|
Name |
Accession |
Description |
Interval |
E-value |
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-996 |
1.81e-58 |
|
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: 218.68 E-value: 1.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 1 MKPLHLKLNNFGPFLKEE-IDFSKIDNneLFLISGKTGSGKTMIFDAMTYALFGKASTEQREENDLRSHFADGKQPMSVT 79
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHtIDFTALGP--IFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAFAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 80 FEFQLNNRIYKVHRQgpFIKEGNTTKTNAKFDVFEMVDGKYEIRESKVISGTQ-FIIEILGVNADQFRQLFILPQGEFKR 158
Cdd:TIGR00618 79 LEFSLGTKIYRVHRT--LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEeVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 159 FLISNSREKQGILRTLFNSEKFEAIREILKEEVKKEKAQIENRYQQIDLLWQeiesfdddkikgLLEVATQQIDKVIENI 238
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL------------CTPCMPDTYHERKQVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 239 PLLQARSKEILAFVNESKETAIKEYEIIEKKTLENNILKDNINQLNINKIDFVQLKEQQPEIEEIEAKLKLLQDITNLLN 318
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 319 YIENREKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEEngdLIESKISFIDKTRVLFNDINKYQQSYLNIERL 398
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT---LHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 399 RTEGEQ---LGDELNNLIKGLEKVEDSIGNNESDYEKIIELNNAITNINNEI---------------NVIKENEKAKAEL 460
Cdd:TIGR00618 382 HTLQQQkttLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQelqqryaelcaaaitCTAQCEKLEKIHL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 461 DKLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFI--SEIKSAVKI-------GDQCPICGNE------- 524
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLcgSCIHPNPARqdidnpgPLTRRMQRGEqtyaqle 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 525 --IQDLGHHIdfDSIAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNINIKTQSDL--------SLEVLNKRLLE 594
Cdd:TIGR00618 542 tsEEDVYHQL--TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTeklseaedMLACEQHALLR 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 595 NENALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRdlITEFETLSKYNNITNFEVDYKKYIQ------ 668
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS--IRVLPKELLASRQLALQKMQSEKEQltywke 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 669 DVNQHQEHSKEIEDKLIQLSqRKLIEQNNLNHYENQLETYNNDL------ELNEQSIEMEMSRLNLTDNNDIDEIIAWRG 742
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYD-REFNEIENASSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAHFNNNEEVTAALQT 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 743 EQAELEQKRDTYKKRyhefeMEIARLESLTKNKELLDSDKLKDEYELKKGKMNTLIDEYSAVHYQCQNNiNKTQSIVSH- 821
Cdd:TIGR00618 777 GAELSHLAAEIQFFN-----RLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEK-SATLGEITHq 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 822 -------INYLNQELKDQQEIFQLAEIVSGKNNKNLTLENFVLIYYLDQIIAQANLRLATMSDNRY--QLIRREAVSHGL 892
Cdd:TIGR00618 851 llkyeecSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFhgRYADSHVNARKY 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 893 SGLEIDVFDLHSNKSRHISSLSGGETFQSSLALALGLSEIVqQQSGGISLESIFIDEGFGTLDQETLETALDTLLNLKST 972
Cdd:TIGR00618 931 QGLALLVADAYTGSVRPSATLSGGETFLASLSLALALADLL-STSGGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREG 1009
|
1050 1060
....*....|....*....|....
gi 612532491 973 GRMVGIISHVSELKNRIPLVLEVK 996
Cdd:TIGR00618 1010 SKMIGIISHVPEFRERIPHRILVK 1033
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-161 |
3.03e-43 |
|
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: 156.66 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 1 MKPLHLKLNNFGPFLKEE-IDFSKIDNNELFLISGKTGSGKTMIFDAMTYALFGKASTEQREENdLRSHFADGKQPMSVT 79
Cdd:cd03279 1 MKPLKLELKNFGPFREEQvIDFTGLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQEN-LRSVFAPGEDTAEVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 80 FEFQLNNRIYKVHRQgpfikegnttktnakfdvfemvdgkyeireskvisgtqfiieiLGVNADQFRQLFILPQGEFKRF 159
Cdd:cd03279 80 FTFQLGGKKYRVERS-------------------------------------------RGLDYDQFTRIVLLPQGEFDRF 116
|
..
gi 612532491 160 LI 161
Cdd:cd03279 117 LA 118
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
874-1003 |
1.29e-39 |
|
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: 146.26 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 874 TMSDNRYQLIRReavshglSGLEIDVFD----LHSNK-----SRHISSLSGGETFQSSLALALGLSEIVQQqSGGISLES 944
Cdd:cd03279 83 QLGGKKYRVERS-------RGLDYDQFTrivlLPQGEfdrflARPVSTLSGGETFLASLSLALALSEVLQN-RGGARLEA 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 612532491 945 IFIDEGFGTLDQETLETALDTLLNLKSTGRMVGIISHVSELKNRIPLVLEVKSDQYQSS 1003
Cdd:cd03279 155 LFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPGGSR 213
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1-996 |
1.41e-25 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 114.51 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 1 MKPLHLKLNNFGPfLKEE--IDFSK--IDNNELFLISGKTGSGKTMIFDAMTYALFGKA---STEQREENDLRSHfaDGK 73
Cdd:PRK10246 1 MKILSLRLKNLNS-LKGEwkIDFTAepFASNGLFAITGPTGAGKTTLLDAICLALYHETprlNNVSQSQNDLMTR--DTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 74 QPMS-VTFE--------FQLNNRIykvhRQGPfikEGNTTKtnAKFDVFEMVDGKyeIRESKVISGTQFIIEILGVNADQ 144
Cdd:PRK10246 78 ECLAeVEFEvkgeayraFWSQNRA----RNQP---DGNLQA--PRVELARCADGK--ILADKVKDKLELTATLTGLDYGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 145 FRQLFILPQGEFKRFLISNSREKQGILRTLFNSEKFEAIREILKEEVKKEKAQIENRYQQIdllwqeiesfdddkiKGLL 224
Cdd:PRK10246 147 FTRSMLLSQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQA---------------SGVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 225 EVATQQIDKVIENIPLLQARSKEILAfvneSKETAIKEYEIIEKKTlennilkDNINQLNINKIDFVQLKEQQPEIEEIE 304
Cdd:PRK10246 212 LLTPEQVQSLTASLQVLTDEEKQLLT----AQQQQQQSLNWLTRLD-------ELQQEASRRQQALQQALAAEEKAQPQL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 305 AKLKLLQDITNLLNYIENREKIETKIANSKKDISETNNKILNLVCDKRNI--DKEKKMLEENGDLIESK--ISFIDKTRV 380
Cdd:PRK10246 281 AALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhHAAKQSAELQAQQQSLNtwLAEHDRFRQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 381 LFNDINKYQQSYLNIERLRTEGEQLGDELNNLIKGLEKVEDSIGNNESDyekiiELNNAITNINNEINV----------I 450
Cdd:PRK10246 361 WNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD-----EVAAALAQHAEQRPLrqrlvalhgqI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 451 KENEKAKAELDKLLGSKQELENQINEEktilknLEIKLDRYDKSKLDLND------KESFISEIKSA---VKIGDQCPIC 521
Cdd:PRK10246 436 VPQQKRLAQLQVAIQNVTQEQTQRNAA------LNEMRQRYKEKTQQLADvkticeQEARIKDLEAQraqLQAGQPCPLC 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 522 GNeiqdlghhidfdsiakrqneikeieanihTMKSNIAVHNSeikfvnekisniniktqsdLSLEVLNKRLLEnenalnn 601
Cdd:PRK10246 510 GS-----------------------------TSHPAVEAYQA-------------------LEPGVNQSRLDA------- 534
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 602 qreLNKFIEQMKEEKDNLTLQIHNKQLRLNKNESE----LKLCRDLITEFETLSKYNNITnfeVDYKKYIQDVNQHQEhs 677
Cdd:PRK10246 535 ---LEKEVKKLGEEGAALRGQLDALTKQLQRDESEaqslRQEEQALTQQWQAVCASLNIT---LQPQDDIQPWLDAQE-- 606
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 678 kEIEDKLIQLSQRKLIeQNNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTDNNDIDEIiAW---RGEQAELEQKRDTy 754
Cdd:PRK10246 607 -EHERQLRLLSQRHEL-QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEA-SWlatRQQEAQSWQQRQN- 682
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 755 kkRYHEFEMEIARLESLTKNkeLLDSDKLKDEYElkkgkmNTLIDEYSAVHYQC-----------QNNINKTQSIVSHIN 823
Cdd:PRK10246 683 --ELTALQNRIQQLTPLLET--LPQSDDLPHSEE------TVALDNWRQVHEQClslhsqlqtlqQQDVLEAQRLQKAQA 752
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 824 YLNQELK----DQQEIF------------------------QLAEIVSGKNNKNLT---------LENFVLIYYLDQIIA 866
Cdd:PRK10246 753 QFDTALQasvfDDQQAFlaalldeetltqleqlkqnlenqrQQAQTLVTQTAQALAqhqqhrpdgLDLTVTVEQIQQELA 832
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 867 QANLRL---ATM-----------SDNRYQL---------IRREA--------------------VSHGLS---------- 893
Cdd:PRK10246 833 QLAQQLrenTTRqgeirqqlkqdADNRQQQqalmqqiaqATQQVedwgylnsligskegdkfrkFAQGLTldnlvwlanq 912
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 894 -----------------GLEIDVFDL-HSNKSRHISSLSGGETFQSSLALALGLSEIVQQQSggiSLESIFIDEGFGTLD 955
Cdd:PRK10246 913 qltrlhgryllqrkaseALELEVVDTwQADAVRDTRTLSGGESFLVSLALALALSDLVSHKT---RIDSLFLDEGFGTLD 989
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|.
gi 612532491 956 QETLETALDTLLNLKSTGRMVGIISHVSELKNRIPLVLEVK 996
Cdd:PRK10246 990 SETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVK 1030
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-208 |
2.97e-23 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 98.54 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 2 KPLHLKLNNFGPFL-KEEIDFSKidnnELFLISGKTGSGKTMIFDAMTYALFGKASTEQREENDLRShfaDGKQPMSVTF 80
Cdd:COG0419 1 KLLRLRLENFRSYRdTETIDFDD----GLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLIN---VGSEEASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 81 EFQLNNRIYKVHRqgpfikegnttktnakfdvfemvdgkyeireskvisgtqfiieilgvnadqfrqlfilPQGEFKRFL 160
Cdd:COG0419 74 EFEHGGKRYRIER----------------------------------------------------------RQGEFAEFL 95
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 612532491 161 ISNSREKQGILRTLFNSEKFEAIREILKEevkkEKAQIENRYQQIDLL 208
Cdd:COG0419 96 EAKPSERKEALKRLLGLEIYEELKERLKE----LEEALESALEELAEL 139
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
6-996 |
4.07e-16 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 83.41 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 6 LKLNNFGPFLKEEIDFSKIDNnelfLISGKTGSGKTMIFDAMTYALFGKASTEQREEndlrsHFADGKQPMSVTFEFQLN 85
Cdd:PRK01156 6 IRLKNFLSHDDSEIEFDTGIN----IITGKNGAGKSSIVDAIRFALFTDKRTEKIED-----MIKKGKNNLEVELEFRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 86 NRIYKVHRQgpFIKEGNTTKTNAKFdvfeMVDGkyEIRESKVISGTQFI-IEILGVNADQFRQLFILPQGEFKRFLISNS 164
Cdd:PRK01156 77 GHVYQIRRS--IERRGKGSRREAYI----KKDG--SIIAEGFDDTTKYIeKNILGISKDVFLNSIFVGQGEMDSLISGDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 165 REKQGILRTLFNSEKFEAIREILKEEVKKEKAQIENryqqIDLLWQEIESFDDDkikgllevatqqidkvIENIPLLQAR 244
Cdd:PRK01156 149 AQRKKILDEILEINSLERNYDKLKDVIDMLRAEISN----IDYLEEKLKSSNLE----------------LENIKKQIAD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 245 SKEILAFVNESKETAIKEYEIIEKKTlenNILKDNINQLNinkidfVQLKEQQPEIEEIEAKLKLLQDITNLLNYIENRE 324
Cdd:PRK01156 209 DEKSHSITLKEIERLSIEYNNAMDDY---NNLKSALNELS------SLEDMKNRYESEIKTAESDLSMELEKNNYYKELE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 325 KIETKIANSKkdISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKISFIDKTRVLFNDINKYQqsylnierlrtEGEQ 404
Cdd:PRK01156 280 ERHMKIINDP--VYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI-----------KKKS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 405 LGDELNNLIKGLEkvedsigNNESDYEKIIelnNAITNINNEI-NVIKENEKAKAELDKLLGSK----QELENQINEEKT 479
Cdd:PRK01156 347 RYDDLNNQILELE-------GYEMDYNSYL---KSIESLKKKIeEYSKNIERMSAFISEILKIQeidpDAIKKELNEINV 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 480 ILKNLEIKLDRYDKSKLDLNDKESFISEIKSAVKIGDQCPICGNeiqDLGHHIDFDSIAKRQNEIKEIEANIHTMKsnia 559
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGT---TLGEEKSNHIINHYNEKKSRLEEKIREIE---- 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 560 vhnSEIKFVNEKISNInIKTQSDLSLEVLNKRLLENENALNNQRELNKFIEQMKEEKDnltlqihnKQLRLNkneselkl 639
Cdd:PRK01156 490 ---IEVKDIDEKIVDL-KKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKD--------KHDKYE-------- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 640 crdlitefETLSKYNNITNFEVDYKKyiqdvnqhqehskeiEDKLIQLSQRKLIEQNNLNHYENQLETYNNDLELNEQSI 719
Cdd:PRK01156 550 --------EIKNRYKSLKLEDLDSKR---------------TSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEI 606
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 720 EMEMSRLNLTDNNDI----DEIIAWRGEQAELEQK---RDTYKKRYHEFEMEIARLESLTKNKELLDSDKLKDEYELKkg 792
Cdd:PRK01156 607 EIGFPDDKSYIDKSIreieNEANNLNNKYNEIQENkilIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK-- 684
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 793 KMNTLIDEYSAVHYQCQNNInktQSIVSHINYLNQELKDQQEIFQLAEIVSGKNNKNLTLENFVLIYYLDQIIAQanlrl 872
Cdd:PRK01156 685 KSRKALDDAKANRARLESTI---EILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRK----- 756
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 873 aTMSDNRYQLIRREAVSHGLSGLEIDV-FDLHSNKSRH-----ISSLSGGETFQSSLALALGLSEIVQQqsggiSLESIF 946
Cdd:PRK01156 757 -SASQAMTSLTRKYLFEFNLDFDDIDVdQDFNITVSRGgmvegIDSLSGGEKTAVAFALRVAVAQFLNN-----DKSLLI 830
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|...
gi 612532491 947 IDEGFGTLDQE---TLETALDTLLNLKSTGRMVGIISHVSELKNRIPLVLEVK 996
Cdd:PRK01156 831 MDEPTAFLDEDrrtNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVK 883
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-197 |
1.12e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 73.30 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 6 LKLNNFGPFLKEEIDFSKidnnELFLISGKTGSGKTMIFDAMTYALFGKASTEQREENDLRSHFA-------DGKQPMSV 78
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSK----GLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDiriglegKGKAYVEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 79 TFEFQLNNRIYKVHRQGPFIKEGNTTKTNAKFDVFEMVDGKyeireskvisgtQFIIEILGVNADQFRQLFILPQGEFKR 158
Cdd:pfam13476 77 TFENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQ------------QFISELLKSDKIILPLLVFLGQEREEE 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 612532491 159 FLISNSREKQGILRTLFnsEKFEAIREILKEEVKKEKAQ 197
Cdd:pfam13476 145 FERKEKKERLEELEKAL--EEKEDEKKLLEKLLQLKEKK 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-987 |
3.62e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 1 MKPLHLKLNNFGPFLKEEIDFSKIDNnelfLISGKTGSGKTMIFDAMTYALFGKASTEQR--EENDLRShfaDGKQPMSV 78
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGIN----LIIGQNGSGKSSILEAILVGLYWGHGSKPKglKKDDFTR---IGGSGTEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 79 TFEFQLNNRIYKVHRqgpfikegNTTKTNAkfdvFEMVDGKYEIRESKVISGTQFIIEIlgVNADQFRQLFILPQGEFKR 158
Cdd:PRK03918 74 ELKFEKNGRKYRIVR--------SFNRGES----YLKYLDGSEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQGEIDA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 159 FLISN-SREKqgILRTLFNSEKFEAIREILKEEVKKEKAQIENryqqidlLWQEIESFDDdkIKGLLEVATQQIDKVIEN 237
Cdd:PRK03918 140 ILESDeSREK--VVRQILGLDDYENAYKNLGEVIKEIKRRIER-------LEKFIKRTEN--IEELIKEKEKELEEVLRE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 238 IPLLQARSKEIlafvnesketaIKEYEIIEKKTLENNILKDNINQLNINKidfvqlkeqqpeieeieakLKLLQDItnll 317
Cdd:PRK03918 209 INEISSELPEL-----------REELEKLEKEVKELEELKEEIEELEKEL-------------------ESLEGSK---- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 318 nyienrEKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKISFIDKTRVLFNDINKYQQSYLNIER 397
Cdd:PRK03918 255 ------RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 398 LRTEGEQLGDELNNLIKGLEKVEDSIGNNESD---YEKIIELNNAITNINNEINvIKENEKAKAELDKLLGSKQELENQI 474
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEI 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 475 NEEKTILKNLEIKldrydkskldLNDKESFISEIKSAVKIgdqCPICGNEIQDlghHIDFDSIAKRQNEIKEIEanihtm 554
Cdd:PRK03918 408 SKITARIGELKKE----------IKELKKAIEELKKAKGK---CPVCGRELTE---EHRKELLEEYTAELKRIE------ 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 555 ksniavhnSEIKFVNEKISNiniktqsdlslevLNKRLLENENALNNQRELNKF---IEQMKEEKDNLtlqihnKQLRLN 631
Cdd:PRK03918 466 --------KELKEIEEKERK-------------LRKELRELEKVLKKESELIKLkelAEQLKELEEKL------KKYNLE 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 632 KNESELKLCRDLITEFETLskynnitnfevdyKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNLNHYENQLET--YN 709
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKL-------------KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgFE 585
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 710 NDLELNEQSIEME-MSRLNLTDNNDIDEIiawRGEQAELEQKRDTYKKRYHEFEMEIARLESLTKNKELLDSDKLKDEYE 788
Cdd:PRK03918 586 SVEELEERLKELEpFYNEYLELKDAEKEL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 789 LKKGKMNTLIDEYSAVHYQCQNNINKTQSIVSHINYLNQELKDQQE-------IFQLAEIVSGKNNKNLTLENFVLIYYL 861
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakkelekLEKALERVEELREKVKKYKALLKERAL 742
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 862 DQIIAQANLRLATMSDNRYQLIRREAvshglSGLEIDVFDLHSNKSRHISSLSGGETFQSSLALALGLSEIVqqqSGGIS 941
Cdd:PRK03918 743 SKVGEIASEIFEELTEGKYSGVRVKA-----EENKVKLFVVYQGKERPLTFLSGGERIALGLAFRLALSLYL---AGNIP 814
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 612532491 942 LesIFIDEGFGTLDQETLETALDTLLNLKSTGRMVGIISHVSELKN 987
Cdd:PRK03918 815 L--LILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKD 858
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
865-1003 |
4.11e-11 |
|
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: 63.40 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 865 IAQANLRLATMSDNRYQLIRreavshglsglEIDVFD----LHSNKS-----RHISSLSGGETFQSSLALALGLSEIVqq 935
Cdd:cd03240 70 RAQVKLAFENANGKKYTITR-----------SLAILEnvifCHQGESnwpllDMRGRCSGGEKVLASLIIRLALAETF-- 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 936 qsgGISLESIFIDEGFGTLDQETLETALDTLLN--LKSTGRMVGIISHVSELKNRIPLVLEVKSDQYQSS 1003
Cdd:cd03240 137 ---GSNCGILALDEPTTNLDEENIEESLAEIIEerKSQKNFQLIVITHDEELVDAADHIYRVEKDGRQKS 203
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-986 |
5.38e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 356 KEKKMLEENGDLIESKISFIDKTRVLFNDINKYQQSYLNIERLRTEGEQLGDELNNLIKGLEKVEDSIGNNESDYEKIIE 435
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 436 LNNAITNINNEINVIKENE--KAKAELDKLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIKSAVK 513
Cdd:COG4717 175 LQEELEELLEQLSLATEEElqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 514 IGDQCPICGNEIQDLGHHIDFDSIAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNINIKTQSDLSLEVLNKRLL 593
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 594 ENENALNNQRELNKFIEQMKEEKDnltlqiHNKQLRLNKNEselklcrdliTEFETLSKYNNITNFEvdykkyiqdvnqh 673
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEE------LEEELQLEELE----------QEIAALLAEAGVEDEE------------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 674 qehskEIEDKLIQLSQRKLIEQNnLNHYENQLETYNNDLE-----LNEQSIEMEMSRLnltdnndideiiawRGEQAELE 748
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEE-LEELEEQLEELLGELEelleaLDEEELEEELEEL--------------EEELEELE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 749 QKRDTYKKRYHEFEMEIARLESltkNKELldsDKLKDEYELKKGKMNTLIDEYSAVHYqCQNNINKTQsivshinylnQE 828
Cdd:COG4717 446 EELEELREELAELEAELEQLEE---DGEL---AELLQELEELKAELRELAEEWAALKL-ALELLEEAR----------EE 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 829 LKDQqeifqlaeivsgknnknltlenfvliyYLDQIIAQANLRLATMSDNRYQLIRREavshglSGLEIDVfDLHSNKSR 908
Cdd:COG4717 509 YREE---------------------------RLPPVLERASEYFSRLTDGRYRLIRID------EDLSLKV-DTEDGRTR 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612532491 909 HISSLSGGETFQSSLALALGLSEIVQQQSGgisleSIFIDEGFGTLDQETLETALDTLLNLKSTGRMVGIISHVSELK 986
Cdd:COG4717 555 PVEELSRGTREQLYLALRLALAELLAGEPL-----PLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVE 627
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-788 |
1.07e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 1 MKPLHLKLNNFGPFLKEEIDFskidNNELFLISGKTGSGKTMIFDAMTYALFG-KASTEQREEndlrsHFADGKQPMSVT 79
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRL----EDGVTVIHGVNGSGKSSLLEACFFALYGsKALDDTLDD-----VITIGAEEAEIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 80 FEFQLNNRIYKVHRQGPFIKEGNTTKTNAKFDVFEMVDGKYEIREskvisgtqFIIEILGVNADQFRQLFILPQGEFKRF 159
Cdd:PRK02224 72 LWFEHAGGEYHIERRVRLSGDRATTAKCVLETPEGTIDGARDVRE--------EVTELLRMDAEAFVNCAYVRQGEVNKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 160 LISNSREKQGILRTLFNSEKFEAIREILKEE---VKKEKAQIENRYQQIDLLWQEIESFDDDKIKGLLEVATQQIDKVIE 236
Cdd:PRK02224 144 INATPSDRQDMIDDLLQLGKLEEYRERASDArlgVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 237 NIPLLQARSKEILafvnESKETAIKEYEiiEKKTlENNILKDNINqlninkidfvqlkeqqpeieeieaklKLLQDITNL 316
Cdd:PRK02224 224 RYEEQREQARETR----DEADEVLEEHE--ERRE-ELETLEAEIE--------------------------DLRETIAET 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 317 lnyIENREKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKIS----FIDKTRVLFNDINKYQQSY 392
Cdd:PRK02224 271 ---EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEelrdRLEECRVAAQAHNEEAESL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 393 L-NIERLRTEGEQLGDELNNLIKGLEKVEDSIGNNEsdyEKIIELNNAITNINNEINVIKEN-EKAKAELDKLLGSKQEL 470
Cdd:PRK02224 348 ReDADDLEERAEELREEAAELESELEEAREAVEDRR---EEIEELEEEIEELRERFGDAPVDlGNAEDFLEELREERDEL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 471 ENQINEEKTILKNLEiklDRydkskldLNDKESFISEIKsavkigdqCPICGNEIQDLGHhidFDSIAKRQNEIKEIEAN 550
Cdd:PRK02224 425 REREAELEATLRTAR---ER-------VEEAEALLEAGK--------CPECGQPVEGSPH---VETIEEDRERVEELEAE 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 551 IHTMKSNIAVHNSEIKFVNEKISNINIKTQSDLSLEVLNKRLLENENALNNQRELnkfIEQMKEEKDNLTLQIHNKQLRL 630
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER---AEELRERAAELEAEAEEKREAA 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 631 NKNESELKLCRDLITEFET-----------LSKYNNITNFEVDYKKYIQDVNQHQEHSKEIED----KLIQLSQRKliEQ 695
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSklaelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDerreRLAEKRERK--RE 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 696 NNLNHYENQLETYNNDLELNEQSIEmemsrlNLTDNNDideiiawrgeqaELEQKRDTYKKRYHEFEMEIARLESLTKNK 775
Cdd:PRK02224 639 LEAEFDEARIEEAREDKERAEEYLE------QVEEKLD------------ELREERDDLQAEIGAVENELEELEELRERR 700
|
810
....*....|....*
gi 612532491 776 ELLDS--DKLKDEYE 788
Cdd:PRK02224 701 EALENrvEALEALYD 715
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
423-774 |
1.14e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 423 IGNNESDYEKIIELNNAITNINNEIN-VIKENEKAKAELDKLLGSKQELENQINEektILKNLEIKLDRYDKSKLDLNDK 501
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSsLQSELRRIENRLDELSQELSDASRKIGE---IEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 502 ESFISEIKSAVKIGDQcpicgnEIQDLGHHIDF--DSIAKRQNEIKEIEANI-HTMKSNIAVHNSEIKFVNEKISNINIK 578
Cdd:TIGR02169 743 EEDLSSLEQEIENVKS------ELKELEARIEEleEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 579 TQSDLSLEVLNKRLLENE--NALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELklcRDLITEFETLSKynNI 656
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL---RDLESRLGDLKK--ER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 657 TNFEVDYKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNLNHYENQL---------ETYNNDLELNEQSIEMEMSRLN 727
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeELSLEDVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 612532491 728 LTDNNDIDEIIAWRGEQAELEQKRDTYKKRYHEFEMEIARLESLTKN 774
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-93 |
5.47e-09 |
|
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: 57.23 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 3 PLHLKLNNFGPFLK-EEIDFSKidnnELFLISGKTGSGKTMIFDAMTYALFGKASTEQREENDLRSHFADGKQPMSVTFE 81
Cdd:cd03240 1 IDKLSIRNIRSFHErSEIEFFS----PLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLA 76
|
90
....*....|...
gi 612532491 82 FQLNN-RIYKVHR 93
Cdd:cd03240 77 FENANgKKYTITR 89
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
907-966 |
1.55e-08 |
|
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: 53.01 E-value: 1.55e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612532491 907 SRHISSLSGGET-FQSSLALALGLSEIVQQQSG-GISLESIFIDEGFGTLDQETLETALDTL 966
Cdd:pfam13558 27 YRRSGGLSGGEKqLLAYLPLAAALAAQYGSAEGrPPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
264-801 |
2.01e-08 |
|
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: 58.49 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 264 EIIEKKTLENNIL-KDNINQLNINKIDFVQLKEQQPEIEEIEAKLKLLQDITNLLNYIENREKIETK----IANSKKDIS 338
Cdd:TIGR04523 76 KIKILEQQIKDLNdKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKflteIKKKEKELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 339 ETNNKILNLVCDKRNIDKEKKMLEENGDLIESKISFIDktrvlfNDINKYQQSYLNIERLRTEGEQLGDELNNLIKGLEK 418
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK------NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 419 VEDSignnesdyekIIELNNAITNINNEINVIkenekakaeldkllgsKQELENQINEEKTILKNLEIKLDRYDKSKLDL 498
Cdd:TIGR04523 230 LKDN----------IEKKQQEINEKTTEISNT----------------QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 499 NDKESFISEIKSavkigdqcpicgnEIQDLGHHIDFDSIAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNI-NI 577
Cdd:TIGR04523 284 KELEKQLNQLKS-------------EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 578 KTQSDLSLEVLNKRLLENENALnnqRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKL----CRDLITEFETLSK- 652
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEI---EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQkdeqIKKLQQEKELLEKe 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 653 YNNITNFEVDYKKYIQDVNQhQEHSKEIEDKliQLSQRKLIEQNNLNHYENQLETYNNDLELNEQSIEMEMSRLnltdNN 732
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTN-QDSVKELIIK--NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL----KK 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612532491 733 DIDEIIAWRGEQAELEQKRDTYKKRYHEFEMEIARLESLTKNKElldSDKLKDEYELKKGKMNTLIDEY 801
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE---DELNKDDFELKKENLEKEIDEK 566
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
18-491 |
1.92e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.02 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 18 EIDFSKIDNNelfLISGKTGSGKTMIFDAMTYALFGKAsteqreendlrshFADGKQPM----------SVTFEFQLNNR 87
Cdd:PHA02562 21 EIQLDKVKKT---LITGKNGAGKSTMLEALTFALFGKP-------------FRDIKKGQlinsinkkdlLVELWFEYGEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 88 IYKVHRqgpfikegnttktNAKFDVFEM-VDGKYEIRESKVISGTQFIIEILGVNADQFRQLFILPQGEFKRFLISNSRE 166
Cdd:PHA02562 85 EYYIKR-------------GIKPNVFEIyCNGKLLDESASSKDFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFMQLSAPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 167 KQGILRTLFNSEKFEAIREILKEEVKKEKAQIENRYQQIDLLWQEIESFDDdkikgllevatqqidkvieNIPLLQARSK 246
Cdd:PHA02562 152 RRKLVEDLLDISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNK-------------------NIEEQRKKNG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 247 EILAFVNESKETAIKEYEIIekktlennilKDNINQLNINKIDFVqlkeqqpeieeieaklKLLQDITNLLNyienreKI 326
Cdd:PHA02562 213 ENIARKQNKYDELVEEAKTI----------KAEIEELTDELLNLV----------------MDIEDPSAALN------KL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 327 ETKIANSKKDISetnnkilnlvcdkrNIDKEKKMLEENGDL------IESKISFIDKTRvlfNDINKYQQSYLNIERLRT 400
Cdd:PHA02562 261 NTAAAKIKSKIE--------------QFQKVIKMYEKGGVCptctqqISEGPDRITKIK---DKLKELQHSLEKLDTAID 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 401 EGEQLGDELNNLIKglekvedsignnesdyeKIIELNNAITNINNEI-NVIKENEKAKAELDKLLGS----KQELEN-QI 474
Cdd:PHA02562 324 ELEEIMDEFNEQSK-----------------KLLELKNKISTNKQSLiTLVDKAKKVKAAIEELQAEfvdnAEELAKlQD 386
|
490
....*....|....*..
gi 612532491 475 NEEKTILKNLEIKLDRY 491
Cdd:PHA02562 387 ELDKIVKTKSELVKEKY 403
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-770 |
4.17e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 452 ENEKAKAELDKLLGSKQELENQINEEKTILKNLEI---KLDRYDKSKLDLNDKESFI--SEIKSAVKigdQCPICGNEIQ 526
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRereKAERYQALLKEKREYEGYEllKEKEALER---QKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 527 DLGHHIdfdsiAKRQNEIKEIEANIHTMKSNIAVHNSEIK--------FVNEKISNINIK-TQSDLSLEVLNKRLlenEN 597
Cdd:TIGR02169 248 SLEEEL-----EKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGELEAEiASLERSIAEKEREL---ED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 598 ALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRD----LITEFETLSKYNNITNFEV-DYKKYIQDVNQ 672
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeledLRAELEEVDKEFAETRDELkDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 673 HQEHSKEIEDKLIQLSQRKLIEQNNLNhyenqletynNDLElneqSIEMEMSRLNLTDNNDIDEIIAWRGEQAELEQKRD 752
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLN----------AAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330
....*....|....*...
gi 612532491 753 TYKKRYHEFEMEIARLES 770
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEK 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
241-683 |
5.75e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 241 LQARSKEILAFVNESKETAIKEYEIIEKKTLENNILKDNINQLNINKIDFVQLKEQQPEIEEIEAKLKLLQDITNLLNYI 320
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 321 ENREKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEENGdliESKISFIDKTRVLFNDINKYQQSYL-NIERLR 399
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN---SEKQRELEEKQNEIEKLKKENQSYKqEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 400 TEGEQLGDELNNLIKGLEKVEDSIGNNESDYEK----IIELNNAITNINNEI-NVIKENEKAKAELDKLLGSKQELENQI 474
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELlekeIERLKETIIKNNSEIkDLTNQDSVKELIIKNLDNTRESLETQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 475 NEEKTILKNLEIKLDrydKSKLDLNDKESFISEIKSAVKIGDqcpicgNEIQDLGhhidfDSIAKRQNEIKEIEANIHTM 554
Cdd:TIGR04523 471 KVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELE------EKVKDLT-----KKISSLKEKIEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 555 KSNIAVHNSEIKFVNEKISNINIKTQSDLSLEVLNKRLLENENALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNE 634
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 612532491 635 SELKLCRDlitEFETLSkyNNITNFEVDYKKYIQDVNQHQEHSKEIEDK 683
Cdd:TIGR04523 617 KELEKAKK---ENEKLS--SIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-800 |
8.19e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 155 EFKRFLISNSREKQGILRTLFNS-----EKFEAIREILKEEVKKEKAQIENRYQQIDLLWQEIEsfDDDKIKGLLEVATQ 229
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYAlaneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLD--ELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 230 QIDKVIENIPLLQARSKEILAFVNESKETAIKEYEIIEKKTLE-NNILKDNINQLNINKIDFVQLKEQQPeieeieaklK 308
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlELQIASLNNEIERLEARLERLEDRRE---------R 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 309 LLQDITNLLnyienREKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKIsfidktRVLFNDINKY 388
Cdd:TIGR02168 419 LQQEIEELL-----KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL------DAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 389 QQSYLNIERLRTEGEQLGDELNNLIKGLEKVEDSIG------NNESDYEKIIE------LNNAITNINNE----INVIKE 452
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEaalggrLQAVVVENLNAakkaIAFLKQ 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 453 NEKAKA---ELD-----KLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIKSAVKIGDQCPICGNE 524
Cdd:TIGR02168 568 NELGRVtflPLDsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 525 IQDLGHHIDFD------------SIAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNIN-----IKTQSDLSLEV 587
Cdd:TIGR02168 648 VTLDGDLVRPGgvitggsaktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqLRKELEELSRQ 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 588 LNKRLLENENALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRDLITEFETLSK--YNNITNFEVDYKK 665
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlKEELKALREALDE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 666 YIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNLNHYENQLEtynnDLELNEQSIEMEMSRLNLTDNNDIDEIIAWRGEQA 745
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 612532491 746 ELEQKRDTYKKRYHEFEMEIARLES--LTKNKELLDSDKLKDEYELKKGKMNTLIDE 800
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESkrSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
909-982 |
1.79e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 1.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612532491 909 HISSLSGGETfqsslaLALGLSEIVqqqsggisleSIFIDegFGTLDQETLETALDTLLNLkstgrmvGIISHV 982
Cdd:COG0419 155 PIETLSGGER------LRLALADLL----------SLILD--FGSLDEERLERLLDALEEL-------AIITHV 203
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-514 |
3.31e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 6 LKLNNFGPFLKE-EIDFSKidnnELFLISGKTGSGKTMIFDAMTYALFGKASTEQREEN--DLRSHFADGKQPM--SVTF 80
Cdd:TIGR02169 5 IELENFKSFGKKkVIPFSK----GFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERlsDLISNGKNGQSGNeaYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 81 EFQLNNRI----YKVHRQGPFIKEGNTTK--------TNAKFDVFEMVDGKYEIRESKVISGTqfIIEILGVNADQFRQL 148
Cdd:TIGR02169 81 TFKNDDGKfpdeLEVVRRLKVTDDGKYSYyylngqrvRLSEIHDFLAAAGIYPEGYNVVLQGD--VTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 149 F--ILPQGEFKRfLISNSREKQGILRTlfNSEKFEAIREILKEEVKK---EKAQIEnRYQQIDLLWQEIESFDDDKIKGL 223
Cdd:TIGR02169 159 IdeIAGVAEFDR-KKEKALEELEEVEE--NIERLDLIIDEKRQQLERlrrEREKAE-RYQALLKEKREYEGYELLKEKEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 224 LEVATQQIDKVIENIPLLQARSKEILAFVNESKETAIKEYEIIEKKTleNNILKDNINQLNiNKIDFVQLKEQQPEIEEI 303
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI--KDLGEEEQLRVK-EKIGELEAEIASLERSIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 304 EAKLKLLQDITNLLNYIENREKIETKIANSKKDISETNNKilnlvcdKRNIDKEKKMLEENGDLIESKISFIDKtrvlfn 383
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-------RDKLTEEYAELKEELEDLRAELEEVDK------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 384 dinKYQQSYLNIERLRTEGEQLGDELNNLIKGLEKVEDSIGNNESDYEkiiELNNAITNINNEIN-VIKENEKAKAELDK 462
Cdd:TIGR02169 379 ---EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA---DLNAAIAGIEAKINeLEEEKEDKALEIKK 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 612532491 463 LLGSKQELENQINEEKTILKNLEIKLDRYDKsklDLNDKESFISEIKSAVKI 514
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEK---ELSKLQRELAEAEAQARA 501
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
5-58 |
5.36e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.82 E-value: 5.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612532491 5 HLKLNNFGPFLKEEIDFskiDNNELFLISGKTGSGKTMIFDAMTYAL-------FGKASTE 58
Cdd:pfam13555 3 RLQLINWGTFDGHTIPI---DPRGNTLLTGPSGSGKSTLLDAIQTLLvpakrarFNKAANA 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-768 |
5.51e-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: 47.36 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 457 KAELDKLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIKSAVKIgdQCPICGNEIQDLGHHIDFDS 536
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK--DLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 537 --IAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNINI-KTQSDLSLEVLNKRL-LENENALNNQRELNKFIEQM 612
Cdd:TIGR02168 754 keLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEeLKALREALDELRAELtLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 613 KEEK---DNLTLQIHNKQLRLNKNESELKLCRDLITEFETlskynNITNFEVDYKKYIQDVNQHQEHSKEIEDKLIQLSQ 689
Cdd:TIGR02168 834 AATErrlEDLEEQIEELSEDIESLAAEIEELEELIEELES-----ELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612532491 690 RKLIEQNNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTDNNDIDEIIAwrgEQAELEQKRDTYKKRYHEFEMEIARL 768
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA---LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
4-59 |
8.78e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 45.66 E-value: 8.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 612532491 4 LHLKLNNFGPFLKEEIDFSKidnnELFLISGKTGSGKTMIFDAMTYALFGKASTEQ 59
Cdd:cd03241 2 LELSIKNFALIEELELDFEE----GLTVLTGETGAGKSILLDALSLLLGGRASADL 53
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
910-996 |
1.11e-04 |
|
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: 43.89 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 910 ISSLSGGETFQSSLALALGLSEIvqqqsGGISLesIFIDEGFGTLDQETLETALDTLLNLKSTGRMVGIISHVSELKNRI 989
Cdd:cd03227 75 RLQLSGGEKELSALALILALASL-----KPRPL--YILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELA 147
|
....*..
gi 612532491 990 PLVLEVK 996
Cdd:cd03227 148 DKLIHIK 154
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
398-683 |
1.29e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.88 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 398 LRTEGEQLGDELNNLIKGLEKVEDSIGNNESDYEKIIE-LNNAITNINNEINVIKENEKAKAEL-DKLLGSKQELENQIN 475
Cdd:COG4694 104 LEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEdLAKSIKDDLKKLFASSGRNYRKANLeKKLSALKSSSEDELK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 476 EEKTILKNLEIKLDRYDKSKLDLNDKESFISEI--------------------------KSAVKI-----GDQCPICGNE 524
Cdd:COG4694 184 EKLKLLKEEEPEPIAPITPLPDLKALLSEAETLleksavssaieelaaliqnpgnsdwvEQGLAYhkeeeDDTCPFCQQE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 525 -----IQDLGHHIDfDSIAKRQNEIKEIEANIHTMKSNIavhnSEIKFVNEKISNINIKTQSDLSLEVLNKRLLENENAL 599
Cdd:COG4694 264 laaerIEALEAYFD-DEYEKLLAALKDLLEELESAINAL----SALLLEILRTLLPSAKEDLKAALEALNALLETLLAAL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 600 NNQR---------ELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRDLITEFETLSKYNNITNFEVDYKKYIQDV 670
Cdd:COG4694 339 EEKIanpstsidlDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEEL 418
|
330
....*....|...
gi 612532491 671 NQHQEHSKEIEDK 683
Cdd:COG4694 419 KTIKALKKALEDL 431
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
178-857 |
2.64e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 178 EKFEAIREILKEEVKKEKAQIENRyqqidllwQEIESFDDDKIKGLLEVATQQIDKVIENIPL--LQARSKEILAFVNES 255
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKES--------NLIEKSYKDKFDNTLIDKINELDKAFKDASLndYEAKNNELIKYFNDL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 256 KETAIKE------YEIIEKKTLENNILKDNIN-QLNINKIDFVqlkeqqpeieeieaklkLLQDITNLLNYIENREKIET 328
Cdd:TIGR01612 1006 KANLGKNkenmlyHQFDEKEKATNDIEQKIEDaNKNIPNIEIA-----------------IHTSIYNIIDEIEKEIGKNI 1068
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 329 KIANsKKDISETNNKILNLvcdkrNIDKEKKMLEENGDLI-ESKISFIDKTRVLFNDINKYQQSYLN----IERLRTEGE 403
Cdd:TIGR01612 1069 ELLN-KEILEEAEINITNF-----NEIKEKLKHYNFDDFGkEENIKYADEINKIKDDIKNLDQKIDHhikaLEEIKKKSE 1142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 404 QLGDELNNLIKGLEKVEDSIGNNESDYEKIIELNNAITNINNEINVIKENEKAKAELDKLLGSKQELENQINEEKTILKN 483
Cdd:TIGR01612 1143 NYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKN 1222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 484 L-EIKLDRYDKSKldlNDKESFISEIKSAVKigdqcpicgneiqdlghhiDFDSIAKRQNEIKE---IEANIHTMKSNIA 559
Cdd:TIGR01612 1223 LgKLFLEKIDEEK---KKSEHMIKAMEAYIE-------------------DLDEIKEKSPEIENemgIEMDIKAEMETFN 1280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 560 VHNSEIK--FVNEKISNINIKTQSDLSLEVLnKRLLENENALNNQRELNKFIEQMKEEKDNLTLQIHN-----KQLRLNK 632
Cdd:TIGR01612 1281 ISHDDDKdhHIISKKHDENISDIREKSLKII-EDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEianiyNILKLNK 1359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 633 NESELKLCRDLITEFETLSKYNN--ITNFEVDYKKYIQDVNQHQEHSK-----------EIEDKLIQLSQRKLIEQNNLN 699
Cdd:TIGR01612 1360 IKKIIDEVKEYTKEIEENNKNIKdeLDKSEKLIKKIKDDINLEECKSKiestlddkdidECIKKIKELKNHILSEESNID 1439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 700 HYENQLETYNNDLELNEQSIEMEMSRL-----NLTDN--NDIDEIIawrgeqAELEQKRDTYKKRYHEFEMEIARLEslt 772
Cdd:TIGR01612 1440 TYFKNADENNENVLLLFKNIEMADNKSqhilkIKKDNatNDHDFNI------NELKEHIDKSKGCKDEADKNAKAIE--- 1510
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 773 KNKELldsdklkdeYELKKGKMNTLIDEYSAVhyQCQNNINKTQsivSHINYLNQELKDQQEIFQLAEIVSGKNNKNLTL 852
Cdd:TIGR01612 1511 KNKEL---------FEQYKKDVTELLNKYSAL--AIKNKFAKTK---KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKK 1576
|
....*
gi 612532491 853 ENFVL 857
Cdd:TIGR01612 1577 EKFRI 1581
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-738 |
5.81e-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: 43.89 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 323 REKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKISfiDKTRVLFNDINKYQQSYLNIERLRTEG 402
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--QLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 403 EQLGDELNNLIKGLEKVEDSIgnnESDYEKIIELNNAITNINNEInvikenEKAKAELDKLLGSKQELENQINEEKTILK 482
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEI---EELEERLEEAEEELAEAEAEI------EELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 483 NLEIkldRYDKSKLDLNDKESFISEiksavkigdqcpiCGNEIQDLGhhidfDSIAKRQNEIKEIEANIHTMKSNIAVHN 562
Cdd:TIGR02168 814 LLNE---EAANLRERLESLERRIAA-------------TERRLEDLE-----EQIEELSEDIESLAAEIEELEELIEELE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 563 SEIKfvnekiSNINIKTQSDLSLEVLNKRLlenENALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRD 642
Cdd:TIGR02168 873 SELE------ALLNERASLEEALALLRSEL---EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 643 LITEfetlsKYNniTNFEVDYKKYIQDVNQhqehSKEIEDKLIQLsQRKLIEQNNLN-----HYENQLETYNndlELNEQ 717
Cdd:TIGR02168 944 RLSE-----EYS--LTLEEAEALENKIEDD----EEEARRRLKRL-ENKIKELGPVNlaaieEYEELKERYD---FLTAQ 1008
|
410 420
....*....|....*....|..
gi 612532491 718 SIEMEMSRLNLTDN-NDIDEII 738
Cdd:TIGR02168 1009 KEDLTEAKETLEEAiEEIDREA 1030
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-69 |
6.90e-04 |
|
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: 41.19 E-value: 6.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612532491 5 HLKLNNFGPFLKEE-IDFSkidNNELFLISGKTGSGKTMIFDAMTYALFGKASTEQREENDLRSHF 69
Cdd:cd03227 1 KIVLGRFPSYFVPNdVTFG---EGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCI 63
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
176-925 |
7.50e-04 |
|
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: 43.81 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 176 NSEKFEAIREILKEEVKKEKAQIENRYQQIDLLWQEIESFDDDKIKgLLEVATQQIDKVIENIPLLQARSKEILAFVNES 255
Cdd:pfam02463 350 KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 256 KETAIKEYEIIEKKTLENNILKDNIN-QLNINKIDFVQLKEQQPEIEEIEAKLKLLQDITNLLNYIENREKIETKIANSK 334
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEkQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 335 KDISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKISFIDKTRVLFNDINKYQQSYLNIER-----LRTEGEQLGDEL 409
Cdd:pfam02463 509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgARKLRLLIPKLK 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 410 NNLIKGLEKVEDSIGNNESDYEKIIELNNAITNINNEINVIKENEKAKAELDKLLGSKQELENQINEEKTILKNLEIKLD 489
Cdd:pfam02463 589 LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASL 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 490 RYDKSKLDLNDKESFISEIKSAVKigdQCPICGNEIQDLGHHIDFDSIAKRQNEIKEIEANIHTMKSNIAVHNSEIK-FV 568
Cdd:pfam02463 669 SELTKELLEIQELQEKAESELAKE---EILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKqKI 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 569 NEKISNINIKTQSDLSLEVLNKRLLENENAL---------NNQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKL 639
Cdd:pfam02463 746 DEEEEEEEKSRLKKEEKEEEKSELSLKEKELaeerektekLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIE 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 640 CRDLITEFETLSKYNNITNFEVDYKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNLNHYENQLEtynnDLELNEQSI 719
Cdd:pfam02463 826 QEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE----EKEKEEKKE 901
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 720 EMEMSRLNLTDNNDIDEIIAWRGEQAELEQKRDTYKKRYHEFEMEIARLESLTKNKELLDSDKLKDEYELKKGKMNTLID 799
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 800 EYSAVhyqcqnninktQSIVSHINYLNQELKDQQEIFQLAEIVSGKNNKNLTLENFVLIYYLDQIIAQANLrlatmSDNR 879
Cdd:pfam02463 982 EFEEK-----------EERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLE-----LGGS 1045
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 612532491 880 YQLIRREAVSHGLSGLEIDVfDLHSNKSRHISSLSGGETFQSSLAL 925
Cdd:pfam02463 1046 AELRLEDPDDPFSGGIEISA-RPPGKGVKNLDLLSGGEKTLVALAL 1090
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
450-841 |
7.63e-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: 43.47 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 450 IKENEKAKAELDKLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIKSAVKI-GDQCPICGNEIQDL 528
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 529 GHHI--DFDSIAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNINIKTQSdlslevLNKRLLENENALNnqrELN 606
Cdd:TIGR04523 109 NSEIknDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND------LKKQKEELENELN---LLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 607 KFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRDLITEFETLSKYNNITNFEVDYKKyiQDVNQHQEHSKEIEDKLIQ 686
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ--QEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 687 LSQRKLIEQNNLNHYENQLETYNN---DLELNEQSIEMEMSRLNLTDNNDID-----EIIAWRGEQAELEQKRDTYKKRY 758
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 759 HEFEMEIARLESLTKNKElLDSDKLKDEYELKKGKMNTLIDEYsavhyqcQNNINKTQSIVSHINYLNQELKDQQEIFQL 838
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSE-SENSEKQRELEEKQNEIEKLKKEN-------QSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
...
gi 612532491 839 AEI 841
Cdd:TIGR04523 410 KDE 412
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
355-853 |
7.90e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 355 DKEKKMLEENGDLIESKISFIDKTRVLFNDINKYQQSYLNIERLR---TEGEQLGDELNNLIKGLEKVEDSIGNNESDYE 431
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEkreAEAEEALREQAELNRLKKKYLEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 432 -KIIELNNAITNINNEINVIKEN-EKAKAELDKLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIk 509
Cdd:pfam05557 97 sQLADAREVISCLKNELSELRRQiQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKEL- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 510 savkigdqcpicgneIQDLGHHIDFDSIAKrqnEIKEIEANIHTMKSNIAVHNSEIKFVNEKISNINI------------ 577
Cdd:pfam05557 176 ---------------EFEIQSQEQDSEIVK---NSKSELARIPELEKELERLREHNKHLNENIENKLLlkeevedlkrkl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 578 ----KTQSDL-SLEVLNKRLLENENA-----------LNNQRELNKFIEQM-------KEEKDNLTLQIHNKQLRLNKNE 634
Cdd:pfam05557 238 ereeKYREEAaTLELEKEKLEQELQSwvklaqdtglnLRSPEDLSRRIEQLqqreivlKEENSSLTSSARQLEKARRELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 635 SELKLCRDLITEFET-----------LSKYNNITNFEVDY-----KKYIQDVN------QHQEHSKEIEDkLIQLSQRKL 692
Cdd:pfam05557 318 QELAQYLKKIEDLNKklkrhkalvrrLQRRVLLLTKERDGyrailESYDKELTmsnyspQLLERIEEAED-MTQKMQAHN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 693 IE-QNNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTDNNDIDEII-AWRGEQAELEQKRDTYKKRYHEFEMEIARLEs 770
Cdd:pfam05557 397 EEmEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVdSLRRKLETLELERQRLREQKNELEMELERRC- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 771 ltknkelldsdkLKDEYELKKGKMNTLIDEYSAVHYQC-QNNINKTQSIVSHINYLNQELKDQQEIFQLAEIVSGKNNKN 849
Cdd:pfam05557 476 ------------LQGDYDPKKTKVLHLSMNPAAEAYQQrKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK 543
|
....
gi 612532491 850 LTLE 853
Cdd:pfam05557 544 EVLD 547
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
431-707 |
9.16e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 431 EKIIELNNAITNINNEINVIKE-NEKAKAELDKLLGSKQELENQINEEK-----------TILKNLEIKLDRY------- 491
Cdd:pfam06160 93 ELLDDIEEDIKQILEELDELLEsEEKNREEVEELKDKYRELRKTLLANRfsygpaideleKQLAEIEEEFSQFeeltesg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 492 ---------DKSKLDLNDKESFISEIKSAVK-----IGDQCpicgNEIQDL-------GHHIDFDSIAKrqnEIKEIEAN 550
Cdd:pfam06160 173 dylearevlEKLEEETDALEELMEDIPPLYEelkteLPDQL----EELKEGyremeeeGYALEHLNVDK---EIQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 551 IHTMKSNIAvhNSEIKFVNEKISNINikTQSDLSLEVLNKRLLENENALNNQRELNKFIEQMKEEKDNLTLQIHNKQLRL 630
Cdd:pfam06160 246 LEENLALLE--NLELDEAEEALEEIE--ERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSY 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 631 NKNESELKLCRDLITEFETLSKY-----NNITNFEV-------DYKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNL 698
Cdd:pfam06160 322 TLNENELERVRGLEKQLEELEKRydeivERLEEKEVayselqeELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
|
....*....
gi 612532491 699 NHYENQLET 707
Cdd:pfam06160 402 DEFKLELRE 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-512 |
1.23e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 172 RTLFNSEKFEAIREILKEEVKKEKAQIE--NRYQ---------QIDLLWQEIESFDD--DKIKGLLEVATQQIDKVIENI 238
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQAEkaERYKelkaelrelELALLVLRLEELREelEELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 239 PLLQARSKEILAFVNESKEtaikEYEIIEKKTLENNILKDNINQlNINKIDF------VQLKEQQPEIEEIEAKLKLLQD 312
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ-QKQILRErlanleRQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 313 ITNLLNyiENREKIETKIANSKKDISETNNKILNLVcdKRNIDKEKKMLEENGDLIEskisfidktrvlfndinKYQQSY 392
Cdd:TIGR02168 338 ELAELE--EKLEELKEELESLEAELEELEAELEELE--SRLEELEEQLETLRSKVAQ-----------------LELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 393 LN---IERLRTEGEQLGDELNNLIKGLEKVEDSIGNNESDY------EKIIELNNAITNINNEINVIKENEKAKAELDKL 463
Cdd:TIGR02168 397 SLnneIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 612532491 464 LGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIKSAV 512
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
318-732 |
2.08e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 318 NYIENREKIETKIANSKKDISETNNKILNLVCDKRNIDKEKKMLEENGDLIESKISFIDKTRVLFNDINKYQQSYLNIER 397
Cdd:PTZ00440 447 KYDEKINELKKSINQLKTLISIMKSFYDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIED 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 398 LRTEGEQLGDELNNLIKGLEKVEDSIGNNESDYEKIielNNAITNINNEINVIKENEKAkaeLDKLLGSKQELENQINEE 477
Cdd:PTZ00440 527 YYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLK---RSMKNDIKNKIKYIEENVDH---IKDIISLNDEIDNIIQQI 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 478 KTILKNLEIKLDRYDKSKLDLNDKesfISEIKSAVKIGDQCPICGNEIQDLGHHIDFDSIAKRQNEIKEIEANIHTMKSN 557
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDLQEK---VKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEK 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 558 IAVHNSEIkfVNEKISNINIKTQSDLSL-EVLNKRLLEN---------ENALNNQRELNKFIEQMKEEKDNLTLQIHNKQ 627
Cdd:PTZ00440 678 LEFMKSDN--IDNIIKNLKKELQNLLSLkENIIKKQLNNieqdisnslNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQII 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 628 LRLNKNESELKlcrdliTEFETLSKYNNItnfevdYKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNLNHYENQLET 707
Cdd:PTZ00440 756 NRKNEFILHLY------ENDKDLPDGKNT------YEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQK 823
|
410 420
....*....|....*....|....*
gi 612532491 708 YNNDLELNEQSIEMEMSRLNLTDNN 732
Cdd:PTZ00440 824 LEAHTEKNDEELKQLLQKFPTEDEN 848
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-755 |
2.52e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 361 LEENGDLIESKISFIDKTRVLFNdiNKYQQSYLNIERLRTEGEQLGDELNNLIKGLEKVEDSIGNNESDYEKIIE--LNN 438
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLAN--SELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDrdTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 439 AITnINNEINVIKENEKAKAELDKLLGS-KQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFISEIKSAVKiGDQ 517
Cdd:pfam15921 411 SIT-IDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT-AKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 518 CPICGNE--IQDLGhhidfDSIAKRQNEIKEIEANIHTMKSNIAVHNSEIKFVN---EKISNINIK--------TQSDLS 584
Cdd:pfam15921 489 MTLESSErtVSDLT-----ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTEcealklqmAEKDKV 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 585 LEVLNKRLlENENALNNQRelNKFIEQMKEEKDNLTLQIHNKQLRLNknesELKLCRDL----ITEFETlskynNITNFE 660
Cdd:pfam15921 564 IEILRQQI-ENMTQLVGQH--GRTAGAMQVEKAQLEKEINDRRLELQ----EFKILKDKkdakIRELEA-----RVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 661 VDYKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQNNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTdnndideiiaW 740
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ----------L 701
|
410
....*....|....*
gi 612532491 741 RGEQAELEQKRDTYK 755
Cdd:pfam15921 702 KSAQSELEQTRNTLK 716
|
|
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
316-738 |
2.88e-03 |
|
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];
Pssm-ID: 440834 [Multi-domain] Cd Length: 835 Bit Score: 41.63 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 316 LLNYIENREKIETKIANSKKD--ISETNNKILNLVCDKRNIDKE--KKMLEENGDLIESKISFIDKTRVLFNDINKYQQS 391
Cdd:COG1221 369 LLKLKENREELDKLSEYLEEYliISPDTEKKLISEEDEYELPYNfyEIIEDKYEELKSEGLSEEEINKIISKDIESYFKK 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 392 YLNIERLRTEGEQLG------DELNNLIKGLEKVEDSIGNNESDY-----------EKIIELNNAITNINNEINVIKENE 454
Cdd:COG1221 449 LIFKLDKSNISEELLlivvdeVIVNVVEIFEEAEKKLLRYNSSNLfialslhllstLLRIKKGKKIINPQLNEIKKKYYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 455 KAKAELDKLLGSKQELENQINEEKTILKNLEIKLDRYDKSKLDLNDKESFI--------SEIKSAVKIGDQCPICGNEIQ 526
Cdd:COG1221 529 EFILAAEAIKIIEEELKILIPDEEEGFILLLLIELKEEKSLSENVIVVVVIahggaaasSSMAVVNLLLLEVAVAAIDDP 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 527 DLghHIDFDSIAKRQNEIKEIEANIH------TMKSNIAVHNSEIKFVNEKISNINIKTqSDLSLEVLNKRLLENENALN 600
Cdd:COG1221 609 PL--EVVDVLIEEKTIVVIINKGKGGllllldDGGSLFGIIIIEEEGIIIVTVVIVSTT-TVLEAAARKKLLELDLDEII 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 601 NQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRDLITEFETLSKYNNITNFEVDYKKYIQDVNQHQEHSKEI 680
Cdd:COG1221 686 VLEELLKNPLESKKIKISTSKKKKIIVTTIAITTGEAGGILILILIIELLDKDLILIIIEILLIIIKEEILEKIIEEKKE 765
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612532491 681 EDKLIQLSQRKLIE---QNNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTDNNDIDEII 738
Cdd:COG1221 766 VIIIVIISIIPLIIppiILLLALKLIILIEILVLLEILIDKEKIENIIKELLSLLNIIIVL 826
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
584-841 |
7.68e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 584 SLEVLNKRLLENENALN----NQRELNKFIEQMKEEKDNLTLQIHNKQLRLNKNESELKLCRDLITEFETLSKY--NNIT 657
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSleQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 658 NFEVDYKKYIQDVNQHQEHSKEIEDKLIQLSQRKLIEQ-NNLNHYENQLETYNNDLELNEQSIEMEMSRLNLTDNNDIDE 736
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 737 IIAWRGEQAELEQKRDTYKKRYHEFEMEIARLESLTKNKELLDSDkLKDEYELKKGKMNTLIDEYSAVhyqcQNNINKTQ 816
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD-LESRLGDLKKERDELEAQLREL----ERKIEELE 909
|
250 260
....*....|....*....|....*..
gi 612532491 817 SIVSHINYLNQELKDQQEIF--QLAEI 841
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALeeELSEI 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-67 |
7.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612532491 5 HLKLNNFGPF-LKEEIDFSkidnNELFLISGKTGSGKTMIFDAMTYAL-------FGKASTEQRE-ENDLRS 67
Cdd:COG4913 5 RLQLINWGTFdGVHTIDFD----GRGTLLTGDNGSGKSTLLDAIQTLLvpakrprFNKAANDAGKsDRTLLS 72
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
408-715 |
8.32e-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: 40.42 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 408 ELNNLIKGLEKVEDSIGNNESDYEKIiELNNAITNINNEINVIKENEK-AKAELDKllgskqELENQINEEKTILKNLEI 486
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVEL-HLSNIENKKNELLDIIVEIKKhIHGEINK------DLNKILEDFKNKEKELSN 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 487 KLDRYDKSKLDLNDKESFISEIKSavKIGDQCPICGNEIQDLGHHID-----FDSIAKRQNEIKEIEANIHTMKSNIAVH 561
Cdd:TIGR01612 770 KINDYAKEKDELNKYKSKISEIKN--HYNDQINIDNIKDEDAKQNYDkskeyIKTISIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 562 -NSEIKFVNEKISNINIKTQSDLSL------EVLNKRLLENENALNNQREL-NKFIEQMKEEKDNLTlqihnkqlRLNKN 633
Cdd:TIGR01612 848 vDKFINFENNCKEKIDSEHEQFAELtnkikaEISDDKLNDYEKKFNDSKSLiNEINKSIEEEYQNIN--------TLKKV 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 634 ESELKLCRDLITEFETLSKYNNITNFEVDYK-KYIQDVNQ-HQEHSKEIEDKLIQLSQR--KLIEQNNLNHYE---NQLE 706
Cdd:TIGR01612 920 DEYIKICENTKESIEKFHNKQNILKEILNKNiDTIKESNLiEKSYKDKFDNTLIDKINEldKAFKDASLNDYEaknNELI 999
|
....*....
gi 612532491 707 TYNNDLELN 715
Cdd:TIGR01612 1000 KYFNDLKAN 1008
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
320-700 |
8.37e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.04 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 320 IENREKIETKiansKKDISETNNKILNLVCDKRNIDKEKKMLEENgdlieskisfidktrvlFNDINKYQQSYLNIERLR 399
Cdd:pfam13166 92 IEIQEKIAKL----KKEIKDHEEKLDAAEANLQKLDKEKEKLEAD-----------------FLDECWKKIKRKKNSALS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 400 TEGEQLGDELNNLIKGLEKVEDSIGNNE--SDYEKIIELNNAItninneinvikeNEKAKAELDKLLGSKQELE----NQ 473
Cdd:pfam13166 151 EALNGFKYEANFKSRLLREIEKDNFNAGvlLSDEDRKAALATV------------FSDNKPEIAPLTFNVIDFDalekAE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 474 INEEKTILKNLEIkldrydKSKLDLNDKESFISE-IKSAVKIGDQCPICGNEIQD-----LGHHIDfDSIAKRQNEIKEI 547
Cdd:pfam13166 219 ILIQKVIGKSSAI------EELIKNPDLADWVEQgLELHKAHLDTCPFCGQPLPAerkaaLEAHFD-DEFTEFQNRLQKL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 548 EANIHTMKSNI----------AVHNSEIKFVNEKISNIniktqsdlsLEVLNKRLLENENALNNQRE----------LNK 607
Cdd:pfam13166 292 IEKVESAISSLlaqlpavsdlASLLSAFELDVEDIESE---------AEVLNSQLDGLRRALEAKRKdpfksieldsVDA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612532491 608 FIEQMKEEKDNLTLQI--HNKQ---LRLNKNESELKLCRDLITEFETlskynNITNFEVDYKKYIQDVNQHQEHSKEIED 682
Cdd:pfam13166 363 KIESINDLVASINELIakHNEItdnFEEEKNKAKKKLRLHLVEEFKS-----EIDEYKDKYAGLEKAINSLEKEIKNLEA 437
|
410
....*....|....*....
gi 612532491 683 KLIQLSQR-KLIEQNNLNH 700
Cdd:pfam13166 438 EIKKLREEiKELEAQLRDH 456
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
906-981 |
8.92e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 38.67 E-value: 8.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612532491 906 KSRHISSLSGGETFQSSLALALglseiVQQQsggislESIFIDEGFGTLDQETLETALDTLLNLKSTGRMVGIISH 981
Cdd:cd03235 126 ADRQIGELSGGQQQRVLLARAL-----VQDP------DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| |
