|
Name |
Accession |
Description |
Interval |
E-value |
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-920 |
2.91e-59 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 214.63 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 1 MKLQAIDIFGYGKFVHRQFQLTDDFNVFLGPNGSGKSTLMSFVLSIMfgfpnqrrkgsrdfdtndqvrfggrlyfkdtqw 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 81 gdcaiertrangkqvlkmsiagqeakevdhfkqlfgdltrdtylayfgftepdlmqfiweseedfarslvnlgvtgklsl 160
Cdd:COG4717 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 161 sqeVDQLQADADSLYRPQGQNPKLNQEmvELERQNQDLVAARQEEDAYFDLDQELSDKKAALAEVQSAEQNARQSLMDLE 240
Cdd:COG4717 48 ---LERLEKEADELFKPQGRKPELNLK--ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 241 KADQQSASDEERVALGFELAQYDgprfsdkdvdqwqnivntkdrlvEEYQELnpegfvimdsveaepeeelntggqwisd 320
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-----------------------ERLEEL---------------------------- 151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 321 hlgiseqmLAEARAYREQIRQNENLHDQIVEKRYQESRLLSALGAETIDELPRdfTNEEREEWQKRQKAIDSRrvfYKNT 400
Cdd:COG4717 152 --------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD--LAEELEELQQRLAELEEE---LEEA 218
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 401 KAGLENLMEDRESLGQERQEissnyDDFKATVYKYTQSWIrpigmtLLAVGIICYAISLFHTSPFWRGAGMPALILGLIF 480
Cdd:COG4717 219 QEELEELEEELEQLENELEA-----AALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 481 VLIAWFQERKGKHYVNEEEKAYQLDLRDIDSEtaeiqrqidnqnqqiaeleeeskqftkDLEAFLQAKGGSPYIMPLVWL 560
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEE---------------------------ELEELLAALGLPPDLSPEELL 340
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 561 qtDYVKQIEDLEREINQLihqsgagafgqahqaewsdyrqashnqalsldslfqqfeddyhnyrlyaanldyedqEQKAK 640
Cdd:COG4717 341 --ELLDRIEELQELLREA---------------------------------------------------------EELEE 361
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 641 QARLSQLADHIDQLekteenfLKQYNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNE-----DEAEVSEKI 715
Cdd:COG4717 362 ELQLEELEQEIAAL-------LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealDEEELEEEL 434
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 716 KTTKDQINSYEGQRQVLLADIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAWASDTLAAKTMEEATLGQGQDTV 795
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 796 QRVLAQANRYLFDLTNTKFEKMRYTDDSVEVYQPMRDQWTSVNQLSRGEKALLFVAMRFAFLDAQLGHQdLPILIDEGFA 875
Cdd:COG4717 515 PPVLERASEYFSRLTDGRYRLIRIDEDLSLKVDTEDGRTRPVEELSRGTREQLYLALRLALAELLAGEP-LPLILDDAFV 593
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 503434879 876 HLDQEYRQNIYRFLKEKSLSRQIIVFTFDQEITQGLHSDQVHHLE 920
Cdd:COG4717 594 NFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQEEGAHVIE 638
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
1-204 |
7.03e-17 |
|
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain contains a P-loop motif.
Pssm-ID: 433272 [Multi-domain] Cd Length: 207 Bit Score: 80.29 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 1 MKLQAIDIFGYGKFVHRQFQL---TDDFNVFLGPNGSGKSTLMSFVLSIMFGFPNQRRKGSRdFDtNDQVRFGGRLYFKD 77
Cdd:pfam13514 1 MRIRRLDLERYGPFTDRSLDFpagGPDLHLIYGPNEAGKSTALRAISDLLFGIPLRTPYNFL-HD-YSDLRIGATLENAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 78 TQwgDCAIERTRANGKQVLkmSIAGQEAKEvDHFKQLFGDLTRDTYLAYFGFTEPDLMQ---FIWESEEDFARSLVNLGv 154
Cdd:pfam13514 79 GE--TLEFRRRKGRKNTLL--DADGQPLPD-DVLAPFLGGLDRETFERMFGLDHERLREggeAILEAEGDLGQALFAAG- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503434879 155 TGKLSLSQEVDQLQADADSLYRPQGQNPKlnqEMVELERQNQDLVAARQE 204
Cdd:pfam13514 153 SGLAGLRRVLEALDAEADALFKPRGSSPR---AFNQALARLDEAQRELRE 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-902 |
2.85e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 495 VNEEEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAF------LQAKGGSpyimpLVWLQTDYVKQI 568
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltlLNEEAAN-----LRERLESLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 569 EDLEREINQLIHQSGAgafgQAHQAEwsdyrQASHNQAlSLDSLFQQFEDDyhnyrlyaanLDYEDQEQKAKQARLSQLA 648
Cdd:TIGR02168 834 AATERRLEDLEEQIEE----LSEDIE-----SLAAEIE-ELEELIEELESE----------LEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 649 DHIDQLEKTEENFLKQyNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSEKikttkdQINSYEGQ 728
Cdd:TIGR02168 894 SELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA------LENKIEDD 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 729 RQVLLADIARIENQLKQMKNSQaLQAMEQdkQEQVDQSYDTAVAWASDTLAAKT--------MEEATLGQGQDTVQRVLA 800
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPVN-LAAIEE--YEELKERYDFLTAQKEDLTEAKEtleeaieeIDREARERFKDTFDQVNE 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 801 QANR---YLFDLTNTKfekMRYTDDS------VEVY-QPMRDQWTSVNQLSRGEKALLFVAMRFAFLDAQlghqdlPI-- 868
Cdd:TIGR02168 1044 NFQRvfpKLFGGGEAE---LRLTDPEdlleagIEIFaQPPGKKNQNLSLLSGGEKALTALALLFAIFKVK------PApf 1114
|
410 420 430
....*....|....*....|....*....|....*...
gi 503434879 869 -LIDEGFAHLDQeyrQNIYRF---LKEKSLSRQIIVFT 902
Cdd:TIGR02168 1115 cILDEVDAPLDD---ANVERFanlLKEFSKNTQFIVIT 1149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
487-906 |
1.40e-06 |
|
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: 52.28 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 487 QERKGKHYVNEEEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQF-TKDLEAFLQAKGGSPYIMPLVWLQTDYV 565
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEeEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 566 KQIEDLEREINQ--LIHQSGAGAFGQAHQAEwsdYRQASHNQALSLDSLFQQFEDDYHNYRLYAANLDYEDQEQ-KAKQA 642
Cdd:pfam02463 778 EEREKTEKLKVEeeKEEKLKAQEEELRALEE---ELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLeKLAEE 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 643 RLSQLADHIDQLEKTEENFLKQYNLTDRADLE----KALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEV------- 711
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDelesKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAeillkye 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 712 SEKIKTTKDQINSYEGQRQVLLADIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAwasdTLAAKTMEEATLGQG 791
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL----EKERLEEEKKKLIRA 1010
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 792 QDTVQRVLAQANRYLFDLTNTKFEK------------MRYTD------DSVEV-YQPMRDQWTSVNQLSRGEKALLFVAM 852
Cdd:pfam02463 1011 IIEETCQRLKEFLELFVSINKGWNKvffylelggsaeLRLEDpddpfsGGIEIsARPPGKGVKNLDLLSGGEKTLVALAL 1090
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 503434879 853 RFAFLDAQlghqdlPI---LIDEGFAHLDQEYRQNIYRFLKEKSLSRQIIVFTFDQE 906
Cdd:pfam02463 1091 IFAIQKYK------PApfyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREE 1141
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
820-920 |
4.67e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 47.62 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 820 TDDSVEVYQPMRDQWTSVNQLSRGEKALLFVAMRFAfLDAQLghqdlpILIDEGFAHLDQEYRQNIYRFLKEKSLS-RQI 898
Cdd:cd00267 61 KDIAKLPLEELRRRIGYVPQLSGGQRQRVALARALL-LNPDL------LLLDEPTSGLDPASRERLLELLRELAEEgRTV 133
|
90 100
....*....|....*....|..
gi 503434879 899 IVFTFDQEITQgLHSDQVHHLE 920
Cdd:cd00267 134 IIVTHDPELAE-LAADRVIVLK 154
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-116 |
4.69e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 2 KLQAIDIFGYGKFVHRQ-FQLTDDFNVFLGPNGSGKSTLMSFVLSIMFGFPNQRRKGSRDFDTNDQVRFGGRLYFKDtqw 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTEtIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEH--- 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 503434879 81 GDCAIERTRANGKQVLKMSIAGQEAKEVdhFKQLFG 116
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEAKPSERKEA--LKRLLG 111
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
498-907 |
6.93e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 498 EEKAYQLdLRDIDSETAEIQRQIDNQNQQIAELEEESKQFtKDLEAFLQAKGGSPYImplvwlqtDYVKQIEDLEREINQ 577
Cdd:PRK01156 464 EEKSNHI-INHYNEKKSRLEEKIREIEIEVKDIDEKIVDL-KKRKEYLESEEINKSI--------NEYNKIESARADLED 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 578 LIHQsgagafgQAHQAEWSDYRQASHNQALSLD-SLFQQFEDDYHNYRLYAANLDYEDQeQKAKQARLSQLADHIDQLEK 656
Cdd:PRK01156 534 IKIK-------INELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNALAVISLIDIETN-RSRSNEIKKQLNDLESRLQE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 657 TEENF--LKQYNLTDRADLEKALTAY----GQFKDKEARYQFLNQYLD--KKASA----LNEDEAEVSEKIKTTKDQINS 724
Cdd:PRK01156 606 IEIGFpdDKSYIDKSIREIENEANNLnnkyNEIQENKILIEKLRGKIDnyKKQIAeidsIIPDLKEITSRINDIEDNLKK 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 725 YEGQRQVLLADIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAWASDTlaaKTMEEATLGQG------QDTVQRV 798
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL---KRLREAFDKSGvpamirKSASQAM 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 799 LAQANRYLFDLtNTKFEKMRYTDD-SVEVYQpmRDQWTSVNQLSRGEKALLFVAMRFAFldAQLGHQDLPILI-DEGFAH 876
Cdd:PRK01156 763 TSLTRKYLFEF-NLDFDDIDVDQDfNITVSR--GGMVEGIDSLSGGEKTAVAFALRVAV--AQFLNNDKSLLImDEPTAF 837
|
410 420 430
....*....|....*....|....*....|....*
gi 503434879 877 LDQEYRQN----IYRFLKEKSLSRQIIVFTFDQEI 907
Cdd:PRK01156 838 LDEDRRTNlkdiIEYSLKDSSDIPQVIMISHHREL 872
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-920 |
2.91e-59 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 214.63 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 1 MKLQAIDIFGYGKFVHRQFQLTDDFNVFLGPNGSGKSTLMSFVLSIMfgfpnqrrkgsrdfdtndqvrfggrlyfkdtqw 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 81 gdcaiertrangkqvlkmsiagqeakevdhfkqlfgdltrdtylayfgftepdlmqfiweseedfarslvnlgvtgklsl 160
Cdd:COG4717 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 161 sqeVDQLQADADSLYRPQGQNPKLNQEmvELERQNQDLVAARQEEDAYFDLDQELSDKKAALAEVQSAEQNARQSLMDLE 240
Cdd:COG4717 48 ---LERLEKEADELFKPQGRKPELNLK--ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 241 KADQQSASDEERVALGFELAQYDgprfsdkdvdqwqnivntkdrlvEEYQELnpegfvimdsveaepeeelntggqwisd 320
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-----------------------ERLEEL---------------------------- 151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 321 hlgiseqmLAEARAYREQIRQNENLHDQIVEKRYQESRLLSALGAETIDELPRdfTNEEREEWQKRQKAIDSRrvfYKNT 400
Cdd:COG4717 152 --------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD--LAEELEELQQRLAELEEE---LEEA 218
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 401 KAGLENLMEDRESLGQERQEissnyDDFKATVYKYTQSWIrpigmtLLAVGIICYAISLFHTSPFWRGAGMPALILGLIF 480
Cdd:COG4717 219 QEELEELEEELEQLENELEA-----AALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 481 VLIAWFQERKGKHYVNEEEKAYQLDLRDIDSEtaeiqrqidnqnqqiaeleeeskqftkDLEAFLQAKGGSPYIMPLVWL 560
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEE---------------------------ELEELLAALGLPPDLSPEELL 340
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 561 qtDYVKQIEDLEREINQLihqsgagafgqahqaewsdyrqashnqalsldslfqqfeddyhnyrlyaanldyedqEQKAK 640
Cdd:COG4717 341 --ELLDRIEELQELLREA---------------------------------------------------------EELEE 361
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 641 QARLSQLADHIDQLekteenfLKQYNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNE-----DEAEVSEKI 715
Cdd:COG4717 362 ELQLEELEQEIAAL-------LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealDEEELEEEL 434
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 716 KTTKDQINSYEGQRQVLLADIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAWASDTLAAKTMEEATLGQGQDTV 795
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 796 QRVLAQANRYLFDLTNTKFEKMRYTDDSVEVYQPMRDQWTSVNQLSRGEKALLFVAMRFAFLDAQLGHQdLPILIDEGFA 875
Cdd:COG4717 515 PPVLERASEYFSRLTDGRYRLIRIDEDLSLKVDTEDGRTRPVEELSRGTREQLYLALRLALAELLAGEP-LPLILDDAFV 593
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 503434879 876 HLDQEYRQNIYRFLKEKSLSRQIIVFTFDQEITQGLHSDQVHHLE 920
Cdd:COG4717 594 NFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQEEGAHVIE 638
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
1-204 |
7.03e-17 |
|
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain contains a P-loop motif.
Pssm-ID: 433272 [Multi-domain] Cd Length: 207 Bit Score: 80.29 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 1 MKLQAIDIFGYGKFVHRQFQL---TDDFNVFLGPNGSGKSTLMSFVLSIMFGFPNQRRKGSRdFDtNDQVRFGGRLYFKD 77
Cdd:pfam13514 1 MRIRRLDLERYGPFTDRSLDFpagGPDLHLIYGPNEAGKSTALRAISDLLFGIPLRTPYNFL-HD-YSDLRIGATLENAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 78 TQwgDCAIERTRANGKQVLkmSIAGQEAKEvDHFKQLFGDLTRDTYLAYFGFTEPDLMQ---FIWESEEDFARSLVNLGv 154
Cdd:pfam13514 79 GE--TLEFRRRKGRKNTLL--DADGQPLPD-DVLAPFLGGLDRETFERMFGLDHERLREggeAILEAEGDLGQALFAAG- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503434879 155 TGKLSLSQEVDQLQADADSLYRPQGQNPKlnqEMVELERQNQDLVAARQE 204
Cdd:pfam13514 153 SGLAGLRRVLEALDAEADALFKPRGSSPR---AFNQALARLDEAQRELRE 199
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
631-902 |
9.19e-08 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 55.90 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 631 DYEDQEQKAKQArLSQLADHIDQLEKTEENFLKQYNLTDRADLEKALTAYgqfkdKEARYQFLNQYLDKKASALNEDEAE 710
Cdd:COG4694 279 EYEKLLAALKDL-LEELESAINALSALLLEILRTLLPSAKEDLKAALEAL-----NALLETLLAALEEKIANPSTSIDLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 711 VSEKIKTTKDQINSYEGQRQVLLADIARIENQLKQMKnsQALQAMEQDKQEQVDQSYDTAV-AWASDTLAAKTMEEA--- 786
Cdd:COG4694 353 DQELLDELNDLIAALNALIEEHNAKIANLKAEKEEAR--KKLEAHELAELKEDLSRYKAEVeELIEELKTIKALKKAled 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 787 ------TLGQGQDTVQRVLAQANRYL--FDLTNTKFEKMRYTDDSVEVYQPMRDQWTSVNQLSRGEK---ALLFvamrfa 855
Cdd:COG4694 431 lkteisELEAELSSVDEAADEINEELkaLGFDEFSLEAVEDGRSSYRLKRNGENDAKPAKTLSEGEKtaiALAY------ 504
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 503434879 856 FL----DAQLGHQDLPILIDEGFAHLDQEYRQNIYRFLKEKSLS-RQIIVFT 902
Cdd:COG4694 505 FLaeleGDENDLKKKIVVIDDPVSSLDSNHRFAVASLLKELSKKaKQVIVLT 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-902 |
2.85e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 495 VNEEEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAF------LQAKGGSpyimpLVWLQTDYVKQI 568
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltlLNEEAAN-----LRERLESLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 569 EDLEREINQLIHQSGAgafgQAHQAEwsdyrQASHNQAlSLDSLFQQFEDDyhnyrlyaanLDYEDQEQKAKQARLSQLA 648
Cdd:TIGR02168 834 AATERRLEDLEEQIEE----LSEDIE-----SLAAEIE-ELEELIEELESE----------LEALLNERASLEEALALLR 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 649 DHIDQLEKTEENFLKQyNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSEKikttkdQINSYEGQ 728
Cdd:TIGR02168 894 SELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA------LENKIEDD 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 729 RQVLLADIARIENQLKQMKNSQaLQAMEQdkQEQVDQSYDTAVAWASDTLAAKT--------MEEATLGQGQDTVQRVLA 800
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPVN-LAAIEE--YEELKERYDFLTAQKEDLTEAKEtleeaieeIDREARERFKDTFDQVNE 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 801 QANR---YLFDLTNTKfekMRYTDDS------VEVY-QPMRDQWTSVNQLSRGEKALLFVAMRFAFLDAQlghqdlPI-- 868
Cdd:TIGR02168 1044 NFQRvfpKLFGGGEAE---LRLTDPEdlleagIEIFaQPPGKKNQNLSLLSGGEKALTALALLFAIFKVK------PApf 1114
|
410 420 430
....*....|....*....|....*....|....*...
gi 503434879 869 -LIDEGFAHLDQeyrQNIYRF---LKEKSLSRQIIVFT 902
Cdd:TIGR02168 1115 cILDEVDAPLDD---ANVERFanlLKEFSKNTQFIVIT 1149
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-68 |
9.99e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.93 E-value: 9.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503434879 1 MKLQAIDIFGYGKFVHRQFQLTDDFNVFLGPNGSGKSTLMSfVLSIMFGFPNQRRKGSRDFDTNDQVR 68
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILE-ALRLLLGPSSSRKFDEEDFYLGDDPD 67
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
487-906 |
1.40e-06 |
|
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: 52.28 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 487 QERKGKHYVNEEEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQF-TKDLEAFLQAKGGSPYIMPLVWLQTDYV 565
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEeEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 566 KQIEDLEREINQ--LIHQSGAGAFGQAHQAEwsdYRQASHNQALSLDSLFQQFEDDYHNYRLYAANLDYEDQEQ-KAKQA 642
Cdd:pfam02463 778 EEREKTEKLKVEeeKEEKLKAQEEELRALEE---ELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLeKLAEE 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 643 RLSQLADHIDQLEKTEENFLKQYNLTDRADLE----KALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEV------- 711
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDelesKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAeillkye 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 712 SEKIKTTKDQINSYEGQRQVLLADIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAwasdTLAAKTMEEATLGQG 791
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL----EKERLEEEKKKLIRA 1010
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 792 QDTVQRVLAQANRYLFDLTNTKFEK------------MRYTD------DSVEV-YQPMRDQWTSVNQLSRGEKALLFVAM 852
Cdd:pfam02463 1011 IIEETCQRLKEFLELFVSINKGWNKvffylelggsaeLRLEDpddpfsGGIEIsARPPGKGVKNLDLLSGGEKTLVALAL 1090
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 503434879 853 RFAFLDAQlghqdlPI---LIDEGFAHLDQEYRQNIYRFLKEKSLSRQIIVFTFDQE 906
Cdd:pfam02463 1091 IFAIQKYK------PApfyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREE 1141
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
820-920 |
4.67e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 47.62 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 820 TDDSVEVYQPMRDQWTSVNQLSRGEKALLFVAMRFAfLDAQLghqdlpILIDEGFAHLDQEYRQNIYRFLKEKSLS-RQI 898
Cdd:cd00267 61 KDIAKLPLEELRRRIGYVPQLSGGQRQRVALARALL-LNPDL------LLLDEPTSGLDPASRERLLELLRELAEEgRTV 133
|
90 100
....*....|....*....|..
gi 503434879 899 IVFTFDQEITQgLHSDQVHHLE 920
Cdd:cd00267 134 IIVTHDPELAE-LAADRVIVLK 154
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-116 |
4.69e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 2 KLQAIDIFGYGKFVHRQ-FQLTDDFNVFLGPNGSGKSTLMSFVLSIMFGFPNQRRKGSRDFDTNDQVRFGGRLYFKDtqw 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTEtIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEH--- 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 503434879 81 GDCAIERTRANGKQVLKMSIAGQEAKEVdhFKQLFG 116
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEAKPSERKEA--LKRLLG 111
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
498-907 |
6.93e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 498 EEKAYQLdLRDIDSETAEIQRQIDNQNQQIAELEEESKQFtKDLEAFLQAKGGSPYImplvwlqtDYVKQIEDLEREINQ 577
Cdd:PRK01156 464 EEKSNHI-INHYNEKKSRLEEKIREIEIEVKDIDEKIVDL-KKRKEYLESEEINKSI--------NEYNKIESARADLED 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 578 LIHQsgagafgQAHQAEWSDYRQASHNQALSLD-SLFQQFEDDYHNYRLYAANLDYEDQeQKAKQARLSQLADHIDQLEK 656
Cdd:PRK01156 534 IKIK-------INELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNALAVISLIDIETN-RSRSNEIKKQLNDLESRLQE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 657 TEENF--LKQYNLTDRADLEKALTAY----GQFKDKEARYQFLNQYLD--KKASA----LNEDEAEVSEKIKTTKDQINS 724
Cdd:PRK01156 606 IEIGFpdDKSYIDKSIREIENEANNLnnkyNEIQENKILIEKLRGKIDnyKKQIAeidsIIPDLKEITSRINDIEDNLKK 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 725 YEGQRQVLLADIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAWASDTlaaKTMEEATLGQG------QDTVQRV 798
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL---KRLREAFDKSGvpamirKSASQAM 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 799 LAQANRYLFDLtNTKFEKMRYTDD-SVEVYQpmRDQWTSVNQLSRGEKALLFVAMRFAFldAQLGHQDLPILI-DEGFAH 876
Cdd:PRK01156 763 TSLTRKYLFEF-NLDFDDIDVDQDfNITVSR--GGMVEGIDSLSGGEKTAVAFALRVAV--AQFLNNDKSLLImDEPTAF 837
|
410 420 430
....*....|....*....|....*....|....*
gi 503434879 877 LDQEYRQN----IYRFLKEKSLSRQIIVFTFDQEI 907
Cdd:PRK01156 838 LDEDRRTNlkdiIEYSLKDSSDIPQVIMISHHREL 872
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
505-748 |
1.39e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 505 DLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAflqakggspyimplvwLQTDYV---KQIEDLEREINQLIHQ 581
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN----------------SESENSekqRELEEKQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 582 sgagafgqahQAEWSDYRQASHNQALSLDSLFQQFEDDYHNY--RLYAANLDYE--DQEQKAKQARLSQLADHIDQLEKT 657
Cdd:TIGR04523 379 ----------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeQIKKLQQEKEllEKEIERLKETIIKNNSEIKDLTNQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 658 EENFLKQYNLTD--RADLEKALTAY-GQFKDKEARYQFLNQYLDKKAS---ALNEDEAEVSEKIKTTKDQINSYEGQRQV 731
Cdd:TIGR04523 449 DSVKELIIKNLDntRESLETQLKVLsRSINKIKQNLEQKQKELKSKEKelkKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
250
....*....|....*..
gi 503434879 732 LLADIARIENQLKQMKN 748
Cdd:TIGR04523 529 LESEKKEKESKISDLED 545
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
839-906 |
2.06e-04 |
|
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: 43.36 E-value: 2.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503434879 839 QLSRGEKALLFVAMRFAFldAQLGHQDLPILI-DEGFAHLDQEYRQN----IYRFLKEKSLsRQIIVFTFDQE 906
Cdd:cd03240 115 RCSGGEKVLASLIIRLAL--AETFGSNCGILAlDEPTTNLDEENIEEslaeIIEERKSQKN-FQLIVITHDEE 184
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-65 |
2.07e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 43.25 E-value: 2.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503434879 6 IDIFGYGKFVHRQFQLTDDFNVFLGPNGSGKSTLMSFVLSIMFGF-PNQRRKGSRDFDTND 65
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKtSRLKRKSGGGFVKGD 61
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
471-754 |
2.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 471 MPALILGLIFVLIAWFQE------RKGKHYVNEEEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAF 544
Cdd:COG4942 2 RKLLLLALLLALAAAAQAdaaaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 545 LQakggspyimplvwlqtdyvkQIEDLEREINQLIHQSgagafgQAHQAEWSD-----YRQASHNQALSLDSlFQQFEDD 619
Cdd:COG4942 82 EA--------------------ELAELEKEIAELRAEL------EAQKEELAEllralYRLGRQPPLALLLS-PEDFLDA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 620 YHNYRLYAANLDYEDQEQKAKQARLSQLADHIDQLEKteenflkqynltDRADLEKALTAygqfkdkearyqflnqyLDK 699
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEA------------ERAELEALLAE-----------------LEE 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503434879 700 KASALNEDEAEVSEKIKTTKDQINSYEGQRQVLLADIARIENQLKQMKNSQALQA 754
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-806 |
4.46e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 621 HNYRLYAANLDYEDQEQKAKQARLSQLADHIDQLEKTEENfLKQYNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKK 700
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 701 ASALNEDEAEVSEKIKTTKDQINSYEGQRQVLLADIARIENQLKQMKNS-----QALQAMEQDKQEQVDQSYDTAVAwAS 775
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAElaeaeEALLEAEAELAEAEEELEELAEE-LL 389
|
170 180 190
....*....|....*....|....*....|.
gi 503434879 776 DTLAAKTMEEATLGQGQDTVQRVLAQANRYL 806
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLE 420
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
500-804 |
5.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 500 KAYQLDLRDIDSETA-----EIQRQIDNQNQQIAELEEESKQFTKDLEAfLQAkggspyimplvwlqtdyvkQIEDLERE 574
Cdd:COG1196 216 RELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAE-LEA-------------------ELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 575 INQLIHQSgagafgQAHQAEWSDYRQASHNQALSLDSLFQQFEDdyhnyrlYAANLDYEDQEQKAKQARLSQLADHIDQL 654
Cdd:COG1196 276 LEELELEL------EEAQAEEYELLAELARLEQDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 655 EKTEENflkqynltDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSEKIKTTKDQINSYEGQRQVLLA 734
Cdd:COG1196 343 EEELEE--------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 735 DIARIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAWASDTLAAKTMEEATLGQGQDTVQRVLAQANR 804
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-751 |
6.11e-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: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 158 LSLSQEVD----QLQADADSLYRPQGQNPKLNQEMVELERQNQDLVAARQE-EDAYFDLDQELSDKKAALAEVQSAEQNA 232
Cdd:TIGR02168 291 YALANEISrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 233 RQSLMDLEKADQQSASD-----EERVALGFELAQYDgprfsdkdvDQWQNIVNTKDRLVEEYQELNPEgfvIMDSVEAEP 307
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKvaqleLQIASLNNEIERLE---------ARLERLEDRRERLQQEIEELLKK---LEEAELKEL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 308 EEELNTGGQWISDHLGISEQMLAEARAYREQIRQNENlhdQIVEKRYQESRLLSALGA-ETIDELPRDFTNEEREEWQKR 386
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQ---ALDAAERELAQLQARLDSlERLQENLEGFSEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 387 QK--AIDSRRVFYKNTKAGLEN-------------LMEDRESLGQERQEISSNyDDFKATVYKYTQSW---IRPIGMTLL 448
Cdd:TIGR02168 516 SGlsGILGVLSELISVDEGYEAaieaalggrlqavVVENLNAAKKAIAFLKQN-ELGRVTFLPLDSIKgteIQGNDREIL 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 449 AV--GIICYAISLFHTSPFWRGAGmpALILGLIFVL----IAWFQERKGKHYVNEEEKAYQLDLRD--IDSETAEIQRQI 520
Cdd:TIGR02168 595 KNieGFLGVAKDLVKFDPKLRKAL--SYLLGGVLVVddldNALELAKKLRPGYRIVTLDGDLVRPGgvITGGSAKTNSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 521 DNQNQQIAELEEESKQFTKDLEAFLQAkggspyimplvwlQTDYVKQIEDLEREINQLihqsgagafgqahQAEWSDYRQ 600
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKA-------------LAELRKELEELEEELEQL-------------RKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 601 ASHNQALSLDSLFQQFEDDYHNY-RLYAANLDYEDQEQKAKQAR------LSQLADHIDQLEKTEENFLKQYNlTDRADL 673
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIaQLSKELTELEAEIEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELK-ALREAL 805
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503434879 674 EKALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSEKIKTTKDQINSYEGQRQVLLADIARIENQLKQMKNSQA 751
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
504-736 |
8.82e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 504 LDLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAFLQAkggspyimplvwlqtdyvkqIEDLEREINQLihqsg 583
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE--------------------LEDLEKEIKRL----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 584 agafgqahqaewsdyrqashnqalsldslfqqfeddyhnyrlyaaNLDYEDQEQKAK--QARLSQLADH--IDQLEKtEE 659
Cdd:COG1579 65 ---------------------------------------------ELEIEEVEARIKkyEEQLGNVRNNkeYEALQK-EI 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503434879 660 NFLKQynltDRADLEKA-LTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSEKIKTTKDQINSYEGQRQVLLADI 736
Cdd:COG1579 99 ESLKR----RISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-39 |
1.32e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.52 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503434879 1 MKLQAIDIFGYGKFVHRQ--FQLTDDFNVFLGPNGSGKSTL 39
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEidFDNPPRLTVLVGENGSGKTTL 41
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
836-919 |
1.35e-03 |
|
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: 40.42 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 836 SVNQLSRGEKALLFVAMRFAFLDaqlgHQDLP-ILIDEGFAHLDQEYRQNIYRFLKEKSLS-RQIIVFTFDQEITqgLHS 913
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS----LKPRPlYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELA--ELA 147
|
....*.
gi 503434879 914 DQVHHL 919
Cdd:cd03227 148 DKLIHI 153
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
832-909 |
1.77e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 41.09 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 832 DQWTSVNQLSRGEKALLFVAMRFAFldaqlgHQDLP---ILIDEGFAHLDQEYRQNIYRFLKEKSLSRQIIVFTFDQEIT 908
Cdd:cd03272 151 DEQQEMQQLSGGQKSLVALALIFAI------QKCDPapfYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELL 224
|
.
gi 503434879 909 Q 909
Cdd:cd03272 225 E 225
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
23-46 |
2.36e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 40.63 E-value: 2.36e-03
10 20
....*....|....*....|....*..
gi 503434879 23 DDFNVFLGPNGSGKSTLM---SFVLSI 46
Cdd:cd03275 22 DRFTCIIGPNGSGKSNLMdaiSFVLGE 48
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
836-891 |
3.62e-03 |
|
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: 37.60 E-value: 3.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503434879 836 SVNQLSRGEKALLFVAMRFAFLDAQLGHQDL------PILIDEGFAHLDQEYRQNIYRFLKE 891
Cdd:pfam13558 29 RSGGLSGGEKQLLAYLPLAAALAAQYGSAEGrppaprLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
6-47 |
3.85e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.34 E-value: 3.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503434879 6 IDIFGYGKFVHRQFQLTDdFNVFLGPNGSGKSTLMSFVLSIM 47
Cdd:COG4938 4 ISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLIQALLLLL 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
487-713 |
5.01e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 487 QERKGKHYVNEEEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAFLQAkggspyimplvwlQTDYVK 566
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-------------LAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 567 QIEDLEREINQLIhqsgagafgQAHQAEWSDYRQASHNQALSLDSLFQQFEDDYHNYRLYAANLDYEDQEQKAKQARLSQ 646
Cdd:COG1196 366 ALLEAEAELAEAE---------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503434879 647 LADHIDQLEKTEENFLKQYNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSE 713
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-40 |
6.36e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 39.89 E-value: 6.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503434879 1 MKLQAIDIFGYGKFVHRQFQLTDDFNVFLGPNGSGKSTLM 40
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSIL 40
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
498-805 |
6.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 498 EEKAYQLDLRDIDSETAEIQRQIDNQNQQIAELEEESKQFTKDLEAfLQAKggspyimplvwlQTDYVKQIEDLEREINQ 577
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-LQAE------------IDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 578 LIHQSGAgafgQAHQAewsdyrQASHNQALSLDSLFQQfeddyhnyrlyaanldyedqeqkakqarlSQLADHIDQLEkt 657
Cdd:COG3883 84 RREELGE----RARAL------YRSGGSVSYLDVLLGS-----------------------------ESFSDFLDRLS-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 658 eenFLKQYNLTDRADLEKALTAYGQFKDKEARYQFLNQYLDKKASALNEDEAEVSEKIKTTKDQINSYEGQRQVLLADIA 737
Cdd:COG3883 123 ---ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503434879 738 RIENQLKQMKNSQALQAMEQDKQEQVDQSYDTAVAWASDTLAAKTMEEATLGQGQDTVQRVLAQANRY 805
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGA 267
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-42 |
7.82e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 7.82e-03
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
497-762 |
8.10e-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: 40.05 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 497 EEEKAYQLDLRDID-----SETAEIQRQIDNQNQQIAELEEESKQFTKDLEAFLQAkggspyIMPLVWLQTDYVKQIEDL 571
Cdd:TIGR02169 211 ERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 572 -EREINQLihQSGAGAFgQAHQAEWSDYRQASHNQALSLDSLFQQFEDDYHNYRLYAANLdyeDQEQKAKQARLSQLADH 650
Cdd:TIGR02169 285 gEEEQLRV--KEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL---EREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503434879 651 IDQLEKTEEnflkqynlTDRADLEKALTAYGQFKDKEARYQF-----------LNQYLDKKASALNEDEAEVSE---KIK 716
Cdd:TIGR02169 359 YAELKEELE--------DLRAELEEVDKEFAETRDELKDYREkleklkreineLKRELDRLQEELQRLSEELADlnaAIA 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 503434879 717 TTKDQINSYEGQRQVLLADIARIENQLKQMKN--SQALQAMEQDKQEQ 762
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlSKYEQELYDLKEEY 478
|
|
| |
