|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-1294 |
2.35e-133 |
|
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: 442.18 E-value: 2.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 2 SAIYKLSIQGIRSF--DSNDRETIQFGKPLTLIVGSNGSGKTTIIECLKYATTGDLPPNSKGGAFVHDPKITGEKDVRAQ 79
Cdd:TIGR00606 1 AKFLKMSILGVRSFgiEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 80 VKLAFTSANALNMIVTRNIQLLTKKTTATFKTLEGqLVIVNGNGDRNTLGTRSLELDAQVPLYLGVPKAILEYVIFCHQE 159
Cdd:TIGR00606 81 IRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEG-VITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 160 DSLWPLSEPSNLKKKFDEIFQAMKFTRALDNLKGIKKDMTVDIKLLKQAVEHLKVDKDRSRVMTMNITRLQAKSEEYQAQ 239
Cdd:TIGR00606 160 DSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 240 VKEVEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLG-KEELENLLSNFSSSLTEKEE 318
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGtDEQLNDLYHNHQRTVREKER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 319 ELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSYALSGFTENLD-----DFAHSLK 393
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFserqiKNFHTLV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 394 ----ELVHKTENNLLNFTHSN----KSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLELQVDISDFTDED 465
Cdd:TIGR00606 400 ierqEDEAKTAAQLCADLQSKerlkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 466 LEGARQDLNKFseklkdwEKQGLVSSISQQIKEKNEQMLILEYEIEELQVKISRTNQQADLFAKLGLLKKSLQDRQLELg 545
Cdd:TIGR00606 480 LRKAERELSKA-------EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI- 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 546 kftqsfkMDSKSKEWGLQCGHDVDMDFKKfyiNMQKNLSTKSRQQNELDKKFMEGSLQLTNTEMD---LRKNEEFIINAT 622
Cdd:TIGR00606 552 -------RKIKSRHSDELTSLLGYFPNKK---QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNknhINNELESKEEQL 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 623 KHLQESLPEDCTIDDYTEVVAEAEASYRTALENLKIHQTTLEFNKKALE--VAKTESCCYLCTRKFDDEGFKSSILLRLQ 700
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITqlTDENQSCCPVCQRVFQTEAELQEFISDLQ 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 701 EKTdgkfnTILKESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDK-VTDMRNRNVKMREELDTVNKEL---ESMKED 776
Cdd:TIGR00606 702 SKL-----RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKeIPELRNKLQKVNRDIQRLKNDIeeqETLLGT 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 777 KDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEGKVeTVEELQNEQRNKNESLRRLRKEVGQLQDERETK 856
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDR-TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 857 SKEHSNL---LNLIREKDLKISE-----------IEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSL 922
Cdd:TIGR00606 856 QEQIQHLkskTNELKSEKLQIGTnlqrrqqfeeqLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 923 KVDLERKTHDFEKSLDENNKEFKAMvlnnerFISINQQVKGFTASVPLEYEKCVAELESAKKQlvdldhiNENMNSGITE 1002
Cdd:TIGR00606 936 NKKAQDKVNDIKEKVKNIHGYMKDI------ENKIQDGKDDYLKQKETELNTVNAQLEECEKH-------QEKINEDMRL 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1003 LAKKLNDSNREKRNLKENLDLMELRADLSSIERQIDELDIQNAEAERDRYQQESMRLRSQFERLSSENAGKLGERKQLQN 1082
Cdd:TIGR00606 1003 MRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1083 QIDSMQQQLRT-DYKDVDVKYQKQWVELQAKTFVTDDIDTYSNALDSAIMRYHKLKMEDINRIIDELWKRTYSGTDVDTI 1161
Cdd:TIGR00606 1083 EIKHFKKELREpQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYI 1162
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1162 QLRS---EEVGSGVKMKSYNYRVVMFKQDAELDMRGRCSAGQKVLASIIIRLALSETFGVNCGVIALDEPTTNLDEENIE 1238
Cdd:TIGR00606 1163 EIRSdadENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIE 1242
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 254584660 1239 SLARSLHNIIELRRHQKNFQLIVITHDEKFLNHMDASQFTDHFFKVKRDDRQKSQI 1294
Cdd:TIGR00606 1243 SLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEI 1298
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1190-1292 |
2.75e-44 |
|
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: 159.70 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1190 LDMRGRCSAGQKVLASIIIRLALSETFGVNCGVIALDEPTTNLDEENIEslaRSLHNIIELRRHQKNFQLIVITHDEKFL 1269
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|...
gi 254584660 1270 NHMdasqftDHFFKVKRDDRQKS 1292
Cdd:cd03240 187 DAA------DHIYRVEKDGRQKS 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-168 |
2.05e-39 |
|
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: 145.44 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 4 IYKLSIQGIRSFDsnDRETIQFGKPLTLIVGSNGSGKTTIIECLKYATTGDLPPNSKGGAfvHDPKITGEKDVRAQVKLA 83
Cdd:cd03240 1 IDKLSIRNIRSFH--ERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGA--HDPKLIREGEVRAQVKLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 84 FTSANALNMIVTRNIqlltkkttatfktlegqlvivngngdrntlgtrsleldaqvplylgvpkAILEYVIFCHQEDSLW 163
Cdd:cd03240 77 FENANGKKYTITRSL-------------------------------------------------AILENVIFCHQGESNW 107
|
....*
gi 254584660 164 PLSEP 168
Cdd:cd03240 108 PLLDM 112
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-196 |
2.02e-20 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 90.63 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 7 LSIQGIRSFDSndrETIQFGKPLTLIVGSNGSGKTTIIECLKYATTG---DLPPNSKGGAFVHDPKITGEKDVRAQVKLA 83
Cdd:pfam13476 1 LTIENFRSFRD---QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGktsRLKRKSGGGFVKGDIRIGLEGKGKAYVEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 84 FTSANALNMIVTRNIQLLTKKTTATFKTLEGQLVIVNgngdrntlgtrslELDAQVPLYLGVPKAILEYVIFCHQEDS-- 161
Cdd:pfam13476 78 FENNDGRYTYAIERSRELSKKKGKTKKKEILEILEID-------------ELQQFISELLKSDKIILPLLVFLGQEREee 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 254584660 162 ---LWPLSEPSNLKKKFDEIFQAMKFTRALDNLKGIKK 196
Cdd:pfam13476 145 ferKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKK 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-1114 |
2.18e-19 |
|
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: 94.74 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 186 RALDNLKgIKKDMTVDIKLLKQAVEHLKVDkdrsrVMTMNITRLQAKSEEYQAQVKEVEKQLKDITEQSDKLFKSNQDFQ 265
Cdd:TIGR02168 200 RQLKSLE-RQAEKAERYKELKAELRELELA-----LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 266 KVLSKLESLKNSQQSKLEQidrLSNSIDPIDLGKEELENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLM 345
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYA---LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 346 QRQGELSASKENHERNKSVLRELQRELQtsyalsgftENLDDFAHSLKELvhktennllnfthsnKSELNSSNNELSELN 425
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELE---------EQLETLRSKVAQL---------------ELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 426 NSLIVQTQRLDYSKMDKQKLASEIQNLELQVdisdfTDEDLEGARQDLNKFSEKLKDWEKQglVSSISQQIKEKNEQMLI 505
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKE-----LQAELEELEEELEELQEELERLEEA--LEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 506 LEYEIEELQVKIsrtnqqadlfaklgllkKSLQDRQLELGKFTQSFKMDSKSKEWgLQCGHDVDMDFkkfyinmqknLST 585
Cdd:TIGR02168 480 AERELAQLQARL-----------------DSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSEL----------ISV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 586 KSRQQNELDKkFMEGSLQ--LTNTEMDLRKNEEFIINATKHLQESLPEDCTIDDYTEVV-AEAEASYRTALENLKIHQTT 662
Cdd:TIGR02168 532 DEGYEAAIEA-ALGGRLQavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNdREILKNIEGFLGVAKDLVKF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 663 LEFNKKALEvaktesccYLCTRKFDDEGFKSSILLRLQEKTDGKFNT-----------ILKESLESEK---EYLNSLRNL 728
Cdd:TIGR02168 611 DPKLRKALS--------YLLGGVLVVDDLDNALELAKKLRPGYRIVTldgdlvrpggvITGGSAKTNSsilERRREIEEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 729 EKDV----ISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESD 804
Cdd:TIGR02168 683 EEKIeeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 805 IKSITDELAIYRS----SEGKVETVEELQNEQRNKNESLRR----LRKEVGQLQDERETKSkehsnllnlirekdlkise 876
Cdd:TIGR02168 763 IEELEERLEEAEEelaeAEAEIEELEAQIEQLKEELKALREaldeLRAELTLLNEEAANLR------------------- 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 877 ieksiSMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEKSLDENNKEFKAMVLNNERFIS 956
Cdd:TIGR02168 824 -----ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 957 INQQVKgftasvplEYEKCV----AELESAKKQLVDLDHINENMNSGITELAKKLNDSNR------EKRNLKENLDLMEL 1026
Cdd:TIGR02168 899 LSEELR--------ELESKRselrRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleeaEALENKIEDDEEEA 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1027 RADLSSIERQIDELDIQNAEAErDRYQQESMR---LRSQFERLSSenagklgERKQLQNQIDSMQQQLRTDYKDVDVKYQ 1103
Cdd:TIGR02168 971 RRRLKRLENKIKELGPVNLAAI-EEYEELKERydfLTAQKEDLTE-------AKETLEEAIEEIDREARERFKDTFDQVN 1042
|
970
....*....|.
gi 254584660 1104 KQWVELQAKTF 1114
Cdd:TIGR02168 1043 ENFQRVFPKLF 1053
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
582-1266 |
8.66e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 582 NLSTKSRQQNELDKKFMEGSLQLTNTEMDLRKNEEFIINATKHLQESLPEdctIDDYTEVVAEAEASYRTALENLKIHQT 661
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE---IEELEEKVKELKELKEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 662 TLEFNKKALEVAKTESccylctrkfDDEGFKSSILLRLQEKTDGKfnTILKESLESEKEYLNSLRNLEKDVISLNDSRSr 741
Cdd:PRK03918 302 YEEYLDELREIEKRLS---------RLEEEINGIEERIKELEEKE--ERLEELKKKLKELEKRLEELEERHELYEEAKA- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 742 itglsdKVTDMRNRNVKMR-EELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSItdelaiyRSSEG 820
Cdd:PRK03918 370 ------KKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-------KKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 821 KVETVEELQNEQrNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISMR------KNLESDLdnK 894
Cdd:PRK03918 437 KCPVCGRELTEE-HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelaeqlKELEEKL--K 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 895 KNQLKVLEETVKKLEGdVKEGSRKVN----SLKVDLERKtHDFEKSLDENNKEFKAMvlnNERFISINQQVKGFTASVPL 970
Cdd:PRK03918 514 KYNLEELEKKAEEYEK-LKEKLIKLKgeikSLKKELEKL-EELKKKLAELEKKLDEL---EEELAELLKELEELGFESVE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 971 EYEKCVAELESAKKQLVDLDHINENMNSgitelakklndsnREKRNLKENLDLMELRADLSSIERQIDELDIQNAEAERD 1050
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELER-------------EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1051 RYQQESMRLRSQFERLSSENAGKLGERKQLQNQIDSMQQQLRTDYKDVD-VKYQKQWVEL--QAKTFVTD---DIDTYSN 1124
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEeREKAKKELEKleKALERVEElreKVKKYKA 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1125 ALDSAIMRyhklKMEDI-NRIIDELWKRTYSGtdvdtIQLRSEEvgsgvkmksYNYRVVMFKQDAELDMrGRCSAGQKVL 1203
Cdd:PRK03918 736 LLKERALS----KVGEIaSEIFEELTEGKYSG-----VRVKAEE---------NKVKLFVVYQGKERPL-TFLSGGERIA 796
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254584660 1204 ASIIIRLALSETFGVNCGVIALDEPTTNLDEENieslARSLHNIIElRRHQKNFQLIVITHDE 1266
Cdd:PRK03918 797 LGLAFRLALSLYLAGNIPLLILDEPTPFLDEER----RRKLVDIME-RYLRKIPQVIIVSHDE 854
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
232-1092 |
1.42e-14 |
|
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: 79.34 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 232 KSEEYQAQVKEVEKQLKDITEQSDKLFKSnQDFQKVLSKLES--LKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNF 309
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 310 SSSLTEKEEELRSMEKSLRE-SKAKAAGIQNKCNSLmqrQGELSASKENHERNKSVLRELQRELQTSYA-LSGFTENLDD 387
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGEL---EAEIASLERSIAEKERELEDAEERLAKLEAeIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 388 FAHSLKELVHKTENnLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLELQVDISDFTDEDLE 467
Cdd:TIGR02169 341 LEREIEEERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 468 GARQDLNkfsEKLKDwekqglvssISQQIKEKNEQMLILEYEIEELQVKISRTNqqadlfAKLGLLKKSLQDRQLELGKf 547
Cdd:TIGR02169 420 EELADLN---AAIAG---------IEAKINELEEEKEDKALEIKKQEWKLEQLA------ADLSKYEQELYDLKEEYDR- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 548 tqsfkmdskskewglqcghdvdmdfkkfyinMQKNLSTKSRQQNELDKK---FMEGSLQLTNTEMDLRKNEEFIINATKH 624
Cdd:TIGR02169 481 -------------------------------VEKELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 625 LQESLPEDCTI------DDYTEVVAEAEASYRTALENLKIHQ----TTLEFNK-----KALEVAKTESCCYLCTRKFD-D 688
Cdd:TIGR02169 530 LGSVGERYATAievaagNRLNNVVVEDDAVAKEAIELLKRRKagraTFLPLNKmrderRDLSILSEDGVIGFAVDLVEfD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 689 EGFKSSILLRLQEktdgkfnTILKESLESEKEYLNSLR--NLEKDVIslnDSRSRITGLSDKVTDMRNRNVKMREELDTV 766
Cdd:TIGR02169 610 PKYEPAFKYVFGD-------TLVVEDIEAARRLMGKYRmvTLEGELF---EKSGAMTGGSRAPRGGILFSRSEPAELQRL 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 767 NKELESMKEDKDHAEKEVRplvenivRLRKASNELESDIKSITdelaiyRSSEGKVETVEELQNEQRNKNESLRRLRKEV 846
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELR-------RIENRLDELSQELSDAS------RKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 847 GQLQDERETKSKEHSNLLNLIREKDLKISEIEKSIS--MRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKV 924
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 925 DLErKTHDFEKSLDENNKEFKAMVLNNERFISINQQVKGFTASVPLEYEKCVAELEsakKQLVDLDHINENMNSGITELA 1004
Cdd:TIGR02169 827 EKE-YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE---SRLGDLKKERDELEAQLRELE 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1005 KKLNDSNREKRNLKENLDLMELRA-----DLSSIERQIDE--------LDIQNAEAERDRYQQESMRLRS-------QFE 1064
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLealeeELSEIEDPKGEdeeipeeeLSLEDVQAELQRVEEEIRALEPvnmlaiqEYE 982
|
890 900 910
....*....|....*....|....*....|....*
gi 254584660 1065 R-------LSSENAGKLGERKQLQNQIDSMQQQLR 1092
Cdd:TIGR02169 983 EvlkrldeLKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-1097 |
1.74e-14 |
|
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: 78.95 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 351 LSASKENHERNKSVLRELQRELQT---------------------SYALSG-----FTENLDDFAHSLKELVH--KTENN 402
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSlerqaekaerykelkaelrelELALLVlrleeLREELEELQEELKEAEEelEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 403 LLNFTHSNKSELNSsnnELSELNNSLIVQTQRLDYSKMDKQKLASEIQ----NLELQVDISDFTDEDLEGARQDLNKFSE 478
Cdd:TIGR02168 261 ELQELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 479 KLKDWEK-----QGLVSSISQQIKEKNEQMLILEYEIEELQVKI--------SRTNQQADLFAKLGLLKKSLQDRQLELG 545
Cdd:TIGR02168 338 ELAELEEkleelKEELESLEAELEELEAELEELESRLEELEEQLetlrskvaQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 546 KFTQSFKMDSKSKEwgLQCGHDVDMDFKKFYINMQKNLSTKSRQQNELDKKfmEGSLQLTNTEMDLRKNEEFIINATKHL 625
Cdd:TIGR02168 418 RLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEEL--REELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 626 QESLPEDctIDDYTEVVAEAEASYRTALENLKIHQTTLEFNKK---ALEVAKTESCCYLCTRKFDD-----------EGF 691
Cdd:TIGR02168 494 LERLQEN--LEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaAIEAALGGRLQAVVVENLNAakkaiaflkqnELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 692 KSSILLrLQEKTDGKFNTILKESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDMRNRN---VKMREELDTVNK 768
Cdd:TIGR02168 572 RVTFLP-LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALelaKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 769 ELESMK---------EDKDHAEKEVRplvENIVRLRKASNELESDIKSITDELAIYRSS--------EGKVETVEELQNE 831
Cdd:TIGR02168 651 DGDLVRpggvitggsAKTNSSILERR---REIEELEEKIEELEEKIAELEKALAELRKEleeleeelEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 832 QRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISM----RKNLESDLDNKKNQLKVLEETVKK 907
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEaeaeIEELEAQIEQLKEELKALREALDE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 908 LEGDVKEGSRKVNSLKV---DLERKTHDFEKSLDENNKEFKAMvlnNERFISINQQVKGFTASVpleyEKCVAELESAKK 984
Cdd:TIGR02168 808 LRAELTLLNEEAANLRErleSLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELI----EELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 985 QLVDLDHINENMNSGITELAKKLNDSNREKRNLKENLDlmELRADLSSIERQIDELDiqnaeaerdryqqesMRLRSQFE 1064
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQLELRLEGLE---------------VRIDNLQE 943
|
810 820 830
....*....|....*....|....*....|...
gi 254584660 1065 RLSSENAGKLGERKQLQNQIDSMQQQLRTDYKD 1097
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
706-1275 |
4.16e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 67.62 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 706 KFNTILKESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDM----------RNRNVKMREELDTVNKELESMKE 775
Cdd:PRK01156 281 RHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIikklsvlqkdYNDYIKKKSRYDDLNNQILELEG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 776 DkdhaEKEVRPLVENIVRLRKASNELESDIKSITDElaIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQD---- 851
Cdd:PRK01156 361 Y----EMDYNSYLKSIESLKKKIEEYSKNIERMSAF--ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQrira 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 852 --ERETKSKEHSNLLN-------------------LIREKDLKISEIEKSISMRKNLESDLDNKKNQLKVLEETVKKleG 910
Cdd:PRK01156 435 lrENLDELSRNMEMLNgqsvcpvcgttlgeeksnhIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--E 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 911 DVKEGSRKVNSLKvDLERKTHDFEKSLDE-NNKEFKAMVLNNErfisINQqvkgftasvpLEYEKCVAELESAKKQLVDL 989
Cdd:PRK01156 513 EINKSINEYNKIE-SARADLEDIKIKINElKDKHDKYEEIKNR----YKS----------LKLEDLDSKRTSWLNALAVI 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 990 DHIN-ENMNSGITELAKKLNDSNREKRNLKENLDLMELRAD--LSSIERQIDELDIQNAEAERDRYQQEsmRLRSQFERL 1066
Cdd:PRK01156 578 SLIDiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksIREIENEANNLNNKYNEIQENKILIE--KLRGKIDNY 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1067 SSENAGKlGERKQLQNQIDSMQQQLRTDYKDVDVKYQKQWVELQAKTFVTDDIDTYSNALDSAIMRYHKL--KMEDINRI 1144
Cdd:PRK01156 656 KKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETleSMKKIKKA 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1145 IDELwKRTYSGTDVDTIQLRSEEVGSGV---KMKSYNYRVVMFKQDAELD-------MRG-------RCSAGQKVLASII 1207
Cdd:PRK01156 735 IGDL-KRLREAFDKSGVPAMIRKSASQAmtsLTRKYLFEFNLDFDDIDVDqdfnitvSRGgmvegidSLSGGEKTAVAFA 813
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1208 IRLALSETFGVNCGVIALDEPTTNLDEENIESLArslhNIIE--LRRHQKNFQLIVITHDEKFLNHMDAS 1275
Cdd:PRK01156 814 LRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLK----DIIEysLKDSSDIPQVIMISHHRELLSVADVA 879
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
658-710 |
2.27e-10 |
|
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. The Rad50 coiled-coil region contains a dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn ion. This alignment includes the zinc hook motif and a short stretch of coiled-coil on either side.
Pssm-ID: 427940 [Multi-domain] Cd Length: 52 Bit Score: 57.20 E-value: 2.27e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 254584660 658 IHQTTLEFNKKALEVAKTESCCYLCTRKFDDEGfKSSILLRLQEKTDGKFNTI 710
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEGCCPLCGRPLDEEH-RSELIKELQSKLERLPEEL 52
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
706-1093 |
3.58e-10 |
|
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: 64.66 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 706 KFNTILKESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVR 785
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 786 PLVENIVRLRKASNELESDIKSITDELaiyrssEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLN 865
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEI------KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 866 LIREKDLKISEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEKSLDENNKEFK 945
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 946 AMVLNNERFISINQQVKGFTASVP-LEYEKCVAELESAKKQLVDLDHINENMNSGITELAKKLNDSNREKRNLKEnlDLM 1024
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK--ELT 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254584660 1025 ELRADLSSIERQIDE--LDIQNAEAERDRYQQESMRLRSQFERLSSENAGKLGERKQLQNQIDSMQQQLRT 1093
Cdd:TIGR04523 353 NSESENSEKQRELEEkqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1192-1286 |
5.60e-10 |
|
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: 59.30 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1192 MRGRCSAGQKVLASIIIRLALSETfgVNCGVIALDEPTTNLDEENIESLARSLhniieLRRHQKNFQLIVITHDEKFLNh 1271
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASL--KPRPLYILDEIDRGLDPRDGQALAEAI-----LEHLVKGAQVIVITHLPELAE- 145
|
90
....*....|....*
gi 254584660 1272 mdasqFTDHFFKVKR 1286
Cdd:cd03227 146 -----LADKLIHIKK 155
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
774-1104 |
5.61e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 774 KEDKDHAEKEVRPLVENIVRLRKASNELESDIKSItdelaiYRSSEgKVETVEELQNEQRNKNESL-----RRLRKEVGQ 848
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSL------ERQAE-KAERYKELKAELRELELALlvlrlEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 849 LQDERETKSKEHSNLLNLIREKDLKISEIEKSISmrkNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLER 928
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 929 KTHDFEKSLDENNKEFKAMVLNNERFISINQQVKGFtasvpleyekcVAELESAKKQLvdldhinENMNSGITELAKKLN 1008
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESL-----------EAELEELEAEL-------EELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1009 DSNREKRNLKENLDLmeLRADLSSIERQIDELdiqnaEAERDRYQQE-----SMRLRSQFERLSSENAGKLGERKQLQNQ 1083
Cdd:TIGR02168 383 TLRSKVAQLELQIAS--LNNEIERLEARLERL-----EDRRERLQQEieellKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340
....*....|....*....|.
gi 254584660 1084 IDSMQQQLRTDYKDVDVKYQK 1104
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQA 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
712-1287 |
8.23e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 712 KESLESEKEYLNslRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENI 791
Cdd:PRK02224 316 REELEDRDEELR--DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 792 VRLRKASN-------ELESDIKSITDELAIYRSSEGKVETVEELQNEQRNKNESLRRL---------------------- 842
Cdd:PRK02224 394 EELRERFGdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetieed 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 843 RKEVGQLQDERETKSKEHSNLLNLI-REKDLKISE--IEKSISMRKNLESDLDNKKNQLKVLEETVKKL---------EG 910
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLeRAEDLVEAEdrIERLEERREDLEELIAERRETIEEKRERAEELreraaeleaEA 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 911 DVK-EGSRKVNSLKVDLERKTHDFEKSLDENNKEFKAmvLNNerfisinqqvkgfTASVPLEYEKCVAELESAKKQLVDL 989
Cdd:PRK02224 554 EEKrEAAAEAEEEAEEAREEVAELNSKLAELKERIES--LER-------------IRTLLAAIADAEDEIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 990 DHINEnmnsgitELAKKLNDSNREKRNLKENLD---LMELRADLSSIERQIDELD--IQNAEAERDRYQQESMRLRSQFE 1064
Cdd:PRK02224 619 AELND-------ERRERLAEKRERKRELEAEFDearIEEAREDKERAEEYLEQVEekLDELREERDDLQAEIGAVENELE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1065 RLSSENAgklgERKQLQNQidsmQQQLRTDYKDVDvkyqkqwvELQAktfvtddidTYSNAldSAIMRyhKLKMEDINRI 1144
Cdd:PRK02224 692 ELEELRE----RREALENR----VEALEALYDEAE--------ELES---------MYGDL--RAELR--QRNVETLERM 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1145 IDELWKRTYSGTDVDTIQLRSEevgsgvkmksynYRVVMFKQDAELDMRGRCSAGQKVLASIIIRLA----LSETFGVNC 1220
Cdd:PRK02224 743 LNETFDLVYQNDAYSHIELDGE------------YELTVYQKDGEPLEPEQLSGGERALFNLSLRCAiyrlLAEGIEGDA 810
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254584660 1221 GV--IALDEPTTNLDEENIESLARslhnIIELRRHQKNFQLIVITHDEKFLnhmDASqftDHFFKVKRD 1287
Cdd:PRK02224 811 PLppLILDEPTVFLDSGHVSQLVD----LVESMRRLGVEQIVVVSHDDELV---GAA---DDLVRVEKD 869
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
696-1067 |
1.68e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 696 LLRLQEKTDGKfnTILKESLESEKEYLNSLRNLEKDVIS-----LNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKEL 770
Cdd:TIGR02169 676 LQRLRERLEGL--KRELSSLQSELRRIENRLDELSQELSdasrkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 771 ESMKEDKDHAEKEVRPLVENIVRLRKASNELE-----SDIKSITDELaiyrssegkvetvEELQNEQRNKNESLRRLRKE 845
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAEL-------------SKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 846 VGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISMRK----NLESDLDNKKNQLKVLEETVKKLEGDV-------KE 914
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkeELEEELEELEAALRDLESRLGDLKKERdeleaqlRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 915 GSRKVNSLKVDLERKthdfeKSLDENNKEFKAMVLNNERFISINQQVKGFTASVPLEYEKCVAELESAKKQLVDLDHINE 994
Cdd:TIGR02169 901 LERKIEELEAQIEKK-----RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254584660 995 NMNSGITELAKKLNDsnrekrnLKENldLMELRADLSSIERQIDELDIQNAEAERDRYQQESMRLRSQFERLS 1067
Cdd:TIGR02169 976 LAIQEYEEVLKRLDE-------LKEK--RAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS 1039
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-85 |
2.66e-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: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 4 IYKLSIQGIRSFdsNDRETIQFGKPLTLIVGSNGSGKTTIIECLKYATTGDLPPNSKGGA-FVHDPkitgekDVRAQVKL 82
Cdd:COG0419 2 LLRLRLENFRSY--RDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSdLINVG------SEEASVEL 73
|
...
gi 254584660 83 AFT 85
Cdd:COG0419 74 EFE 76
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-948 |
2.97e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 342 NSLMQRQGELSASKENHERNKSVLRELQR--ELQTSYA-LSGFTENLDDFAHSLKELVHKTEnNLLNFTHSNKSELNSSN 418
Cdd:PRK03918 128 NAIYIRQGEIDAILESDESREKVVRQILGldDYENAYKnLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEKELEEVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 419 NELSELNNSLIvqtqrldyskmdkqKLASEIQNLELQVdisdftdEDLEGARQDLNKFSEKLKDWEKQglVSSISQQIKE 498
Cdd:PRK03918 207 REINEISSELP--------------ELREELEKLEKEV-------KELEELKEEIEELEKELESLEGS--KRKLEEKIRE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 499 KNEQMLILEYEIEELQVKISRTNQ---QADLFAKLGLLKKSLQDRQLELGKFTQSFKMDSKSKEWGLqcghdvdmdfkkf 575
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI------------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 576 yinmqKNLSTKSRQQNELDKKFMEGSLQLTNTEMDLRKNEEfiINATKHLQESLPEDCTIDDYTEVVAEAEASYRTALE- 654
Cdd:PRK03918 331 -----KELEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEi 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 655 ------------NLKIHQTTLEFNKKALEVAKTEscCYLCTRKFDDEGFKssillRLQEKTDGKFNTILKESLESEKEyL 722
Cdd:PRK03918 404 eeeiskitarigELKKEIKELKKAIEELKKAKGK--CPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEK-E 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 723 NSLRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMR----EELDTVNKELESMKEDKDHAEKEVRPLVENIVR---LR 795
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 796 KASNELESDIKSITDELA--IYRSSEGKVETVEELQ-------------NEQRNKNESLRRLRKEVGQLQDERETKSKEH 860
Cdd:PRK03918 556 KKLAELEKKLDELEEELAelLKELEELGFESVEELEerlkelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 861 SNLLNLIREKDLKISEIEKSISMR--KNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLE------RKTHD 932
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEerekakKELEK 715
|
650 660
....*....|....*....|..
gi 254584660 933 FEKSLD------ENNKEFKAMV 948
Cdd:PRK03918 716 LEKALErveelrEKVKKYKALL 737
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
234-1062 |
4.18e-09 |
|
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: 61.29 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 234 EEYQAQVKEVEKQLKDITEQSDK----LFKSNQDFQKVLSKLESLKNS--------QQSKLEQIDRLSNSIDPIDLGKEE 301
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAmadirrreSQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 302 LENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASkenHERN-KSVLRELQRELQTSYA-LS 379
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM---HFRSlGSAISKILRELDTEISyLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 380 GFTENLDDFAHSLK-ELVHKTEnnLLNFTHSNKSELNSSNNElselnnsliVQTQRLDYSKMDKQKLASEIQNlelQVDI 458
Cdd:pfam15921 238 GRIFPVEDQLEALKsESQNKIE--LLLQQHQDRIEQLISEHE---------VEITGLTEKASSARSQANSIQS---QLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 459 SDftdedlEGARQDLNKFSEKLKDWEkqglvSSISQQIKEKNEQMLILEYEIEELQVKISRTNQ-------QADLFAK-L 530
Cdd:pfam15921 304 IQ------EQARNQNSMYMRQLSDLE-----STVSQLRSELREAKRMYEDKIEELEKQLVLANSelteartERDQFSQeS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 531 GLLKKSLQDRQLELGKFTQSFKMDSKSKE--WGLQCGHDVDMDFKKFYI---NMQKNL------STKSRQQNELDKKFme 599
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELddrNMEVQRleallkAMKSECQGQMERQM-- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 600 GSLQLTNTEMDLRKNEEFIINATKHLQESLPEDCTIDDYTevvaeAEASYRTALEnlkiHQTTLEFNKKALEVAKTEScc 679
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT-----LESSERTVSD----LTASLQEKERAIEATNAEI-- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 680 ylctrkfddEGFKSSILLRLQEKTDGKFNTILKESLESEKEYLNsLRNLEKDVIsLNDSRSRITGLSDKVTD-------M 752
Cdd:pfam15921 520 ---------TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK-LQMAEKDKV-IEILRQQIENMTQLVGQhgrtagaM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 753 RNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLrkasnELEsdiksitdELAIYRSSEGKVETVEELQNEQ 832
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-----ELE--------KVKLVNAGSERLRAVKDIKQER 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 833 RNKNESLRRLRKEVGQLQDERETKSKehsNLLNLIREKDLKISEIEKSIsmrKNLESDLDNKKNQLKVLE----ETVKKL 908
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQL---KSAQSELEQTRNTLKSMEgsdgHAMKVA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 909 EGDVKEGSRKVNSLKVdLERKTHDFEKSLDENNKEFKAMvlnNERFISINQQVkgftASVPLEYEKCVAELESAKKQlvd 988
Cdd:pfam15921 730 MGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFL---KEEKNKLSQEL----STVATEKNKMAGELEVLRSQ--- 798
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254584660 989 ldhinenmnsgitelakklndsnreKRNLKENLDLMELRADLSSierqideldIQNAEAER--DRYQQESMRLRSQ 1062
Cdd:pfam15921 799 -------------------------ERRLKEKVANMEVALDKAS---------LQFAECQDiiQRQEQESVRLKLQ 840
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1197-1287 |
4.43e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 56.30 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1197 SAGQKVlasiiiRLALSETFGVNCGVIALDEPTTNLDEENIESLARSLhniielrrhqKNFQ--LIVITHDEKFLNhmda 1274
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYFLD---- 131
|
90
....*....|...
gi 254584660 1275 sQFTDHFFKVKRD 1287
Cdd:cd03221 132 -QVATKIIELEDG 143
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
720-1073 |
4.46e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 720 EYLNSLRNLEKDVIS----LNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLR 795
Cdd:PRK02224 206 ERLNGLESELAELDEeierYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 796 KASNELESDIKSITDELAIyrsSEGKVETVEELQNEQRNKNESLRRlrkevgQLQDEReTKSKEHSNLLNLIREKDLKI- 874
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGL---DDADAEAVEARREELEDRDEELRD------RLEECR-VAAQAHNEEAESLREDADDLe 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 875 SEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKThDFEKSLDENN-------KEFKAM 947
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-DFLEELREERdelrereAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 948 VLNNERFISINQQV----KGFTASVPLEYEKCVAELESAKKQLVDLDHINENMNSGITELAKKLNDSNREKRNLKENLDL 1023
Cdd:PRK02224 435 LRTARERVEEAEALleagKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERL 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 254584660 1024 MELRADLSSIerqideLDIQNAEAERDRYQQESmrLRSQFERLSSENAGK 1073
Cdd:PRK02224 515 EERREDLEEL------IAERRETIEEKRERAEE--LRERAAELEAEAEEK 556
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-559 |
1.76e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.36 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 189 DNLKGIKKDMTVDIKLLKQavEHLKVDKDRSRVMTMNITRLQAKSEEYQAQVKEVEKQLKDITEQSDklfKSNQDFQKVL 268
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQ--QHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR---NQNSMYMRQL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 269 SKLESLKNSQQSKLEQIDRLSNsiDPIdlgkEELENLLSNFSSSLTEKEEElrsMEKSLRESKAKAAGIQNKCNSLMQRQ 348
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYE--DKI----EELEKQLVLANSELTEARTE---RDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 349 GELSASKENHER-------NKSVLRELQREL--------------------------QTSYALSGFTENLDDFA------ 389
Cdd:pfam15921 391 KELSLEKEQNKRlwdrdtgNSITIDHLRRELddrnmevqrleallkamksecqgqmeRQMAAIQGKNESLEKVSsltaql 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 390 HSLKELVHKTENNLLnfthSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLASEIqNLELQvdisdftdedlegA 469
Cdd:pfam15921 471 ESTKEMLRKVVEELT----AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-DLKLQ-------------E 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 470 RQDLNKFSEKLKDweKQGLVSSISQQIKEKNEQMLILEYEIEELQVKISRTNQQAD-LFAKLGLLKKSLQDRQLELGKF- 547
Cdd:pfam15921 533 LQHLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGaMQVEKAQLEKEINDRRLELQEFk 610
|
410
....*....|..
gi 254584660 548 TQSFKMDSKSKE 559
Cdd:pfam15921 611 ILKDKKDAKIRE 622
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
761-1148 |
4.41e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 761 EELDTVNKELESMKEDKDH---AEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEGKVETVEELQNEQRnKNE 837
Cdd:COG4717 71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE-RLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 838 SLRRLRKEVGQLQDERETKSKEHSNLlnlirEKDLKISEIEKSISMRKNLES---DLDNKKNQLKVLEETVKKLEGDVKE 914
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAEL-----QEELEELLEQLSLATEEELQDlaeELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 915 GSRKVNSLKVDLERktHDFEKSLDENNKEFKAM------VLNNERFISINQQVKGFTASV-------PLEYEKCVAELES 981
Cdd:COG4717 225 LEEELEQLENELEA--AALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVlgllallFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 982 AKKQLVDLDHINENMNSGITELAKKLN-DSNREKRNLKENLDLM-ELRADLSSIERQIDELDIQNAEAERDR-YQQESMR 1058
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIeELQELLREAEELEEELQLEELEQEIAAlLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1059 LRSQFERLssenAGKLGERKQLQNQIDSMQQQLRTDYKDVdvkyqKQWVELQAKTFVTDDIDTYSNALDSAIMRYHKLKM 1138
Cdd:COG4717 383 DEEELRAA----LEQAEEYQELKEELEELEEQLEELLGEL-----EELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410
....*....|..
gi 254584660 1139 E--DINRIIDEL 1148
Cdd:COG4717 454 ElaELEAELEQL 465
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
433-1119 |
1.15e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 433 QRLDYSKMDKQKLASEIQNLElqvdisdftdEDLEGARQDLNKFSEKLKDWEKQGLVSSISQQIKEKNEQMLILEYEIEE 512
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLR----------EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 513 LQVKISRTNQQADLFAKLGLLKKSLQDRQLELGKFTQsfKMDSKSKEWGLQCGH---DVDMDFKKFYINMQKNLSTKSRQ 589
Cdd:TIGR00618 282 TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS--KMRSRAKLLMKRAAHvkqQSSIEEQRRLLQTLHSQEIHIRD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 590 QNELDKKFMEGSLQLTNTEMDLRKNEEFIINATKHLQESLPEDCTIDDYTEVVAEAEASYRTALENLKIHQTTLEFNKKA 669
Cdd:TIGR00618 360 AHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 670 LEVAKTESCC-YLCTRKFDDEGFKSSILLRLQEKTDGKFNTILKESLESEKEYLNSL-------RNLEKDVISLNDSRSR 741
Cdd:TIGR00618 440 AELCAAAITCtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQD 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 742 I---TGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYR-- 816
Cdd:TIGR00618 520 IdnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdl 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 817 ---SSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKE---HSNLLNLIREKdlkisEIEKSISMRKNLESD 890
Cdd:TIGR00618 600 tekLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalHALQLTLTQER-----VREHALSIRVLPKEL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 891 LDNKKNQLKVLEETVKKLEGDvKEGSRKVNSLkvdlerkTHDFEKSLDENNKEFKAMVLNNERFISINQQVKGFTASVPL 970
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYW-KEMLAQCQTL-------LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 971 EYEkcvaelESAKKQLVDLDHINENMNSGIT---ELAKKLNDSNREKRNLKENL--DLMELRADLSSIERQIDElDIQNA 1045
Cdd:TIGR00618 747 ELM------HQARTVLKARTEAHFNNNEEVTaalQTGAELSHLAAEIQFFNRLReeDTHLLKTLEAEIGQEIPS-DEDIL 819
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254584660 1046 EAERDRYQQEsmrlRSQFERLSSENAGKLGERKQLQNQIDSMQQQLRTDYKDvdvkyQKQWVELQAKTFVTDDI 1119
Cdd:TIGR00618 820 NLQCETLVQE----EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE-----QAKIIQLSDKLNGINQI 884
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
201-944 |
1.29e-07 |
|
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: 56.60 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 201 DIKLLKQAVEH----LKVDKDRSR----VMTMNITRLQAKSEE--YQAQVKEVEKQLKDITEQSDKLFKSNQDFQKVLSK 270
Cdd:TIGR01612 1119 DIKNLDQKIDHhikaLEEIKKKSEnyidEIKAQINDLEDVADKaiSNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 271 LESLKNSQQSkLEQIDRLSNSidpidLGKEELENLLSNFSSSLTEKEEELRSME---KSLRESKAKAAGIQNKCNSLMQR 347
Cdd:TIGR01612 1199 IAEIEKDKTS-LEEVKGINLS-----YGKNLGKLFLEKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 348 QGELSA-------------SKENHERNKSVLRELQRELqtsyaLSGFTE--NLDDFAHSLKELV-----HKTE------- 400
Cdd:TIGR01612 1273 KAEMETfnishdddkdhhiISKKHDENISDIREKSLKI-----IEDFSEesDINDIKKELQKNLldaqkHNSDinlylne 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 401 -NNLLNFTHSNK-----SELNSSNNELSELNNSLivqTQRLDYSKMDKQKLASEIQNLELQVDI-SDFTDEDLEGARQDL 473
Cdd:TIGR01612 1348 iANIYNILKLNKikkiiDEVKEYTKEIEENNKNI---KDELDKSEKLIKKIKDDINLEECKSKIeSTLDDKDIDECIKKI 1424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 474 NKFSEKLKDWEKQglVSSISQQIKEKNEQMLILEYEIE------ELQVKISRTNQQADLFAKLGLLKKSLQDRQLELGKF 547
Cdd:TIGR01612 1425 KELKNHILSEESN--IDTYFKNADENNENVLLLFKNIEmadnksQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEA 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 548 TQSFKMDSKSKEWGLQCGHDVDMDFKKFYINMQKNLSTKSRQQNEldkkfmegslQLTNTEMDLRKneEFIINATKHLQ- 626
Cdd:TIGR01612 1503 DKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSE----------IIIKEIKDAHK--KFILEAEKSEQk 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 627 --ESLPEDCTIDDYtevVAEAEASYRTALENlkihQTTLE-FNKKALEVAKTESccylctrkfddegfKSSILLRLQEKT 703
Cdd:TIGR01612 1571 ikEIKKEKFRIEDD---AAKNDKSNKAAIDI----QLSLEnFENKFLKISDIKK--------------KINDCLKETESI 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 704 DGKFNTILKESLESE-KEYLNSLRNLEKDVISLNDSRSRItglSDKvtdmrnrnvkmREELDTVNKELESMKEDKDHAEK 782
Cdd:TIGR01612 1630 EKKISSFSIDSQDTElKENGDNLNSLQEFLESLKDQKKNI---EDK-----------KKELDELDSEIEKIEIDVDQHKK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 783 EVR-PLVENIVRLRKAS-NELESDIKSITDELAIYRSSEGKVETveelqnEQRNKNESLRRLRKEVGQLQDERETKSKEH 860
Cdd:TIGR01612 1696 NYEiGIIEKIKEIAIANkEEIESIKELIEPTIENLISSFNTNDL------EGIDPNEKLEEYNTEIGDIYEEFIELYNII 1769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 861 SNLLNLIREKDLKISEIEKS-ISMRKNLESDLDNKKNQLKVLEETvkklegDVKEGSRKVNSLKVDLERKTHDFEKSLDE 939
Cdd:TIGR01612 1770 AGCLETVSKEPITYDEIKNTrINAQNEFLKIIEIEKKSKSYLDDI------EAKEFDRIINHFKKKLDHVNDKFTKEYSK 1843
|
....*
gi 254584660 940 NNKEF 944
Cdd:TIGR01612 1844 INEGF 1848
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
226-1274 |
2.48e-07 |
|
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: 55.36 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 226 ITRLQAKSEEYQAQVKE---VEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKNS-QQSKLEQIDRLSNSIDPIDLGKEE 301
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEeaaGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQeLKLKEQAKKALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 302 LENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSyalsgf 381
Cdd:pfam02463 224 EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 382 tenlddfahslKELVHKTENNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDyskmdKQKLASEIQNLELQVDISDF 461
Cdd:pfam02463 298 -----------LKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE-----KELKELEIKREAEEEEEEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 462 TDEDLEGARQDLNKFSEKLKDWEKqglvssISQQIKEKNEQMLILEYEIEELQVKISRTNQQADLFA-----KLGLLKKS 536
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESER------LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKeekkeELEILEEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 537 LQDRQLELGKFTQSFKMDSKSKEWGLQCGHDVDMDFKKFYiNMQKNLSTKSRQQNELDKKFMEGSLQLTNTEMDLRKNEE 616
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK-ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 617 FIInatkhlQESLPEDCTIDDYTEVVAEAEASYRTALENLKIHQTTLEFNKKALEVAKTESCCYLCTRKFDDEGFKSSIL 696
Cdd:pfam02463 515 LIK------DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 697 LRLQEKTDGKFNTILKESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMReeldTVNKELESMKED 776
Cdd:pfam02463 589 LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV----SLEEGLAEKSEV 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 777 KDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETK 856
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 857 SKEHSNLLNLIREKDLKISEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEKS 936
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 937 LDENNKEFKAMVLNNERFISINQQVKGFTASVPLEYEKCVAELESAKK--QLVDLDHINENMNSGITELAKKLNDSNREK 1014
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELllKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1015 RNLKENLDLMELRADLSSIERQIDELDIQNAEAERDRYQQEsmrLRSQFERLSSENAGKLGERKQLQNQIDS-MQQQLRT 1093
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA---DEKEKEENNKEEEEERNKRLLLAKEELGkVNLMAIE 981
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1094 DYKDVDVKYQKQWVELQAKTFVTDDIDTYSNALDSAIMRYHkLKMEDINRIIDELWKRTYSGTDVDTIQLRSEE--VGSG 1171
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF-LELFVSINKGWNKVFFYLELGGSAELRLEDPDdpFSGG 1060
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1172 VKMKsynyrvVMFKQDAELDMRgRCSAGQKVLASIIIRLALSEtFGVNCGVIaLDEPTTNLDEENIESLARSLHNiielr 1251
Cdd:pfam02463 1061 IEIS------ARPPGKGVKNLD-LLSGGEKTLVALALIFAIQK-YKPAPFYL-LDEIDAALDDQNVSRVANLLKE----- 1126
|
1050 1060
....*....|....*....|...
gi 254584660 1252 rHQKNFQLIVITHDEKFLNHMDA 1274
Cdd:pfam02463 1127 -LSKNAQFIVISLREEMLEKADK 1148
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1197-1271 |
3.85e-07 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 51.09 E-value: 3.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254584660 1197 SAGQKVlasiiiRLALSETFGVNCGVIALDEPTTNLDEENIESLARSLHNIielrrHQKNFQLIVITHDEKFLNH 1271
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-----AEEGRTVIIVTHDPELAEL 145
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
737-1060 |
4.81e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 737 DSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMkEDKDHAEKEVRPLVENIVRLRKASNELESdiksITDELAIYR 816
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEIDVASAEREIAE----LEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 817 SSEGKVETVEELQNEQRnknESLRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSIsmRKNLESDLDNKKN 896
Cdd:COG4913 682 ASSDDLAALEEQLEELE---AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 897 QL---KVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFeksldennkefkamvlnNERFISINQQVKGFTASVPlEYE 973
Cdd:COG4913 757 AAlgdAVERELRENLEERIDALRARLNRAEEELERAMRAF-----------------NREWPAETADLDADLESLP-EYL 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 974 KCVAELEsakkqlvdldhinenmNSGITELAKKLNDS-NREKRNLKENLdLMELRADLSSIERQIDELdiqNAEAERDRY 1052
Cdd:COG4913 819 ALLDRLE----------------EDGLPEYEERFKELlNENSIEFVADL-LSKLRRAIREIKERIDPL---NDSLKRIPF 878
|
....*...
gi 254584660 1053 QQESmRLR 1060
Cdd:COG4913 879 GPGR-YLR 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
603-1149 |
5.36e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 603 QLTNTEMDLRKNEEFIINATKHLQESLPEDCTIDDYTEVVAEAEASYRTALENLKIHQTTLEFNKKALEVAKTESCCYLC 682
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 683 TRKFDDEGFKSSILLRLQEKTDgkfntiLKESLESEKEYLNSLRN-LEKDVISLNDSRSRITGLSDKVTDMRNRNVKMRE 761
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAE------LEEKLEELKEELESLEAeLEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 762 ELDTVNKELESMKEDKDHAEKEVRPLVENI---------VRLRKASNELESDIKSITDELAIYRSSEGKVET----VEEL 828
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIeellkkleeAELKELQAELEELEEELEELQEELERLEEALEElreeLEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 829 QNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLK------ISEI-------EKSI-------------- 881
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvLSELisvdegyEAAIeaalggrlqavvve 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 882 ---SMRKNLESDLDNKKNQLKVLEETVKK------LEGDVKEGSRKVNSLKVDLERKTHDFEKSLD-------------- 938
Cdd:TIGR02168 554 nlnAAKKAIAFLKQNELGRVTFLPLDSIKgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldn 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 939 ------ENNKEFKAMVLNNERFISINQQVKGF--TASVPLEY-------EKCVAELES----AKKQLVDLDHINENMNSG 999
Cdd:TIGR02168 634 alelakKLRPGYRIVTLDGDLVRPGGVITGGSakTNSSILERrreieelEEKIEELEEkiaeLEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1000 ITELAKKLNDSNREKRNLKENLDLMELradlssiERQIDELDIQNAEAERDRYQQESMRLRSQFERLSSENAGKLGERKQ 1079
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEA-------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1080 LQNQIDSMQQQ----------LRTDYKDVDVKYQKQWVELQAKTFVTDDIDTYSNALDSAIMRyHKLKMEDINRIIDELW 1149
Cdd:TIGR02168 787 LEAQIEQLKEElkalrealdeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE-LSEDIESLAAEIEELE 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
225-928 |
5.59e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 225 NITRLQAKSEEYQAQVKEVEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELEN 304
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 305 LLSNFSSSLTEKEEELRSMEKSLRESKakaagiqnkcnSLMQRQGELSASKENHERNKSVLRELQRELqtsyalsgftEN 384
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELK-----------ELKEKAEEYIKLSEFYEEYLDELREIEKRL----------SR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 385 LDDFAHSLKELVHKTEnnllnfthSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLAseiqnlelqvdisdftde 464
Cdd:PRK03918 319 LEEEINGIEERIKELE--------EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE------------------ 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 465 dlegarqDLNKFSEKLKDWEKQGLVSSISQQIKEKNEqmliLEYEIEELQVKISRTNQQadlfaklgllKKSLQDRQLEL 544
Cdd:PRK03918 373 -------ELERLKKRLTGLTPEKLEKELEELEKAKEE----IEEEISKITARIGELKKE----------IKELKKAIEEL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 545 gkftqsfkmdSKSKEWGLQCGHDVDMDFKKFYIN-MQKNLSTKSRQQNELDKKFMEGSLQLTNTEMDLRKNEEFIinatk 623
Cdd:PRK03918 432 ----------KKAKGKCPVCGRELTEEHRKELLEeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI----- 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 624 hlqeslpedctiddytevvaeaeaSYRTALENLK-IHQTTLEFNKKALEVAKTESccylctrkfddegfkssillrlqEK 702
Cdd:PRK03918 497 ------------------------KLKELAEQLKeLEEKLKKYNLEELEKKAEEY-----------------------EK 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 703 TDGKFNTilkeslesekeylnslrnLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMK----EDKD 778
Cdd:PRK03918 530 LKEKLIK------------------LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 779 HAEKEVRPLVENIVRLRKASNELESDIKSITDElaiyrssegkVETVEELQNEQRNKNESLRRLRKEVGQL-----QDER 853
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKL----------EEELDKAFEELAETEKRLEELRKELEELekkysEEEY 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 854 ETKSKEHSNLLNLIREKDLKISEIEKSismRKNLESDLDNKKNQLKVLEETVKKLE------GDVKEGSRKVNSLKVDLE 927
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKR---REEIKKTLEKLKEELEEREKAKKELEklekalERVEELREKVKKYKALLK 738
|
.
gi 254584660 928 R 928
Cdd:PRK03918 739 E 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
711-929 |
5.80e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 711 LKESLESEKEYLNSLRN-LEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVE 789
Cdd:COG1196 237 LEAELEELEAELEELEAeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 790 NIVRLRKASNELESDIKSITDELAiyRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIRE 869
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 870 KDLKISEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERK 929
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-541 |
6.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 225 NITRLQAKSEEYQAQVKEVEKQ------LKDITEQSDKLfksnqDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLG 298
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQaekaerYRELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 299 KEELENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSYA- 377
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEe 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 378 ----LSGFTENLDDFAHSLKELVHKTENNLLNFtHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLE 453
Cdd:COG1196 342 leeeLEEAEEELEEAEAELAEAEEALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 454 LQVDISDFTDEDLEGARQDLNKFSEKLKDWEKQglvssISQQIKEKNEQMLILEYEIEELQVKISRTNQQADLFAKLGLL 533
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAE-----LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*...
gi 254584660 534 KKSLQDRQ 541
Cdd:COG1196 496 LLEAEADY 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
758-1090 |
1.26e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 758 KMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDELA--------IYRSSEGKVETVEELQ 829
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqneiekLKKENQSYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 830 NEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIreKDLKiSEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLE 909
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI--ERLK-ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 910 GDVKEGSRKVNSLKVDLERKThdfeKSLDENNKEFKAMvlnNERFISINQQVKgftasvplEYEKCVAELESAKKQLvdl 989
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQ----KELKSKEKELKKL---NEEKKELEEKVK--------DLTKKISSLKEKIEKL--- 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 990 dhinenmNSGITELAKKLNDSNREKRNLKENLDLMELRADLSSIERQIDEL--DIQNAEAERDRYQQESMRLRSQFERLS 1067
Cdd:TIGR04523 530 -------ESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELkqTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
330 340
....*....|....*....|...
gi 254584660 1068 SENAGKLGERKQLQNQIDSMQQQ 1090
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKE 625
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
711-921 |
1.43e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 711 LKESLESEKEYLNSLRNLEKDVIS-LNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVE 789
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 790 NIVRLRKASNELE----SDIKSITDELAIYRS-SEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLL 864
Cdd:COG4942 112 ALYRLGRQPPLALllspEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254584660 865 NLIREKDLKISEIEKSIsmrKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNS 921
Cdd:COG4942 192 ALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-64 |
2.20e-06 |
|
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: 48.90 E-value: 2.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 6 KLSIQGIRSFDsnDRETIQFGKP-LTLIVGSNGSGKTTIIECLKYATTGDLPPNSKGGAF 64
Cdd:cd03227 1 KIVLGRFPSYF--VPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGV 58
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
443-947 |
2.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 443 QKLASEIQNLELQVDISDFTDEDLEGARQDLNKFSEKLKDwEKQGLVS----------SISQQIKEKNEQMLILEYEIEE 512
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE-ERDDLLAeaglddadaeAVEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 513 LQVKISRTNQQADlfaklgllkkSLQDRQLELGKFTQSFKMDSKSKEWGLQcghdvdmdfkkfyiNMQKNLSTKSRQQNE 592
Cdd:PRK02224 333 CRVAAQAHNEEAE----------SLREDADDLEERAEELREEAAELESELE--------------EAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 593 LDKKFMEGSLQLTNTEMDLRKNEEFIinatkhlqESLPEDctIDDYTEVVAEAEASYRTALENLKIHQTTLEFNKkalev 672
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFL--------EELREE--RDELREREAELEATLRTARERVEEAEALLEAGK----- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 673 aktescCYLCTRKFDDegfkSSILLRLQEKTD--GKFNTIL------KESLESEKEYLNSLRNLEKDVISLNDSRSRITG 744
Cdd:PRK02224 454 ------CPECGQPVEG----SPHVETIEEDRErvEELEAELedleeeVEEVEERLERAEDLVEAEDRIERLEERREDLEE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 745 LsdkVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDElaiyRSSEGKVET 824
Cdd:PRK02224 524 L---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER----IESLERIRT 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 825 VEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSnllNLIREKDLKISE--IEKSISMRKNLESDLDNKKNQLKVLE 902
Cdd:PRK02224 597 LLAAIADAEDEIERLREKREALAELNDERRERLAEKR---ERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELR 673
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 254584660 903 ETVKKLE---GDVKEGSRKVNSLKVDLER--KTHDFEKSLDENNKEFKAM 947
Cdd:PRK02224 674 EERDDLQaeiGAVENELEELEELRERREAleNRVEALEALYDEAEELESM 723
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
342-929 |
2.69e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 342 NSLMQRQGELSA--SKENHERnKSVLRELQRelqtsyalsgfTENLDDFAHSLKELVHKTENNLLNFTHSnKSELNSSNN 419
Cdd:PRK01156 131 NSIFVGQGEMDSliSGDPAQR-KKILDEILE-----------INSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 420 ELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLELQVDISDFTDEDLEGARQDLNKFSEKLKDWEkqglvsSISQQIKEK 499
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE------SDLSMELEK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 500 NEQMLILEYEIEELQ-----VKISRTNQQADLFAKLGLLKKSLQDRQLELGKFTQSFKmdsksKEWGLQCGHDVdmdfkk 574
Cdd:PRK01156 272 NNYYKELEERHMKIIndpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK-----KLSVLQKDYND------ 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 575 fYINMQKNLSTKSRQQNELDKKFMEGSLQLTNTEMDLRKNEEFIINATKHLQE-SLPEDCTIDDYTEVVAEAEA------ 647
Cdd:PRK01156 341 -YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFiSEILKIQEIDPDAIKKELNEinvklq 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 648 SYRTALENLKIHQTTLEFNKKAL----EVAKTESCCYLCTRKFDDEGFKSSI------LLRLQEKTDGKFNTIL-----K 712
Cdd:PRK01156 420 DISSKVSSLNQRIRALRENLDELsrnmEMLNGQSVCPVCGTTLGEEKSNHIInhynekKSRLEEKIREIEIEVKdidekI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 713 ESLESEKEYLNS--LRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVN----KELESMKEDKDHAeKEVRP 786
Cdd:PRK01156 500 VDLKKRKEYLESeeINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKslklEDLDSKRTSWLNA-LAVIS 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 787 LVEnIVRLRKASNELESDIKSITDEL-----------AIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERET 855
Cdd:PRK01156 579 LID-IETNRSRSNEIKKQLNDLESRLqeieigfpddkSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKK 657
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254584660 856 KSKEHSNLLNLIREKDLKISEIEKSIsmrKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERK 929
Cdd:PRK01156 658 QIAEIDSIIPDLKEITSRINDIEDNL---KKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1196-1269 |
3.47e-06 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 49.18 E-value: 3.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254584660 1196 CSAGQKVlasiiiRLALSETFGVNCGVIALDEPTTNLDEENIESLARSlhnIIELRRHQKnfQLIVITHDEKFL 1269
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL---IRELAAQGK--AVIVITHDYEFL 189
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1191-1246 |
3.83e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 46.46 E-value: 3.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254584660 1191 DMRGRCSAGQK-VLASIIIRLALSETFGVN------CGVIALDEPTTNLDEENIESLARSLHN 1246
Cdd:pfam13558 28 RRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1092 |
3.84e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 850 QDERETKSKEHSNLLNLIREKDLKISEIEKSismRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERK 929
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 930 thdfEKSLDENNKEFKAMVLNNERFISINQQVKGFTASVPLEyekcvaelesAKKQLVDLDHINENMNSGITELAKKLND 1009
Cdd:COG4942 96 ----RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD----------AVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1010 SNREKRNLKEnldlmelradlssiERQIDELDIQNAEAERDRYQQE-------SMRLRSQFERLSSENAGKLGERKQLQN 1082
Cdd:COG4942 162 LAALRAELEA--------------ERAELEALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEA 227
|
250
....*....|
gi 254584660 1083 QIDSMQQQLR 1092
Cdd:COG4942 228 LIARLEAEAA 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1197-1269 |
4.04e-06 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 49.00 E-value: 4.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254584660 1197 SAGQKVLASIIIRLALsetfgvNCGVIALDEPTTNLDEENIESLARSLHNIielrrHQKNFQLIVITHDEKFL 1269
Cdd:cd03225 136 SGGQKQRVAIAGVLAM------DPDILLLDEPTAGLDPAGRRELLELLKKL-----KAEGKTIIIVTHDLDLL 197
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
756-1302 |
4.33e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 51.28 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 756 NVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIvrlrkaSNELESDIKSITDELAIYRSSEGKVETVEELQNE-QRN 834
Cdd:COG4694 101 NIELEEEIEELEKEIEDLKKELDKLEKELKEAKKAL------EKLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKlSAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 835 KNESLRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISmrKNLESDLDNKKNQLKvLEETVKKLEGDVKE 914
Cdd:COG4694 175 KSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAV--SSAIEELAALIQNPG-NSDWVEQGLAYHKE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 915 GSRKVNSL---KVDLERKTHdFEKSLDENNKEFKAmvlnneRFISINQQVKGFTASVP-LEYEKCVAELESAKKQLVDld 990
Cdd:COG4694 252 EEDDTCPFcqqELAAERIEA-LEAYFDDEYEKLLA------ALKDLLEELESAINALSaLLLEILRTLLPSAKEDLKA-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 991 hINENMNSGITELAKKLNdsnrEKRNLKENLDLMELRADLSSIERQIDELD--IQNAEAERDRYQQESMRLRSQFERLss 1068
Cdd:COG4694 323 -ALEALNALLETLLAALE----EKIANPSTSIDLDDQELLDELNDLIAALNalIEEHNAKIANLKAEKEEARKKLEAH-- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1069 enagklgERKQLQNQIdsmqqqlrTDYKDVDVKYQKQWVELQAKTFVTDDIDTYSNALDSAIMRYHKLKmEDINRIIDEL 1148
Cdd:COG4694 396 -------ELAELKEDL--------SRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAA-DEINEELKAL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1149 WKRTYS----GTDVDTIQLRSEEVGSGVKMKSYnyrvvmfkqdaeldmrgrcSAGQKVLASIIIRLAL--SETFGVNCGV 1222
Cdd:COG4694 460 GFDEFSleavEDGRSSYRLKRNGENDAKPAKTL-------------------SEGEKTAIALAYFLAEleGDENDLKKKI 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1223 IALDEPTTNLDEENIESLARSLhniieLRRHQKNFQLIVITHDEKFLN------HMDASQFTDHFFKVKRDDRQKSQIEW 1296
Cdd:COG4694 521 VVIDDPVSSLDSNHRFAVASLL-----KELSKKAKQVIVLTHNLYFLKelrdlaDEDNKKKNCAFYEIRKDNRGSKIIKL 595
|
....*.
gi 254584660 1297 VDINKV 1302
Cdd:COG4694 596 DLLNPY 601
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
711-1150 |
6.71e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 711 LKESLES----EKEYLNSLRNLEKDV----ISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEK 782
Cdd:pfam05483 217 LKEDHEKiqhlEEEYKKEINDKEKQVslllIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 783 EVRPLVENIVRLRKASNELESDIKSITDelAIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQD----ERETKSK 858
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATK--TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 859 EHSNLLNLIREKDLKISEIEKSISMRKNLESDLDNKKNQL----KVLEET--VKKLEGDVKEGSRKVNSLKVDLERKTHD 932
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILaedeKLLDEKkqFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 933 FE-------KSLDENNKEFKAMV--LNNERFISI------------NQQVKGFTASVPLEYEKCVAELESAKKQLVDLDH 991
Cdd:pfam05483 455 LEiqltaikTSEEHYLKEVEDLKteLEKEKLKNIeltahcdkllleNKELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 992 INENMNSGITELAKKLNDSNREkrnLKENLDLMELRADLSSIERQIDELDIQNAEAERDRYQQESMRLRSQFERLSSENA 1071
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1072 GKLGERKQLQNQIDSMQQQLRTdykdVDVKYQKQWVELQ-AKTFVTDDIDTYSNALDSAIMRYHKL--KMEDINRIIDEL 1148
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNA----YEIKVNKLELELAsAKQKFEEIIDNYQKEIEDKKISEEKLleEVEKAKAIADEA 687
|
..
gi 254584660 1149 WK 1150
Cdd:pfam05483 688 VK 689
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
4-58 |
8.59e-06 |
|
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: 49.62 E-value: 8.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 254584660 4 IYKLSIQGIRSFDsndRETIQFGKPLTLIVGSNGSGKTTIIECLKYATTGDLPPN 58
Cdd:COG3593 3 LEKIKIKNFRSIK---DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRK 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-540 |
9.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 217 DRSRVMTMNITRLQAKSEEYQAQVKEVEKQLKDITEQ-------SDKLFKSNQDFQKVLSKLES----LKNSQQSKLEQI 285
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSElrrienrLDELSQELSDASRKIGEIEKeieqLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 286 DRLSNSIDPIDLGKEELENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQnkcnsLMQRQGELSASKENHERNKSVL 365
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 366 RELQRELQTSYALSGFTE-------NLDDFAHSLKELVHKTENNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYS 438
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEkeiqelqEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 439 KMDKQKLASEIQNLELQVDISDFTDEDLEGARQDLNKFSEKLKDWEKQGLVSS--------ISQQIKEKNEQMLILE--- 507
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelsledVQAELQRVEEEIRALEpvn 974
|
330 340 350
....*....|....*....|....*....|....
gi 254584660 508 -YEIEELQVKISRTNQQADLFAKLGLLKKSLQDR 540
Cdd:TIGR02169 975 mLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-384 |
9.42e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 166 SEPSNLKKKFDEIFQAMKFTRA-LDNLKGIKKDMTVDIKLLKQAVEH----LKVDKDRSRVMTMNITRLQAKSEEYQAQV 240
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKeLAALKKEEKALLKQLAALERRIAAlarrIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 241 KEVEKQLKDI--------TEQSDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFSSS 312
Cdd:COG4942 100 EAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254584660 313 LTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSYALSGFTEN 384
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
734-945 |
1.06e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 734 SLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDEL- 812
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 813 AIYRSSEGKVETVEELQNEQRNKN---ESLRRLRKEVGQLQDERETKSkehsnlLNLIREKDL--KISEIEKSISMRK-- 885
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNkagGSIDKLRKEIERLEWRQQTEV------LSPEEEKELveKIKELEKELEKAKka 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254584660 886 -NLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLK---VDLERKTHDFEKSLDENNKEFK 945
Cdd:COG1340 156 lEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHeemIELYKEADELRKEADELHKEIV 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-367 |
1.18e-05 |
|
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: 50.07 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 170 NLKKKFDEIFQAMKFTRA-LDNLKGIKKDMTVDIKLLKQAVEHLKVDKDRSRVMTmnitrLQAKSEEYQAQVKEVEKQLK 248
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSeLKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE-----IQAELSKLEEEVSRIEARLR 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 249 DIteqsdklfksNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFSSSLTEKEEELRSMEKSLR 328
Cdd:TIGR02169 816 EI----------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190
....*....|....*....|....*....|....*....
gi 254584660 329 ESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRE 367
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
768-946 |
1.33e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 768 KELESMKEDKDHAEKEVR---PLVENIVRLRKASNELEsdiksITDELAIYRSSEGKVETVEELQNEQRNKNESLRRLRK 844
Cdd:COG4913 235 DDLERAHEALEDAREQIEllePIRELAERYAAARERLA-----ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 845 EVGQLQDERETKSKEHSNLLNLIREKDL-KISEIEKSIsmrKNLESDLDNKKNQLKVLEETVKKL-------EGDVKEGS 916
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGGdRLEQLEREI---ERLERELEERERRRARLEALLAALglplpasAEEFAALR 386
|
170 180 190
....*....|....*....|....*....|
gi 254584660 917 RKVNSLKVDLERKTHDFEKSLDENNKEFKA 946
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
800-1148 |
1.44e-05 |
|
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: 49.68 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 800 ELESDIKSITDELAIYRSSEGKVETVeelqneqrnknesLRRLRKEVGQLQDERETKSKehsnLLNLIREK-DLKISEIE 878
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLI-------------IDEKRQQLERLRREREKAER----YQALLKEKrEYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 879 KSIsmrKNLESDLDNKKNQLKVLEETVKKLEgdvkegsrkvnSLKVDLERKTHDFEKSLDENNKEFKAmvLNNERFISIN 958
Cdd:TIGR02169 230 KEK---EALERQKEAIERQLASLEEELEKLT-----------EEISELEKRLEEIEQLLEELNKKIKD--LGEEEQLRVK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 959 QQVKGFTASVpleyEKCVAELESAKKQLVDLDHIN-------ENMNSGITELAKKLNDSNREKRNLKENLDlmELRADLS 1031
Cdd:TIGR02169 294 EKIGELEAEI----ASLERSIAEKERELEDAEERLakleaeiDKLLAEIEELEREIEEERKRRDKLTEEYA--ELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1032 SIERQIDELDIQNAEA---------ERDRYQQESMRLRSQFERLSSENAGKLGERKQLQNQIDSMQQ---QLRTDYKDVD 1099
Cdd:TIGR02169 368 DLRAELEEVDKEFAETrdelkdyreKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKA 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 254584660 1100 VKYQKQwvELQAKTFVTDdidtysnaLDSAIMRYHKLKmEDINRIIDEL 1148
Cdd:TIGR02169 448 LEIKKQ--EWKLEQLAAD--------LSKYEQELYDLK-EEYDRVEKEL 485
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
976-1147 |
2.05e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 976 VAELESAKKQLVDLDHINENMNSGITELAKKLNDSNREKRNLKENLDLMELRADLSSIERQIDEL---------DIQNAE 1046
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1047 AERDRYQQE-SMRLRSQFERLSSENAGKLGERKQLQNQIDSMQQQLRTdykdvDVKYQKQWVELQAktfvtdDIDTYSNA 1125
Cdd:COG3206 298 AQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLER------EVEVAREL 366
|
170 180
....*....|....*....|....*...
gi 254584660 1126 LDSAIMRYHKLKME------DInRIIDE 1147
Cdd:COG3206 367 YESLLQRLEEARLAealtvgNV-RVIDP 393
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
239-940 |
2.34e-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: 48.86 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 239 QVKEVEKQLKDITeqsDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFSSSLTEKEE 318
Cdd:TIGR04523 76 KIKILEQQIKDLN---DKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 319 ELRSMEKSLRESKAKAAGIQNKCNSLmqrqgelsaSKENHERNKSVLRELQRELQTSYALSgfteNLDDFAHSLKELVHK 398
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLL---------EKEKLNIQKNIDKIKNKLLKLELLLS----NLKKKIQKNKSLESQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 399 TeNNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLELQVDISDFTDEDLEGARQDLNKFSE 478
Cdd:TIGR04523 220 I-SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 479 KLKDWEKQGLVSSISQQIKEKNEQMLILEYEIEELQVKISRTNQQadlfakLGLLKKSLQDRQLELGKFTQSFKmDSKSK 558
Cdd:TIGR04523 299 DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ------ISQLKKELTNSESENSEKQRELE-EKQNE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 559 EWGLQCGHDVDMDFKKFYINMQKNLSTKSRQQNELDKKFMEgslQLTNTEMDLRKNEEFIinaTKHLQESLPEDCTIDDY 638
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEI---ERLKETIIKNNSEIKDL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 639 TEVVAEAEASYrtalENLKIHQTTLEFNKKAL--EVAKTESCCYLCTRKFDDEGFKSSILLRLQEKTDGKFNTILKESle 716
Cdd:TIGR04523 446 TNQDSVKELII----KNLDNTRESLETQLKVLsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI-- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 717 seKEYLNSLRNLEKDVISLNdsrSRITGLSDKVTDM--RNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIvrl 794
Cdd:TIGR04523 520 --SSLKEKIEKLESEKKEKE---SKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI--- 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 795 rkasNELESDIKSITDELAIYRSS----EGKVETVEE----LQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNL 866
Cdd:TIGR04523 592 ----DQKEKEKKDLIKEIEEKEKKisslEKELEKAKKenekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 867 IREKDLKISEI---------EKSISMRKNLESDLDNKKnqLKVLEETVKKLEGDVKegsrKVNSLKVDLERKTHDFEKSL 937
Cdd:TIGR04523 668 IKESKTKIDDIielmkdwlkELSLHYKKYITRMIRIKD--LPKLEEKYKEIEKELK----KLDEFSKELENIIKNFNKKF 741
|
...
gi 254584660 938 DEN 940
Cdd:TIGR04523 742 DDA 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
740-899 |
2.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 740 SRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDEL-----AI 814
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerarAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 815 YRSSE------------------GKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEhsnLLNLIREKDLKISE 876
Cdd:COG3883 96 YRSGGsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAELEAAKAE 172
|
170 180
....*....|....*....|...
gi 254584660 877 IEKSISMRKNLESDLDNKKNQLK 899
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAE 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1194-1269 |
2.53e-05 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 46.70 E-value: 2.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254584660 1194 GRCSAGQKVlasiiiRLALSETFGVNCGVIALDEPTTNLDEENIESLARslhniiELRRHQKNFQLIVI-THDEKFL 1269
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVALLAE------LIAAHLARGGAVLLtTHQPLEL 194
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
759-939 |
3.29e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 759 MREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELEsdiksitdelaiyrssegkvETVEELQNEQRNKNES 838
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--------------------AEVEELEAELEEKDER 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 839 LRRLRKEVGQLQDERETKskehsnllnlIReKDLKISEIEKSIsmrKNLESDLDNKKNQLKVLEETVKKL-EGDVKEGSR 917
Cdd:COG2433 443 IERLERELSEARSEERRE----------IR-KDREISRLDREI---ERLERELEEERERIEELKRKLERLkELWKLEHSG 508
|
170 180
....*....|....*....|..
gi 254584660 918 KVNSLKVdLERKTHDFEKSLDE 939
Cdd:COG2433 509 ELVPVKV-VEKFTKEAIRRLEE 529
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
739-1111 |
3.82e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 739 RSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEkevRPLVENIVRLRKASNELESDIKSITDELAiyrss 818
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQSEKDKKNKALA----- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 819 EGKVETVEELQNEQRNKNESLRRLRKEVGQLQDE-RETKSKEHSNLLNLIREKDLKISEIEKSISMR--------KNLES 889
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkREARTEKQAYWQVVEGALDAQLALLKAAIAARrsgakaelKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 890 DLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLE--RKTHDFEKS-LDENNKEFKAMVLNNERFIS-INQQVKGFT 965
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQevLRYFDWYQEtWLQRRPRLATQLSNIERAISeLQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 966 ASVPLEYEKCVAELESAKKQLVDLDhinenmnsgitELAKKLNDSNREKRNLKENLDLMELRADLSSIERQIDELDIQNA 1045
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQVRLS-----------ENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1046 EAERDrYQQESMRLRSQFERLSS----ENAGKLGERKQLQNqidsmQQQLRTDYKDVDVKYQKQWVELQA 1111
Cdd:pfam12128 904 YLSES-VKKYVEHFKNVIADHSGsglaETWESLREEDHYQN-----DKGIRLLDYRKLVPYLEQWFDVRV 967
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
6-50 |
4.33e-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: 45.92 E-value: 4.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 254584660 6 KLSIQGIRSFdsNDRETIQFGKPLTLIVGSNGSGKTTIIECLKYA 50
Cdd:cd03278 3 KLELKGFKSF--ADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWV 45
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
12-900 |
4.50e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 12 IRSFDSNDRETIQFGKPLTLIVGSNGSGKTTIIECLKYATTGDlppnsKGGAFVHDPKITGEKDVraQVKLAFTSANAlN 91
Cdd:PRK01156 8 LKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTD-----KRTEKIEDMIKKGKNNL--EVELEFRIGGH-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 92 MIVTRNIQLLTKKTTATFKTLEGQLVIVNGNGDRNTLGTRSLeldaqvplyLGVPKAILEYVIFCHQ--EDSLWPlSEPS 169
Cdd:PRK01156 80 YQIRRSIERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKNI---------LGISKDVFLNSIFVGQgeMDSLIS-GDPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 170 NLKKKFDEIFQAMKFTRALDNLKGIKKDMTVDIKllkqavehlkvdkdrsrvmtmNITRLQAKSEEYQAQVKEVEKQLKD 249
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRAEIS---------------------NIDYLEEKLKSSNLELENIKKQIAD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 250 ItEQSDKLfksnqdfqkVLSKLESLKNSQQSKLEQIDRLsnsidpidlgKEELENLLSnfssslteKEEELRSMEKSLRE 329
Cdd:PRK01156 209 D-EKSHSI---------TLKEIERLSIEYNNAMDDYNNL----------KSALNELSS--------LEDMKNRYESEIKT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 330 SKAKAAGIQNKCNslmqrqgELSASKENHERNKSVLRELQRELQTSY-ALSGFTENLDDFAHSLKELVHKTENNLlnfth 408
Cdd:PRK01156 261 AESDLSMELEKNN-------YYKELEERHMKIINDPVYKNRNYINDYfKYKNDIENKKQILSNIDAEINKYHAII----- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 409 snkselnssnNELSELnnslivQTQRLDYSKMDKQKLASEIQNLELQVDISDFtdedlEGARQDLNKFSEKLKDWEK--Q 486
Cdd:PRK01156 329 ----------KKLSVL------QKDYNDYIKKKSRYDDLNNQILELEGYEMDY-----NSYLKSIESLKKKIEEYSKniE 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 487 GLVSSISQQIKEKNEQMLILEYEIEELQVKISRTNQQadlFAKLGLLKKSLQDRQLELGKFTQSFKMDSKSKEWGLQCGH 566
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK---VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGE 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 567 DVDMDFKKFYINmqknlsTKSRQQNELDKKFMEGSlQLTNTEMDLRKNEEFIinATKHLQESLPEDCTIDdytevvaeae 646
Cdd:PRK01156 465 EKSNHIINHYNE------KKSRLEEKIREIEIEVK-DIDEKIVDLKKRKEYL--ESEEINKSINEYNKIE---------- 525
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 647 aSYRTALENLKIHQTTLEFNKKALEVAKTEsccylctrkfddegfkssillrlqektdgkFNTILKESLESEKEYLNSLr 726
Cdd:PRK01156 526 -SARADLEDIKIKINELKDKHDKYEEIKNR------------------------------YKSLKLEDLDSKRTSWLNA- 573
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 727 NLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIK 806
Cdd:PRK01156 574 LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID 653
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 807 SITDELAiyrSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISMRKN 886
Cdd:PRK01156 654 NYKKQIA---EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
|
890
....*....|....*..
gi 254584660 887 LE---SDLDNKKNQLKV 900
Cdd:PRK01156 731 IKkaiGDLKRLREAFDK 747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
717-1091 |
4.73e-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: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 717 SEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKE--------DKDHAEKEVRPLV 788
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 789 ENIVRLRKASNELESDIKSItdELAIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNLLNLIR 868
Cdd:COG4913 352 RELEERERRRARLEALLAAL--GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 869 EKDLKISEI-EKSISMRKNLESDLDNKKNQLKVLEETVkklegDVKEG-----------------------------SRK 918
Cdd:COG4913 430 SLERRKSNIpARLLALRDALAEALGLDEAELPFVGELI-----EVRPEeerwrgaiervlggfaltllvppehyaaaLRW 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 919 VNSLK----VDLER------------------------KTHDFEKSLD------------ENNKEFKamvlNNERFISIN 958
Cdd:COG4913 505 VNRLHlrgrLVYERvrtglpdperprldpdslagkldfKPHPFRAWLEaelgrrfdyvcvDSPEELR----RHPRAITRA 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 959 QQVK--------------------GFTASVPLEYEKcvAELESAKKQLVDLDHINENMNSGITELAKKLNDSNREKRNLK 1018
Cdd:COG4913 581 GQVKgngtrhekddrrrirsryvlGFDNRAKLAALE--AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW 658
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254584660 1019 ENLDLMELRADLSSIERQIDEL-----DIQNAEAERDRYQQESMRLRSQFERLSSENAGKLGERKQLQNQIDSMQQQL 1091
Cdd:COG4913 659 DEIDVASAEREIAELEAELERLdassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-50 |
5.22e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.53 E-value: 5.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 254584660 4 IYKLSIQGIRSFDSndrETIQFGKP--LTLIVGSNGSGKTTIIECLKYA 50
Cdd:COG3950 3 IKSLTIENFRGFED---LEIDFDNPprLTVLVGENGSGKTTLLEAIALA 48
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
232-504 |
6.84e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 232 KSEEYQAQVKEVEkQLKDITEQSDK-LFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDP--IDLGKEELENLLSN 308
Cdd:COG5022 883 QLQELKIDVKSIS-SLKLVNLELESeIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGpsIEYVKLPELNKLHE 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 309 FSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSYALSGFTENLDDF 388
Cdd:COG5022 962 VESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 389 AHSLKELVHKTENNLLNFTHSNKSELNssnnelselnnsliVQTQRLDYSKMDKQKLASEIQNLELqvdiSDFTDEDLEG 468
Cdd:COG5022 1042 LSILKPLQKLKGLLLLENNQLQARYKA--------------LKLRRENSLLDDKQLYQLESTENLL----KTINVKDLEV 1103
|
250 260 270
....*....|....*....|....*....|....*.
gi 254584660 469 ARQDLNKFSEKLKDWEKQGLVSSISQQIKEKNEQML 504
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLV 1139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
711-911 |
6.89e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 711 LKESLESEKEYLNSLRNLEKDVISL----NDSRSRITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRP 786
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLeerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 787 LVENIVRLRKASNELESDIKSITDELA---------------IYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQD 851
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLealraaaelaaqleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 852 ERETKSKEHSNLLNLIREKDLKISEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGD 911
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
793-1173 |
1.11e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 793 RLRKASNELESDIKSITDELAIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDER---ETKSKEHSNLLNLIRE 869
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKnryESEIKTAESDLSMELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 870 KDLKISEIEK--------SISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKvDLERKTHDFEK------ 935
Cdd:PRK01156 271 KNNYYKELEErhmkiindPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKkksryd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 936 SLDENNKEFKAMVLNNERFISINQQVKGFTASVPLEYEKCVAEL-ESAKKQLVDLDHIN---ENMNSGITELAKKLNDSN 1011
Cdd:PRK01156 350 DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIsEILKIQEIDPDAIKkelNEINVKLQDISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1012 REKRNLKENLDLMELRA------------------------------DLSSIERQIDELDIQNAEAERDRYQQESMrlrs 1061
Cdd:PRK01156 430 QRIRALRENLDELSRNMemlngqsvcpvcgttlgeeksnhiinhyneKKSRLEEKIREIEIEVKDIDEKIVDLKKR---- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1062 qferLSSENAGKLGERKQLQNQIDSMQQQLRTDYKDVDvkyqkqwvELQAKTFVTDDIDTYSNALDSAIMRYHKLKMEDI 1141
Cdd:PRK01156 506 ----KEYLESEEINKSINEYNKIESARADLEDIKIKIN--------ELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNA 573
|
410 420 430
....*....|....*....|....*....|..
gi 254584660 1142 NRIIDELwkrtysgtDVDTIQLRSEEVGSGVK 1173
Cdd:PRK01156 574 LAVISLI--------DIETNRSRSNEIKKQLN 597
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
188-380 |
1.18e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 188 LDNLKGIKKDMTVDIKLLKQAVEHLKVDKDRSRVmtmNITRLQAKSEEYQAQVKEVEKQLKDITEQSDKLFKSNQ----- 262
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 263 -----------DFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFSSSLTEKEEELRSMEKSLRESK 331
Cdd:COG3883 102 vsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254584660 332 AKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSYALSG 380
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
240-505 |
1.41e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 46.30 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 240 VKEVEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDrLSNSIDPidlgKEELENLLsnfsssltEKEEE 319
Cdd:pfam18971 572 LQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYDEVKKAQKD-LEKSLRK----REHLEKEV--------EKKLE 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 320 LRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERN-KSVLRELQRELQT-SYALSGFTENLDDFAHSLKELVH 397
Cdd:pfam18971 639 SKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNlKGIKRELSDKLEKiSKDLKDFSKSFDEFKNGKNKDFS 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 398 KTENNLLNFTHSNK---------SELNSSNNELSELNNSLIVQTQRLDYSKMD----------KQKLASEIQNLELQVDI 458
Cdd:pfam18971 719 KAEETLKALKGSVKdlginpewiSKVENLNAALNEFKNGKNKDFSKVTQAKSDlensvkdviiNQKVTDKVDNLNQAVSV 798
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 254584660 459 S----DFTdeDLEGARQDLNKFSEKLKDWEKQ-------GLVSSISQQIKEKNEQMLI 505
Cdd:pfam18971 799 AkamgDFS--RVEQVLADLKNFSKEQLAQQAQknedfntGKNSELYQSVKNSVNKTLV 854
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
6-53 |
1.41e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 45.53 E-value: 1.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 254584660 6 KLSIQGIRSFDSNDretIQFGKPLTLIVGSNGSGKTTIIECLKYATTG 53
Cdd:COG1195 4 RLSLTNFRNYESLE---LEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-374 |
1.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 232 KSEEYQAQVKEVEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSID--PIDLGKEELENLLSNF 309
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254584660 310 SS---SLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQR-----QGELSASKENHERNKSVLRELQRELQT 374
Cdd:COG4717 145 PErleELEERLEELRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEELQQRLAELEEELEE 217
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
214-1132 |
1.55e-04 |
|
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: 46.58 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 214 VDKDRSRVMTMNITRLQAKSEEYQAQVKEVEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKN--SQQSKLEQIdrLSNS 291
Cdd:TIGR01612 873 TNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKfhNKQNILKEI--LNKN 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 292 IDPIDLGKEELENLLSNFSSSLTEKEEELrsmEKSLREskAKAAGIQNKCNSLMQRQGELsasKENHERNKSvlrelqre 371
Cdd:TIGR01612 951 IDTIKESNLIEKSYKDKFDNTLIDKINEL---DKAFKD--ASLNDYEAKNNELIKYFNDL---KANLGKNKE-------- 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 372 lqtsyalSGFTENLDDFAHSLKELVHKTENNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLA----S 447
Cdd:TIGR01612 1015 -------NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINitnfN 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 448 EIQNLELQVDISDFTDEDLEGARQDLNKFSEKLKDWEKQglvssISQQIKEKNEQMLILEYEIEELQVKISRTNQQADlf 527
Cdd:TIGR01612 1088 EIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQK-----IDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD-- 1160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 528 aklgllKKSLQDRQLELGKFTQSF--KMDSKskewglqcghdvdmdfKKFYINMQKNLSTKSRQqnELDKKFME------ 599
Cdd:TIGR01612 1161 ------KAISNDDPEEIEKKIENIvtKIDKK----------------KNIYDEIKKLLNEIAEI--EKDKTSLEevkgin 1216
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 600 -------GSLQLTNTEMDLRKNEEFIINATKHLQ------ESLPEDCTIDDYTEVVAEAEASYRTALENLKIHQTTLEFN 666
Cdd:TIGR01612 1217 lsygknlGKLFLEKIDEEKKKSEHMIKAMEAYIEdldeikEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKH 1296
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 667 KKALEVAKTESccYLCTRKFDDEGFKSSILLRLQektdgkfntilKESLESEK------EYLNSLRNLeKDVISLNDSRS 740
Cdd:TIGR01612 1297 DENISDIREKS--LKIIEDFSEESDINDIKKELQ-----------KNLLDAQKhnsdinLYLNEIANI-YNILKLNKIKK 1362
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 741 RITGLSDKVTDMRNRNVKMREELDTVNKELESMKEDKDHaeKEVRPLVENIVRlrkaSNELESDIKSITDELAIYRSSEG 820
Cdd:TIGR01612 1363 IIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINL--EECKSKIESTLD----DKDIDECIKKIKELKNHILSEES 1436
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 821 KVETVEELQNEQrNKNESLRRLRKEVGQLQDERETKSKEHsnllNLIREKDLKISEIEKSISMRKNLESDLDNKKNQLKV 900
Cdd:TIGR01612 1437 NIDTYFKNADEN-NENVLLLFKNIEMADNKSQHILKIKKD----NATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEK 1511
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 901 LEETVKKLEGDVKEGSRKVNS--LKVDLERKTHDFEKSLDENNKEFKAMVLNNERFISINQQVKGFTASVpleyEKCVAE 978
Cdd:TIGR01612 1512 NKELFEQYKKDVTELLNKYSAlaIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRI----EDDAAK 1587
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 979 LESAKKQLVDLDHINENMNSG---ITELAKKLNDSNREKRnlkenldlmelradlsSIERQIDELDIQNAEAERDRYQQE 1055
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFENKflkISDIKKKINDCLKETE----------------SIEKKISSFSIDSQDTELKENGDN 1651
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254584660 1056 SMRLRSQFERLSSENAGKLGERKQLQNqIDSMQQQLRTDYKDVDVKYQKQWVELQAKTFVT--DDIDTYSNALDSAIMR 1132
Cdd:TIGR01612 1652 LNSLQEFLESLKDQKKNIEDKKKELDE-LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAnkEEIESIKELIEPTIEN 1729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-373 |
2.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 201 DIKLLKQAVEHLKVDKDRSRvmtMNITRLQAKSEEYQAQVKEVEKQL-----------KDITEQSDKLFKSNQDFQKVLS 269
Cdd:COG1196 226 EAELLLLKLRELEAELEELE---AELEELEAELEELEAELAELEAELeelrleleeleLELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 270 KLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQG 349
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180
....*....|....*....|....
gi 254584660 350 ELSASKENHERNKSVLRELQRELQ 373
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELE 406
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1221-1298 |
2.29e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.92 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254584660 1221 GVIALDEPTTNLDEENIESLARslhniiELRRHQKNFQLIVITHDEKFLNHMDAsqftDHFFKVKRDDRQKSQIEWVD 1298
Cdd:COG4637 280 PLLCIEEPENGLHPDLLPALAE------LLREASERTQVIVTTHSPALLDALEP----EEVLVLEREDDGETRIRRLS 347
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
760-899 |
2.82e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.44 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 760 REELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEGKVETVEELQNEQRNKNES- 838
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETr 759
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254584660 839 -------LRRLRKEVGQLQDERETKSKEHSNLLNLIREKDLKIseieKSISMRKNLESDLDNKKNQLK 899
Cdd:pfam05911 760 lteleaeLNELRQKFEALEVELEEEKNCHEELEAKCLELQEQL----ERNEKKESSNCDADQEDKKLQ 823
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
761-1112 |
3.16e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 761 EELDTVNKELESMKED-KDHA---EKEVRPLVENIVRLRKASNElesdIKSITDELAIYRSSEGKVETVEELQNEQRNKN 836
Cdd:pfam05622 69 EQLQEENFRLETARDDyRIKCeelEKEVLELQHRNEELTSLAEE----AQALKDEMDILRESSDKVKKLEATVETYKKKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 837 ESLRRLRKEVGQLQDEretkskehsNLLNLIREKDLKiSEIEKSISMRknleSDLDNKKNQL-----KVLEETVK--KLE 909
Cdd:pfam05622 145 EDLGDLRRQVKLLEER---------NAEYMQRTLQLE-EELKKANALR----GQLETYKRQVqelhgKLSEESKKadKLE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 910 GDVKEGSRKVNSLKVDLERKTHDfEKSLDENNKEFKAMVLNNERFISINQQVKGFTAS--------VPLEYEKCVAELES 981
Cdd:pfam05622 211 FEYKKLEEKLEALQKEKERLIIE-RDTLRETNEELRCAQLQQAELSQADALLSPSSDPgdnlaaeiMPAEIREKLIRLQH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 982 AKKQLvdLDHINENMNSGITELAKKLNDSNREKRNLKENLDLMELRadLSSIERQIDELdiQNAEAERDRYQQESMRLRS 1061
Cdd:pfam05622 290 ENKML--RLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQR--ILELQQQVEEL--QKALQEQGSKAEDSSLLKQ 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 254584660 1062 QFERLssenagkLGERKQLQNQIDSMQQQLRTDYKDVDVKYQKQWVELQAK 1112
Cdd:pfam05622 364 KLEEH-------LEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEA 407
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-48 |
3.18e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 3.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 254584660 4 IYKLSIQGIRSFDSndrETIQFGkPLTLIVGSNGSGKTTIIECLK 48
Cdd:COG4637 2 ITRIRIKNFKSLRD---LELPLG-PLTVLIGANGSGKSNLLDALR 42
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
746-946 |
3.89e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 746 SDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAiyrssegkvetv 825
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 826 eELQNEQRNKNESLRRLRKEVGQLQDEREtKSKEHSNLLNLIREKDlkISEIEKSISM-------RKNLESDLDNKKNQL 898
Cdd:COG4942 87 -ELEKEIAELRAELEAQKEELAELLRALY-RLGRQPPLALLLSPED--FLDAVRRLQYlkylapaRREQAEELRADLAEL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 254584660 899 KVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEKSLDENNKEFKA 946
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-529 |
5.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 257 LFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAG 336
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 337 IQNKcnsLMQRQGELSAskenhernksVLRELQRELQTSYALSGFteNLDDFAHSLKELVHktennllnfthsnkseLNS 416
Cdd:COG4942 95 LRAE---LEAQKEELAE----------LLRALYRLGRQPPLALLL--SPEDFLDAVRRLQY----------------LKY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 417 SNNELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLElqvdisdftdEDLEGARQDLnkfsEKLKDwEKQGLVSSISQQI 496
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALL----------AELEEERAAL----EALKA-ERQKLLARLEKEL 208
|
250 260 270
....*....|....*....|....*....|...
gi 254584660 497 KEKNEQMLILEYEIEELQVKISRTNQQADLFAK 529
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
713-946 |
5.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 713 ESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDMRNRnvkmREELDTVNKELESMKEDKDHAEKEVRPLVENIV 792
Cdd:COG4913 634 EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELD 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 793 RLRKASNELESDIKSITDEL----AIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVG-QLQDERETKSKEHSNLLNLI 867
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELdelqDRLEAAEDLARLELRALLEERFAAALGDAVERELReNLEERIDALRARLNRAEEEL 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 868 REkdlKISE-IEKSISMRKNLESDLDNKKNQLKVLEetvkKLEGDvkegsrkvnslkvDLERKTHDFEKSLDENNKEFKA 946
Cdd:COG4913 790 ER---AMRAfNREWPAETADLDADLESLPEYLALLD----RLEED-------------GLPEYEERFKELLNENSIEFVA 849
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1187-1273 |
7.95e-04 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 43.81 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1187 DAELDMRGR-CSAGQKVlasiiiRLALSETFGVNCGVIALDEPTTNLDEeniESLARSLHNIIELRRhqkNFQLIVITHD 1265
Cdd:TIGR02857 449 DTPIGEGGAgLSGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDA---ETEAEVLEALRALAQ---GRTVLLVTHR 516
|
....*...
gi 254584660 1266 EKFLNHMD 1273
Cdd:TIGR02857 517 LALAALAD 524
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
13-53 |
8.59e-04 |
|
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: 42.67 E-value: 8.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 254584660 13 RSFDSNDRETIQFGKPLTLIVGSNGSGKTTIIECLKYATTG 53
Cdd:cd03242 7 RNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATG 47
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
226-377 |
9.46e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 226 ITRLQAKSEEYQAQVKEVEKQLKDITEQSDKLfksNQDFQKVLSKLESLKNSQQSKLEQIDRL----------------- 288
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEEL---NEEYNELQAELEALQAEIDKLQAEIAEAeaeieerreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 289 ----SNSIDPID--LGKEELENLLSNFS--SSLTEKE-EELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHE 359
Cdd:COG3883 95 lyrsGGSVSYLDvlLGSESFSDFLDRLSalSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170
....*....|....*...
gi 254584660 360 RNKSVLRELQRELQTSYA 377
Cdd:COG3883 175 AQQAEQEALLAQLSAEEA 192
|
|
| COG6 |
pfam06419 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
234-346 |
1.11e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localization.
Pssm-ID: 461904 Cd Length: 611 Bit Score: 43.36 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 234 EEYQAQVKEVEKQLKDITEQSDKLfksNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPIDLGKEELENLLSNFssSL 313
Cdd:pfam06419 33 GEFLKEFGPVVEQLKRIETDVEKL---NNSCDEMRKRLSAAKEDTAPLLEEASSLQEQKKKIELKQKLLDAFLDKF--TL 107
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 254584660 314 TEKEEE-LRSMEKSLRE------SKAKAagIQNKCNSLMQ 346
Cdd:pfam06419 108 SEEEEAaLTSGEEPVNDeffkalAKVKK--IHEDCKILLG 145
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
228-1103 |
1.16e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 228 RLQAKSEEYQAQVKEVEKQLKDITEQSDKLFKSNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIDPI------DLGKEE 301
Cdd:pfam01576 121 KLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdleeRLKKEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 302 --------------------------LENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASK 355
Cdd:pfam01576 201 kgrqelekakrklegestdlqeqiaeLQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 356 ENHE--RNKS--VLRELQRELQtsyALSGFTENLDDFAHSLKELVHKTENNLLNFTHSNKSELNSSNNELSEL----NNS 427
Cdd:pfam01576 281 ESERaaRNKAekQRRDLGEELE---ALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMrqkhTQA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 428 LIVQTQRLDYSK-----MDKQKLASEIQNLELQVDISdftdeDLEGARQDLNKFSEKLKDW--EKQGLVSSISQQIKEKN 500
Cdd:pfam01576 358 LEELTEQLEQAKrnkanLEKAKQALESENAELQAELR-----TLQQAKQDSEHKRKKLEGQlqELQARLSESERQRAELA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 501 EQMLILEYEIEELQVKISRTNQQADLFAK-LGLLKKSLQDRQLELGKFTQsfkmdskskewglqcghdvdmdfkkfyinm 579
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKdVSSLESQLQDTQELLQEETR------------------------------ 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 580 QK-NLSTKSRQQNELDKKFMEgslQLTNTEMDLRKNEEFIINATKHLQESLPEdctIDDYTEVVAEAEASYRTALENLKi 658
Cdd:pfam01576 483 QKlNLSTRLRQLEDERNSLQE---QLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGTLEALEEGKKRLQRELE- 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 659 hQTTLEFNKKALEVAKTESCCYLCTRKFDD----EGFKSSILLRLqEKTDGKFNTILKEslesekEYLNSLRNLEKDVIS 734
Cdd:pfam01576 556 -ALTQQLEEKAAAYDKLEKTKNRLQQELDDllvdLDHQRQLVSNL-EKKQKKFDQMLAE------EKAISARYAEERDRA 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 735 LNDSRSRIT---GLSDKVTDMRNRnvkmREELDTVNKELESMKED----KDHAEKEVRPLVENIVRLRKASNELESDIKS 807
Cdd:pfam01576 628 EAEAREKETralSLARALEEALEA----KEELERTNKQLRAEMEDlvssKDDVGKNVHELERSKRALEQQVEEMKTQLEE 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 808 ITDELAIYRSSEGKVETV---------EELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSNllnlirekdlkiseie 878
Cdd:pfam01576 704 LEDELQATEDAKLRLEVNmqalkaqfeRDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQ---------------- 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 879 kSISMRKNLESDLDNKKNQL----KVLEETVKKLegdvkegsRKVNSLKVDLERKTHDFEKSLDennkEFKAMVLNNERf 954
Cdd:pfam01576 768 -AVAAKKKLELDLKELEAQIdaanKGREEAVKQL--------KKLQAQMKDLQRELEEARASRD----EILAQSKESEK- 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 955 isinqQVKGFTASVpLEYEKCVAELESAKKQlVDLDHinenmnsgiTELAKKLNDSNREKRNLKEnlDLMELRADLSSIE 1034
Cdd:pfam01576 834 -----KLKNLEAEL-LQLQEDLAASERARRQ-AQQER---------DELADEIASGASGKSALQD--EKRRLEARIAQLE 895
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254584660 1035 RQIDELDiQNAEAERDRYQqesmRLRSQFERLSSENAgklGERKQLQNQiDSMQQQLRTDYKDVDVKYQ 1103
Cdd:pfam01576 896 EELEEEQ-SNTELLNDRLR----KSTLQVEQLTTELA---AERSTSQKS-ESARQQLERQNKELKAKLQ 955
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-75 |
1.17e-03 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 41.72 E-value: 1.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 254584660 22 TIQFGKPLTLIvGSNGSGKTTIIECLkyatTGDLPPNSkGGAFVHDPKITGEKD 75
Cdd:cd03263 24 NVYKGEIFGLL-GHNGAGKTTTLKML----TGELRPTS-GTAYINGYSIRTDRK 71
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1222-1273 |
1.55e-03 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 41.32 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 254584660 1222 VIALDEPTTNLDEENieslARSLHNIIELRRHQKNFQLIVITHDEKFLNHMD 1273
Cdd:cd03255 161 IILADEPTGNLDSET----GKEVMELLRELNKEAGTTIVVVTHDPELAEYAD 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1222-1273 |
1.61e-03 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 41.57 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 254584660 1222 VIAlDEPTTNLDEENieslARSLHNIieLRRHQKNFQ--LIVITHDEKFLNHMD 1273
Cdd:COG1136 166 ILA-DEPTGNLDSKT----GEEVLEL--LRELNRELGttIVMVTHDPELAARAD 212
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
758-968 |
1.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 758 KMREELDTVNKELESMKEDKD--HAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEGKVETVEELQNEQRNK 835
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 836 NESLRRLRKEVGQLQDERETKSKEHSNLLNLIREkdlkISEIEKSIsmRKNLESDLDNKKNQLKVLEETVKKLEGDVKEG 915
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTPNHPDVIALRAQ----IAALRAQL--QQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254584660 916 SRKVNSLKvDLERKTHDFEKSLDENNKEFKAMvLNNERFISINQQVKGFTASV 968
Cdd:COG3206 340 EARLAELP-ELEAELRRLEREVEVARELYESL-LQRLEEARLAEALTVGNVRV 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
741-1060 |
2.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 741 RITGLsDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEG 820
Cdd:PRK03918 153 QILGL-DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 821 KVETVEELQNEQRNKNESL----RRLRKEVGQLQDERETKSKEHSNL------LNLIREKDLKISEI----EKSISMRKN 886
Cdd:PRK03918 232 ELEELKEEIEELEKELESLegskRKLEEKIRELEERIEELKKEIEELeekvkeLKELKEKAEEYIKLsefyEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 887 LESDLDNKKNQLKVLEETVKKLEGDVKEgSRKVNSLKVDLERKTHDFEKSLDENNkefKAMVLNNErfisINQQVKGFTA 966
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYE---EAKAKKEE----LERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 967 SVPLEYEKCVAELESAKKQLV-DLDHINE---NMNSGITELAKKLNDSNREK-------RNLKEN--LDLM-ELRADLSS 1032
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEeEISKITArigELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrKELLeEYTAELKR 463
|
330 340
....*....|....*....|....*...
gi 254584660 1033 IERQIDELDIQNAEAERDRYQQESMRLR 1060
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKK 491
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
769-928 |
2.63e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 769 ELESMKEDKDHAEKEVRPLVENIVRLRKASNELES----DIKSITDELAIYRssegkvetvEELQNEQRNKNESLRRLRK 844
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAqqqeEAESSREQLQELE---------EQLATERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 845 EVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKV 924
Cdd:pfam09787 119 LQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVL 198
|
....
gi 254584660 925 DLER 928
Cdd:pfam09787 199 QLER 202
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
6-85 |
2.68e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.72 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 6 KLSIQGIRSFdsNDRETIQF----GKPLTLIVGSNGSGKTTIIECLKYATTGDLPPNSKGGAfVHDPKITGEKdvRAQVK 81
Cdd:cd03279 5 KLELKNFGPF--REEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQEN-LRSVFAPGED--TAEVS 79
|
....
gi 254584660 82 LAFT 85
Cdd:cd03279 80 FTFQ 83
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1129 |
2.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 867 IREKDLKISEIEKSIsmrKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKthdfEKSLDENNKEFKA 946
Cdd:COG3883 18 IQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 947 MVlnnerfisINQQVKGFTASVpleyekcVAELESAK------KQLVDLDHINENMNSGITELAKKLNDSNREKRNLKEN 1020
Cdd:COG3883 91 RA--------RALYRSGGSVSY-------LDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1021 LDlmelradlsSIERQIDELDIQNAEAERDRYQQESM--RLRSQFERLSSENAGKLGERKQLQNQIDSMQQQLRTDYKDV 1098
Cdd:COG3883 156 LA---------ELEALKAELEAAKAELEAQQAEQEALlaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250 260 270
....*....|....*....|....*....|.
gi 254584660 1099 DVKYQKQWVELQAKTFVTDDIDTYSNALDSA 1129
Cdd:COG3883 227 AAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
302-939 |
3.84e-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: 41.54 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 302 LENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQ--------------NKCNSLMQRQGELSaSKENHERNK----- 362
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDknlnkdeekinnsnNKIKILEQQIKDLN-DKLKKNKDKinkln 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 363 SVLRELQRELQTSYALSGFTENLDDFAHSLKELVHKTENNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDK 442
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 443 QKLASEIQNLELQVDISDFTDEDLEGARQDLNKFSEKLKDWEKQglVSSISQQIKEKNEqmlileyEIEELQVKISRTNQ 522
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ--NNQLKDNIEKKQQ-------EINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 523 Q-ADLFAKLGLLKKSLQDRQLELGKFTQSFK--------MDSKSKEWGLQCGHDVDMDFKKFYINMQKNLSTKSRQQNEL 593
Cdd:TIGR04523 254 QlNQLKDEQNKIKKQLSEKQKELEQNNKKIKelekqlnqLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 594 DKKFMEGSLQLTNTEMDLRKNEEFIINATKHLQESLPEdctiddyTEVVAEAEASYRTALENLKIHQTTLEFNKKALEVA 673
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE-------IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 674 KTESccylctrkfdDEGFKSsilLRLQEKTDGKFNTILKESLESEKEYLNSLRN----LEKDVISLNDSRS----RITGL 745
Cdd:TIGR04523 407 NQQK----------DEQIKK---LQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvKELIIKNLDNTREsletQLKVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 746 SDKVTDMRNRNVKMREELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSITDELAIYRSSEGKVETV 825
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 826 ---EELQNEQRNKNESLRRLR-------KEVGQLQDERETKSKEHSNLLNLIREKDLKISEIEKSISMRKNLESDLDNKK 895
Cdd:TIGR04523 554 lkkENLEKEIDEKNKEIEELKqtqkslkKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 254584660 896 NQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEKSLDE 939
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
4-45 |
3.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.52 E-value: 3.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 254584660 4 IYKLSIQGIRSFdsndrETIQFGKPLTLIVGSNGSGKTTIIE 45
Cdd:COG3910 19 AYPFNLPAVRNL-----EGLEFHPPVTFFVGENGSGKSTLLE 55
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
265-525 |
3.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 265 QKVLSKLESLKNSQQSKLEQIDRLSNSIDPIdlgKEELENLLSnfssSLTEKEEELRSMEKSLRESKAKAAgiqnkcnsl 344
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEEL---NEEYNELQA----ELEALQAEIDKLQAEIAEAEAEIE--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 345 mQRQGELsaskenhernKSVLRELQRELQTSYALSGFT--ENLDDFAHSLkelvhkteNNLLNFTHSNKSELNSSNNELS 422
Cdd:COG3883 83 -ERREEL----------GERARALYRSGGSVSYLDVLLgsESFSDFLDRL--------SALSKIADADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 423 ELNNslivqtqrldyskmDKQKLASEIQNLELQVDisdftdeDLEGARQDLNKFSEklkdwEKQGLVSSISQQIKEKNEQ 502
Cdd:COG3883 144 ELEA--------------KKAELEAKLAELEALKA-------ELEAAKAELEAQQA-----EQEALLAQLSAEEAAAEAQ 197
|
250 260
....*....|....*....|...
gi 254584660 503 MLILEYEIEELQVKISRTNQQAD 525
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAA 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1187-1273 |
4.03e-03 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 41.27 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1187 DAELDMRGRC-SAGQKVlasiiiRLALSETFgvnCG---VIALDEPTTNLDEENIESLARSlhnIIELRRHQKNfqLIVI 1262
Cdd:COG4618 458 DTRIGEGGARlSGGQRQ------RIGLARAL---YGdprLVVLDEPNSNLDDEGEAALAAA---IRALKARGAT--VVVI 523
|
90
....*....|.
gi 254584660 1263 THDEKFLNHMD 1273
Cdd:COG4618 524 THRPSLLAAVD 534
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
242-1121 |
4.14e-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: 41.58 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 242 EVEKQLKDITEQSDKLFK--SNQDFQKVLSKLESLKNSQQSKLEQIDRLSNSIdpidlgKEELENLLSNFSSSLTEKEEE 319
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDkiQNMETATVELHLSNIENKKNELLDIIVEIKKHI------HGEINKDLNKILEDFKNKEKE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 320 LRS-------MEKSLRESKAKAAGIQNKCNSLMQRQG-ELSASKENHERNKSVLRELQ-RELQTSYALSGFTENLDDFAH 390
Cdd:TIGR01612 767 LSNkindyakEKDELNKYKSKISEIKNHYNDQINIDNiKDEDAKQNYDKSKEYIKTISiKEDEIFKIINEMKFMKDDFLN 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 391 SLkelvhkteNNLLNFTHSNKSELNSSNNELSELNNSL---IVQTQRLDYSKM--DKQKLASEIQN-------------- 451
Cdd:TIGR01612 847 KV--------DKFINFENNCKEKIDSEHEQFAELTNKIkaeISDDKLNDYEKKfnDSKSLINEINKsieeeyqnintlkk 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 452 LELQVDISDFTDEDLEGARQDLNKFSEKL-KDWEKQGLVSSISQQIKEKNEQMLIleYEIEELQvKISRTNQQADLFAKL 530
Cdd:TIGR01612 919 VDEYIKICENTKESIEKFHNKQNILKEILnKNIDTIKESNLIEKSYKDKFDNTLI--DKINELD-KAFKDASLNDYEAKN 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 531 GLLKKSLQDRQLELGK-----FTQSFKMDSKSKEWGLQCGHDVDMDFKKFYINMQKNLSTKSRQ-QNELDKkfmegSLQL 604
Cdd:TIGR01612 996 NELIKYFNDLKANLGKnkenmLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEiEKEIGK-----NIEL 1070
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 605 TNTEMdLRKNEEFIINATKhlqesLPEDCTIDDYTEVVAEAEASYRTALENLKIHQTTL----EFNKKALEVAKTESCCY 680
Cdd:TIGR01612 1071 LNKEI-LEEAEINITNFNE-----IKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLdqkiDHHIKALEEIKKKSENY 1144
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 681 LCT--------RKFDDEGFKSSILLRLQEKTDGKFNTILKES--LESEKEYLNSLRNLEKDVISLNdsrsritglsdkvt 750
Cdd:TIGR01612 1145 IDEikaqindlEDVADKAISNDDPEEIEKKIENIVTKIDKKKniYDEIKKLLNEIAEIEKDKTSLE-------------- 1210
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 751 DMRNRNVKMREELDTVNKE-LESMKEDKDHAEKEVRPLVENIVRLRKASNELES------DIKSITDELAIYRSSEGKVE 823
Cdd:TIGR01612 1211 EVKGINLSYGKNLGKLFLEkIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENemgiemDIKAEMETFNISHDDDKDHH 1290
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 824 TVEELQNEQ----RNKNESLRRLRKEVGQLQDERET------KSKEHSNLLNLIREK------DLKISEIEKSIS----- 882
Cdd:TIGR01612 1291 IISKKHDENisdiREKSLKIIEDFSEESDINDIKKElqknllDAQKHNSDINLYLNEianiynILKLNKIKKIIDevkey 1370
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 883 ------MRKNLESDLDNKKNQLKV------LEETVKKLEG-----DVKEGSRKVNSLKVDL---ERKTHDFEKSLDENNK 942
Cdd:TIGR01612 1371 tkeieeNNKNIKDELDKSEKLIKKikddinLEECKSKIEStlddkDIDECIKKIKELKNHIlseESNIDTYFKNADENNE 1450
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 943 E----FK--AMVLNNERFISINQQVKG-----FTASVPLEY----EKCVAELESAKKQLVDLDHINENMNSGITELAKKL 1007
Cdd:TIGR01612 1451 NvlllFKniEMADNKSQHILKIKKDNAtndhdFNINELKEHidksKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKY 1530
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1008 NDSNREKRNLKENLDLMELRADLSSIERQIdELDIQNAEAERDRYQQESMRLRSQFERLSSENAGKLGERKQLQNQIDSM 1087
Cdd:TIGR01612 1531 SALAIKNKFAKTKKDSEIIIKEIKDAHKKF-ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKF 1609
|
970 980 990
....*....|....*....|....*....|....
gi 254584660 1088 QQQLRTDYKDVDVKYQKQWVELQAKTFVTDDIDT 1121
Cdd:TIGR01612 1610 LKISDIKKKINDCLKETESIEKKISSFSIDSQDT 1643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
821-1141 |
4.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 821 KVETVEELQNEQrnkneslRRLRKEvGQLQDERETkskehsnllnliREKDlkiseieksisMRKNLESDL----DNKKn 896
Cdd:COG4913 563 CVDSPEELRRHP-------RAITRA-GQVKGNGTR------------HEKD-----------DRRRIRSRYvlgfDNRA- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 897 QLKVLEETVKKLEGDVKEGSRKVNSLKVDLERkthdfeksldennkefkamvlnNERFISINQQVKGFTASvPLEYEKCV 976
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDA----------------------LQERREALQRLAEYSWD-EIDVASAE 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 977 AELESAKKQLVDLDhineNMNSGITELAKKLNDSNREKRNLKENLDLM-----ELRADLSSIERQIDELDIQNAEAERDR 1051
Cdd:COG4913 668 REIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELkgeigRLEKELEQAEEELDELQDRLEAAEDLA 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1052 YQQESMRLRSQFERLSSENAGKlGERKQLQNQIDSMQQQLRTDYKDVD---VKYQKQWvelqakTFVTDDIDTYSNALDS 1128
Cdd:COG4913 744 RLELRALLEERFAAALGDAVER-ELRENLEERIDALRARLNRAEEELEramRAFNREW------PAETADLDADLESLPE 816
|
330
....*....|...
gi 254584660 1129 AIMRYHKLKMEDI 1141
Cdd:COG4913 817 YLALLDRLEEDGL 829
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
762-948 |
5.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 762 ELDTVNKELESMKEDKDHAEKEVRPLVENIVRLRKASNELESDIKSItdelaiyrssEGKVETVEELqneqrnknesLRR 841
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL----------ELEIEEVEAR----------IKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 842 LRKEVGQLQDERETKSKEHsnllnlirekdlkisEIEKSISMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNS 921
Cdd:COG1579 78 YEEQLGNVRNNKEYEALQK---------------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
170 180
....*....|....*....|....*..
gi 254584660 922 LKVDLERKTHDFEKSLDENNKEFKAMV 948
Cdd:COG1579 143 KKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
780-1049 |
5.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 780 AEKEVRPLVENIVRLRKASNELESDIKSITDElaiyrsSEGKVETVEELQ---NEQRNKNESLRRLRKEVGQLQDERETK 856
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQ------REQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 857 SKEHSNLLNLIREKDLKISEIEksiSMRKNLESDLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEkS 936
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELE---EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE-S 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 937 LDENNKEFKamvlnnERfisiNQQVKGFTASVPLEYEKCVAELESAKKQLVDLDhinenmnSGITELAKKLNDSNREKRN 1016
Cdd:PRK02224 347 LREDADDLE------ER----AEELREEAAELESELEEAREAVEDRREEIEELE-------EEIEELRERFGDAPVDLGN 409
|
250 260 270
....*....|....*....|....*....|....*...
gi 254584660 1017 LKENLDLM-----ELRADLSSIERQIDELDIQNAEAER 1049
Cdd:PRK02224 410 AEDFLEELreerdELREREAELEATLRTARERVEEAEA 447
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-57 |
5.84e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 40.87 E-value: 5.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 254584660 8 SIQGIRSFDSNDreTIQFGKPLTLIVGSNGSGKTTIIECLKYATTGDLPP 57
Cdd:COG4694 7 KLKNVGAFKDFG--WLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSS 54
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
230-501 |
5.99e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 230 QAKSEEYQAQVKEVEKQLKDITEQSDKLFKSNQ-DFQKVLS---------KLESLKNSQQSKLEQIDRLSNsIDPIDLGK 299
Cdd:PTZ00108 1053 KKKSEKITAEEEEGAEEDDEADDEDDEEELGAAvSYDYLLSmpiwsltkeKVEKLNAELEKKEKELEKLKN-TTPKDMWL 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 300 EELENLLSNFSSSLTEKEEELRSMEKSLRESKAKAAGIQNKcnslmqrqgeLSASKENHERNKSVLRELQRELQTSYALS 379
Cdd:PTZ00108 1132 EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKP----------KLKKKEKKKKKSSADKSKKASVVGNSKRV 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 380 GFTENLDDFAHSLKELVHKTENNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLASEIQNLELQVDIS 459
Cdd:PTZ00108 1202 DSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAV 1281
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 254584660 460 DFTDEDLEGARQDLNKFSEKLKDWEKQGLVSSISQQIKEKNE 501
Cdd:PTZ00108 1282 QYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKK 1323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
711-1097 |
6.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 711 LKESLESEKEYLNSLRNLEKDVISLNDSRSRITGLSDKVTDMRN--RNVKMREELDTVNKELESMKEDKDHAEKEVRPLV 788
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 789 ENIVRLRKASNELESDIKSITDEL-----AIYRSSEGKVETVEELQNEQRNKNESLRRLRKEVGQLQDERETKSKEHSN- 862
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLeqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAa 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 863 --------------------------------------------------LLNLIREKDLKISEIEK--SISMRKNLES- 889
Cdd:COG4717 240 aleerlkearlllliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEElqALPALEELEEe 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 890 DLDNKKNQLKVLEETVKKLEGDVKEGSRKVNSLKVDLERKTHDFEksLDENNKEFKAM-----VLNNERFISINQQVKgf 964
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALlaeagVEDEEELRAALEQAE-- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 965 tasvplEYEKCVAELESAKKQLvdldhinENMNSGITELAKKLNDSNREKRNLKENLDLMELRADLSSIERQIDELDIQN 1044
Cdd:COG4717 396 ------EYQELKEELEELEEQL-------EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 254584660 1045 AEAERDRyqqESMRLRSQFERLSSENAgKLGERKQLQNQIDSMQQQLRTDYKD 1097
Cdd:COG4717 463 EQLEEDG---ELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYRE 511
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1194-1270 |
6.16e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 40.82 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 1194 GRCSAGQKVlasiiiRLALSETF--GVNcgVIALDEPTTNLDEENIESLARSLhniielrrhqKNFQ--LIVITHDEKFL 1269
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLlsPPN--VLLLDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFL 492
|
.
gi 254584660 1270 N 1270
Cdd:COG0488 493 D 493
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
188-452 |
6.71e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 188 LDNLKGIKkDMTVDIKLLKQAVEhlkvdkdRSRVMTMNITRLQAKSEEYQAQVKEVEKQLKDITEQsdklfksnqdfqkv 267
Cdd:PRK11281 45 LDALNKQK-LLEAEDKLVQQDLE-------QTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE-------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 268 lskLESLKNSQQSKLEQidRLSNsidpidLGKEELENLLSNFSSSLTEKEEELrsmekslreskakaagiqNKCNSLmqr 347
Cdd:PRK11281 103 ---LEALKDDNDEETRE--TLST------LSLRQLESRLAQTLDQLQNAQNDL------------------AEYNSQ--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 348 qgeLSASKENHERNKSVLRE-LQRELQTSYALSGFTENLDDFAHSLKELVhKTENNLLNFTHSNKSELNSSNNELSELNN 426
Cdd:PRK11281 151 ---LVSLQTQPERAQAALYAnSQRLQQIRNLLKGGKVGGKALRPSQRVLL-QAEQALLNAQNDLQRKSLEGNTQLQDLLQ 226
|
250 260
....*....|....*....|....*.
gi 254584660 427 SlivqtqRLDYSKMDKQKLASEIQNL 452
Cdd:PRK11281 227 K------QRDYLTARIQRLEHQLQLL 246
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
4-44 |
7.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.95 E-value: 7.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 254584660 4 IYKLSIQGIRSFDSndrETIQFgKPLTLIVGSNGSGKTTII 44
Cdd:COG4938 1 IKSISIKNFGPFKE---AELEL-KPLTLLIGPNGSGKSTLI 37
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
315-552 |
8.30e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 40.53 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 315 EKEEELRSMEKSLRESKAKAAGIQNKCNSLMQRQGELSASKENHERNKSVLRELQRELQTSYALSGFTENLDDFAHSLKE 394
Cdd:pfam18971 611 EVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSD 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 395 LVHKTENNLLNFTHSNKSELNSSNNELSELNNSLIVQTQRLDYSKMDKQKLaSEIQNLELQVdisdftDEDLEGARQDLN 474
Cdd:pfam18971 691 KLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWI-SKVENLNAAL------NEFKNGKNKDFS 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 475 KFSEKLKDWEKQGLVSSISQQIKEKNEQmLILEYEIEELQVKISRTNQ-QADL--FAKLGLLKKSLQDRQLELGKFTQSF 551
Cdd:pfam18971 764 KVTQAKSDLENSVKDVIINQKVTDKVDN-LNQAVSVAKAMGDFSRVEQvLADLknFSKEQLAQQAQKNEDFNTGKNSELY 842
|
.
gi 254584660 552 K 552
Cdd:pfam18971 843 Q 843
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
713-854 |
8.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 713 ESLESEKEYLNslRNLEKDVISLNDSRSRITGLSDKVTDMRNRNVKMREELDTV---------NKELESMKEDKDHAEKE 783
Cdd:COG1579 34 AELEDELAALE--ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254584660 784 VRPLVENIvrlrkasNELESDIKSITDELAiyrssegkvETVEELQNEQRNKNESLRRLRKEVGQLQDERE 854
Cdd:COG1579 112 ILELMERI-------EELEEELAELEAELA---------ELEAELEEKKAELDEELAELEAELEELEAERE 166
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
463-654 |
8.52e-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: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 463 DEDLEGARQDLNKFSEKLKDWEKQglVSSISQQIKEKNEQMLILEYEIEELQVKISRTNQQADlfaklgLLKKSLQDRQL 542
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE--LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 543 ELGKFTQSFKMDSKSKEWglqcghdVDM-----DFKKFyINMQKNLSTKSRQQNELDKKFMEGSLQLTNTEMDLRKNEEF 617
Cdd:COG3883 87 ELGERARALYRSGGSVSY-------LDVllgseSFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 254584660 618 IINATKHLQESLPE-DCTIDDYTEVVAEAEASYRTALE 654
Cdd:COG3883 159 LEALKAELEAAKAElEAQQAEQEALLAQLSAEEAAAEA 196
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
697-1010 |
8.58e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 40.53 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 697 LRLQEKtdgkfNTILKESLESEKEYLNSLRNLEKDVislndSRSRITGLSDkvtdmrnrnvkmreELDTVNKELESMKED 776
Cdd:pfam18971 570 LSLQEA-----NKLIKDFLSSNKELAGKALNFNKAV-----AEAKSTGNYD--------------EVKKAQKDLEKSLRK 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 777 KDHAEKEVRPLVEnivrlrkasnelesdiksitdelaiyrSSEGKVETVEELQNEQRNKNESLRRLRKEVGqlQDERETK 856
Cdd:pfam18971 626 REHLEKEVEKKLE---------------------------SKSGNKNKMEAKAQANSQKDEIFALINKEAN--RDARAIA 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 857 SKEhsNLLNLIREKDLKISEIEKSIS-MRKNLESDLDNKKNQLKVLEETVKKLEGDVK------EGSRKVNSLKVDLER- 928
Cdd:pfam18971 677 YTQ--NLKGIKRELSDKLEKISKDLKdFSKSFDEFKNGKNKDFSKAEETLKALKGSVKdlginpEWISKVENLNAALNEf 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254584660 929 ---KTHDFEKSLDENN---KEFKAMVLNN---ERFISINQQVKGFTASVPL-EYEKCVAELES-AKKQLVDLDHINENMN 997
Cdd:pfam18971 755 kngKNKDFSKVTQAKSdleNSVKDVIINQkvtDKVDNLNQAVSVAKAMGDFsRVEQVLADLKNfSKEQLAQQAQKNEDFN 834
|
330
....*....|....
gi 254584660 998 SGI-TELAKKLNDS 1010
Cdd:pfam18971 835 TGKnSELYQSVKNS 848
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1222-1280 |
9.72e-03 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 38.57 E-value: 9.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254584660 1222 VIALDEPTTNLDeenieslarsLHNIIE----LRRHQKNFQLIVI--THDekfLNHmdASQFTDH 1280
Cdd:cd03214 118 ILLLDEPTSHLD----------IAHQIEllelLRRLARERGKTVVmvLHD---LNL--AARYADR 167
|
|
| |
