEFGPNINFLVGNNGSGKSAVITAL--ALGlTSSARATnRASSIQKLIKNGEVS------ATISITLSNS-GLRPFKADi 185
Cdd:TIGR02168 19 INFDKGITGIVGPNGCGKSNIVDAIrwVLG-EQSAKAL-RGGKMEDVIFNGSETrkplslAEVELVFDNSdGLLPGADY- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 186 fgPHLTVVRQI-RHSSSTY----------DLQD--------ARGKSV--SKKVSDI-------RRMLL--CFGIN----- 230
Cdd:TIGR02168 96 --SEISITRRLyRDGESEYfingqpcrlkDIQDlfldtglgKRSYSIieQGKISEIieakpeeRRAIFeeAAGISkyker 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 231 ---VENPIFVLNQEAAR--EFLKEL-----------EPASNYKLL---MKATQLDVCTSSLTECHALRRHFTQELEQLEK 291
Cdd:TIGR02168 174 rkeTERKLERTRENLDRleDILNELerqlkslerqaEKAERYKELkaeLRELELALLVLRLEELREELEELQEELKEAEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 292 KKEMMIKHIAAEEEKLSILEDKEMVKENLQQCKTKlawmAVTSYQNELNNLEHSIKLIENKKASLEQTTSKKESTQATMN 371
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQK----ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 372 QKLKEFEASKNQIlatqkfqDERLKTAKKAVQDLLLEASQVKAKIGNAERRMRedqrsydECEKLIGNYHADFNRVNEQR 451
Cdd:TIGR02168 330 SKLDELAEELAEL-------EEKLEELKEELESLEAELEELEAELEELESRLE-------ELEEQLETLRSKVAQLELQI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 452 EENANKIEMLKKQVVKSEEIIAQLRAEQQEIKRDITS-----VQERLDAVKNGRIQL---HKSKQNISWEIEALSRNKSN 523
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELqeeLERLEEALEELREELEEAEQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 524 KLSVYGEQTIQ------VVHALRTQYAG---------SNMHRMP--RGPLGQYISAPnPKYRDLIENQLMHCLRSFIV-G 585
Cdd:TIGR02168 476 ALDAAERELAQlqarldSLERLQENLEGfsegvkallKNQSGLSgiLGVLSELISVD-EGYEAAIEAALGGRLQAVVVeN 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 586 SDRERQSLRALLQNKFQGGNM-PTIITSPFTDRVYDVSRNKVQPTTPNTTVLIDEISCDDPVVMNYLIDILRI------- 657
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFlPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvddldna 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 658 ---------ETVLVTE-------------------------SKEIAE------FLTSDTENVPPNLTRVLVPNLGLE--- 694
Cdd:TIGR02168 635 lelakklrpGYRIVTLdgdlvrpggvitggsaktnssilerRREIEEleekieELEEKIAELEKALAELRKELEELEeel 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 695 -----YIPSPNYAVYSTRITPARYIQK--NVDDRIRQLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKVISQKSTMIGQH 767
Cdd:TIGR02168 715 eqlrkELEELSRQISALRKDLARLEAEveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 768 QSRNQKAMQKIMELQNfDYQELP-EYDRLKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINK 846
Cdd:TIGR02168 795 KEELKALREALDELRA-ELTLLNeEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 847 KLTALDTEAGEVESKMRSLDLHY----------EENTRRFQKTLQLERKMLGEKETVLSEL------------EKARTEA 904
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELeelseelrelESKRSELRRELEELREKLAQLELRLEGLevridnlqerlsEEYSLTL 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 905 EKLGEFIATTQTE-EKIREAISRYKSKIKQVEELNYN-PEELERgLAELRDELELQSRHL----AVVDSVVKKLRMAYHQ 978
Cdd:TIGR02168 954 EEAEALENKIEDDeEEARRRLKRLENKIKELGPVNLAaIEEYEE-LKERYDFLTAQKEDLteakETLEEAIEEIDREARE 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 979 R-AQLFQRSRHHYFTMVQFQFEQALAmrQFKVSFETSDKEKTWKINVFPPsGNETSNTRSLSGGERSFTTVSLLKGLWST 1057
Cdd:TIGR02168 1033 RfKDTFDQVNENFQRVFPKLFGGGEA--ELRLTDPEDLLEAGIEIFAQPP-GKKNQNLSLLSGGEKALTALALLFAIFKV 1109
|
1130
....*....|....*....
gi 7301120 1058 SDHPFYFLDEYDVFTDEVN 1076
Cdd:TIGR02168 1110 KPAPFCILDEVDAPLDDAN 1128
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
115-1084 |
2.25e-19 |
|
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: 94.65 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 115 IEFGPNINFLVGNNGSGKSAVITALA--LGLTSSarATNRASSIQKLI----KNGEVSATISITLSNSGLRPFkadIFGP 188
Cdd:pfam02463 19 LPFSPGFTAIVGPNGSGKSNILDAILfvLGERSA--KSLRSERLSDLIhsksGAFVNSAEVEITFDNEDHELP---IDKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 189 HLTVVRQI-RHSSSTYDLQdarGKSVSKKvsDIRRMLLCFGINVENPIFVLNQ-------EAAREFLKELEPAS------ 254
Cdd:pfam02463 94 EVSIRRRVyRGGDSEYYIN---GKNVTKK--EVAELLESQGISPEAYNFLVQGgkieiiaMMKPERRLEIEEEAagsrlk 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 255 -----NYKLLMKATQ--LDVCTSSLTECHALRRHFTQELEQLEKKKEMMIKHIAAE------------------------ 303
Cdd:pfam02463 169 rkkkeALKKLIEETEnlAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldylklneeridllqellrd 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 304 ----EEKLSILEDKEMVKENLQQCKTKLAWMAVTSYQNELNNLEHSIKLIENKKASLEQTTSKKESTQATMNQKLKEFEA 379
Cdd:pfam02463 249 eqeeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 380 SKNQILATQKFQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKLIGNYHADFNRVNEQREENANKI- 458
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAq 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 459 ---EMLKKQVVKSEEIIAQLRAEQQEIKRDITSVQERLDAVKNGRIQLHKSKQNISWEIEALSRNKSNKLSVYGEQTIQV 535
Cdd:pfam02463 409 lllELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 536 VHALRTQYAGSNMHR------------MPRGPLGQYISAPNPKYRDLIENQLMHCLRSFIVGSDRERQSLRALLQNKFQG 603
Cdd:pfam02463 489 LLSRQKLEERSQKESkarsglkvllalIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 604 G------NMPTIITSPFTDRVYDVSRNKVQPTTPNTTVLIDEISCD---DPVVMNYLIDILRIETVLVTESKEIA----- 669
Cdd:pfam02463 569 AltelplGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEadeDDKRAKVVEGILKDTELTKLKESAKAkesgl 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 670 -------------------EFLTSDTENVPPNLTRVLVPNLGLEYIPSPNYAVYSTRITPARYIQKNVDDRIRQLQMEQS 730
Cdd:pfam02463 649 rkgvsleeglaeksevkasLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 731 DLQEKEPSLEIDYMQHKKVLENTQKVISQKSTMIGQ---HQSRNQKAMQKIMELQNFDYQELPEYDRLKShLADSGEKIE 807
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEeksELSLKEKELAEEREKTEKLKVEEEKEEKLKA-QEEELRALE 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 808 KCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLHYEENTRRFQKTLQLERK-M 886
Cdd:pfam02463 808 EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKdE 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 887 LGEKETVLSELEKARTEAEKLGEFIATTQTEEKIREAISRYKS-------------KIKQVEELNYNPEELERGLAELRD 953
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILlkyeeepeellleEADEKEKEENNKEEEEERNKRLLL 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 954 ELELQSRHLAVVDSVVKKLRMAYHQRAQLFQRSRHHYfTMVQFQFEQALAMRQFKVSFETSDKEKTWKINV--------- 1024
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK-KKLIRAIIEETCQRLKEFLELFVSINKGWNKVFfylelggsa 1046
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7301120 1025 ------------------FPPSGNETSNTRSLSGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFTDEVNRKFITEIL 1084
Cdd:pfam02463 1047 elrledpddpfsggieisARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLL 1124
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-1076 |
1.88e-18 |
|
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: 91.67 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 115 IEFGPNINFLVGNNGSGKSAVITAL--ALGLTSSarATNRASSIQKLIKNGE-----VSATISITLSNSGLRpfkadiFG 187
Cdd:TIGR02169 19 IPFSKGFTVISGPNGSGKSNIGDAIlfALGLSSS--KAMRAERLSDLISNGKngqsgNEAYVTVTFKNDDGK------FP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 188 PHLTVVRQIR----HSSSTYDLQdarGKSVSkkVSDIRRMLLCFGINVENPIFVL----------NQEAAREFLKELEPA 253
Cdd:TIGR02169 91 DELEVVRRLKvtddGKYSYYYLN---GQRVR--LSEIHDFLAAAGIYPEGYNVVLqgdvtdfismSPVERRKIIDEIAGV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 254 SNY--KLLMKATQLDVCTSSLTECHALRRHFTQELEQLEKKKEMMIKHIAAEEEKLS-----ILEDKEMVKENLQQCKTK 326
Cdd:TIGR02169 166 AEFdrKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyeLLKEKEALERQKEAIERQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 327 LAwmavtSYQNELNNLEHSIKLIENKKASLEQTTS--------KKESTQATMNQKLKEFEASKNQILATQKFQDERLKTA 398
Cdd:TIGR02169 246 LA-----SLEEELEKLTEEISELEKRLEEIEQLLEelnkkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 399 KKAVQDLLLEASQVKAKIGNAERRMREDQRSYD----ECEKLIGNYHADFNRVNEQREENA----------NKIEMLKKQ 464
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDklteEYAELKEELEDLRAELEEVDKEFAetrdelkdyrEKLEKLKRE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 465 V--------------VKSEEIIAQLRAEQQEIKRDITSVQERLDAV--------------KNGRIQLHKSKQNISWEIEA 516
Cdd:TIGR02169 401 InelkreldrlqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKaleikkqewkleqlAADLSKYEQELYDLKEEYDR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 517 LSRNKSNKLSVYGEQTIQVVHALRTQYAGSNMHRMPR-------GPLGQYISApNPKYRDLIENQLMHCLRSFIVGSDRE 589
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhGTVAQLGSV-GERYATAIEVAAGNRLNNVVVEDDAV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 590 RQSLRALLQNKfQGGNMPTIitsPFTdRVYDVSRNKVQPTTPNTT-VLIDEISCDD---PVVMNYLIDIL---RIETV-- 660
Cdd:TIGR02169 560 AKEAIELLKRR-KAGRATFL---PLN-KMRDERRDLSILSEDGVIgFAVDLVEFDPkyePAFKYVFGDTLvveDIEAArr 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 661 ------LVTESKEIAEFLTSDTENVPPNLTRVLVPNLGLEYIPSPNYAVYSTRITPA------RYIQKNVDD-------- 720
Cdd:TIGR02169 635 lmgkyrMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSslqselRRIENRLDElsqelsda 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 721 --RIRQLQMEQSDLQEKEPSL---------EIDYMQHKKV-----LENTQKVISQKSTMIGQHQSRNQK-----AMQKIM 779
Cdd:TIGR02169 715 srKIGEIEKEIEQLEQEEEKLkerleeleeDLSSLEQEIEnvkseLKELEARIEELEEDLHKLEEALNDlearlSHSRIP 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 780 ELQNfDYQELPEY-DRLKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEV 858
Cdd:TIGR02169 795 EIQA-ELSKLEEEvSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 859 ESKMRSLD--------------LHYEENTRRFQK---TLQLERKMLGEKETVLSELEKARTEAEKLG----EFIATTQTE 917
Cdd:TIGR02169 874 EAALRDLEsrlgdlkkerdeleAQLRELERKIEEleaQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeEIPEEELSL 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 918 EKIREAISRYKSKIKQVEELNYN-PEELERGLAELRDELELQSRHLAVVDSVVKKLRMAYHQRAQLFQRSrhhyFTMVQF 996
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA----FEAINE 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 997 QFEQ---ALAMRQFKVSFETSDKEKTWKINV-FPPSGNETSNTRSLSGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFT 1072
Cdd:TIGR02169 1030 NFNEifaELSGGTGELILENPDDPFAGGLELsAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFL 1109
|
....
gi 7301120 1073 DEVN 1076
Cdd:TIGR02169 1110 DGVN 1113
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
97-177 |
1.41e-14 |
|
ATP-binding cassette domain of eukaryotic SMC5 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: 213244 [Multi-domain] Cd Length: 213 Bit Score: 73.78 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 97 GKVISMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSIQKLIKNGEVSATISITLSNS 176
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYGN 80
|
.
gi 7301120 177 G 177
Cdd:cd03277 81 P 81
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
102-292 |
5.60e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 71.76 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 102 MRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSIQ------KLIKNGEVSATISITLSN 175
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGfvkgdiRIGLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 176 SGLRPFKADIFGPHLtvvrqIRHSSSTYDLQDARGKSVSKKVSDIRRMLLCFGInvENPIFVLNQEAAREFLKELEPASN 255
Cdd:pfam13476 81 NDGRYTYAIERSREL-----SKKKGKTKKKEILEILEIDELQQFISELLKSDKI--ILPLLVFLGQEREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 7301120 256 YKLLMKATQLDVCTSSLTECHALRRHFTQELEQLEKK 292
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
101-176 |
1.22e-10 |
|
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: 61.56 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 101 SMRLTNFMCHSNLFIEFGPN-INFLVGNNGSGKSAVITALALGLTSSARATNRASSIQKL---IKNGEVSATISITLSNS 176
Cdd:cd03239 3 QITLKNFKSYRDETVVGGSNsFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAgggVKAGINSASVEITFDKS 82
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
101-506 |
1.28e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 101 SMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSaratNRASSIQKLIKNGEVSATISITLSNSGlrp 180
Cdd:PRK01156 5 RIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTD----KRTEKIEDMIKKGKNNLEVELEFRIGG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 181 fkaDIFGPHLTVVRQIRHSSSTYDLQdARGKSVSKKVSDIRRMLLCFGINVENPIF---VLNQEAAREFLKELEPASNYK 257
Cdd:PRK01156 78 ---HVYQIRRSIERRGKGSRREAYIK-KDGSIIAEGFDDTTKYIEKNILGISKDVFlnsIFVGQGEMDSLISGDPAQRKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 258 LLMKATQ--------------LDVCTSSLTECHALRR----------HFTQELEQLEKKKEMMIKHI-AAEEEKLSILED 312
Cdd:PRK01156 154 ILDEILEinslernydklkdvIDMLRAEISNIDYLEEklkssnleleNIKKQIADDEKSHSITLKEIeRLSIEYNNAMDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 313 KEMVKENLQQcktklawmaVTSYQNELNNLEHSIKLIENKKASLEQTTSK-KESTQATMNQKLKEFEASKNQILATQKFQ 391
Cdd:PRK01156 234 YNNLKSALNE---------LSSLEDMKNRYESEIKTAESDLSMELEKNNYyKELEERHMKIINDPVYKNRNYINDYFKYK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 392 DErLKTAKKAVQDLLLEASQVKAKIGNAE------RRMREDQRSYDECEKLIGN---YHADFN-------RVNEQREENA 455
Cdd:PRK01156 305 ND-IENKKQILSNIDAEINKYHAIIKKLSvlqkdyNDYIKKKSRYDDLNNQILElegYEMDYNsylksieSLKKKIEEYS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7301120 456 NKIE--------MLKKQVVKSEEIIA---QLRAEQQEIKRDITSVQERLDAVKNGRIQLHKS 506
Cdd:PRK01156 384 KNIErmsafiseILKIQEIDPDAIKKelnEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
98-179 |
2.01e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 58.48 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 98 KVISMRLTNFMCHSN-LFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSiqKLIKNGEVSATISITLSNS 176
Cdd:COG0419 1 KLLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRS--DLINVGSEEASVELEFEHG 78
|
...
gi 7301120 177 GLR 179
Cdd:COG0419 79 GKR 81
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
103-177 |
2.52e-09 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 60.55 E-value: 2.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7301120 103 RLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALA-LGLTSSAratnRASSIQKLIKNGEVSATISITLSNSG 177
Cdd:COG1195 6 SLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIYlLATGRSF----RTARDAELIRFGADGFRVRAEVERDG 77
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-523 |
4.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 98 KVISMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSIQKLIKNGEVSATISITLSNSG 177
Cdd:PRK03918 2 KIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 178 LRpfkadifgphLTVVRQIRHSSSTYDLQDARGKSVSKKVSDIRRMLLCFGINV-ENPIFVlNQEAAREFLKELEpaSNY 256
Cdd:PRK03918 82 RK----------YRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVfLNAIYI-RQGEIDAILESDE--SRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 257 KLLMKATQLDVCTSSLTECHALRRHFTQELEQLEK--KKEMMIKHI--AAEEEKLSILEDKEMVKENLQQCKTKLAWMA- 331
Cdd:PRK03918 149 KVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKfiKRTENIEELikEKEKELEEVLREINEISSELPELREELEKLEk 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 332 ----VTSYQNELNNLEHSIKLIENKKASLEQTTSKKESTQATMNQKLKEFEASKNQILATQKFQDERLKTaKKAVQDLLL 407
Cdd:PRK03918 229 evkeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL-SEFYEEYLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 408 EASQVKAKIGNAERRMREDQRSYDECEKLignyHADFNRVNEQREENANKIEMLKKQVVKSEEiIAQLRAEQQEIKRDIT 487
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLT 382
|
410 420 430
....*....|....*....|....*....|....*.
gi 7301120 488 SvqERLDAVKNGRIQLHKSKQNISWEIEALSRNKSN 523
Cdd:PRK03918 383 G--LTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1035-1122 |
5.99e-09 |
|
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: 56.55 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 1035 TRSLSGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFTDEVNRKFITEILIGEGLEwlSRQYCFLTPQDTKVEASN-LIT 1113
Cdd:cd03239 92 EQILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH--TSQFIVITLKKEMFENADkLIG 169
|
....*....
gi 7301120 1114 VHKLEAPER 1122
Cdd:cd03239 170 VLFVHGVST 178
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
279-542 |
7.61e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 279 RRHFTQELEQLEKKKEMMIKHIAAEEEKLSILEDKEMVKENLQQCKTKlawmAVTSYQNELNNLEHSIKLIENKKASLEQ 358
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 359 TTSKKESTQATMNQKLKEFEASKNQILATQKFQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKlig 438
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 439 nyhaDFNRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEIKRDITSVQERLDAVKNGRIQLHKSKQNISWEIEALS 518
Cdd:COG1196 387 ----ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260
....*....|....*....|....
gi 7301120 519 RNKSNKLSVYGEQTIQVVHALRTQ 542
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEEL 486
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
101-171 |
3.96e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 55.77 E-value: 3.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7301120 101 SMRLTNFMCHSNLFIEF--GPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSIQKLIKNGEVSATISI 171
Cdd:COG3950 5 SLTIENFRGFEDLEIDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKL 77
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
102-175 |
5.37e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.54 E-value: 5.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7301120 102 MRLTNFMC-HSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNR-ASSIQKLIKNGEVSATISITLSN 175
Cdd:cd03240 4 LSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKgGAHDPKLIREGEVRAQVKLAFEN 79
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
99-173 |
5.97e-08 |
|
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: 53.52 E-value: 5.97e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7301120 99 VISMRltNFMCH-SNLFIEFG-PNINFLVGNNGSGKSAVITALALGLTSSARATNRassiQKLIKNGEVSATISITL 173
Cdd:cd03227 1 KIVLG--RFPSYfVPNDVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR----RSGVKAGCIVAAVSAEL 71
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
715-981 |
9.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 715 QKNVDDRIRQLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKVISQKSTMIGQHQSRNQKAMQKIMELQNfdyqelpEYDR 794
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 795 LKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDlhyeentR 874
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-------E 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 875 RFQKTLQLERKMLGEKETVLSELEKARTEAEklgefiATTQTEEKIREAISRYKSKIKQVEELNYNPEELERGLAELRDE 954
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEE------EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|....*..
gi 7301120 955 LELQSRHLAVVDSVVKKLRMAYHQRAQ 981
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
101-185 |
1.09e-07 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 55.16 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 101 SMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALA-LGLTSSARATNRASsiqkLIKNGEVSATISITLSNSGlR 179
Cdd:PRK00064 5 RLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYlLAPGRSHRTARDKE----LIRFGAEAAVIHGRVEKGG-R 79
|
....*.
gi 7301120 180 PFKADI 185
Cdd:PRK00064 80 ELPLGL 85
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
98-174 |
1.47e-07 |
|
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: 55.01 E-value: 1.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7301120 98 KVISMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSARATNRASSIQKLIKNGEVSATISITLS 174
Cdd:COG3593 2 KLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFG 78
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
117-240 |
2.98e-07 |
|
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: 53.07 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 117 FGPNINFLVGNNGSGKSAVITAL--ALGLTSSARAtnRASSIQKLI-KNGE---VSATISITLSNSGLR--PFKADIFgP 188
Cdd:cd03273 23 FDPQFNAITGLNGSGKSNILDAIcfVLGITNLSTV--RASNLQDLIyKRGQagiTKASVTIVFDNSDKSqsPIGFENY-P 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 7301120 189 HLTVVRQIRHSSSTYDLqdargksVSKKVSDIRRMLLCF---GINVENPIFVLNQ 240
Cdd:cd03273 100 EITVTRQIVLGGTNKYL-------INGHRAQQQRVQDLFqsvQLNVNNPHFLIMQ 147
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
101-177 |
4.43e-07 |
|
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: 52.68 E-value: 4.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7301120 101 SMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITALALGLTSSaraTNRASSIQKLIKNGEVSATISITLSNSG 177
Cdd:cd03242 3 SLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGK---SHRTSRDKELIRWGAEEAKISAVLERQG 76
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
115-177 |
5.17e-07 |
|
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: 51.31 E-value: 5.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7301120 115 IEFGPNINFLVGNNGSGKSAVITAL--ALGLtSSARATnRASSIQKLIKNGEVS------ATISITLSNSG 177
Cdd:cd03278 18 IPFPPGLTAIVGPNGSGKSNIIDAIrwVLGE-QSAKSL-RGEKMSDVIFAGSETrkpanfAEVTLTFDNSD 86
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
791-982 |
5.24e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 791 EYDRLKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAE------ERRALEGINKKLTALDTEAGEVESKMRS 864
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEleklekEVKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 865 LDLHYEEnTRRFQKTLQLERKMLGEKETVLSELEKARTEAEKLGEFIA-TTQTEEKIREAISRYKSKIKQVEELNYNPEE 943
Cdd:PRK03918 257 LEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 7301120 944 LERGLAELRDELELQSRHLAVVDSVVKKLRMAYHQRAQL 982
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
200-567 |
5.40e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 200 SSTYDLQDARGKSVSKKVSDIRRMLLcfgiNVENPIFVLNQEAAREFLKELEPASNYKLLMKATQLDVCTSSLTE--CHA 277
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQ----DISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEekSNH 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 278 LRRHFTQELEQLEKKkemmIKHIAAEEEKLSilEDKEMVKENLQQCKTKLAWMAVTSYqNELNNLEHSIKLIENKKASLE 357
Cdd:PRK01156 470 IINHYNEKKSRLEEK----IREIEIEVKDID--EKIVDLKKRKEYLESEEINKSINEY-NKIESARADLEDIKIKINELK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 358 QTTSKKESTQATMNQ-KLKEFEASKNQ------------ILATQKFQDE---RLKTAKKAVQDLLLEASQVKAKIGNAER 421
Cdd:PRK01156 543 DKHDKYEEIKNRYKSlKLEDLDSKRTSwlnalavislidIETNRSRSNEikkQLNDLESRLQEIEIGFPDDKSYIDKSIR 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 422 RMREDQRSYDECEKLIGNYHAdfnrvneQREENANKIEMLKKQVVKSEEII---AQLRAEQQEIKRDITSVQERLDAVKN 498
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKI-------LIEKLRGKIDNYKKQIAEIDSIIpdlKEITSRINDIEDNLKKSRKALDDAKA 695
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7301120 499 GRIQLHKSKQNISWEIEALS-----RNKSNKLSVYGEQTIQVVHALRTQYAGSNMHRMPRGPLGQYISAPNPKY 567
Cdd:PRK01156 696 NRARLESTIEILRTRINELSdrindINETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKY 769
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
98-177 |
2.43e-06 |
|
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: 51.20 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 98 KVISMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITAL-ALGLTSSaratNRASSIQKLIKNGEVSATISITLSNS 176
Cdd:TIGR00611 2 YLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIyYLALGRS----HRTSRDKPLIRFGAEAFVIEGRVSKG 77
|
.
gi 7301120 177 G 177
Cdd:TIGR00611 78 D 78
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
716-973 |
4.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 716 KNVDDRIRQLQMEQSDLQEKEPSLEIDYMQHKKvlENTQKVISQKSTMIGQHQSRNQKAMQKIMELQNFDY------QEL 789
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgREL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 790 PEYDRlKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALeginkKLTALDTEAGEVESKMRSLDLH- 868
Cdd:PRK03918 446 TEEHR-KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI-----KLKELAEQLKELEEKLKKYNLEe 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 869 YEENTRRFQKTLQLERKMLGEKETVLSELEKA--------------RTEAEKLGEFIatTQTEEKIREAISRYKSKIKQV 934
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelkkklaelekklDELEEELAELL--KELEELGFESVEELEERLKEL 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 7301120 935 EELnYNP-----------EELERGLAELRDELELQSRHLAVVDSVVKKLR 973
Cdd:PRK03918 598 EPF-YNEylelkdaekelEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
747-973 |
4.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 747 KKVLENTQKVISQKSTMIGQHQSRNQkamqkIMELQNfdyqELPEYDRlkshladsgEKIEKCRLEREMLQEKLLSIQHR 826
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAEQ-----LKELEE----KLKKYNL---------EELEKKAEEYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 827 QTELEStEAEErraLEGINKKLTALDTEAGEVESKMRslDLHYEENTRRFQKTLQLERKmLGEKETVLS---ELEKARTE 903
Cdd:PRK03918 541 IKSLKK-ELEK---LEELKKKLAELEKKLDELEEELA--ELLKELEELGFESVEELEER-LKELEPFYNeylELKDAEKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 904 AEKLGEFIATTQTE-EKIREAISRYKSKI----KQVEEL--NYNPEE----------LERGLAELRDELELQSRHLAVVD 966
Cdd:PRK03918 614 LEREEKELKKLEEElDKAFEELAETEKRLeelrKELEELekKYSEEEyeelreeyleLSRELAGLRAELEELEKRREEIK 693
|
....*..
gi 7301120 967 SVVKKLR 973
Cdd:PRK03918 694 KTLEKLK 700
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
788-956 |
8.95e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 788 ELPEYDRLKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELEsteaEERRALEGINKKLTALDTEAGEVEsKMRSLDL 867
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKELKELKEKAEEYI-KLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 868 HYEENTRRFQKTLQLERKMLGEKETVLSELEKARTEAEKLGEFIATTQTE----EKIREAISRYKSKIKQVEEL-----N 938
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleelEERHELYEEAKAKKEELERLkkrltG 383
|
170
....*....|....*...
gi 7301120 939 YNPEELERGLAELRDELE 956
Cdd:PRK03918 384 LTPEKLEKELEELEKAKE 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
721-982 |
1.76e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 721 RIRQLQMEQSDLQEkepslEIDymQHKKVLENTQKVISQKSTMIGQHQSRNQKAMQKIMELQNFDYQELPEYDRLKSHLA 800
Cdd:COG1196 233 KLRELEAELEELEA-----ELE--ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 801 DSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKM-----------RSLDLHY 869
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaeaelaeaeEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 870 EENTRRFQKTLQLERKMLGEKETVLSEL-EKARTEAEKLGEFIATTQTEEKIREAISRYKSKIKQVEELNYNPEELERGL 948
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLeRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270
....*....|....*....|....*....|....
gi 7301120 949 AELRDELELQSRHLAVVDSVVKKLRMAYHQRAQL 982
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1029-1076 |
2.28e-05 |
|
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: 46.30 E-value: 2.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 7301120 1029 GNETSNTRSLSGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFTDEVN 1076
Cdd:cd03278 105 GKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDAN 152
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-542 |
3.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 338 ELNNLEHSIKLIENKKASLEQTTSKKESTQATMnQKLKEFEASKNQilATQKFQDERLKTAKKAVQDLLLEASQVKAKIG 417
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAAAR-ERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 418 NAERRMREDQRSYDEC---------------EKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEI 482
Cdd:COG4913 313 RLEARLDALREELDELeaqirgnggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7301120 483 KRDITS----VQERLDAVKNGRIQLHKSKQNISWEIEALSRNKSNklsvYGEQTIQVVHALRTQ 542
Cdd:COG4913 393 LEALEEeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSN----IPARLLALRDALAEA 452
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
116-240 |
5.75e-05 |
|
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: 46.10 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 116 EFGPNINFLVGNNGSGKSAVITALALGLtSSARATNRASSIQKLIKNGE----VSATISITLSNSGLRpfkADIFGPHLT 191
Cdd:cd03272 20 PFSPKHNVVVGRNGSGKSNFFAAIRFVL-SDEYTHLREEQRQALLHEGSgpsvMSAYVEIIFDNSDNR---FPIDKEEVR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 7301120 192 VVRQIRHSSSTYDLQDargKSVSKkvSDIRRMLLCFGINVENPIFVLNQ 240
Cdd:cd03272 96 LRRTIGLKKDEYFLDK---KNVTK--NDVMNLLESAGFSRSNPYYIVPQ 139
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1038-1084 |
6.51e-05 |
|
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: 44.66 E-value: 6.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 7301120 1038 LSGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFTDEVNRKFITEIL 1084
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
716-957 |
6.86e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 716 KNVDDRIRQLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKVISQKSTM--IGQHQSRNQKAMQKIMELQN--------FD 785
Cdd:COG4913 207 GDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIELLepIRELAERYAAARERLAELEYlraalrlwFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 786 YQEL----PEYDRLKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEE-RRALEGINKKLTALDTEAGEVES 860
Cdd:COG4913 287 QRRLelleAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 861 KMRSLDLHYEENTRRFQKTLQLERKMLGEKETVLSELEKARTEAEklgefiattQTEEKIREAISRYKSKIKQVEE--LN 938
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE---------AALRDLRRELRELEAEIASLERrkSN 437
|
250
....*....|....*....
gi 7301120 939 YnPEELERGLAELRDELEL 957
Cdd:COG4913 438 I-PARLLALRDALAEALGL 455
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-523 |
7.21e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 284 QELEQLEKKKEMMIKHIAAEEEKLSILEDK-EMVKENLQQCKTKLawmavTSYQNELNNLEHSIKLIENKKASLEQTTS- 361
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKyNDLKKQKEELENEL-----NLLEKEKLNIQKNIDKIKNKLLKLELLLSn 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 362 --KKESTQATMNQKLKEFEASKNQ-----ILATQKFQD--ERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDE 432
Cdd:TIGR04523 206 lkKKIQKNKSLESQISELKKQNNQlkdniEKKQQEINEktTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 433 CEKLIGNYHADFNRVNEQREEN------------ANKIEMLKKQVVKSEEIIAQLRAEQQEIKRDIT-------SVQERL 493
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDwnkelkselknqEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQREL 365
|
250 260 270
....*....|....*....|....*....|
gi 7301120 494 DAVKNGRIQLHKSKQNISWEIEALSRNKSN 523
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
115-143 |
7.32e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 45.53 E-value: 7.32e-05
10 20
....*....|....*....|....*....
gi 7301120 115 IEFGPNINFLVGNNGSGKSAVITALALGL 143
Cdd:COG3910 33 LEFHPPVTFFVGENGSGKSTLLEAIAVAA 61
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
816-956 |
9.80e-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: 45.30 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 816 LQE---KLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLHYEENTRRFQKtlqLERKMLG---- 888
Cdd:COG1579 12 LQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNvrnn 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7301120 889 -EKETVLSELEKARTEAEKLgefiattqtEEKIREAISRYKSKIKQVEELNYNPEELERGLAELRDELE 956
Cdd:COG1579 89 kEYEALQKEIESLKRRISDL---------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
728-956 |
1.19e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 728 EQSDLQEKEPSLEIDYMQHKKVLENTQKVISQKSTmigqHQSRNQKAMQKIMELQNFDYQELPEYDR-LKSHLADSGEKI 806
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA----DELKKAEELKKAEEKKKAEEAKKAEEDKnMALRKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 807 EKCRLEREML----QEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLHYEENTRRFQktlQL 882
Cdd:PTZ00121 1590 EEARIEEVMKlyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA---EE 1666
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7301120 883 ERKMLGEKEtvlsELEKARTEAEKlgefiattqtEEKIREAISRYKSKIKQVEELNYNPEELERGLAELRDELE 956
Cdd:PTZ00121 1667 AKKAEEDKK----KAEEAKKAEED----------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
349-524 |
1.61e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 349 IENKKASLEQTTSKKESTQATMNQKLKEFEASKNQILATQkfqdERLKTAKKAVQDLLLEASQVKAKIGNAERRMRE--- 425
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 426 ----------------DQRSYDE-------CEKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEI 482
Cdd:COG3883 94 alyrsggsvsyldvllGSESFSDfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 7301120 483 KRDITSVQERLDAVKNGRIQLHKSKQNISWEIEALSRNKSNK 524
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
115-519 |
1.78e-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: 45.81 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 115 IEFGPNINFLVGNNGSGKSAVITALAL---GLTSSARATNRASSIQKLIKNGEVSATISITLsnsglrpfkADIFGPHLT 191
Cdd:TIGR00606 24 IDFFSPLTILVGPNGAGKTTIIECLKYictGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQF---------RDVNGEECA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 192 VVRQIRHSSST------------YDLQDARGKSVSKKVSDI-RRMLLCFGIN--VENPIFVLNQEAAREFLKelEPASNY 256
Cdd:TIGR00606 95 VVRSMVCTQKTkktefktlegviTRYKHGEKVSLSSKCAEIdREMISHLGVSkaVLNNVIFCHQEDSNWPLS--EGKALK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 257 KLLMKATQLDVCTSSLTECHALRRHFTQELeqleKKKEMMIKHIAAEEEKLSILEDKEMVKENLQQCKTKLawmaVTSYQ 336
Cdd:TIGR00606 173 QKFDEIFSATRYIKALETLRQVRQTQGQKV----QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI----VKSYE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 337 NELNNLEHSIKLIENKKASLEQttskkestqatMNQKLKEFEASKNQIlatqkfQDERLKTAKKAVQDLLLEASQVKAKI 416
Cdd:TIGR00606 245 NELDPLKNRLKEIEHNLSKIMK-----------LDNEIKALKSRKKQM------EKDNSELELKMEKVFQGTDEQLNDLY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 417 GNAERRMREDQRSYDECEKLIGNYHADFNRVNEQREENANKIEMLKkqvVKSEEIIAQLRAEQQEIKRDITsvQERLDAV 496
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ---LQADRHQEHIRARDSLIQSLAT--RLELDGF 382
|
410 420
....*....|....*....|...
gi 7301120 497 KNGRIQLHKSKQNISWEIEALSR 519
Cdd:TIGR00606 383 ERGPFSERQIKNFHTLVIERQED 405
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
717-976 |
2.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 717 NVDDRIRQLQMEQSDLQEKEPSLEidymQHKKVLENTQKVISQKSTmigqhqsrNQKAMQKIMELQNfdyqelpEYDRLK 796
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEE--------RHELYEEAKAKKE-------ELERLK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 797 SHLADSG-----EKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINK------------------------- 846
Cdd:PRK03918 379 KRLTGLTpekleKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 847 -KLTALDTEAGEVESKMRSLdlhyEENTRRFQKTLQLERKMLGEKETV--------------LSELEKARTEAEKLGEFI 911
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKL----RKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKL 534
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7301120 912 ATTQTEEK-IREAISRYKSKIKQVEELNYNPEELERGLAELRDEL-ELQSRHLAVVDSVVKKLRMAY 976
Cdd:PRK03918 535 IKLKGEIKsLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeELGFESVEELEERLKELEPFY 601
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
393-516 |
2.07e-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: 44.15 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 393 ERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKLIGNYHADFNRVNEQREENA--NKIEMLKKQVVKSEE 470
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqKEIESLKRRISDLED 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 7301120 471 IIAQLRAEQQEIKRDITSVQERLDAVKNGRIQLHKSKQNISWEIEA 516
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
787-956 |
2.12e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 787 QELPEYDRLKSHLADSGEKIEKCRLEREMLQEKLLSIQHRQTELEStEAEERRA--------LEGINKKLTALDTEAGEV 858
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE-ERDDLLAeaglddadAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 859 ESKMRsldlhyEENTRRFQKTLQLERkMLGEKETVLSELEKARTEAEKLGEFIATTQTE-EKIREAISRYKSKIKQVEE- 936
Cdd:PRK02224 327 RDRLE------ECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESELEEAREAvEDRREEIEELEEEIEELREr 399
|
170 180
....*....|....*....|
gi 7301120 937 LNYNPEELErGLAELRDELE 956
Cdd:PRK02224 400 FGDAPVDLG-NAEDFLEELR 418
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-436 |
2.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 283 TQELEQLEKKKEMM---IKHIAAEEEKLSILEDKEMVKENLQQCKTKLAwmavtSYQNELNNLEHSIKLIENKKASLEQT 359
Cdd:COG4717 94 QEELEELEEELEELeaeLEELREELEKLEKLLQLLPLYQELEALEAELA-----ELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7301120 360 TSKKESTQATMNQKLKEFEASKNQILATQKFQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKL 436
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-517 |
2.72e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 274 ECHALRRHFTQELEQLEKKKEMMIKHIAAEEEKLSILEDKEMVKENLQQCKTKLawmavtsyQNELNNLEHSIKLIENKK 353
Cdd:pfam01576 41 EKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL--------QNEKKKMQQHIQDLEEQL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 354 ASLEQTTSKKESTQATMNQKLKEFEASknqiLATQKFQDERLKTAKKAVQDLLLEAS------QVKAK------------ 415
Cdd:pfam01576 113 DEEEAARQKLQLEKVTTEAKIKKLEED----ILLLEDQNSKLSKERKLLEERISEFTsnlaeeEEKAKslsklknkheam 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 416 IGNAERRMREDQRSYDECEKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSEEII--AQLRAEQQ------------E 481
Cdd:pfam01576 189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELqaALARLEEEtaqknnalkkirE 268
|
250 260 270
....*....|....*....|....*....|....*.
gi 7301120 482 IKRDITSVQERLDAVKNGRIQLHKSKQNISWEIEAL 517
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRDLGEELEAL 304
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
284-484 |
3.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 284 QELEQLEKKKEMMIKHIAAEEEKLSILEDK---------EMVKENLQQCKtklawmavtSYQNELNNLEHSIKLIENKKA 354
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKEleelgfesvEELEERLKELE---------PFYNEYLELKDAEKELEREEK 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 355 SLEQTTSKKESTQATMNQKLKEFEASKNQILATQK-FQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDEC 433
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 7301120 434 EklignyhadfnRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEIKR 484
Cdd:PRK03918 700 K-----------EELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-957 |
3.87e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 98 KVISMRLTNFMCHSNLF-IEFGPNINFLV--GNNGSGKSAVITALALGLTSSARATNRASSIQKLIKNG---EVSATISI 171
Cdd:TIGR00618 2 KPLRLTLKNFGSYKGTHtIDFTALGPIFLicGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAApseAAFAELEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 172 TLSNSglrpfkadIFGPHLTVVRQIRHSSSTYDLQ------DARGKSVSKKVSDIRRMLL-CFGINVEN--PIFVLNQEA 242
Cdd:TIGR00618 82 SLGTK--------IYRVHRTLRCTRSHRKTEQPEQlyleqkKGRGRILAAKKSETEEVIHdLLKLDYKTftRVVLLPQGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 243 AREFLKElEPASNYKLLMKATQLDVCTSSLTECHALRRHFTQELEQLekKKEMMIKHIAAEEEKLSILEDKEMVKENLQQ 322
Cdd:TIGR00618 154 FAQFLKA-KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELL--TLRSQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 323 CKTKLAWMAVTsyqnelnnlehsikliENKKASLEQTTSKKESTQATMNQKLKEFEASKNQILATQKFQDERLKTAKKAv 402
Cdd:TIGR00618 231 LREALQQTQQS----------------HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 403 qDLLLEASQVKAKIGNAERRMREDQRSYDECEKLIGNYHAdfnrVNEQREENANKIEMLkkQVVKSEEIIAQLRAEQQEI 482
Cdd:TIGR00618 294 -PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA----HVKQQSSIEEQRRLL--QTLHSQEIHIRDAHEVATS 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 483 KRDITSVQERLdavkngRIQLHKSKQNISWEIEALSRNKSNKLSVYGEQ-TIQVVHALRTQYAGSNMHRMPRGPLGQYIS 561
Cdd:TIGR00618 367 IREISCQQHTL------TQHIHTLQQQKTTLTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 562 ApnpKYRDLIENQLmHCLRSFIVGSDRERQSLRALlqnKFQGGNMPTIITSpfTDRVYDVSRNKVQPTTPNTTVLidEIS 641
Cdd:TIGR00618 441 E---LCAAAITCTA-QCEKLEKIHLQESAQSLKER---EQQLQTKEQIHLQ--ETRKKAVVLARLLELQEEPCPL--CGS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 642 CDDPVVMNYLIDILRIETVLVTESKEIAEFLTSDTENVPPNLTRVLvpnlgleyipsPNYAVYSTRITPARYIQKNVDDR 721
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER-----------KQRASLKEQMQEIQQSFSILTQC 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 722 IRQLQMEQSDLQEKEPSLEiDYMQHKKVLENTQKVISQKSTMIGQHQSRNQkamQKIMELQNFD---YQELPEYDRLKSH 798
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQ-DLTEKLSEAEDMLACEQHALLRKLQPEQDLQ---DVRLHLQQCSqelALKLTALHALQLT 654
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 799 LADSGEKiEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTaldteagevesKMRSLDLHYEENTRRFQK 878
Cdd:TIGR00618 655 LTQERVR-EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT-----------LLRELETHIEEYDREFNE 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 879 TLQ----LERKMLGEKET---VLSELEKARTEAEKLGEFI---------ATTQTEEKIREAISRYKSKIKQVEELNYNPE 942
Cdd:TIGR00618 723 IENasssLGSDLAAREDAlnqSLKELMHQARTVLKARTEAhfnnneevtAALQTGAELSHLAAEIQFFNRLREEDTHLLK 802
|
890
....*....|....*
gi 7301120 943 ELERGLAELRDELEL 957
Cdd:TIGR00618 803 TLEAEIGQEIPSDED 817
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
720-984 |
4.14e-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: 44.72 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 720 DRIRQLQMEQSdlqekepsLEIDYMQHKKVLENTQKVISQKSTMIGQHQSRNQKA--MQKIMELQNFDYQELPEYDRLKS 797
Cdd:pfam15921 267 DRIEQLISEHE--------VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmyMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 798 HLADSGEKIEK-----------CRLEREMLQ----------EKLLSIQHRQTELESTEAEErralegiNKKLTALDT-EA 855
Cdd:pfam15921 339 MYEDKIEELEKqlvlanselteARTERDQFSqesgnlddqlQKLLADLHKREKELSLEKEQ-------NKRLWDRDTgNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 856 GEVESKMRSLDLHYEEnTRRFQKTLQ-LERKMLGEKETVLSELEKARTEAEKLGEFIATTQ-TEEKIREAISRYKSKIKQ 933
Cdd:pfam15921 412 ITIDHLRRELDDRNME-VQRLEALLKaMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEsTKEMLRKVVEELTAKKMT 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 7301120 934 VeelnynpEELERGLAELRDELELQSRHLAVVDSVVKKLRMAYHQRAQLFQ 984
Cdd:pfam15921 491 L-------ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
826-959 |
4.88e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 826 RQTELESTEAE-ERRALEGINKKLTALDTEAGEVESKMRsldlHYEENTRRFQKTLQLERKMLGEKETVLSELEKARTEA 904
Cdd:PRK02224 185 QRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIE----RYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 7301120 905 EKLGEFIATTQTEekiREAISRykskikQVEELNYNPEELERGLAELRDELELQS 959
Cdd:PRK02224 261 EDLRETIAETERE---REELAE------EVRDLRERLEELEEERDDLLAEAGLDD 306
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
101-174 |
5.05e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.77 E-value: 5.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7301120 101 SMRLTNFMCHSNLFIEFGPnINFLVGNNGSGKSAVITALALgLTSSAR-----ATNRASSIQKLIKNGEVSATISITLS 174
Cdd:COG4637 4 RIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRF-LSDAARgglqdALARRGGLEELLWRGPRTITEPIRLE 80
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
717-956 |
5.44e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 717 NVDDRIRQLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKVISQ-KSTMIGQ------HQSRNQKAMQKIMELQNFDYQEL 789
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgKCPECGQpvegspHVETIEEDRERVEELEAELEDLE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 790 PEYDRLKSHLaDSGEKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLHY 869
Cdd:PRK02224 489 EEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 870 EEntrrfqktlqlERKMLGEKETVLSELEKARTEAEKLGEFIATTqteEKIREAISRYKSKIKQVEELnyNPEELERgLA 949
Cdd:PRK02224 568 EE-----------AREEVAELNSKLAELKERIESLERIRTLLAAI---ADAEDEIERLREKREALAEL--NDERRER-LA 630
|
250
....*....|
gi 7301120 950 ELRD---ELE 956
Cdd:PRK02224 631 EKRErkrELE 640
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
816-985 |
6.52e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 816 LQEKLLSIQHRQTELESTEAEERRA---LEGINKKLTALDTEAGEVESKMRSLDLHYEENTRRFQKTLQLERKMLGEKET 892
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELeaeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 893 VLSELEKARTEAEKLGEFIAttQTEEKIREAISRYKSKIKQVEELNynpEELERGLAELRDELELQSRHLAVVDSVVKKL 972
Cdd:COG1196 307 LEERRRELEERLEELEEELA--ELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170
....*....|...
gi 7301120 973 RMAYHQRAQLFQR 985
Cdd:COG1196 382 EELAEELLEALRA 394
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
375-512 |
6.72e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 375 KEFEASKNQILAtqkFQDERLKTAKKAVQdlllEASQVKAKIGNAERRMREDQRSYDECEKLIGNYHADfnrvnEQREEN 454
Cdd:cd22656 110 EELEEAKKTIKA---LLDDLLKEAKKYQD----KAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD-----EGGAIA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 7301120 455 ANKIEMLKKQVVK-SEEIIAQLRAEQQEIKRDITSVQERLDAVKNGRIQLHKSKQNISW 512
Cdd:cd22656 178 RKEIKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDN 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
724-993 |
7.26e-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: 43.56 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 724 QLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKvisQKSTMIGQHQSRNQKAMQKIMELQNFDYQELPEYDRLKSHLADSG 803
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKK---QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 804 EKIEKCRLEREMLQEKLLSIQH------RQTELESTEAEE--------RRALEGINKKLTALDTEAGEVESKMRSLDLHY 869
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEElhqenkalKKKGSAENKQLNAYEIKVNKLELELASAKQKF 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 870 EENTRRFQKtlQLERKMLGEkETVLSELEKART---EAEKLGEFIaTTQTEEKIREAISRYKSKIKQ----VEELN---- 938
Cdd:pfam05483 653 EEIIDNYQK--EIEDKKISE-EKLLEEVEKAKAiadEAVKLQKEI-DKRCQHKIAEMVALMEKHKHQydkiIEERDselg 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 7301120 939 -YNPEELERGLAELRDELELQSRHLAVVdSVVKKLRMAYHQRAQLFQRSRHHYFTM 993
Cdd:pfam05483 729 lYKNKEQEQSSAKAALEIELSNIKAELL-SLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
302-495 |
8.81e-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: 42.22 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 302 AEEEKLSILEDkemvkenLQQCKTKLAwmavtSYQNELNNLEHSIKLIENKKASLEQTTSKKESTQATMNQKLKEFEASK 381
Cdd:COG1579 1 AMPEDLRALLD-------LQELDSELD-----RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 382 NQILATQKFQDERLKTAK--KAVQDLLLEASQVKAKIGNAERRMREdqrSYDECEKLignyHADFNRVNEQREENANKIE 459
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILE---LMERIEEL----EEELAELEAELAELEAELE 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 7301120 460 MLKKQVvksEEIIAQLRAEQQEIKRDITSVQERLDA 495
Cdd:COG1579 142 EKKAEL---DEELAELEAELEELEAEREELAAKIPP 174
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1039-1102 |
9.74e-04 |
|
ATP-binding cassette domain of eukaryotic SMC5 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: 213244 [Multi-domain] Cd Length: 213 Bit Score: 41.81 E-value: 9.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7301120 1039 SGGERSFTTVSLLKGLWSTSDHPFYFLDEYDVFTDEVNRKFITEILIGEGLEWLSRQYCFLTPQ 1102
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITPK 191
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
791-985 |
1.34e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 791 EYDRLKSHLADSGEKIekcrlerEMLQEKllSIQHRQTELESTEAEERRAL-----EGINKKLTALDTEAGEVESKMRSL 865
Cdd:COG3096 390 EVDSLKSQLADYQQAL-------DVQQTR--AIQYQQAVQALEKARALCGLpdltpENAEDYLAAFRAKEQQATEEVLEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 866 DLHY---EENTRRFQKTLQLERKMLGEKETvLSELEKARTEAEKLGEFIATTQTEEKIREAIS-------RYKSKIKQVE 935
Cdd:COG3096 461 EQKLsvaDAARRQFEKAYELVCKIAGEVER-SQAWQTARELLRRYRSQQALAQRLQQLRAQLAeleqrlrQQQNAERLLE 539
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 7301120 936 ELNY-------NPEELERGLAELRDELElqsRHLAVVDSVVKKLRMAYHQRAQLFQR 985
Cdd:COG3096 540 EFCQrigqqldAAEELEELLAELEAQLE---ELEEQAAEAVEQRSELRQQLEQLRAR 593
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
98-139 |
1.35e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.59 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 7301120 98 KVISMRLTNFMCHSNLFIEFGPNINFLVGNNGSGKSAVITAL 139
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
791-958 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 791 EYDRLKSHLADSGEKIEKCRLEREMLQEKL--LSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDlh 868
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELekLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 869 yEENTRRFQKTLQLERKMLGEKETVLSELEKARTEAEKLgefiattqtEEKIREAISRYKSKIKQVEELNYNPEELERGL 948
Cdd:COG4717 167 -ELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL---------QQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170
....*....|
gi 7301120 949 AELRDELELQ 958
Cdd:COG4717 237 EAAALEERLK 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
716-975 |
1.65e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 716 KNVDDRIRQLQMEQSdlqekepSLEIDYMQHKKVLENTQKVISQKSTMIGQHqSRNQKAMQ----KIMELQNFDYQELPE 791
Cdd:pfam15921 537 KNEGDHLRNVQTECE-------ALKLQMAEKDKVIEILRQQIENMTQLVGQH-GRTAGAMQvekaQLEKEINDRRLELQE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 792 YDRLKShladsgEKIEKCRlereMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLHYEE 871
Cdd:pfam15921 609 FKILKD------KKDAKIR----ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 872 NTRRFQ-KTLQLE---RKMLGEKETVLSELEKARTEAEKL----GEFIATTQTEEK----IREAISRYKSKIKQVEELNY 939
Cdd:pfam15921 679 LKRNFRnKSEEMEtttNKLKMQLKSAQSELEQTRNTLKSMegsdGHAMKVAMGMQKqitaKRGQIDALQSKIQFLEEAMT 758
|
250 260 270
....*....|....*....|....*....|....*.
gi 7301120 940 NPEELERGLAELRDELelqSRHLAVVdsVVKKLRMA 975
Cdd:pfam15921 759 NANKEKHFLKEEKNKL---SQELSTV--ATEKNKMA 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
789-956 |
2.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 789 LPEYDRLKSHLADSGEKIEKCRLeremLQEKLLSIQHRQTELESTEAEERRALEGINKKLTALDT--EAGEVESKMRSLD 866
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 867 LHYEENTRRFQKTLQLERkmlgEKETVLSELEKARTEAEKLGEFIaTTQTEEKIREAIsrykskiKQVEELNYNPEELER 946
Cdd:COG4717 146 ERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQL-SLATEEELQDLA-------EELEELQQRLAELEE 213
|
170
....*....|
gi 7301120 947 GLAELRDELE 956
Cdd:COG4717 214 ELEEAQEELE 223
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
101-141 |
2.74e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.11 E-value: 2.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 7301120 101 SMRLTNFMCHSNLFIEFGPnINFLVGNNGSGKSAVITALAL 141
Cdd:COG4938 3 SISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLIQALLL 42
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-515 |
2.77e-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: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 284 QELEQLEKKK---EMMIKHIAAEEEKLSI-LEDKEMVKENLQQCKTKLawmavtSYQNELNNLEhsIKLIENKKASLEQT 359
Cdd:TIGR04523 384 QEIKNLESQIndlESKIQNQEKLNQQKDEqIKKLQQEKELLEKEIERL------KETIIKNNSE--IKDLTNQDSVKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 360 TSKKESTQATMNQKLKEFEASKNQILATQKFQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKLIGN 439
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7301120 440 YHADFNRVNEQREEN--ANKIEMLKKQVVKSEEIIAQLRAEQQEIKRDITSVQERLDavkngriQLHKSKQNISWEIE 515
Cdd:TIGR04523 536 KESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-------QKEKEKKDLIKEIE 606
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
721-865 |
3.41e-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: 40.29 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 721 RIRQLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKVISQKSTMIGQHQSRNQKAMQKIMELQNFDyqelpEYDRLKShla 800
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQK--- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7301120 801 dsgeKIEKCRLEREMLQEKLLSIQHRQTELESTEAEERRALEGINKKLTA----LDTEAGEVESKMRSL 865
Cdd:COG1579 97 ----EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEEL 161
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
719-985 |
3.57e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 719 DDRIRQLQMEQSDLQEKEPSLEIDY-------------MQHKKVLENTQKVISQKSTMIGQHQSRNQKAMQKIMELQNFD 785
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 786 YQELPEYDRLKSHLADSGEKIekcrlerEMLQEKLLSIQHRQTELESTE------------AEERraLEGINKKLTALDT 853
Cdd:PRK04863 386 EAAEEEVDELKSQLADYQQAL-------DVQQTRAIQYQQAVQALERAKqlcglpdltadnAEDW--LEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 854 EAGEVESKMRSLDLHYEentrRFQKTLQLERKMLGEKE---------TVLSELEKARTEAE-------KLGEFIATTQTE 917
Cdd:PRK04863 457 ELLSLEQKLSVAQAAHS----QFEQAYQLVRKIAGEVSrseawdvarELLRRLREQRHLAEqlqqlrmRLSELEQRLRQQ 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7301120 918 EKIREAISRYKSKIKQVEElnyNPEELERGLAELRDELELQSRHLAVVDSVVKKLRmayHQRAQLFQR 985
Cdd:PRK04863 533 QRAERLLAEFCKRLGKNLD---DEDELEQLQEELEARLESLSESVSEARERRMALR---QQLEQLQAR 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
716-936 |
3.95e-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: 40.90 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 716 KNVDDRIRQLQMEQSDLQEKEPSLEIDYMQHKKVLENTQKVISQKSTMIGQHQSRNQKAMQKIMELQNfdyqelpEYDRL 795
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-------ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 796 KSHLADSGEKIEKC-RLEREML---QEKLLSIQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLHYEE 871
Cdd:COG4942 103 KEELAELLRALYRLgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7301120 872 NTRRfQKTLQLERKmlgEKETVLSELEKARTEAEKlgEFIATTQTEEKIREAISRYKSKIKQVEE 936
Cdd:COG4942 183 LEEE-RAALEALKA---ERQKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
284-534 |
4.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 284 QELEQLEKKKEMmikhiaaeEEKLSILEDKEMVK---ENLQQCKTKLAWMAVTSYQNELNNLEHSIKLIENKKASLEQTT 360
Cdd:PTZ00121 1555 EELKKAEEKKKA--------EEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 361 SKKESTQATMNQKLKEFEASKN--------QILATQKFQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDE 432
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKaeelkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 433 CEKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEIKRditsVQERLDAVKNGRIQLHKSKQNIsw 512
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK----IAHLKKEEEKKAEEIRKEKEAV-- 1780
|
250 260
....*....|....*....|..
gi 7301120 513 eIEALSRNKSNKLSVYGEQTIQ 534
Cdd:PTZ00121 1781 -IEEELDEEDEKRRMEVDKKIK 1801
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
336-527 |
4.84e-03 |
|
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: 41.19 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 336 QNELNNLEHSIKLIENKkASLEQTTSKKEST--QATMNQKLKEFEASKNQILATQKFQDERLKTAKKAVQDLLLEASQV- 412
Cdd:TIGR01612 1382 KDELDKSEKLIKKIKDD-INLEECKSKIESTldDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIe 1460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 413 ----------KAKIGNAERRMREDQRSYDECEKLIGNYHADFNRVNEQREENANKIEMLKKQV---------VKSEEIIA 473
Cdd:TIGR01612 1461 madnksqhilKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVtellnkysaLAIKNKFA 1540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7301120 474 QLRAEQQEIKRDITSVQER--LDAVKNGRIQLHKSKQNISWEIEALSRNKSNKLSV 527
Cdd:TIGR01612 1541 KTKKDSEIIIKEIKDAHKKfiLEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAI 1596
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
793-972 |
4.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 793 DRLKSHLADSGEKIEKCRLEREMLqEKLLS----IQHRQTELESTEAEERRALEGINKKLTALDTEAGEVESKMRSLDLH 868
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERL-EKFIKrtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 869 YEENTRRFQKTLQLERKMLGEKETvLSELEKARTEAEKLGEfiattQTEEKIREaISRYKSKIKQVEELNYNPEELERGL 948
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEK-IRELEERIEELKKEIE-----ELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180
....*....|....*....|....
gi 7301120 949 AELRDELELQSRHLAVVDSVVKKL 972
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKEL 333
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
283-484 |
5.44e-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: 40.52 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 283 TQELEQLEKKKEMMIKHIAAEEEKLSILE-DKEMVKENLQQCKTKLAwmavtSYQNELNNLEHSIKLIENKKASLEQTTS 361
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKkEEKALLKQLAALERRIA-----ALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 362 KKESTQATMNQKLKEF--EASKNQ-------ILATQKFQD-------------------ERLKTAKKAVQDLLLEASQVK 413
Cdd:COG4942 94 ELRAELEAQKEELAELlrALYRLGrqpplalLLSPEDFLDavrrlqylkylaparreqaEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7301120 414 AKIGNAERRMREDQRSYdecEKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEIKR 484
Cdd:COG4942 174 AELEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
332-495 |
6.00e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 332 VTSYQNELNNLEHSIKLIENKkasLEQTTSKKESTQATMNQKLKEFEASKNQILATQKFQDERLKTAKKAVQDL------ 405
Cdd:COG3883 25 LSELQAELEAAQAELDALQAE---LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 406 ------LLEA-------SQVKA--KIGNAERRMREDQRS-YDECEKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSE 469
Cdd:COG3883 102 vsyldvLLGSesfsdflDRLSAlsKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180
....*....|....*....|....*.
gi 7301120 470 EIIAQLRAEQQEIKRDITSVQERLDA 495
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
301-520 |
6.64e-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: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 301 AAEEEKLSILEDKEMVKENLQQCKTKLAwmavtSYQNELNNLEHSIKLIENKKASLEQTTSKKESTQATMNQKLKEFEAS 380
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA-----ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 381 KNQILATQKFQDERLKTAKKAVQ--------DLLLEASQVKAkignAERRMREDQRSYDECEKLIGNYHADFNRVNEQRE 452
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYrlgrqpplALLLSPEDFLD----AVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7301120 453 ENANKIEMLKkqvvkseeiiAQLRAEQQEIKRDITSVQERLDAVKngriQLHKSKQNISWEIEALSRN 520
Cdd:COG4942 168 ELEAERAELE----------ALLAELEEERAALEALKAERQKLLA----RLEKELAELAAELAELQQE 221
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
708-956 |
6.88e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 708 ITPARYIqknvDDRIRQLQmEQSDLQEKEPSLEIDYMQHKKVLENTQKViSQKSTMIGQHQSRNQKAMQKIMELQNFDYQ 787
Cdd:PRK05771 12 VTLKSYK----DEVLEALH-ELGVVHIEDLKEELSNERLRKLRSLLTKL-SEALDKLRSYLPKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 788 ELpeydrlKSHLADSGEKIEKcrlEREMLQEKLLSIQHRQTELESteaeERRALEginkKLTALDTE------------- 854
Cdd:PRK05771 86 EL------IKDVEEELEKIEK---EIKELEEEISELENEIKELEQ----EIERLE----PWGNFDLDlslllgfkyvsvf 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 855 AGEVESKmrsldlHYEENTRRFQKTLQLERKMLGEKETVL-----SELEKARTEAEKLGEFIATTQTEEKIREAISRYKS 929
Cdd:PRK05771 149 VGTVPED------KLEELKLESDVENVEYISTDKGYVYVVvvvlkELSDEVEEELKKLGFERLELEEEGTPSELIREIKE 222
|
250 260
....*....|....*....|....*..
gi 7301120 930 KIKQVEELNynpEELERGLAELRDELE 956
Cdd:PRK05771 223 ELEEIEKER---ESLLEELKELAKKYL 246
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
304-502 |
8.84e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 304 EEKLSILEDKEMVKENLQQCKTKLAWMA--VTSYQNELNNL---EHSIKLIENKKASLEQTTSKKESTQATMnQKLKEFE 378
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQLKQQLAQAPakLRQAQAELEALkddNDEETRETLSTLSLRQLESRLAQTLDQL-QNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 379 ASKNQILATQKFQDERLKTAKKAVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKLIGNYHADFNR------------ 446
Cdd:PRK11281 145 AEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRkslegntqlqdl 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7301120 447 VNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEikrdiTSVQERLDAVKNGRIQ 502
Cdd:PRK11281 225 LQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSE-----KTVQEAQSQDEAARIQ 275
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
244-524 |
9.03e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 244 REFLKELEPASNYKLLMKATQLDVCTSSLTECHALRRHFTQELEQLEK--KKE---MMIKHIAAEEEKLSILED------ 312
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKamKSEcqgQMERQMAAIQGKNESLEKvsslta 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 313 -----KEMVKENLQQCKTKLawMAVTSYQNELNNLEHSIkliENKKASLEQTTSKKESTQATMNQKLKEFEASKNQILAT 387
Cdd:pfam15921 469 qlestKEMLRKVVEELTAKK--MTLESSERTVSDLTASL---QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 388 QKFQDE----RLKTAKK--AVQDLLLEASQVKAKIGNAERRMREDQRSYDECEKLIGNYHADFNRVNEQREENANKIEML 461
Cdd:pfam15921 544 RNVQTEcealKLQMAEKdkVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7301120 462 KKQVVKSE-EIIAQLRAEQQEIK--RDITsvQER---LDAVKNGRIQLHkskqNISWEIEALSRNKSNK 524
Cdd:pfam15921 624 EARVSDLElEKVKLVNAGSERLRavKDIK--QERdqlLNEVKTSRNELN----SLSEDYEVLKRNFRNK 686
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
280-494 |
9.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 280 RHFTQELEQLEKKKEMMIKHIAA------EEEKLS---ILEDKEMVKENLQQCKTklAWMAVTSYQNELNNLEHSIKLIE 350
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTynknieEQRKKNgenIARKQNKYDELVEEAKT--IKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7301120 351 NKKASLEQTTSKKESTQATMNQKLKEFEasKNQILAT--QKF--QDERLKTAKKAVQDLLLEASQVKAKIGNAERRM--- 423
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKMYE--KGGVCPTctQQIseGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdef 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7301120 424 REDQRSYDECEKLIGNYHADFNRVNEQREENANKIEMLKKQVVKSEEIIAQLRAEQQEIKRDITSVQERLD 494
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
|
|
| |
