|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-1307 |
0e+00 |
|
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: 1599.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 16 AKFLRLHIRGIRSVGDEDHDVHKIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQN-FIHSTDVARKTRVDAS 94
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNtFVHDPKVAQETDVRAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 95 VTLEFIDVKGRECTAVRRLVVTSGTKAAALAEEHTLAIKYPDGTVNTLSSKVCDFNTALLKHLGVPRAVFKYVIFCHQED 174
Cdd:TIGR00606 81 IRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 175 STWPLSEPKELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEMQTHEMSKQLYET------HVRDKLVARQNQEECERKIS 248
Cdd:TIGR00606 161 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLESSREIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 249 KRKE-ETDELKERkangQKKIEEMRTSIHELEDTLTSFKKTELERQNLKKQLSLIRVEPYFGTEEELKREIEeFRGSEGR 327
Cdd:TIGR00606 241 KSYEnELDPLKNR----LKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH-NHQRTVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 328 SYGEERARIQKKIGKNNQERQELSQKKTEFENRIS--SLKAEVIHCQSLKYDLERLENQLRSELD-LEHDADIDIEIDNA 404
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlQLQADRHQEHIRARDSLIQSLATRLELDgFERGPFSERQIKNF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 405 ITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATKIEVEMK----TLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLK 480
Cdd:TIGR00606 396 HTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 481 KEEALRKSLADLPLLDENALTECKLKREKYLK--QLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAYQRIYDNN 558
Cdd:TIGR00606 476 LDQELRKAERELSKAEKNSLTETLKKEVKSLQneKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 559 WQG---LIGQAPDFPWTPILSKTFHKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSENIFEACSCE 635
Cdd:TIGR00606 556 SRHsdeLTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 636 AEEVseKLENLRKRLKKARKDLAPLSAKSNLYDSYIEES--KSSGCCPLCDRDFKTKKEINEFSKKLENMTLSFPTEQEE 713
Cdd:TIGR00606 636 DEES--DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLtdENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 714 LEKLVSKLEKE-EIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDVGV 792
Cdd:TIGR00606 714 TESELKKKEKRrDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 793 IQQLYEQTEENEKRYEQLVSESDSSDG-LSYTELRKKVEDKDEEYRKIVQEGEELQKCSEERNK----LQSKLNELGTHR 867
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLdRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEqiqhLKSKTNELKSEK 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 868 VSLGEAAAQAGAFAEQLETKIKEIQECITAISQKRNEDLPDAQFKKDDLTRN---VSSKEEEKKKAEMEVQMMKKELDQK 944
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKeelISSKETSNKKAQDKVNDIKEKVKNI 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 945 IFHRKSLFKKVQEGglCERQLMDKENNIATLNASLEENQQRQKRFEEDLR----SFDSSHQRESILKDQLTRMIIENKIK 1020
Cdd:TIGR00606 954 HGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRlmrqDIDTQKIQERWLQDNLTLRKRENELK 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1021 ELKRTLATFDGQINEDRITEQKQAYNKLQNELRLIGNEEVKIYTQMQEYEKQKKIAEAKLSTKECQNAESNYRDAIIELA 1100
Cdd:TIGR00606 1032 EVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMR 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1101 ITKESISDLTKYRNCLDASLIQFHSEKMGRVNGIIDDLWRKVYNSTDITTIRIRSDATSETSSKKVAYEYNVMMVHETG- 1179
Cdd:TIGR00606 1112 TTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGd 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1180 TEVEMRGRCSAGQKMLASLLIRIALAEVFGGSCSMIALDEPTTNLDESKVEGMAIVLADIIAERRgfdengklRGRDMQM 1259
Cdd:TIGR00606 1192 TALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRS--------QQRNFQL 1263
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*...
gi 193208595 1260 VVITHDERLVNRITISCRPEYIYCLGKDEHGISFLSKRYPDGTVKRVN 1307
Cdd:TIGR00606 1264 LVITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEIVKCSPSSLGKRVH 1311
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1171-1293 |
2.47e-34 |
|
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: 130.81 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1171 NVMMVHETGTE---VEMRGRCSAGQKMLASLLIRIALAEVFGGSCSMIALDEPTTNLDESKVEGmaiVLADIIAERRGfd 1247
Cdd:cd03240 96 NVIFCHQGESNwplLDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIEE---SLAEIIEERKS-- 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 193208595 1248 engklrGRDMQMVVITHDERLVNRItiscrpEYIYCLGKDEHGISF 1293
Cdd:cd03240 171 ------QKNFQLIVITHDEELVDAA------DHIYRVEKDGRQKSR 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
18-184 |
5.90e-33 |
|
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: 126.95 E-value: 5.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 18 FLRLHIRGIRSVgdedHDVHKIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNFiHSTDVARKTRVDASVTL 97
Cdd:cd03240 1 IDKLSIRNIRSF----HERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGA-HDPKLIREGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 98 EFIDVKGRECTAVRRLvvtsgtkaaalaeehtlaikypdgtvntlsskvcdfntallkhlgvprAVFKYVIFCHQEDSTW 177
Cdd:cd03240 76 AFENANGKKYTITRSL------------------------------------------------AILENVIFCHQGESNW 107
|
....*..
gi 193208595 178 PLSEPKE 184
Cdd:cd03240 108 PLLDMRG 114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-914 |
6.54e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 183 KELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEMQTHEMSKQLYEthVRDKLVARQNQEECERKISKRKEETDELKE-RK 261
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAED--ARKAEEARKAEDAKRVEIARKAEDARKAEEaRK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 262 ANGQKKIEEMRTSIhELEDTLTSFKKTELERQNLKKQLSLIRVEPYFGTEEELKREIEEFRGSEGRSYGEErARIQKKIG 341
Cdd:PTZ00121 1172 AEDAKKAEAARKAE-EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE-AKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 342 KNNQERQELSQKKTEFENRISSLKAEvihcQSLKYDLERLENQLRSELDLEHDAdidiEIDNAITLKIRGMSDKARMIAK 421
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAE----EARKADELKKAEEKKKADEAKKAE----EKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 422 NCAE-----LQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKK-------EEALRKSL 489
Cdd:PTZ00121 1322 KKAEeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeekkkaDEAKKKAE 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 490 ADLPLLDENALTECKLKREKYLKQLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAYQRIYD-NNWQGLIGQAPD 568
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 569 FPWTPILSKTFHKLRND----KKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSENIFEACSCEAEEVSEKLE 644
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 645 NLRK--RLKKARKDLAPLSAKSNLYDSyIEESKSSGCCPLCDRDFKTKKEINEFSKKLENMTLSFPTEQEELEKLVSKLE 722
Cdd:PTZ00121 1562 EKKKaeEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 723 KEEIIIVKAE--GQANELQRIVK-ELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQT----DVGVIQQ 795
Cdd:PTZ00121 1641 KEAEEKKKAEelKKAEEENKIKAaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaeEKKKAEE 1720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 796 LYEQTEENEKRYEQLVSESDssdglsytELRKKVED---KDEEYRKIVQEGEELQKCSEERNKLQSKLNELGTHRvslge 872
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAE--------EDKKKAEEakkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE----- 1787
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 193208595 873 aaaQAGAFAEQLETKIKEIQECITAISQKRNEDLPDAQFKKD 914
Cdd:PTZ00121 1788 ---EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
21-225 |
2.02e-13 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 70.22 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 21 LHIRGIRSVGDEDhdvhkIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQN----FIHSTDVARKTRVDASVT 96
Cdd:pfam13476 1 LTIENFRSFRDQT-----IDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSgggfVKGDIRIGLEGKGKAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 97 LEFIDVKGRECTAVRRLVVTSGTKAAALAEEHTLAIkypdgtvntlssKVCDFNTALLKHLGVPRAVFKYVIFCHQEDst 176
Cdd:pfam13476 76 ITFENNDGRYTYAIERSRELSKKKGKTKKKEILEIL------------EIDELQQFISELLKSDKIILPLLVFLGQER-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 193208595 177 wplSEPKELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEMQTHEMSKQL 225
Cdd:pfam13476 142 ---EEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEEL 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-896 |
2.32e-13 |
|
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: 75.01 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 17 KFLRLHIRGIRSVgdedHDVHKIDF--LSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNFIHSTDVARKTRvDAS 94
Cdd:TIGR00618 2 KPLRLTLKNFGSY----KGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSE-AAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 95 VTLEFIdVKGRECTAVRRLVVTSGTKAAALAEEHTLAIKYPDGTVntLSSKVCDFNTALLKHLGVPRAVFKYVIFCHQ-E 173
Cdd:TIGR00618 77 AELEFS-LGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRI--LAAKKSETEEVIHDLLKLDYKTFTRVVLLPQgE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 174 DSTWPLSEPKELKKRFDDIFQL------------------TKFVKAQERMKKIVLDFKKEMQTHEMSKQLYETHVRDKLV 235
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLdqytqlalmefakkkslhGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 236 ARQNQEECERKISKRkeetDELKERKANGQKKIEEMRTSIHELEDTLTSFKKTElERQNLKKQlslirVEPYfgteeelk 315
Cdd:TIGR00618 234 ALQQTQQSHAYLTQK----REAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ-ERINRARK-----AAPL-------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 316 reieefrgsegrsygeerARIQKKIGKNNQERQELSqkkTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDLeHDA 395
Cdd:TIGR00618 296 ------------------AAHIKAVTQIEQQAQRIH---TELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL-HSQ 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 396 DIDIEIDNAITLKIRGMSDKARmiakncaELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIkQGQNATAGM 475
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQH-------TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT-SAFRDLQGQ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 476 KDLLKKEEALRKSLADLPLLDENALTECKLKREKYLKQLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAY-QRI 554
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEePCP 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 555 YDNNWQGLIGQAPDFPWTPILSKTFHKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSENIfEACSC 634
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD-NRSKE 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 635 EAEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEESKSSGCCPLCDRDFKTKKEINEFSKKLENMTLSFpTEQEEL 714
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ-ERVREH 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 715 EKLVSKLEKEEIIIVKAEGQA--NELQRIVKELKEVREKNRKL-STEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDVG 791
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKmqSEKEQLTYWKEMLAQCQTLLrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 792 VIQ--------QLYEQTEENEKRYEQLVSESDSSDGLSytELRKKVEDKDEEYRKIVQEGEELQ---------------- 847
Cdd:TIGR00618 744 SLKelmhqartVLKARTEAHFNNNEEVTAALQTGAELS--HLAAEIQFFNRLREEDTHLLKTLEaeigqeipsdedilnl 821
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 193208595 848 ---KCSEERNKLQSKLNELGTHRVSLGEAAAQAGAFAEQLETKIKEIQECIT 896
Cdd:TIGR00618 822 qceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-831 |
5.89e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 20 RLHIRGIRSvgdedHDVHKIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQnfIHSTDVARKTRVDASVTLEF 99
Cdd:PRK03918 5 ELKIKNFRS-----HKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKG--LKKDDFTRIGGSGTEIELKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 100 iDVKGRECTAVRRLvvtsgtkaaalaEEHTLAIKYPDGTVNTL--SSKVCDFNTALlkhlgVPRAVFKYVIFCHQEDSTW 177
Cdd:PRK03918 78 -EKNGRKYRIVRSF------------NRGESYLKYLDGSEVLEegDSSVREWVERL-----IPYHVFLNAIYIRQGEIDA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 178 PLSEPKELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEM---------------QTHEMSKQLYET--HVRDKLVARQNQ 240
Cdd:PRK03918 140 ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIerlekfikrtenieeLIKEKEKELEEVlrEINEISSELPEL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 241 EECERKISKRKEETDELKERKANGQKKIEEMRTSIHELEDTLtsfKKTELERQNLKKQLSLIRvepyfgteeelkreIEE 320
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI---RELEERIEELKKEIEELE--------------EKV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 321 FRGSEGRSYGEERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRS-ELDLEHDADIDI 399
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 400 EIDNAITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIkqgqnatagmkdll 479
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-------------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 480 kkeEALRKSLADLPLLDENaLTECKLKR--EKYLKQLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAYQRIYDN 557
Cdd:PRK03918 429 ---EELKKAKGKCPVCGRE-LTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 558 -----------NWQGLIGQAPDFpwtPILSKTFHKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSE 626
Cdd:PRK03918 505 lkeleeklkkyNLEELEKKAEEY---EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 627 NIFEAcsceAEEVSEKLENLRKrlkkarkdlaplsaksnLYDSYIEESKSsgccplcdrdfktKKEINEFSKKLEnmtls 706
Cdd:PRK03918 582 LGFES----VEELEERLKELEP-----------------FYNEYLELKDA-------------EKELEREEKELK----- 622
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 707 fpTEQEELEKLVSKLEKEEIIIVKAEGQANELQRI--VKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLklaE 784
Cdd:PRK03918 623 --KLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL---E 697
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 193208595 785 DLQTDVGVIQQLYEQTEENEKRYEQLvsesdssdglsyTELRKKVED 831
Cdd:PRK03918 698 KLKEELEEREKAKKELEKLEKALERV------------EELREKVKK 732
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-905 |
1.22e-11 |
|
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: 69.70 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 230 VRDKLVARQNQEECERKISKRKEETDELKERKANGQKKIEEMRTSIHELEDTLTSFKKTELERQNLKKQLSlirvepyfg 309
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 310 TEEELKREIEEFRGSEGRSYGEERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSEL 389
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 390 DLEHDADIDIEID-NAITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATkiEVEMKTLQNEKVKLEKE----------- 457
Cdd:TIGR02168 382 ETLRSKVAQLELQiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEEleelqeelerl 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 458 VEQLKFKIKQGQNATAGMKDLLKKEEALRKSLADLPLLDENALTECKLKREKYLKQL----------------------- 514
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlselisvdegyeaai 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 515 ---------DILKKKCAEAEKNAEKDREKESLKQTL----SIARKKMTAYQRIYDNNWQGLIGQAPDF-----PWTPILS 576
Cdd:TIGR02168 540 eaalggrlqAVVVENLNAAKKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGVAKDLvkfdpKLRKALS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 577 KTFHKLR---------NDKKIMEEDLRDVQLNVQKL------------ETMQHQYRKQEESLTAQELKLSENIFEACSCE 635
Cdd:TIGR02168 620 YLLGGVLvvddldnalELAKKLRPGYRIVTLDGDLVrpggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 636 AEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEESkssgccplcdrdfktKKEINEFSKKLENMTLSFPTEQEELE 715
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---------------EAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 716 KLVSKLEKEEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKN-EKQLETVNAKLKLAEDLQTDVGVIQ 794
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaANLRERLESLERRIAATERRLEDLE 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 795 QLYEQTEENEKRYEQLVSESdssdGLSYTELRKKVEDKDEEYRKIVQEGEELQkcsEERNKLQSKLNELGTHRVSLGEAA 874
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLR---SELEELSEELRELESKRSELRREL 917
|
730 740 750
....*....|....*....|....*....|.
gi 193208595 875 AQAGAFAEQLETKIKEIQECITAISQKRNED 905
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-1074 |
1.87e-11 |
|
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: 68.94 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 38 KIDFLSPCTLISGPNGTGKTTTIEALNFV----TTGQMPTQKKQNFIHSTDVARKTrVDASVTLEFIDVKGR---ECTAV 110
Cdd:TIGR02169 18 VIPFSKGFTVISGPNGSGKSNIGDAILFAlglsSSKAMRAERLSDLISNGKNGQSG-NEAYVTVTFKNDDGKfpdELEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 111 RRLVVTsgtkaaalaEEHTLAIKYPDGTVNTLSskvcDFNTALLKHlGVPRAVFKYVIfchQEDSTWPLS-EPKELKKRF 189
Cdd:TIGR02169 97 RRLKVT---------DDGKYSYYYLNGQRVRLS----EIHDFLAAA-GIYPEGYNVVL---QGDVTDFISmSPVERRKII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 190 DDIFQLTKFvkaqermkkivlDFKKEMQTHEMSkqlyethvrdklVARQNQEECERKISKRKEETDELKERKaNGQKKIE 269
Cdd:TIGR02169 160 DEIAGVAEF------------DRKKEKALEELE------------EVEENIERLDLIIDEKRQQLERLRRER-EKAERYQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 270 EMRTSIHELEDTLTSFKKTELERQ--NLKKQLSLIRVEpyfgteEELKREIEEFRGSEGRSYGEERARIQKKIGKNNQER 347
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQkeAIERQLASLEEE------LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 348 QELSQKKT-EFENRISSLKAEVIHCQSLKYDLERLENQLRSELDlEHDADIDiEIDNAI-TLKIRGMSDKARMiakncAE 425
Cdd:TIGR02169 289 QLRVKEKIgELEAEIASLERSIAEKERELEDAEERLAKLEAEID-KLLAEIE-ELEREIeEERKRRDKLTEEY-----AE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 426 LQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKeeaLRKSLADLplldENALTECKL 505
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR---LSEELADL----NAAIAGIEA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 506 KREKYLKQLDILKKKCAEAEKNAE---KDREKES-----LKQTLSIARKKMTAYQRIYDNnwqgLIGQApdfpwtPILSK 577
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEqlaADLSKYEqelydLKEEYDRVEKELSKLQRELAE----AEAQA------RASEE 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 578 TFHKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKlsenifeACSCEAEEVSEKLENLRKRLKKARKDL 657
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLN-------NVVVEDDAVAKEAIELLKRRKAGRATF 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 658 APLSaKSNLYDSYIEESKSSGCCPL------CD-----------------RDFKTKKEI----------NEFSKKLENMT 704
Cdd:TIGR02169 578 LPLN-KMRDERRDLSILSEDGVIGFavdlveFDpkyepafkyvfgdtlvvEDIEAARRLmgkyrmvtleGELFEKSGAMT 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 705 LSFPTEQEELEKLVSKLEKEEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAE 784
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 785 DLQTDVGVIQQLYEQTEENEKRYEQLVSESDSSDGLSYTELRKKVED-KDEEYRKIVQE-GEELQKCSEERNKLQSKLNE 862
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEiQAELSKLEEEVSRIEARLRE 816
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 863 LGTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAISQKRNEDlpdaQFKKDDLTRNVSSKEEEKKKAEMEVQMMKKELD 942
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL----NGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 943 QKIFHRKSLFKKVQEgglCERQLMDKENNIATLNASLEENQQRQKRFEEDLRSFDSSHQRESILKDqltrmiIENKIKEL 1022
Cdd:TIGR02169 893 ELEAQLRELERKIEE---LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED------VQAELQRV 963
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 193208595 1023 KRTLATFdGQIN---EDRITEQKQAYNKLQNELRLIGNEEVKIYTQMQEYEKQKK 1074
Cdd:TIGR02169 964 EEEIRAL-EPVNmlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
17-112 |
3.48e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 63.88 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 17 KFLRLHIRGIRSVGDEdhdvHKIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNfihsTDVARKTRVDASVT 96
Cdd:COG0419 1 KLLRLRLENFRSYRDT----ETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLR----SDLINVGSEEASVE 72
|
90
....*....|....*.
gi 193208595 97 LEFiDVKGRECTAVRR 112
Cdd:COG0419 73 LEF-EHGGKRYRIERR 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-1114 |
7.28e-11 |
|
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: 67.00 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 257 LKERKANGQKKIEEMRTSIHELEDTLTsfkktELERQ--NLKKQLSliRVEPYFGTEEELKREIEEFRGSEGRSYGEERA 334
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILN-----ELERQlkSLERQAE--KAERYKELKAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 335 RIQKKIGKNNQERQELSQKKTEFENRISSLKAEVihcqslkYDLERLENQLRSELdlehdadidieidNAITLKIRGMSD 414
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEV-------SELEEEIEELQKEL-------------YALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 415 KARMIAKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIkqgqnatAGMKDLLKKEEALRKSLADLPL 494
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 495 LDENALTECKLKREKYLKQLDILKKKCAEAEKNAEK-DREKESLKQTLSIARKKMTAYQRiydnnwQGLIGQAPDfpwtp 573
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRERLQQEIEELLKKLEEAEL------KELQAELEE----- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 574 iLSKTFHKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLtAQELKLSENIFEACSCEAEEVSEKLENlRKRLKKA 653
Cdd:TIGR02168 445 -LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKN-QSGLSGI 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 654 RKDLAPLSAKSNLYDSYIEESKSSGCCPLCDRDFKTKKEINEFSKK------------------LENMTLSFPTEQEELE 715
Cdd:TIGR02168 522 LGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQnelgrvtflpldsikgteIQGNDREILKNIEGFL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 716 KLVSKLEKEEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEM--------------------AEEKSNLSKNEKQLET 775
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitggsAKTNSSILERRREIEE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 776 VNAKLKLAEdlqtdvgviqQLYEQTEENEKRYEQLVSESDssdglsyTELRKKVEDKDEEYRKIVQEGEELQKCSEERNK 855
Cdd:TIGR02168 682 LEEKIEELE----------EKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 856 LQSKLNELGTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAISQKRNEdlpdaqfkkddLTRNVSSKEEEKKKAEMEVQ 935
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-----------LKEELKALREALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 936 MMKKELDQKIFHRKSLFKKVQEgglCERQLMDKENNIATLNASLEENQQRQKRFEEDLRSFDSSHQRESILKDQltrmiI 1015
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-----L 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1016 ENKIKELKRTLATFDGQIN--EDRITEQKQAYNKLQNELRLIGNEEVKIytQMQEYEKQKKIAEakLSTKECQNAESNYR 1093
Cdd:TIGR02168 886 EEALALLRSELEELSEELRelESKRSELRRELEELREKLAQLELRLEGL--EVRIDNLQERLSE--EYSLTLEEAEALEN 961
|
890 900
....*....|....*....|.
gi 193208595 1094 DAIIELAITKESISDLTKYRN 1114
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIK 982
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
217-1013 |
5.12e-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: 60.90 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 217 QTHEMSKQLYET---HVRDKLVARQNQEECERKISKRKEETD---ELKERKANGQKKIE-EMRTSIHELEdTLTSFKKTE 289
Cdd:pfam15921 86 QVKDLQRRLNESnelHEKQKFYLRQSVIDLQTKLQEMQMERDamaDIRRRESQSQEDLRnQLQNTVHELE-AAKCLKEDM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 290 LERQNLK-KQLSLIRVEpYFGTEEELKREIEEFRGSEGRSYGEERARIQ---KKIGknnqerQELSQKKTEFENRISSLK 365
Cdd:pfam15921 165 LEDSNTQiEQLRKMMLS-HEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfRSLG------SAISKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 366 AEVIHCQSlkyDLERL--ENQLRSELDLEHDADIDIEIDNAITLKIRGMSDKARMIAKNCAELQSNLRTAQEAA-TKIEV 442
Cdd:pfam15921 238 GRIFPVED---QLEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 443 EMKTLQNekvkLEKEVEQLKFKIKQGQNATAgmkdllKKEEALRKSLadlpLLDENALTECKLKREKYLKQL----DILK 518
Cdd:pfam15921 315 YMRQLSD----LESTVSQLRSELREAKRMYE------DKIEELEKQL----VLANSELTEARTERDQFSQESgnldDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 519 KKCAEAEKnaekdREKEslkqtLSIARKKmtaYQRIYDNNWQGLIgqapdfpwtpilskTFHKLRndkkimeEDLRDVQL 598
Cdd:pfam15921 381 KLLADLHK-----REKE-----LSLEKEQ---NKRLWDRDTGNSI--------------TIDHLR-------RELDDRNM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 599 NVQKLETMQHQYRKQEESLTAQELKLSENIFEACsceaEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSyieeskssg 678
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLES--------- 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 679 ccplcdrdfkTKKEINEFSKKLENMTLSFPTEQEELEKLVSK--LEKEEIIIVKAEGQanelqrivkELKEVREKNRKLS 756
Cdd:pfam15921 494 ----------SERTVSDLTASLQEKERAIEATNAEITKLRSRvdLKLQELQHLKNEGD---------HLRNVQTECEALK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 757 TEMAEEKSNLSKNEKQLETVnakLKLAEDLQTDVGVIQQLYEQTEE--NEKRYE--QLVSESDSSDGlSYTELRKKVEDK 832
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENM---TQLVGQHGRTAGAMQVEKAQLEKeiNDRRLElqEFKILKDKKDA-KIRELEARVSDL 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 833 DEEYRKIVQEGEE----LQKCSEERNKLqskLNELGTHRVSLGEAAAQAGAFAEQLETKIKEIQecitAISQKRNEDLPD 908
Cdd:pfam15921 631 ELEKVKLVNAGSErlraVKDIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME----TTTNKLKMQLKS 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 909 AQFKKDDlTRNVSSKEEEKKKAEMEVQM-MKKELDQKIFHRKSLFKKVQ--EGGLC----ERQLMDKENNiaTLNASLEE 981
Cdd:pfam15921 704 AQSELEQ-TRNTLKSMEGSDGHAMKVAMgMQKQITAKRGQIDALQSKIQflEEAMTnankEKHFLKEEKN--KLSQELST 780
|
810 820 830
....*....|....*....|....*....|..
gi 193208595 982 NQQRQKRFEEDLRSFDSSHQResiLKDQLTRM 1013
Cdd:pfam15921 781 VATEKNKMAGELEVLRSQERR---LKEKVANM 809
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-863 |
9.42e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 245 RKISKRKEETDELKERKANGQKKIEEMRTSIHELEDTLTsfkKTELERQNLKKQLSLirvepyfgteeelkreieefRGS 324
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEE--------------------AQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 325 EGRSYGEERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEVIhcqslkydlERLENQLRSELDLEHDADIDIEIDNA 404
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE---------ELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 405 ITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKEEA 484
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 485 LRKSLADLPLLDENALTEcklkREKYLKQLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAYQRIYDNNWQGLIG 564
Cdd:COG1196 440 EEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 565 QapdfPWTPILSKTFHKLRNDKKIMEEDLRDVQLNVqkletMQHQYRKQEESLTAQELKLSENIFEACSCEAEEVSEKLE 644
Cdd:COG1196 516 L----AGLRGLAGAVAVLIGVEAAYEAALEAALAAA-----LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 645 NLRKRLKKARKDLAPLSAKSNLYDSYIEESKSSGCCPLCDRDFKTKKEINEFSKKLENMTLSFPTEQEELEKLVSKLEKE 724
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 725 EIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDVGVIQQLYEQTEENE 804
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193208595 805 KRYEQLVSESDssDGLSYTELRKKVEDKDEEYRKIvqeG-------EELQKCSEERNKLQSKLNEL 863
Cdd:COG1196 747 LLEEEALEELP--EPPDLEELERELERLEREIEAL---GpvnllaiEEYEELEERYDFLSEQREDL 807
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
238-1084 |
7.14e-08 |
|
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: 57.29 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 238 QNQEECERKISKRKEETDELKERKANGQKKIEEMRTSIHELEDTLTSFKKTE--LERQNLKKQlslirvepyfgteEELK 315
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQElkLKEQAKKAL-------------EYYQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 316 REIEEFRGSEGRSYGEERARIQKKIgKNNQERQELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDLEHDA 395
Cdd:pfam02463 215 LKEKLELEEEYLLYLDYLKLNEERI-DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 396 DIDIEIDNAITLKIRGMSDKarmiaKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQgqnatagM 475
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDE-----EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE-------L 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 476 KDLLKKEEALRKSLADLPLLDENALTECKLKREKYLKQLDILKKKCAEAEKNAEK-----DREKESLKQTLSIARKKMTA 550
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQledllKEEKKEELEILEEEEESIEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 551 YQRIYDNNWQGLIGQAPDFP-WTPILSKTFHKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLtAQELKLSENIF 629
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLkDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL-KVLLALIKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 630 EACSCEAEEVSEKLENLrKRLKKARKDLAPLSAKSNLYDSYIEESKSSGCCPLCDRDFKTKKEINEFSKKLENmtlSFPT 709
Cdd:pfam02463 521 GGRIISAHGRLGDLGVA-VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK---SIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 710 EQEELEKLVSKLEKEEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMaEEKSNLSKNEKQLETVNAKLKLAEDLQTD 789
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES-GLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 790 VGVIQQLYEQTEENEKRYEQLVSESDSSDGLSYTELRKKVEDKDEEyRKIVQEGEELQKCSEERNKLQSKLNELGTHRVS 869
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE-LLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 870 LGEAAAQAGAFAEQLETKIKEIQECITAISQKRNEDLPDAQFKKDDLTRNVSSKEEEKKKAEMEVQMMKKELDQKIFHRK 949
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 950 SLFKKVQEGGLCERQLMDKENNIaTLNASLEENQQRQKRFEEDLRSFDSSHQRESILKDQLTRMIIENKIKELKRTLATF 1029
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELE-RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 193208595 1030 DGQINEDRITEQKQAYNKLQNEL--RLIGNEEVKIYTQMQEYEKQKKIAEAKLSTKE 1084
Cdd:pfam02463 914 EKENEIEERIKEEAEILLKYEEEpeELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-1272 |
1.20e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 710 EQEELEKLVSKLEKEEIIIVKAEGQANELQRIVKELKEVREkNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQtd 789
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRELE-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 790 vgviQQLYEQTEENEKRYEQLVSESDSSDGLSYTELRKKVEDKDEEYRKIVQEGEELQKCSEERNKLQSKLNELGTHRVS 869
Cdd:COG4717 163 ----EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 870 LGEAAAQAGAF---------------AEQLETKIKEIQECITAI---------SQKRNEDLPDAQFKKDDLTRNVSSKEE 925
Cdd:COG4717 239 AALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVlgllallflLLAREKASLGKEAEELQALPALEELEE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 926 EKKKAEMEVQMMKKELDQKIFhrKSLFKKVQEGGLCERQLMDKENNIAtLNASLEENQQRQKRF----EEDLRSFDSSHQ 1001
Cdd:COG4717 319 EELEELLAALGLPPDLSPEEL--LELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAgvedEEELRAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1002 RESILKDQLT--RMIIENKIKELKRTLATFDGQINEDRITEQKQAYNKLQNELRLIGNEEVKIYTQMQEYEKQKKIAEAK 1079
Cdd:COG4717 396 EYQELKEELEelEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1080 LSTKECQNAESNYRDAIIELAITKESISDLTKYrncldasliqFHSEKMGRVNGIIDDLWRKvynstdITTIRIRSDATS 1159
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLALELLEEAREE----------YREERLPPVLERASEYFSR------LTDGRYRLIRID 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1160 EtsskkvayEYNVMMVHETGTEVEMRgRCSAGQKMLASLLIRIALAEVFGGSCSMIALDEPTTNLDESKVEGMAIVLADI 1239
Cdd:COG4717 540 E--------DLSLKVDTEDGRTRPVE-ELSRGTREQLYLALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAEL 610
|
570 580 590
....*....|....*....|....*....|...
gi 193208595 1240 iaerrgfdengklrGRDMQMVVITHDERLVNRI 1272
Cdd:COG4717 611 --------------AKGRQVIYFTCHEELVELF 629
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-892 |
3.38e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 374 LKYDLERLENQLRSELDLEHDADIDIEIDNAITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATKIEvemkTLQNEKVK 453
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 454 LEKEVEQLKFKIKQGQNataGMKDLLKKEEALRKSLADLPLLDENALTECKLKR----------------EKYLKQLDIL 517
Cdd:PRK03918 250 LEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeeyldelreiekrlSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 518 KKKCAEAEKNAEKDRE----KESLKQTLSIARKKMTAYQRIYD--NNWQGLIGQAPDFPWTPIlSKTFHKLRNDKKIMEE 591
Cdd:PRK03918 327 EERIKELEEKEERLEElkkkLKELEKRLEELEERHELYEEAKAkkEELERLKKRLTGLTPEKL-EKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 592 DLRDVQLNVQKLETmqhqyRKQEESLTAQELKLSENIFEACSCEAEEVSEK--LENLRKRLKKARKDLAPLSAK-SNLYD 668
Cdd:PRK03918 406 EISKITARIGELKK-----EIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKeRKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 669 SYIEESKSSGCCPLCDRDFKTKKEINEFSKKLENMTLsfpteqEELEKLVSKLEKEEIIIVKAEGQANELQRIVKELKEV 748
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL------EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 749 REKNRKLSTEMAEEKSNLSKNEKQLEtvNAKLKLAEDLQTDVGVIQQLYE----------QTEENEKRYEQLVSE-SDSS 817
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELE--ELGFESVEELEERLKELEPFYNeylelkdaekELEREEKELKKLEEElDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 818 DGLSYT-----ELRKKVEDK-----DEEYRKIVQEGEELqkcSEERNKLQSKLNELGTHRVSLGEAAAQAGAFAEQLETK 887
Cdd:PRK03918 633 EELAETekrleELRKELEELekkysEEEYEELREEYLEL---SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
....*
gi 193208595 888 IKEIQ 892
Cdd:PRK03918 710 KKELE 714
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
581-918 |
3.42e-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: 55.06 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 581 KLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQE------LKLSENIFEA----CSCEAEEVSEKLENLRKRL 650
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAekaeryKELKAELRELelalLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 651 KKARKDLAPLSAKSNLYDSYIEESKssgccplcDRDFKTKKEINEFSKKLENmtlsfpteqeeLEKLVSKLEKEEIIIVK 730
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELR--------LEVSELEEEIEELQKELYA-----------LANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 731 aegQANELQRIVKELKEVREKNRKLSTEMAEEksnLSKNEKQLETVNAKLK-LAEDLQTDVGVIQQLYEQTEENEKRYEQ 809
Cdd:TIGR02168 310 ---RLANLERQLEELEAQLEELESKLDELAEE---LAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 810 LVSESDS------SDGLSYTELRKKVEDKDEEYRKIVQEGEELQKCSEE--RNKLQSKLNELGTHRVSLGEAAAQAGAFA 881
Cdd:TIGR02168 384 LRSKVAQlelqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEAL 463
|
330 340 350
....*....|....*....|....*....|....*..
gi 193208595 882 EQLETKIKEIQECItaisQKRNEDLPDAQFKKDDLTR 918
Cdd:TIGR02168 464 EELREELEEAEQAL----DAAERELAQLQARLDSLER 496
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
20-99 |
6.03e-07 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 51.31 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 20 RLHIRGIRSVGDEDhdvhKIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQ----MPTQKKQNFIHSTDVARKTRVDASV 95
Cdd:cd03278 3 KLELKGFKSFADKT----TIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQsaksLRGEKMSDVIFAGSETRKPANFAEV 78
|
....
gi 193208595 96 TLEF 99
Cdd:cd03278 79 TLTF 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1184-1271 |
6.66e-07 |
|
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: 50.44 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1184 MRGRCSAGQKMLASLLIRIALAEVfgGSCSMIALDEPTTNLDESKVEGmaivLADIIAERRGfdengklrgRDMQMVVIT 1263
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASL--KPRPLYILDEIDRGLDPRDGQA----LAEAILEHLV---------KGAQVIVIT 138
|
....*...
gi 193208595 1264 HDERLVNR 1271
Cdd:cd03227 139 HLPELAEL 146
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
23-785 |
1.73e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 23 IRGIRSVGDEDHDVHKIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNFIhstdvaRKTRVDASVTLEFidV 102
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEKIEDMI------KKGKNNLEVELEF--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 103 KGRECTAVRRLVVTSGTKAAALAEehtlaIKYpDGTVntLSSKVCDFNTALLKH-LGVPRAVFKYVIFCHQEDSTWPLS- 180
Cdd:PRK01156 75 IGGHVYQIRRSIERRGKGSRREAY-----IKK-DGSI--IAEGFDDTTKYIEKNiLGISKDVFLNSIFVGQGEMDSLISg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 181 EPKELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEMQTHEmskqlyetHVRDKLVARQNQeecerkISKRKEETDELKER 260
Cdd:PRK01156 147 DPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNID--------YLEEKLKSSNLE------LENIKKQIADDEKS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 261 KANGQKKIEEMRTSIHELEDTLTSFKKTelerqnLKKQLSLIrvepyfgteeelkreieefrgSEGRSYGEERARIQKKI 340
Cdd:PRK01156 213 HSITLKEIERLSIEYNNAMDDYNNLKSA------LNELSSLE---------------------DMKNRYESEIKTAESDL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 341 GKNNQERQELSQkKTEFENRISSLKAEVihcqslkydlerLENQLRSELDLEHdadiDIEIDNAITLKIRGMSDKARMIA 420
Cdd:PRK01156 266 SMELEKNNYYKE-LEERHMKIINDPVYK------------NRNYINDYFKYKN----DIENKKQILSNIDAEINKYHAII 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 421 KNCAELQSNLRtaqeaatkievEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKEEALRKSLADLPLLDENAL 500
Cdd:PRK01156 329 KKLSVLQKDYN-----------DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 501 TECKLKREKYLKQLDILKKKCAEAE-KNAEKDREKESLKQTLSIARKKMTAYqriydnNWQGLIGQAPDFPWTPILSKTF 579
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISsKVSSLNQRIRALRENLDELSRNMEML------NGQSVCPVCGTTLGEEKSNHII 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 580 HKLRNDKKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSENIFeacsceaeevsEKLENLRKRLKKARKDLAP 659
Cdd:PRK01156 472 NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY-----------NKIESARADLEDIKIKINE 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 660 LSAKSNLYDSYIEESKSSGCCPLCDR--------------DFKT--------KKEINEFSKKLENMTLSFPTEQEELEKL 717
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKrtswlnalavisliDIETnrsrsneiKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193208595 718 VSKLEKEeiiIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSnlskNEKQLETVNAKLKLAED 785
Cdd:PRK01156 621 IREIENE---ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS----IIPDLKEITSRINDIED 681
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
591-1120 |
2.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 591 EDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSENIFEAcSCEAEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSY 670
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 671 IEESKSSGccplcdrdfKTKKEINEFSKKLENMTLSFPTEQEELEKLVSKLEKEEIIIVKAEGQANELQRIVKELKEVRE 750
Cdd:PRK03918 237 KEEIEELE---------KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 751 KNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDVGVIQQLYEQTEENEKRYEQLVSESDSSDGLSYTELRKKVE 830
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 831 DKDEEYRKIVQEGEELQkcsEERNKLQSKLNELGTHRVSLGEAAAQAGAFAEQL--------ETKIKEIQECITAISQKR 902
Cdd:PRK03918 388 KLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 903 NEDLPDAQFKKDDLtRNVSSKEEEKKKAEMEVQMMKKELDQ--------KIFHRKSLFKKVQEGGLCERQLMDKENNIAT 974
Cdd:PRK03918 465 EKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQlkeleeklKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 975 LNASLEENQQRQKRFEEDLRSFDSSHQRESILKDQLTRM------IIENKIKELKRTLATFDGQIN-EDRITEQKQAYNK 1047
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveELEERLKELEPFYNEYLELKDaEKELEREEKELKK 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193208595 1048 LQNELRLIGNEEVKIYTQMQEYEKQKKIAEAKLSTKECQNAESNYRDAIIELAITKESISDLTKYRNCLDASL 1120
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
256-535 |
3.67e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 256 ELKERKANGQKKIEEMRTSIHELEDTLTsfkktELERQ---------------NLKKQLSLIRVEpyfgteeelkreiee 320
Cdd:COG1196 169 KYKERKEEAERKLEATEENLERLEDILG-----ELERQleplerqaekaeryrELKEELKELEAE--------------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 321 FRGSEGRSYGEERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEvihcqslkydLERLENQLRSELDLEHDADIDIE 400
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------LEELELELEEAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 401 idnAITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLK 480
Cdd:COG1196 299 ---RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 193208595 481 KEEALRKSLADLPLLDENALTECKLKREKYLKQLDILKKKCAEAEKNAEKDREKE 535
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
39-1077 |
1.12e-05 |
|
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: 49.97 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 39 IDFLSPCTLISGPNGTGKTTTIEALNFV----TTGQMPTQKKQNFIHSTDVARKTRvdASVTLEF-----IDVKGRECTA 109
Cdd:pfam02463 19 LPFSPGFTAIVGPNGSGKSNILDAILFVlgerSAKSLRSERLSDLIHSKSGAFVNS--AEVEITFdnedhELPIDKEEVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 110 VRRLVVTSGTkaaalaeehtlaikypdgTVNTLSSKVCDFN--TALLKHLGVPRAVFKYVIFchQEDSTWPLSEPKELKK 187
Cdd:pfam02463 97 IRRRVYRGGD------------------SEYYINGKNVTKKevAELLESQGISPEAYNFLVQ--GGKIEIIAMMKPERRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 188 RFDDIFQLTKFVKAqermkkivldfKKEMQTHEMSKQLYETHVRDKLVARQNQEECERKISKRKEETDELKERKANGQKK 267
Cdd:pfam02463 157 EIEEEAAGSRLKRK-----------KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 268 IEEMRTSIHELEDTLTSFKKTELERQNLKKQLSLIRVEpyfgteeelkREIEEFRGSEGRSYGEERARIQKKIGKNNQER 347
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKE----------EEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 348 QELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSEldLEHDADIDIEIDNAITLKIRGMSDKARMIAKNCAELQ 427
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE--IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 428 SNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKEEALRKSLADLPLLDENALTECKLKR 507
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 508 EKY--LKQLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAYQRIYDNNWQGLIGQAPDFPWTPILSKTFHKLRND 585
Cdd:pfam02463 454 EKQelKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 586 KKIMEEDLRDVQLNVQKLETMqhqyRKQEESLTAQELKLSENIFEACSCEAEEVSEKLENLRKRLKKARKDLAPLSAKSN 665
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVS----ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 666 LYDSYIEESKSSGCCPLCDRDFKTKKEINEFSKKLEnMTLSFPTEQEELEKLVSKLEKEEIIIVKAEGQANELQRIVK-E 744
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE-SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAEsE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 745 LKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDVGVIQQLYEQT------EENEKRYEQLVSESDSSD 818
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKideeeeEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 819 GLSYTELRKKVEDKDEEYRKIVQEGEELQKCSEERNKLQSKLNELGTHrvsLGEAAAQAGAFAEQLETKIKEIQECITAI 898
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEL---LEEEQLLIEQEEKIKEEELEELALELKEE 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 899 SQKRNEDLPDAQFKKDDLTRNVSSKEEEKKKAEMEVQMMKKELDQKIFHRKSLFKKVQEGGLCERQLMDKENNIATLNAS 978
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 979 LEENQQRQKRFEEDLRSFDSSHQRESILKDQLTRmiIENKIKELKRTLATFDGQINEDRITEQKQAYNKLQNELRLIGNE 1058
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
1050
....*....|....*....
gi 193208595 1059 EVKIYTQMQEYEKQKKIAE 1077
Cdd:pfam02463 1004 KKKLIRAIIEETCQRLKEF 1022
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
595-834 |
1.27e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 595 DVQLNV--QKLETmQHQYRKQEESLTAQELKLSENIFEACSCEAEEVSEKLENLRKR--------------LKKARKDLA 658
Cdd:PHA02562 187 DMKIDHiqQQIKT-YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEllnlvmdiedpsaaLNKLNTAAA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 659 PLSAKSNLYDSYIEESKSSGCCPLCDRDFKTKKE-INEFSKKLENMTLsfpteqeeleklvsKLEKEEIIIVKAEGQANE 737
Cdd:PHA02562 266 KIKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDrITKIKDKLKELQH--------------SLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 738 LQRIVKELKEVreknrklstemaeeKSNLSKNEKQLETVNAKLKLAEDlqtdvgVIQQLYEQTEENEKRYEQLVSESDSS 817
Cdd:PHA02562 332 FNEQSKKLLEL--------------KNKISTNKQSLITLVDKAKKVKA------AIEELQAEFVDNAEELAKLQDELDKI 391
|
250
....*....|....*..
gi 193208595 818 DglsyTELRKKVEDKDE 834
Cdd:PHA02562 392 V----KTKSELVKEKYH 404
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
635-1226 |
1.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 635 EAEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEESKSsgccplcdrDFKTKKEINEFSKKLENMTLSFPTEQEEL 714
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK---------EIEELEEKVKELKELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 715 EKLVSKLEKEEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAE---EKSNLSKNEKQLETVNAKLKLAEDLQTDVG 791
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 792 V--IQQLYEQTEENEKRYEQlVSESDSSDGLSYTELRKKVEDK---------------------DEEYRK--IVQEGEEL 846
Cdd:PRK03918 383 GltPEKLEKELEELEKAKEE-IEEEISKITARIGELKKEIKELkkaieelkkakgkcpvcgrelTEEHRKelLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 847 QKCSEERNKLQSKLNELGTHRVSLGEAAAQAGAFaeqleTKIKEIQECITAISQKRNEDLPDAQFKKDDLTRNVSSKEEE 926
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 927 KKKAEMEVQMMKKELDQKIFHRKSLFKKVQEgglCERQLMDKENNIATLN-ASLEENQQRQKRFEEDLRSF----DSSHQ 1001
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDE---LEEELAELLKELEELGfESVEELEERLKELEPFYNEYlelkDAEKE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1002 RESILKDQ-LTRMIIENKIKELKRTLATFD---GQINEDRITEQKQAYNKLQNELRLIGNEEVKIYTQMQEYEKQKKiaE 1077
Cdd:PRK03918 614 LEREEKELkKLEEELDKAFEELAETEKRLEelrKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRRE--E 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1078 AKLSTKECQNAESNYRDAIIELAITKESISDLTKYRNCLDASLIQFHSEKMGRVNGIIDDLWRKVynsTDITTIRIRSDA 1157
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEEL---TEGKYSGVRVKA 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193208595 1158 TSETSSKKVAYEynvmmvhetGTEVEMrGRCSAGQKMLASLLIRIALAEVFGGSCSMIALDEPTTNLDE 1226
Cdd:PRK03918 769 EENKVKLFVVYQ---------GKERPL-TFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLDE 827
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-780 |
2.00e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 352 QKKTEFENRISSLKAEVIHCQ------SLKYDLERLENqlRSELDlEHDADIDieidnAITLKIRGMSDKARMIAKNCAE 425
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILER--RREIE-ELEEKIE-----ELEEKIAELEKALAELRKELEE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 426 LQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNAtagMKDLLKKEEALRKSLADLplldENALTECKL 505
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE---LTELEAEIEELEERLEEA----EEELAEAEA 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 506 KREKYLKQLDILKkkcaeaeknaekdREKESLKQTLSIARKKMTAYQRIYDNNWQGLIGQAPDfpwTPILSKTFHKLRND 585
Cdd:TIGR02168 783 EIEELEAQIEQLK-------------EELKALREALDELRAELTLLNEEAANLRERLESLERR---IAATERRLEDLEEQ 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 586 KKIMEEDLRDVQLNVQKLETMQHQYRKQEESLTAQELKLSENIFEACScEAEEVSEKLENLRKRLKKARKDLAPLSAKSN 665
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS-ELEELSEELRELESKRSELRRELEELREKLA 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 666 LYDSYIEeskssgccplcdrdfKTKKEINEFSKKLENmtlSFPTEQEELEKLVSKLEKEEiiiVKAEGQANELQRIVKEL 745
Cdd:TIGR02168 926 QLELRLE---------------GLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDE---EEARRRLKRLENKIKEL 984
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 193208595 746 KEV---------REKNRKlsTEMAEEKSNLSKNEKQLETVNAKL 780
Cdd:TIGR02168 985 GPVnlaaieeyeELKERY--DFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
689-1240 |
2.94e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 689 TKKEINEFSKKLENMTLSFPTEQEELEKLVSKLE---KEEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSN 765
Cdd:PRK01156 216 TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmknRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 766 -----------LSKNEKQLETVNAKLKLAEDLQTDVGVIQQLYEQTEENEKRYEQLVSESDSSDGL---------SYTEL 825
Cdd:PRK01156 296 yindyfkykndIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYemdynsylkSIESL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 826 RKKVEDKDEEYRKIVQEGEELQKCSE--------ERNKLQSKLNELGTHRVSLGEAAAQagafaeqLETKIKEIQECITA 897
Cdd:PRK01156 376 KKKIEEYSKNIERMSAFISEILKIQEidpdaikkELNEINVKLQDISSKVSSLNQRIRA-------LRENLDELSRNMEM 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 898 ISQKR-----NEDLPDAqfKKDDLTRNVSSKEEEKKKAEMEVQMMKKELDQKIFHRKSLFKKVQEGGL------------ 960
Cdd:PRK01156 449 LNGQSvcpvcGTTLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEInksineynkies 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 961 CERQLMDKENNIATLNASLEENQQRQKRFE----EDLRSFDSSH-----QRESI---------------LKDQLTRM--- 1013
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYKslklEDLDSKRTSWlnalaVISLIdietnrsrsneikkqLNDLESRLqei 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1014 ---------IIENKIKELKRTLATFDGQINEdrITEQKQAYNKLQNELRLIGNEEVKiytqMQEYEKQKKIAEAKLSTKE 1084
Cdd:PRK01156 607 eigfpddksYIDKSIREIENEANNLNNKYNE--IQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1085 --CQNAESNYRDAIIELAITKESISDLTKYRNCLDASL--IQFHSEKMGRVNGIIDDLwRKVYNSTDITTIR--IRSDAT 1158
Cdd:PRK01156 681 dnLKKSRKALDDAKANRARLESTIEILRTRINELSDRIndINETLESMKKIKKAIGDL-KRLREAFDKSGVPamIRKSAS 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1159 SETSSKKVAY---------------EYNVMMVHetGTEVEMRGRCSAGQKMLASLLIRIALAEVFGGSCSMIALDEPTTN 1223
Cdd:PRK01156 760 QAMTSLTRKYlfefnldfddidvdqDFNITVSR--GGMVEGIDSLSGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAF 837
|
650
....*....|....*..
gi 193208595 1224 LDESKVEGmaivLADII 1240
Cdd:PRK01156 838 LDEDRRTN----LKDII 850
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1186-1269 |
3.03e-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: 46.32 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1186 GRCSAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDESKVEgmaiVLADIIAERRGfdengklRGRdmqMVVI-TH 1264
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVA----LLAELIAAHLA-------RGG---AVLLtTH 189
|
....*
gi 193208595 1265 DERLV 1269
Cdd:COG4133 190 QPLEL 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1189-1272 |
4.30e-05 |
|
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: 45.31 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDESkvegMAIVLADIIAErrgfdengkLRGRDMQMVVITHDERL 1268
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPA----SRERLLELLRE---------LAEEGRTVIIVTHDPEL 142
|
....
gi 193208595 1269 VNRI 1272
Cdd:cd00267 143 AELA 146
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1168-1232 |
4.99e-05 |
|
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: 43.38 E-value: 4.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193208595 1168 YEYNVMMVHETGTEVE---MRGRCSAGQK-MLASLLIRIALAEVFGG------SCSMIALDEPTTNLDESKVEGM 1232
Cdd:pfam13558 10 LSFEVEVRDEDGSEVEtyrRSGGLSGGEKqLLAYLPLAAALAAQYGSaegrppAPRLVFLDEAFAKLDEENIRTA 84
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
583-1087 |
5.11e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 583 RNDKKIMEEDLRDVQLNVQKLET----MQHQYRKQEESLTAQELKLSENIFEAcSCEAEEVSEKLENLRKRLKKARKDLA 658
Cdd:pfam15921 309 RNQNSMYMRQLSDLESTVSQLRSelreAKRMYEDKIEELEKQLVLANSELTEA-RTERDQFSQESGNLDDQLQKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 659 PLSAKSNLYDsyiEESKSsgccpLCDRDFKTKKEINEFSKKLENMTLsfptEQEELEKLVSKLEKEeiiivkAEGQANEL 738
Cdd:pfam15921 388 KREKELSLEK---EQNKR-----LWDRDTGNSITIDHLRRELDDRNM----EVQRLEALLKAMKSE------CQGQMERQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 739 QRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDvgviqqLYEQTEENEKRYEQLVSEsdssd 818
Cdd:pfam15921 450 MAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD------LTASLQEKERAIEATNAE----- 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 819 glsYTELRKKVEDKDEEYRKIVQEGEELQKCSEE------------------RNKLQSKLNELGTHRVSLGEAAAQAGAF 880
Cdd:pfam15921 519 ---ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieilRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 881 AEQLETKIKEIQEcITAISQKRNEDLPDAQFKKDDLTRNVSSKEEEKKKAEMEVQMMKKELDQKIFH----RKSLFKKVQ 956
Cdd:pfam15921 596 EKEINDRRLELQE-FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSE 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 957 EGGLCERQLMDKENNIAT----LNASLEENQQRQKRFEEDLRSFDSSHQRESILKDQLTRMI---------IENKIKELK 1023
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLE 754
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193208595 1024 RTLATFDGQinEDRITEQKqayNKLQNELRLIGNEEVKIYTQM-----QEYEKQKKIA-------EAKLSTKECQN 1087
Cdd:pfam15921 755 EAMTNANKE--KHFLKEEK---NKLSQELSTVATEKNKMAGELevlrsQERRLKEKVAnmevaldKASLQFAECQD 825
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-100 |
6.08e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 20 RLHIRGIRSVGDEDhdvhKIDFLSP-CTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNFIHSTDVArktrvdASVTLE 98
Cdd:cd03227 1 KIVLGRFPSYFVPN----DVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIV------AAVSAE 70
|
..
gi 193208595 99 FI 100
Cdd:cd03227 71 LI 72
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
17-847 |
6.62e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 17 KFLRLHIRGIRSVGDEDhdvhkIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNfihstDVARKTRVDASVT 96
Cdd:PRK02224 2 RFDRVRLENFKCYADAD-----LRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLD-----DVITIGAEEAEIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 97 LEFIDVkGRECTAVRRLVVTSGTkaaalAEEHTLAIKYPDGTVNTlSSKVCDFNTALLKhlgVPRAVFKYVIFCHQ-EDS 175
Cdd:PRK02224 72 LWFEHA-GGEYHIERRVRLSGDR-----ATTAKCVLETPEGTIDG-ARDVREEVTELLR---MDAEAFVNCAYVRQgEVN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 176 TWPLSEPKELKKRFDDIFQLTKFVKAQERM-------------KKIVLDFKKEMQTHEMSKQLYETHVRDKLVARQNQEE 242
Cdd:PRK02224 142 KLINATPSDRQDMIDDLLQLGKLEEYRERAsdarlgvervlsdQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 243 CERKISKR------KEETDELKERKANGQKKIEEMRTSIHELEDTLTSfkkTELERQNLKKQLSLIRvepyfgteeelkr 316
Cdd:PRK02224 222 IERYEEQReqaretRDEADEVLEEHEERREELETLEAEIEDLRETIAE---TEREREELAEEVRDLR------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 317 eieefrgSEGRSYGEERARIQKKIGKNNQERQELSQKKTEFENRISSLKaevihcqslkydlERLENQLRSELDLEHDAD 396
Cdd:PRK02224 286 -------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR-------------DRLEECRVAAQAHNEEAE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 397 idieidnaitlkirgmsdkarmiakncaelqsnlrTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAgmk 476
Cdd:PRK02224 346 -----------------------------------SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE--- 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 477 DLLKKEEALRKSLADLPLLDENAltecklkrEKYLKQLdilkkkcaEAEKNAEKDREKEsLKQTLSIARKKMTAYQRIYD 556
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNA--------EDFLEEL--------REERDELREREAE-LEATLRTARERVEEAEALLE 450
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 557 NNWQGLIGQapDFPWTPILSkTFHKLRNDKKIMEEDLRDVQLNVQKLEtmqhqyrkqEESLTAQELKLSENIFEACSCEA 636
Cdd:PRK02224 451 AGKCPECGQ--PVEGSPHVE-TIEEDRERVEELEAELEDLEEEVEEVE---------ERLERAEDLVEAEDRIERLEERR 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 637 EEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEEsKSSGCCPLCDRDFKTKKEINEFSKKLENMTlsfpTEQEELEK 716
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEAEE-KREAAAEAEEEAEEAREEVAELNSKLAELK----ERIESLER 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 717 LVSKLEKeeiiIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSK--NEKQLETVNAKLKLAEDLQTDV-GVI 793
Cdd:PRK02224 594 IRTLLAA----IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefDEARIEEAREDKERAEEYLEQVeEKL 669
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 193208595 794 QQLYEQTEENEKRYEQLVSESDSSDGLSytELRKKVEDKDEEYRKIVQEGEELQ 847
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEELEELR--ERREALENRVEALEALYDEAEELE 721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
508-902 |
7.58e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 508 EKYLKQLDILKKKCAEA-EKNAEKDREKESLKQTLSIARKkmtAYQRIYDNNWQGLIGQAPDFPWTPILSKTFHKLRNDK 586
Cdd:PRK02224 247 EERREELETLEAEIEDLrETIAETEREREELAEEVRDLRE---RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 587 KIMEEDLRDVQLNVQkletmqhQYRKQEESLTAQELKLSEnifeacscEAEEVSEKLENLRKRLKKARKDLAPLSAKSNL 666
Cdd:PRK02224 324 EELRDRLEECRVAAQ-------AHNEEAESLREDADDLEE--------RAEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 667 YDSYIEEskssgccpLCDRDFKTKKEINEFSKKLENMTLSFPTEQEELEKLVSKLEKEEIIIVKAE-----------GQA 735
Cdd:PRK02224 389 LEEEIEE--------LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecGQP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 736 NELQRIVKELKEVREKNRKLSTEMAEEKSnlsknekQLETVNAKLKLAEDLQTDVGVIQQLYEQTEENEKRYEQLVSESD 815
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEE-------EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 816 sSDGLSYTELRKKVEDKD---EEYRKIVQEG-EELQKCSEERNKLQSKLNELGTHRVSLgeaaaqagafaEQLETKIKEI 891
Cdd:PRK02224 534 -EKRERAEELRERAAELEaeaEEKREAAAEAeEEAEEAREEVAELNSKLAELKERIESL-----------ERIRTLLAAI 601
|
410
....*....|.
gi 193208595 892 QECITAISQKR 902
Cdd:PRK02224 602 ADAEDEIERLR 612
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
35-119 |
1.22e-04 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 45.26 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 35 DVHKIDFLSPCTLISGPNGTGKTTTIEALNFV---TTGQMPTQKKQNFIHSTDVARKTRVDASVTLEFIDVKGREcTAVR 111
Cdd:cd03275 14 GRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVlgeKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAVYEDDDGEE-KTFR 92
|
....*...
gi 193208595 112 RLVVTSGT 119
Cdd:cd03275 93 RIITGGSS 100
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
660-711 |
1.45e-04 |
|
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: 40.64 E-value: 1.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 193208595 660 LSAKSNLYDSYIEESKSS-GCCPLCDRDFKTKKeINEFSKKLENMTLSFPTEQ 711
Cdd:pfam04423 1 LHQETLELNKKIEELKEAeGCCPLCGRPLDEEH-RSELIKELQSKLERLPEEL 52
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1189-1273 |
1.49e-04 |
|
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: 43.21 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDESKVEgmaiVLADIIAERRGfdengklrgrdmQMVVITHDERL 1268
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIE----ALEEALKEYPG------------TVILVSHDRYF 129
|
....*
gi 193208595 1269 VNRIT 1273
Cdd:cd03221 130 LDQVA 134
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1175-1270 |
1.97e-04 |
|
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: 45.51 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1175 VHET------G--TEVEMRGRC-SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDEskvEGMAiVLADIIAErrg 1245
Cdd:COG4618 446 VHEMilrlpdGydTRIGEGGARlSGGQRQ------RIGLARALYGDPRLVVLDEPNSNLDD---EGEA-ALAAAIRA--- 512
|
90 100
....*....|....*....|....*
gi 193208595 1246 fdengkLRGRDMQMVVITHDERLVN 1270
Cdd:COG4618 513 ------LKARGATVVVITHRPSLLA 531
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
611-863 |
1.99e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 611 RKQEESLTA-QELklseNIFEACSCEAEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEESKSsgccplcdrdfKT 689
Cdd:PRK05771 16 SYKDEVLEAlHEL----GVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKK-----------VS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 690 KKEINEFSKKLENmtlsfptEQEELEKLVSKLEKEeiiIVKAEgqaNELQRIVKELKEVrEKNRKLSTEMAEEKSnlSKN 769
Cdd:PRK05771 81 VKSLEELIKDVEE-------ELEKIEKEIKELEEE---ISELE---NEIKELEQEIERL-EPWGNFDLDLSLLLG--FKY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 770 EKQ-LETVNAKLKLAEDLQTDVGViqqLYEQTEENEKRYEQLVSESDSSDGLsYTELRK------KVEDK---DEEYRKI 839
Cdd:PRK05771 145 VSVfVGTVPEDKLEELKLESDVEN---VEYISTDKGYVYVVVVVLKELSDEV-EEELKKlgferlELEEEgtpSELIREI 220
|
250 260
....*....|....*....|....
gi 193208595 840 VQEGEELQKcseERNKLQSKLNEL 863
Cdd:PRK05771 221 KEELEEIEK---ERESLLEELKEL 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1173-1274 |
2.18e-04 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 44.12 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1173 MMVHETGTEVemrgrcSAGQKMLasllirIALAEVFGGSCSMIALDEPTTNLDESkvegmaivladiiAERRgFDENGKL 1252
Cdd:cd03245 132 LQIGERGRGL------SGGQRQA------VALARALLNDPPILLLDEPTSAMDMN-------------SEER-LKERLRQ 185
|
90 100
....*....|....*....|....*
gi 193208595 1253 RGRDMQMVVITHDER---LVNRITI 1274
Cdd:cd03245 186 LLGDKTLIIITHRPSlldLVDRIIV 210
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
691-1009 |
2.21e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 691 KEINEFSKKLENMTLSFpTEQEELEKLVSKLEKEEIIIV------KAEGQANELQRIVKELKEVREKNRKLSTEMAEEKS 764
Cdd:COG5022 835 TEEVEFSLKAEVLIQKF-GRSLKAKKRFSLLKKETIYLQsaqrveLAERQLQELKIDVKSISSLKLVNLELESEIIELKK 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 765 NLSKNE-KQLETVNAKLKLAEDL----QTDVGVIQQLYEQTEENEkryeqLVSESdssdglsyTELRKKVEDKDEEYRKI 839
Cdd:COG5022 914 SLSSDLiENLEFKTELIARLKKLlnniDLEEGPSIEYVKLPELNK-----LHEVE--------SKLKETSEEYEDLLKKS 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 840 VQEGEELQKCSEERNKLQSKLNELGTHRVSLgeaaaqaGAFAEQLETKIKEIQECITAISQKRNEDLPDAQFKK-DDLTR 918
Cdd:COG5022 981 TILVREGNKANSELKNFKKELAELSKQYGAL-------QESTKQLKELPVEVAELQSASKIISSESTELSILKPlQKLKG 1053
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 919 NVSSKEEEKKKAEMEVQMMKKELdqkifHRKSLFKKVQEgglcerqlmDKENNIATLNASLEENQQRQKRFEEDLRSFDS 998
Cdd:COG5022 1054 LLLLENNQLQARYKALKLRRENS-----LLDDKQLYQLE---------STENLLKTINVKDLEVTNRNLVKPANVLQFIV 1119
|
330
....*....|.
gi 193208595 999 SHQRESILKDQ 1009
Cdd:COG5022 1120 AQMIKLNLLQE 1130
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
709-904 |
2.78e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 709 TEQEELEKLVSKLEKEEiiivkaEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLklaEDLQT 788
Cdd:COG3883 16 PQIQAKQKELSELQAEL------EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 789 DVG-VIQQLYeQTEENEKRYEQLVSESDSSDGLSYTELRKKVEDKD----EEYRKIVQEGEELQ-KCSEERNKLQSKLNE 862
Cdd:COG3883 87 ELGeRARALY-RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADadllEELKADKAELEAKKaELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 193208595 863 LGTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAISQKRNE 904
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-569 |
2.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 333 RARIQKKIgknnQERQELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDLehdADIDIEIDNAitlkirgM 412
Cdd:COG4913 609 RAKLAALE----AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV---ASAEREIAEL-------E 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 413 SDKARMIAKNC--AELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDllkkeealRKSLA 490
Cdd:COG4913 675 AELERLDASSDdlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED--------LARLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 491 DLPLLDENALTECKLKREKYLKQldILKKKCAEAEKNAEKDREKeslkqtlsiARKKMTAYQRIYDNNWQGL---IGQAP 567
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRAEEE---------LERAMRAFNREWPAETADLdadLESLP 815
|
..
gi 193208595 568 DF 569
Cdd:COG4913 816 EY 817
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1189-1271 |
3.30e-04 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 42.97 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDeskVEGMAIVLADIIAerrgfdengkLRGRDMQMVVITHDERL 1268
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLD---VEGERALNQAIAA----------LKAAGATRIVIAHRPET 158
|
...
gi 193208595 1269 VNR 1271
Cdd:cd03246 159 LAS 161
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
635-1084 |
3.35e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 635 EAEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEESKSSgCCPLCDRDFKTKKEINEFSKKLENMTLSFPT----- 709
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE-LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNlkkki 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 710 -EQEELEKLVSKLEKEEIIIVK-AEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDL- 786
Cdd:TIGR04523 211 qKNKSLESQISELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQl 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 787 ------------QTDVGVIQQLYEQTEENEKRYEQLVSESDSSDGL------SYTELRKKVEDKDEEYRKIVQEGEE--- 845
Cdd:TIGR04523 291 nqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqlneQISQLKKELTNSESENSEKQRELEEkqn 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 846 -LQKCSEERNKLQSKLNELGTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAIsQKRNEDLPDAQFKKDDLTRNVSSKE 924
Cdd:TIGR04523 371 eIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL-EKEIERLKETIIKNNSEIKDLTNQD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 925 EEKKKAEMEVQMMKKELDQKIFHRKSLFKKV-QEGGLCERQLMDKENNIATLNASLEENQQRQKRFEEDLRSFDSSHQRE 1003
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIkQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1004 SILKDQltrmiIENKIKELKRTLATFDGQINEDRITEQKQAYNK----LQNELRLIGNEEVKIYTQMQEYEKQKKIAEAK 1079
Cdd:TIGR04523 530 ESEKKE-----KESKISDLEDELNKDDFELKKENLEKEIDEKNKeieeLKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
....*
gi 193208595 1080 LSTKE 1084
Cdd:TIGR04523 605 IEEKE 609
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-510 |
3.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 194 QLTKFVKAQERMKKIVLDFKKEmqTHEMSKQLYETHvRDKLVARQNQEECERKISKRKEETDELKERKANGQKKIEEMRT 273
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKE--LEELSRQISALR-KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 274 SIHELEDTLTS----FKKTELERQNLKKQLSLIRVEpYFGTEEELKREIEEFRGSEGRSYGEERA--RIQKKIGKNNQER 347
Cdd:TIGR02168 776 ELAEAEAEIEEleaqIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRleDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 348 QELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDlehdadidieidnAITLKIRGMSDKARMIAKNCAELQ 427
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-------------ELSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 428 SNLRTAQEAATKIEVEMKTLQ---NEKVKLEKE-VEQLKFKIKqgqNATAGMKDLLKKeeaLRKSLADLPLLDENALTEC 503
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQerlSEEYSLTLEeAEALENKIE---DDEEEARRRLKR---LENKIKELGPVNLAAIEEY 995
|
....*..
gi 193208595 504 KLKREKY 510
Cdd:TIGR02168 996 EELKERY 1002
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1189-1274 |
3.95e-04 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 44.65 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDEskvEGMAIVLADIIAerrgfdengkLRGRDMQMVVITHDERL 1268
Cdd:TIGR01842 456 SGGQRQ------RIALARALYGDPKLVVLDEPNSNLDE---EGEQALANAIKA----------LKARGITVVVITHRPSL 516
|
....*....
gi 193208595 1269 ---VNRITI 1274
Cdd:TIGR01842 517 lgcVDKILV 525
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
601-810 |
4.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 601 QKLETMQHQYRKQEESLtaQELKLSENIFEAcSCEAEEVSEKLENLRKRLKKARKDLAPLSAKSNLYDSYIEESKSSGCC 680
Cdd:COG3206 182 EQLPELRKELEEAEAAL--EEFRQKNGLVDL-SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 681 PLCDRDFKT-KKEINEFSKKLENMTLSFPTEQEELEKLVSKLEKEEIIIvkaegqANELQRIVKELKEVREKNRKLSTEM 759
Cdd:COG3206 259 LLQSPVIQQlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 193208595 760 AEEKSNLsknEKQLETVNAKLKLAEDLQTDVGVIQQLYEQTeenEKRYEQL 810
Cdd:COG3206 333 QAQLAQL---EARLAELPELEAELRRLEREVEVARELYESL---LQRLEEA 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
737-1077 |
4.59e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 737 ELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDVGVIqqLYEQTEENEKRYEQLVSESDS 816
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYE--LLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 817 SDGlSYTELRKKVEDKDEEYRKIVQEGEELQK-----CSEERNKLQSKLNELGTHRVSLGEAAAQAGAFAEQLETKIKEI 891
Cdd:TIGR02169 249 LEE-ELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 892 QECITAI-SQKRN--EDLPDAQFKKDDLTRNVSSKEEEKKKAEMEVQMMKKELDQKIFHRKSLFKKVQEGGlceRQLMDK 968
Cdd:TIGR02169 328 EAEIDKLlAEIEEleREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK---REINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 969 ENNIATLNASLEENQQRQKRFEEDLRSFdsshqRESILKDQLTRMIIENKIKELKRTLAtfdgQINEDRITEQKQAYNkL 1048
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGI-----EAKINELEEEKEDKALEIKKQEWKLE----QLAADLSKYEQELYD-L 474
|
330 340
....*....|....*....|....*....
gi 193208595 1049 QNELRLIGNEEVKIYTQMQEYEKQKKIAE 1077
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASE 503
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
251-535 |
4.88e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 251 KEETDELKERKANGQKKIEEMRTSIHELEDTLTSFKKtelERQNLKKQLSLIRvepyfgteeelkreieefrgSEGRSYG 330
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAE---KRDELNAQVKELR--------------------EEAQELR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 331 EERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDLEHDADIDIEIDNAITLKIR 410
Cdd:COG1340 64 EKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 411 GMSDKARmiakncaelqsNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKEEALRKSLA 490
Cdd:COG1340 144 ELEKELE-----------KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 193208595 491 DL--------PLLDE--NALTECKLKREKYLKQLDILKKKCAEAEKNAEKDREKE 535
Cdd:COG1340 213 ELhkeiveaqEKADElhEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEE 267
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-492 |
5.27e-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: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 331 EERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEVihcQSLKYDLERLENQLRSELD-------------LEHDADI 397
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AELRAELEAQKEELAELLRalyrlgrqpplalLLSPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 398 DIEIDNAITLK--IRGMSDKARMIAKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAG- 474
Cdd:COG4942 132 LDAVRRLQYLKylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEl 211
|
170 180
....*....|....*....|.
gi 193208595 475 ---MKDLLKKEEALRKSLADL 492
Cdd:COG4942 212 aaeLAELQQEAEELEALIARL 232
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-99 |
5.36e-04 |
|
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: 43.84 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 20 RLHIRGIRSVGDEDhdvhkIDFLSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQ-KKQNFIHSTDVARKTRvdaSVTLE 98
Cdd:COG3593 5 KIKIKNFRSIKDLS-----IELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKfDEEDFYLGDDPDLPEI---EIELT 76
|
.
gi 193208595 99 F 99
Cdd:COG3593 77 F 77
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
688-904 |
8.34e-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: 43.21 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 688 KTKKEINEfskklenmtlsfpteqeeLEKLVSKLEKEEiiivkaEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLS 767
Cdd:COG4942 31 QLQQEIAE------------------LEKELAALKKEE------KALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 768 KNEKQLETVNAKLK-LAEDLQTDVGVIQQLYEQTeenekRYEQLVSESDSSDGLSYTELRKKVEDKD----EEYRKIVQE 842
Cdd:COG4942 87 ELEKEIAELRAELEaQKEELAELLRALYRLGRQP-----PLALLLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193208595 843 GEELQK-CSEERNKLQSKLNELGTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAISQKRNE 904
Cdd:COG4942 162 LAALRAeLEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-64 |
9.27e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 9.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 193208595 17 KFLRLHIRGIRSVGDedhdvHKIDF--LSPCTLISGPNGTGKTTTIEALN 64
Cdd:COG3950 2 RIKSLTIENFRGFED-----LEIDFdnPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
217-504 |
1.36e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 217 QTHEMSKQLYETHVRDKLVARQNQEECERKISKRKEETDELKERKANGQKKIEEMRTSIHELE-----------DTLTSF 285
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagsERLRAV 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 286 KKTELERQNLKKQLSLIRvepyfgteeelkreieefrgSEGRSYGEERARIQKKIgKNNQERQELSQKKtefenrissLK 365
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSR--------------------NELNSLSEDYEVLKRNF-RNKSEEMETTTNK---------LK 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 366 AEVIHCQSlkyDLERLENQLRS-ELDLEHDADIDIEIDNAITLKiRGMSDKarmiakncaeLQSNLRTAQEAATKIEVEM 444
Cdd:pfam15921 699 MQLKSAQS---ELEQTRNTLKSmEGSDGHAMKVAMGMQKQITAK-RGQIDA----------LQSKIQFLEEAMTNANKEK 764
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193208595 445 KTLQNEKVKLEKEVEqlkfKIKQGQNATAGMKDLLKKEE-ALRKSLADLPL-LDENAL--TECK 504
Cdd:pfam15921 765 HFLKEEKNKLSQELS----TVATEKNKMAGELEVLRSQErRLKEKVANMEVaLDKASLqfAECQ 824
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
699-810 |
1.36e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 699 KLENMtlSFPTEQEELEKLVSKLEKEEIIIVK--AEGQANELQRIVKELKEVREKNRKLSTEMAEEKsnlsknekqlETV 776
Cdd:COG0542 403 RMEID--SKPEELDELERRLEQLEIEKEALKKeqDEASFERLAELRDELAELEEELEALKARWEAEK----------ELI 470
|
90 100 110
....*....|....*....|....*....|....
gi 193208595 777 NAKLKLAEDLQTDVGVIQQLYEQTEENEKRYEQL 810
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAEL 504
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
17-99 |
1.49e-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: 41.49 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 17 KFLRLHIRGIRSVGDEdhdvHKIDF----LSPCTLISGPNGTGKTTTIEALNFVTTGQMPTQKKQNFIHSTDVARKTRvd 92
Cdd:cd03279 2 KPLKLELKNFGPFREE----QVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDT-- 75
|
....*..
gi 193208595 93 ASVTLEF 99
Cdd:cd03279 76 AEVSFTF 82
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
321-774 |
1.81e-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: 43.12 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 321 FRGSEGRSYGEERARIQKKIGKNNQER----QELSQKKTEFENRISSLKAEVIhcqslkydlerlenqlrselDLEHDAD 396
Cdd:TIGR01612 1101 FGKEENIKYADEINKIKDDIKNLDQKIdhhiKALEEIKKKSENYIDEIKAQIN--------------------DLEDVAD 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 397 IDIEIDNaitlkIRGMSDKarmiakncaelQSNLRTAQEAATKIEVEMKTLQNEKVKLEKE---VEQLK-FKIKQGQNAt 472
Cdd:TIGR01612 1161 KAISNDD-----PEEIEKK-----------IENIVTKIDKKKNIYDEIKKLLNEIAEIEKDktsLEEVKgINLSYGKNL- 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 473 aGMKDLLKKEEALRKSladlplldENALTecklKREKYLKQLDILKKKCAEAEKNAEKDREKESLKQTLSIARKKMTAYQ 552
Cdd:TIGR01612 1224 -GKLFLEKIDEEKKKS--------EHMIK----AMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHH 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 553 RIYDNNWQGLigqapdfpwTPILSKTFHKLRNDKKimEEDLRDVQLNVQK--LETMQH-----QYRKQEESLTaQELKLS 625
Cdd:TIGR01612 1291 IISKKHDENI---------SDIREKSLKIIEDFSE--ESDINDIKKELQKnlLDAQKHnsdinLYLNEIANIY-NILKLN 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 626 --ENIFEACSCEAEEVSEKLENLRKRLKKARKDLAPLSAKSNLydsyiEESKSSGCCPLCDRD----FKTKKEINEFSKK 699
Cdd:TIGR01612 1359 kiKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINL-----EECKSKIESTLDDKDidecIKKIKELKNHILS 1433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 700 LENMTLSFPTEQEELEKLVSKLEK---------EEIIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNE 770
Cdd:TIGR01612 1434 EESNIDTYFKNADENNENVLLLFKniemadnksQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNK 1513
|
....
gi 193208595 771 KQLE 774
Cdd:TIGR01612 1514 ELFE 1517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-534 |
2.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 179 LSEPKELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEMQTHEMSKQLYETHVRDKLVARQNQEECERKISKRKEETDELK 258
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 259 ERKANGQKKIEEMRTSIHELEdtltsfKKTELERQNLKKQLSLIRvepyfgtEEELKREIEEFRGSEGRSYGEERARIQK 338
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKK------KADEAKKAEEAKKADEAK-------KAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 339 KigKNNQERQELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDLEHDADIDIEIDNAITLKIRgmsdKARM 418
Cdd:PTZ00121 1557 L--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK----KAEE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 419 IAKNCAELQsnlRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKEEALRKSLADLPLLDE- 497
Cdd:PTZ00121 1631 EKKKVEQLK---KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEl 1707
|
330 340 350
....*....|....*....|....*....|....*...
gi 193208595 498 -NALTECKLKREKYLKQLDILKKKCAEAEKNAEKDREK 534
Cdd:PTZ00121 1708 kKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
726-905 |
2.73e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 726 IIIVKAEGQANELQRIVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAE----DLQTDVGV--------- 792
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAAleaelaele 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 793 --IQQLYEQTEENEKRYEQLVSESDSSDGLSYTELRKKVEDKDEEYRKIV-------QEGEELQKCSEERNKLQSKLNEL 863
Cdd:COG4942 90 keIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 193208595 864 GTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAISQKRNED 905
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
349-855 |
2.73e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 349 ELSQKKTEFENRISSLKAEVIHCQSLKYDLERLENQLRSELDLEHDAdidIEIDNAI----TLKIRGMSDKARMIAKNCA 424
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL---IKENNATrhlcNLLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 425 ELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAGMKDLLKKEEALRKSLADLPLLD----ENAL 500
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQitekENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 501 TECKLKREKYLKQLDILKKKCAEAEKNAEKDREKE----SLKQTLSIARKKMTAYQRIYDNNWQgligqapdfpwtpILS 576
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQ-------------IAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 577 KTFHKLRNDKKIMEEDLRDVQ----LNVQKLE----TMQHQYRKQEESLTAQE--LKLSENIFEACSCEAEEVSEKLENL 646
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKaahsFVVTEFEattcSLEELLRTEQQRLEKNEdqLKIITMELQKKSSELEEMTKFKNNK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 647 RKRLKKARKDLA---PLSAKSNLYDSYIEESKSSGCcPLCDRDFKTKKEINEFSKKLENMTLSFPTEQEELEKLVSKLEK 723
Cdd:pfam05483 404 EVELEELKKILAedeKLLDEKKQFEKIAEELKGKEQ-ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 724 EEIIIVKAEGQANELqriVKELKEVREKNRKLSTEMAEEKSNLSKNEKQLETVNAKLKLAEDLQTDV---------GVIQ 794
Cdd:pfam05483 483 EKLKNIELTAHCDKL---LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLrdelesvreEFIQ 559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 795 QLYE------QTEENEKRYEQLVSESDSSDGLSYTE---LRKKVEDKDEEYRKIVQEGEELQKCSEERNK 855
Cdd:pfam05483 560 KGDEvkckldKSEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
32-108 |
2.92e-03 |
|
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain contains a P-loop motif.
Pssm-ID: 433272 [Multi-domain] Cd Length: 207 Bit Score: 40.61 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 32 EDHDVHkidflspctLISGPNGTGKTTTIEALNFVTTGqMPTQKKQNFIHStdvARKTRVDASV------TLEFIDVKGR 105
Cdd:pfam13514 24 GGPDLH---------LIYGPNEAGKSTALRAISDLLFG-IPLRTPYNFLHD---YSDLRIGATLenadgeTLEFRRRKGR 90
|
...
gi 193208595 106 ECT 108
Cdd:pfam13514 91 KNT 93
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
20-66 |
3.80e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 193208595 20 RLHIRGIRSVGDEDhdvhkIDfLSPCTLISGPNGTGKTTTIEALNFV 66
Cdd:COG4637 4 RIRIKNFKSLRDLE-----LP-LGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
424-547 |
3.84e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 424 AELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQGQNATAG------MKDLLKKEEALRKSLADLplldE 497
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeYEALQKEIESLKRRISDL----E 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 193208595 498 NALTECKLKREKYLKQLDILKKKCAEAEKN-----AEKDREKESLKQTLSIARKK 547
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAEleekkAELDEELAELEAELEELEAE 164
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
20-69 |
4.23e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 40.91 E-value: 4.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 193208595 20 RLHIRGIRSvgdedHDVHKIDFLSPCTLISGPNGTGKTTTIEALNFVTTG 69
Cdd:COG1195 4 RLSLTNFRN-----YESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1189-1272 |
4.27e-03 |
|
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: 40.14 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLD-ESKVEGMAIVLadiiaerrgfdengKLRGRDMQMVVITHDER 1267
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDpAGRRELLELLK--------------KLKAEGKTIIIVTHDLD 195
|
....*
gi 193208595 1268 LVNRI 1272
Cdd:cd03225 196 LLLEL 200
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1014-1114 |
4.47e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1014 IIENKIKELKRTLATFDGQIneDRITEQKQAYNKLQNELRLIGNEEVKiytqmqeyEKQKKIAEAKLSTKECQNAESNYR 1093
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKI--DHIQQQIKTYNKNIEEQRKKNGENIA--------RKQNKYDELVEEAKTIKAEIEELT 240
|
90 100
....*....|....*....|..
gi 193208595 1094 DAIIELAITKESIS-DLTKYRN 1114
Cdd:PHA02562 241 DELLNLVMDIEDPSaALNKLNT 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-497 |
4.75e-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: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 331 EERARIQKKIGKNNQERQELSQKKTEFENRISSLKAEVIHCQ------------SLKYDLERLENQL----RSELDLEHD 394
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggdrleQLEREIERLERELeereRRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 395 ADidiEIDNAITLKIRGMSDKARMIAKNCAELQSNLRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKfkiKQGQNATAG 474
Cdd:COG4913 368 LA---ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE---RRKSNIPAR 441
|
170 180
....*....|....*....|....
gi 193208595 475 MKDLLKK-EEALRKSLADLPLLDE 497
Cdd:COG4913 442 LLALRDAlAEALGLDEAELPFVGE 465
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
412-901 |
4.87e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.28 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 412 MSDKARMIAKNCAELQsnlrtaqeaatKIEVEMKTLQ----NEKVKLEK---EVEQLKFKIKQGQNATAGMKDLLKKEEA 484
Cdd:pfam07111 61 LSQQAELISRQLQELR-----------RLEEEVRLLRetslQQKMRLEAqamELDALAVAEKAGQAEAEGLRAALAGAEM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 485 LRKSL-------------------ADLPLLDENALTECKLKREKYLKQLDILK-KKCAEAEKNAEKDREKESLKQTLSIA 544
Cdd:pfam07111 130 VRKNLeegsqreleeiqrlhqeqlSSLTQAHEEALSSLTSKAEGLEKSLNSLEtKRAGEAKQLAEAQKEAELLRKQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 545 RKKMTAyQRIYDNNWQGLIGQA--PDFP---WTP---ILSKTFHKLRNDKKIMEEDLRDVQLNVQKLETMqhqyrkqees 616
Cdd:pfam07111 210 QEELEA-QVTLVESLRKYVGEQvpPEVHsqtWELerqELLDTMQHLQEDRADLQATVELLQVRVQSLTHM---------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 617 LTAQELKLSENIFEACSCEAEEVSEKLENLRKRLKKARKDLAPLSAKSnlydsyIEESKSSGccplcdrdfKTKKEINEF 696
Cdd:pfam07111 279 LALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQD------LEHRDSVK---------QLRGQVAEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 697 SKKLENMTLSFPTEQEELEKLVSKLEKEEIiivkaegQANELQRivkELKEVREKNRKlstemaeEKSNLSKNEKQLETV 776
Cdd:pfam07111 344 QEQVTSQSQEQAILQRALQDKAAEVEVERM-------SAKGLQM---ELSRAQEARRR-------QQQQTASAEEQLKFV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 777 NAKLKLAED-LQTDVGVIQQLYEQTEENEKRYEQLVSESDSSDGL-----SYTELRKKVEDKDEEYRKIVQE-GEELQKC 849
Cdd:pfam07111 407 VNAMSSTQIwLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLmarkvALAQLRQESCPPPPPAPPVDADlSLELEQL 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 850 SEERNKLQSKL--------NELGTHRVSLGEAAAQAGAFAEQLETKIKEIQECITAISQK 901
Cdd:pfam07111 487 REERNRLDAELqlsahliqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQ 546
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
179-358 |
5.35e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 179 LSEPKELKKRFDDIFQLTKFVKAQERMKKIVLDFKKEMQTHEMSKQLYETHVRDKLVARQNQEECERKisKRKEEtdelK 258
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK--RKKLE----L 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 259 ERKANGQKKIEEMRTSIheLEDTLTSFKKTELERQNLKKQLSLiRVEPYFGTEEELKREIEEFRGSEGRSYGEERARIQK 338
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKI--LEKELEERKQAMIEEERKRKLLEK-EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
170 180
....*....|....*....|
gi 193208595 339 KIGKNNQERQELSQKKTEFE 358
Cdd:pfam17380 557 QMRKATEERSRLEAMERERE 576
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1189-1272 |
6.01e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 40.66 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDeskVEGMAIVLaDIIAERRgfdengklRGRDMQMVVITHDERL 1268
Cdd:COG1123 144 SGGQRQ------RVAIAMALALDPDLLIADEPTTALD---VTTQAEIL-DLLRELQ--------RERGTTVLLITHDLGV 205
|
....
gi 193208595 1269 VNRI 1272
Cdd:COG1123 206 VAEI 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
430-865 |
6.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 430 LRTAQEAATKIEVEMKTLQNEKVKLEKEVEQLKFKIKQgqnatagmkdLLKKEEALRKSLADLPLLDEnaLTECKLKREK 509
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE----------LREELEKLEKLLQLLPLYQE--LEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 510 YLKQLDILKKKCAEAEknaEKDREKESLKQTLSIARKKMTAYQRIYDNNWQGLIGQapdfpwtpiLSKTFHKLRNDKKIM 589
Cdd:COG4717 144 LPERLEELEERLEELR---ELEEELEELEAELAELQEELEELLEQLSLATEEELQD---------LAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 590 EEDLRDVQLNVQKLETMQHQYRKQEESLTAQElKLSENIFEACS----CEAEEVSEKLENLRKRLKKARKDLAPLSAKSN 665
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 666 LYDSyieeskssgccplcdrdfKTKKEINEFSKKLENMTLSFPTEQEELEKLVSKLE-KEEIIIVKAEGQANELQRIVKE 744
Cdd:COG4717 291 LLLA------------------REKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 745 LKEVREKNRKLSTEMAEEKSN---LSKNEKQLETVNAKLKLAEDLQTDVGVIQQLYEQTEENEKRYEQLvsesdsSDGLS 821
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL------LEALD 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 193208595 822 YTELRKKVEDKDEEYRKIVQEGEELQkcsEERNKLQSKLNELGT 865
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELR---EELAELEAELEQLEE 467
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
408-534 |
8.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 408 KIRGMSDKARMIAKNcAELQsnlrtAQEAATKIEVEMKT-LQNEKVKLEKEVEQLKFKIKQGQNAtagmkdLLKKEEALR 486
Cdd:PRK12704 32 KIKEAEEEAKRILEE-AKKE-----AEAIKKEALLEAKEeIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLD 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 193208595 487 KSLADLPLLDEnaltECKLKREKYLKQLDILKKKCAEAEKNAEKDREK 534
Cdd:PRK12704 100 RKLELLEKREE----ELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
35-69 |
8.95e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 8.95e-03
10 20 30
....*....|....*....|....*....|....*.
gi 193208595 35 DVHKIDF-LSPCTLISGPNGTGKTTTIEALNFVTTG 69
Cdd:pfam13555 13 DGHTIPIdPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1189-1272 |
9.12e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 40.05 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208595 1189 SAGQKMlaslliRIALAEVFGGSCSMIALDEPTTNLDeskVEgmAIV-LADIIAERRGfdengklrgrdmQMVVITHD-- 1265
Cdd:COG0488 154 SGGWRR------RVALARALLSEPDLLLLDEPTNHLD---LE--SIEwLEEFLKNYPG------------TVLVVSHDry 210
|
....*....
gi 193208595 1266 --ERLVNRI 1272
Cdd:COG0488 211 flDRVATRI 219
|
|
| |
