|
Name |
Accession |
Description |
Interval |
E-value |
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-958 |
1.81e-87 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 293.60 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 1 MIIKSLEIYGYGQFVQRKIEFNKNFTEIFGENEAGKSTIQAFIHSILfgfptkkskeprleprlgnqyggklvlilddgl 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 81 eieverikgsaqgdvkvylpngavrddawlqkklnyiskktyqgifsfdvlglqdihrnlnekqlqdyllqagalgstef 160
Cdd:COG4717 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 161 tsmREVINRKKDELYKKSGKNPIINqqIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMHEEKQ 240
Cdd:COG4717 48 ---LERLEKEADELFKPQGRKPELN--LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 241 KEVALHDHSQEWKSLEQQLNIEPitfpekgvdryekarahkqslerdiglrnERLAQLKEeatqlepvkqsdidafisln 320
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-----------------------------ERLEELEE-------------------- 153
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 321 qQENEIKNKEFELTAIEKDIANKQRDKDELQAnigwsethhdvDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEENKIE 400
Cdd:COG4717 154 -RLEELRELEEELEELEAELAELQEELEELLE-----------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 401 DNAVHSELDSVEEKIVPEETFEKKKEYSQqvielnekenlysklkerfeieqqekqkrqkLLRTTFILLTLVGIGLTAFS 480
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARL-------------------------------LLLIAAALLALLGLGGSLLS 270
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 481 FISnnMLFGIIFAVLTLVFVIGIIMSKSKEVdyseaITDEIEEIKAQLAildenydldfdldeqyrirdhwQQALKNKDI 560
Cdd:COG4717 271 LIL--TIAGVLFLVLGLLALLFLLLAREKAS-----LGKEAEELQALPA----------------------LEELEEEEL 321
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 561 LEekrqyiegrlndakgrhdelqstvenVKDELYLSSKISNDLIVDSISTMANIKALDQHISDLNQQrqqlvqeldtfyn 640
Cdd:COG4717 322 EE--------------------------LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------------- 362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 641 haeavtksqfvyfnklslfhdvqqwlksaedtnekwrinaentklvtnelnhlnAQLEENNKEITALFDFINVGTEEDFY 720
Cdd:COG4717 363 ------------------------------------------------------LQLEELEQEIAALLAEAGVEDEEELR 388
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 721 QHHEDYQTYTSNLSRFNDLTKYLENQNYSYELSSSLSekTTAQLEEEDHLLATQVDEYNEQYLEMQAQVSDLSAQINHME 800
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 801 TDTTLANLRHEYHSLKNQLNDIAKDWASLSYLQSLVDEHIKQIKDKRLPQVINEAVEILKHLTDGRYTMINYNED-SITV 879
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRLTDGRYRLIRIDEDlSLKV 546
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613182489 880 KHVNGQLYDPVELSQSTKELLYVALRISLIKVLRPyYPFPLIVDDAFVHFDKKRTEKMLNYLRSLSEHYQVLYFTCVKD 958
Cdd:COG4717 547 DTEDGRTRPVEELSRGTREQLYLALRLALAELLAG-EPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
1-208 |
8.53e-23 |
|
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: 97.24 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 1 MIIKSLEIYGYGQFVQRKIEFN---KNFTEIFGENEAGKSTIQAFIHSILFGFPTKKS---KEPRLEPRLGnqyggkLVL 74
Cdd:pfam13514 1 MRIRRLDLERYGPFTDRSLDFPaggPDLHLIYGPNEAGKSTALRAISDLLFGIPLRTPynfLHDYSDLRIG------ATL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 75 ILDDGLEIEVERIKGSAQGdvkvyL--PNGAVRDDAWLQKKLNYISKKTYQGIFSFD----VLGLQDIhrnLNEK----Q 144
Cdd:pfam13514 75 ENADGETLEFRRRKGRKNT-----LldADGQPLPDDVLAPFLGGLDRETFERMFGLDherlREGGEAI---LEAEgdlgQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613182489 145 LqdyLLQAGAlGSTEFTSMREVINRKKDELYKKSGKNPI-INQQIEQLKQLESQIREEEAKLETY 208
Cdd:pfam13514 147 A---LFAAGS-GLAGLRRVLEALDAEADALFKPRGSSPRaFNQALARLDEAQRELREATLRPEDW 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
189-461 |
2.15e-08 |
|
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: 58.53 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 189 EQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQlsKMHEEKQKEVALHDHSQEWKSLEQQLNIEpitfpe 268
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQLSKE------ 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 269 kgvdrYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDAfisLNQQENEIKNKEFELTAIEKDIANKQRDKD 348
Cdd:TIGR02168 756 -----LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 349 ELQANIGWSETHHDVdsseamksyVSEQIKNKQEQaayIKQLERSLEENKIEDNAVHSELDSVEEKI--VPEETFEKKKE 426
Cdd:TIGR02168 828 SLERRIAATERRLED---------LEEQIEELSED---IESLAAEIEELEELIEELESELEALLNERasLEEALALLRSE 895
|
250 260 270
....*....|....*....|....*....|....*
gi 613182489 427 YSQQVIELNEKEnlysklKERFEIEQQEKQKRQKL 461
Cdd:TIGR02168 896 LEELSEELRELE------SKRSELRRELEELREKL 924
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-94 |
8.37e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.70 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 2 IIKSLEIYGYGQFVQR-KIEFNKNFTEIFGENEAGKSTIQAFIHSILFGFPTKKSKEPRLEPRLGNQYGGKLVLILDDGL 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTeTIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGK 80
|
90
....*....|....
gi 613182489 81 EIEVERikgsAQGD 94
Cdd:COG0419 81 RYRIER----RQGE 90
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-454 |
1.97e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 169 RKKDELYKKSGKnpiinQQIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENL--------KHNLNQLSKMHEEKQ 240
Cdd:PTZ00121 1546 KKADELKKAEEL-----KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekKMKAEEAKKAEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 241 KEVALHDHSQEWKSLEQQLNIEpitfpEKGVDRYEKARAHkqslERDIGLRNERLAQLKEE----ATQLEPVKQSDIDAF 316
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKE-----AEEKKKAEELKKA----EEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAA 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 317 ISLNQQENEIKNKEFELTAIEKDIANKQRDKDELQANIGWSET---HHDVDSSEAMKSYVSEQIKNKQEQAAyiKQLERS 393
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKDEEEKKKIAHLK--KEEEKK 1769
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613182489 394 LEENKIEDNAV-HSELDSVEEK--IVPEETFEKKKEYSQQVIELNEKENLY-SKLKERFEIEQQE 454
Cdd:PTZ00121 1770 AEEIRKEKEAViEEELDEEDEKrrMEVDKKIKDIFDNFANIIEGGKEGNLViNDSKEMEDSAIKE 1834
|
|
| DUF3784 |
pfam12650 |
Domain of unknown function (DUF3784); This family of proteins is functionally uncharacterized. ... |
451-504 |
7.77e-04 |
|
Domain of unknown function (DUF3784); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 96 and 110 amino acids in length.
Pssm-ID: 463655 Cd Length: 94 Bit Score: 39.50 E-value: 7.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 613182489 451 EQQEKQKRQKLLRTTFILLTLVGIGLTAFSFISN--NMLFGIIFAVLTLVFVIGII 504
Cdd:pfam12650 32 EEKEKYDEKKLCRFMGILLLLIGILFLLLGLLSAfgSEAFLIIAIIAIIIIVIYII 87
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-48 |
3.92e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.76 E-value: 3.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 613182489 3 IKSLEIYGYGQFVQR-KIEFNKNFTEIFGENEAGKSTIqafIHSILF 48
Cdd:cd03278 1 LKKLELKGFKSFADKtTIPFPPGLTAIVGPNGSGKSNI---IDAIRW 44
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-958 |
1.81e-87 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 293.60 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 1 MIIKSLEIYGYGQFVQRKIEFNKNFTEIFGENEAGKSTIQAFIHSILfgfptkkskeprleprlgnqyggklvlilddgl 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 81 eieverikgsaqgdvkvylpngavrddawlqkklnyiskktyqgifsfdvlglqdihrnlnekqlqdyllqagalgstef 160
Cdd:COG4717 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 161 tsmREVINRKKDELYKKSGKNPIINqqIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMHEEKQ 240
Cdd:COG4717 48 ---LERLEKEADELFKPQGRKPELN--LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 241 KEVALHDHSQEWKSLEQQLNIEPitfpekgvdryekarahkqslerdiglrnERLAQLKEeatqlepvkqsdidafisln 320
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELP-----------------------------ERLEELEE-------------------- 153
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 321 qQENEIKNKEFELTAIEKDIANKQRDKDELQAnigwsethhdvDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEENKIE 400
Cdd:COG4717 154 -RLEELRELEEELEELEAELAELQEELEELLE-----------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 401 DNAVHSELDSVEEKIVPEETFEKKKEYSQqvielnekenlysklkerfeieqqekqkrqkLLRTTFILLTLVGIGLTAFS 480
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARL-------------------------------LLLIAAALLALLGLGGSLLS 270
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 481 FISnnMLFGIIFAVLTLVFVIGIIMSKSKEVdyseaITDEIEEIKAQLAildenydldfdldeqyrirdhwQQALKNKDI 560
Cdd:COG4717 271 LIL--TIAGVLFLVLGLLALLFLLLAREKAS-----LGKEAEELQALPA----------------------LEELEEEEL 321
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 561 LEekrqyiegrlndakgrhdelqstvenVKDELYLSSKISNDLIVDSISTMANIKALDQHISDLNQQrqqlvqeldtfyn 640
Cdd:COG4717 322 EE--------------------------LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------------- 362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 641 haeavtksqfvyfnklslfhdvqqwlksaedtnekwrinaentklvtnelnhlnAQLEENNKEITALFDFINVGTEEDFY 720
Cdd:COG4717 363 ------------------------------------------------------LQLEELEQEIAALLAEAGVEDEEELR 388
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 721 QHHEDYQTYTSNLSRFNDLTKYLENQNYSYELSSSLSekTTAQLEEEDHLLATQVDEYNEQYLEMQAQVSDLSAQINHME 800
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 801 TDTTLANLRHEYHSLKNQLNDIAKDWASLSYLQSLVDEHIKQIKDKRLPQVINEAVEILKHLTDGRYTMINYNED-SITV 879
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRLTDGRYRLIRIDEDlSLKV 546
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613182489 880 KHVNGQLYDPVELSQSTKELLYVALRISLIKVLRPyYPFPLIVDDAFVHFDKKRTEKMLNYLRSLSEHYQVLYFTCVKD 958
Cdd:COG4717 547 DTEDGRTRPVEELSRGTREQLYLALRLALAELLAG-EPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
1-208 |
8.53e-23 |
|
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: 97.24 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 1 MIIKSLEIYGYGQFVQRKIEFN---KNFTEIFGENEAGKSTIQAFIHSILFGFPTKKS---KEPRLEPRLGnqyggkLVL 74
Cdd:pfam13514 1 MRIRRLDLERYGPFTDRSLDFPaggPDLHLIYGPNEAGKSTALRAISDLLFGIPLRTPynfLHDYSDLRIG------ATL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 75 ILDDGLEIEVERIKGSAQGdvkvyL--PNGAVRDDAWLQKKLNYISKKTYQGIFSFD----VLGLQDIhrnLNEK----Q 144
Cdd:pfam13514 75 ENADGETLEFRRRKGRKNT-----LldADGQPLPDDVLAPFLGGLDRETFERMFGLDherlREGGEAI---LEAEgdlgQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613182489 145 LqdyLLQAGAlGSTEFTSMREVINRKKDELYKKSGKNPI-INQQIEQLKQLESQIREEEAKLETY 208
Cdd:pfam13514 147 A---LFAAGS-GLAGLRRVLEALDAEADALFKPRGSSPRaFNQALARLDEAQRELREATLRPEDW 207
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
183-463 |
1.44e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 183 IINQQIEQLKQLESQ---------IREEEAKLETYHRLVDDRDKSsRRLENLKHNLNQLSKMHEEKQKEVALHDhsQEWK 253
Cdd:COG1196 194 ILGELERQLEPLERQaekaeryreLKEELKELEAELLLLKLRELE-AELEELEAELEELEAELEELEAELAELE--AELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 254 SLEQQLNIEPITFPEKGVDRYEkARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDAFISLNQQENEIKNKEFEL 333
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 334 TAIEKDIANKQRDKDELQANIGwSETHHDVDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEENKIEDNAVHSELDSVEE 413
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAE-AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 613182489 414 KIvpEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRQKLLR 463
Cdd:COG1196 429 AL--AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
189-461 |
2.15e-08 |
|
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: 58.53 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 189 EQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQlsKMHEEKQKEVALHDHSQEWKSLEQQLNIEpitfpe 268
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQLSKE------ 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 269 kgvdrYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDAfisLNQQENEIKNKEFELTAIEKDIANKQRDKD 348
Cdd:TIGR02168 756 -----LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 349 ELQANIGWSETHHDVdsseamksyVSEQIKNKQEQaayIKQLERSLEENKIEDNAVHSELDSVEEKI--VPEETFEKKKE 426
Cdd:TIGR02168 828 SLERRIAATERRLED---------LEEQIEELSED---IESLAAEIEELEELIEELESELEALLNERasLEEALALLRSE 895
|
250 260 270
....*....|....*....|....*....|....*
gi 613182489 427 YSQQVIELNEKEnlysklKERFEIEQQEKQKRQKL 461
Cdd:TIGR02168 896 LEELSEELRELE------SKRSELRRELEELREKL 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-844 |
1.05e-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: 56.22 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 159 EFTSMREVINRKKDELYKKSGKNPIINQQIEQLKQLESQIREEEAKLETYhrlvddRDKSSRRLENLKHNLNQLSKMHEE 238
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ------LEELESKLDELAEELAELEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 239 KQKEVAlhdhsqewkSLEQQLniepitfpEKGVDRYEKARAHKQSLERDIGLRNERLAQLKEEatqlepvkqsdidafis 318
Cdd:TIGR02168 349 LKEELE---------SLEAEL--------EELEAELEELESRLEELEEQLETLRSKVAQLELQ----------------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 319 LNQQENEIKNKEFELTAIEKDIANKQRDKDELQANIG---WSETHHDVDSSEAMKSYVSEQIKNKQEQAayiKQLERSLE 395
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaeLKELQAELEELEEELEELQEELERLEEAL---EELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 396 ENKIEDNAVHSELDSVEEKI-VPEETFEKKKEYSQQVIEL----NEKENLYSKLKERFEIEQQ----------------- 453
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLdSLERLQENLEGFSEGVKALlknqSGLSGILGVLSELISVDEGyeaaieaalggrlqavv 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 454 -----------EKQKRQKLLRTTFILLTLvgIGLTAFSFISNNMLFGIIFAVLTLVFVIGIIMSKSKEVDY---SEAITD 519
Cdd:TIGR02168 552 venlnaakkaiAFLKQNELGRVTFLPLDS--IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllgGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 520 EIEEIKAQLAILDENYDLdFDLDeQYRIRDHW----------QQALKNK---DILEEKRQYIEGRLNDAKGRHDELQSTV 586
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRI-VTLD-GDLVRPGGvitggsaktnSSILERRreiEELEEKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 587 ENVKDELYLSSKISNDLIVDSISTMANIKALDQHISDLNQQRQQLVQELDTFYNHAEAVtksqfvyfnkLSLFHDVQQWL 666
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL----------EERLEEAEEEL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 667 KSAEDTNEKwrinaentklVTNELNHLNAQLEENNKEITALfdfinvgtEEDFYQHHEDYQTYTSNLSRfndltkyLENQ 746
Cdd:TIGR02168 778 AEAEAEIEE----------LEAQIEQLKEELKALREALDEL--------RAELTLLNEEAANLRERLES-------LERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 747 NYSYELSSSLSEKTTAQLEEEDHLLATQVDEYNEQYLEMQAQVSDLSAQINHMETDttLANLRHEYHSLKNQLNDIAKDW 826
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA--LALLRSELEELSEELRELESKR 910
|
730
....*....|....*...
gi 613182489 827 ASLSYLQSLVDEHIKQIK 844
Cdd:TIGR02168 911 SELRRELEELREKLAQLE 928
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-206 |
6.33e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 50.96 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 6 LEIYGYGQFVQRKIEFNKNFTEIFGENEAGKSTIQAFIHSILFGFPtkkskePRLEPRLGNQYGGKLVLILDDGLEIEVE 85
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKT------SRLKRKSGGGFVKGDIRIGLEGKGKAYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 86 RIKGSAQGDVKVYlpngAVRDDAWLQKKLNYISKKTYQGIFSFDvlGLQDIHRNLNEKQLQDYLLQAGALGSTEFTSMRE 165
Cdd:pfam13476 75 EITFENNDGRYTY----AIERSRELSKKKGKTKKKEILEILEID--ELQQFISELLKSDKIILPLLVFLGQEREEEFERK 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613182489 166 VINRKKDELYKKSGKNPIINQQIEQLKQLESQIREEEAKLE 206
Cdd:pfam13476 149 EKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-589 |
9.35e-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: 53.15 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 3 IKSLEIYGYGQFVQRK-IEFNKNFTEIFGENEAGKSTIqafIHSILFGFPTKKSKEPRLEpRLGNqyggklvLILDDgle 81
Cdd:TIGR02169 2 IERIELENFKSFGKKKvIPFSKGFTVISGPNGSGKSNI---GDAILFALGLSSSKAMRAE-RLSD-------LISNG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 82 ievERIKGSAQGDVKVYLPN-GAVRDDAWLQKKLNYISKKTYQGIFSFDvlglqdiHRNLNEKQLQDYLLQAGALGS--- 157
Cdd:TIGR02169 68 ---KNGQSGNEAYVTVTFKNdDGKFPDELEVVRRLKVTDDGKYSYYYLN-------GQRVRLSEIHDFLAAAGIYPEgyn 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 158 -------TEFTSMREVINRKK-DELYKKSGKNPIINQQIEQLKQLESQIREEEAKLetyhrlvddrDKSSRRLENLKHNL 229
Cdd:TIGR02169 138 vvlqgdvTDFISMSPVERRKIiDEIAGVAEFDRKKEKALEELEEVEENIERLDLII----------DEKRQQLERLRRER 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 230 NQLSKMHE--EKQKEVALHDHSQEWKSLEQQLniepitfpekgvdryEKARAHKQSLERDIGLRNERLAQLKEEATQLEP 307
Cdd:TIGR02169 208 EKAERYQAllKEKREYEGYELLKEKEALERQK---------------EAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 308 VkqsdidafisLNQQENEIKNK-EFELTAIEKDIANKQRDKDELQANIgwSETHHDVDSSEAMKSYVSEQIKNKQEQaay 386
Cdd:TIGR02169 273 L----------LEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSI--AEKERELEDAEERLAKLEAEIDKLLAE--- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 387 IKQLERSLEENKIEDNAVHSELDsveekivpeetfEKKKEYSQQVIELNEKENLYSKLKERFEIEQQE----KQKRQKLL 462
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYA------------ELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELK 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 463 RTTFILLTLVGIGLTAFSFIsNNMLFGIIFAVLTLvfvIGIIMSKSKEVdysEAITDEIEEIKAQLAILDENYdldFDLD 542
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADL-NAAIAGIEAKINEL---EEEKEDKALEI---KKQEWKLEQLAADLSKYEQEL---YDLK 475
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 613182489 543 EQY-RIRDHWQQALKNKDILEEKRQYIEGRLNDAKGRHDELQSTVENV 589
Cdd:TIGR02169 476 EEYdRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-464 |
2.30e-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: 51.98 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 3 IKSLEIYGYGQFVQR-KIEFNKNFTEIFGENEAGKSTIqafIHSILFGFPTKKSKEPRLE-------------PRLgNQY 68
Cdd:TIGR02168 2 LKKLELAGFKSFADPtTINFDKGITGIVGPNGCGKSNI---VDAIRWVLGEQSAKALRGGkmedvifngsetrKPL-SLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 69 GGKLVLILDDGL-------EIEVER-IKGSAQGDvkvYLPNGA------VRD---DAWL---------QKKLNYI----- 117
Cdd:TIGR02168 78 EVELVFDNSDGLlpgadysEISITRrLYRDGESE---YFINGQpcrlkdIQDlflDTGLgkrsysiieQGKISEIieakp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 118 -------------------SKKTYQGIFSF--DVLGLQDIHRNLnEKQLQDYLLQAGAlgSTEFTSMREVINRKKDELYK 176
Cdd:TIGR02168 155 eerraifeeaagiskykerRKETERKLERTreNLDRLEDILNEL-ERQLKSLERQAEK--AERYKELKAELRELELALLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 177 KSgknpiINQQIEQLKQLESQIREEEAKLETYHRLVDDRDKSsrrLENLKHNLNQLSKMHEEKQKEvaLHDHSQEWKSLE 256
Cdd:TIGR02168 232 LR-----LEELREELEELQEELKEAEEELEELTAELQELEEK---LEELRLEVSELEEEIEELQKE--LYALANEISRLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 257 QQlnIEPITFPEKGVDR-YEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDAFISLNQQENEIKNKefeLTA 335
Cdd:TIGR02168 302 QQ--KQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR---LEE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 336 IEKDIANKQRDKDELQANIgwsethhdvdsseamksyvsEQIKNKQEQA-AYIKQLERSLEENKIEDNAVHSELDSVEEK 414
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQI--------------------ASLNNEIERLeARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 613182489 415 IVPEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRQKLLRT 464
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-464 |
8.13e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 159 EFTSMREVINRKKDELYKKSGKNPIINQQIEQLKQLESQIREEEAKLEtyhrlvDDRDKSSRRLENLKHNLNQLSKmhEE 238
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE------EDLSSLEQEIENVKSELKELEA--RI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 239 KQKEVALHDHSQEWKSLEQQLNIEPITFPEKGVDRYEKAR----AHKQSLERDIGLRNERLAQLKEEATQLEpVKQSDID 314
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVsrieARLREIEQKLNRLTLEKEYLEKEIQELQ-EQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 315 AFISLNQQE------------NEIKNKEFELTAIEKDIANKQRDKDELQANI-----GWSETHHDVDSSEAMKSYVSEQI 377
Cdd:TIGR02169 847 EQIKSIEKEienlngkkeeleEELEELEAALRDLESRLGDLKKERDELEAQLrelerKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 378 KNKQEQAAYIKQLERSLEENKIED---NAVHSELDSVEEKIVPEETFEKK--KEYSQQVIELNEKENLYSKLKERFE--- 449
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLaiQEYEEVLKRLDELKEKRAKLEEERKail 1006
|
330
....*....|....*..
gi 613182489 450 --IEQQEKQKRQKLLRT 464
Cdd:TIGR02169 1007 erIEEYEKKKREVFMEA 1023
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-94 |
8.37e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.70 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 2 IIKSLEIYGYGQFVQR-KIEFNKNFTEIFGENEAGKSTIQAFIHSILFGFPTKKSKEPRLEPRLGNQYGGKLVLILDDGL 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTeTIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGK 80
|
90
....*....|....
gi 613182489 81 EIEVERikgsAQGD 94
Cdd:COG0419 81 RYRIER----RQGE 90
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-353 |
7.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 189 EQLKQLESQIREEEAKLETY---HRLVDDRDKSSRRLENLKHNLNQLSkmheekQKEVALHDHSQEWKSLEQQLNIEPIT 265
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFrqkNGLVDLSEEAKLLLQQLSELESQLA------EARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 266 FPEKGVD--------RYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDAFI---------------SLNQQ 322
Cdd:COG3206 256 LPELLQSpviqqlraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILasleaelealqareaSLQAQ 335
|
170 180 190
....*....|....*....|....*....|.
gi 613182489 323 ENEIKNKEFELTAIEKDIANKQRDKDELQAN 353
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-453 |
8.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 188 IEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMHEEKQKEVALHDH--------------SQEWK 253
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaeleaelerldasSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 254 SLEQQLniepitfpEKGVDRYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDAFISLNQQENEIKNKEFEL 333
Cdd:COG4913 689 ALEEQL--------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 334 TAIEKDIANK-QRDKDELQANIGWSEThhdvDSSEAMKSYvseqiknKQEQAAYIKQLERSLEENkiedNAVHSELDSVE 412
Cdd:COG4913 761 DAVERELRENlEERIDALRARLNRAEE----ELERAMRAF-------NREWPAETADLDADLESL----PEYLALLDRLE 825
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 613182489 413 EKIVPEetFEKK-KEYsQQVIELNEKENLYSKLK-ERFEIEQQ 453
Cdd:COG4913 826 EDGLPE--YEERfKEL-LNENSIEFVADLLSKLRrAIREIKER 865
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-454 |
1.97e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 169 RKKDELYKKSGKnpiinQQIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENL--------KHNLNQLSKMHEEKQ 240
Cdd:PTZ00121 1546 KKADELKKAEEL-----KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekKMKAEEAKKAEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 241 KEVALHDHSQEWKSLEQQLNIEpitfpEKGVDRYEKARAHkqslERDIGLRNERLAQLKEE----ATQLEPVKQSDIDAF 316
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKE-----AEEKKKAEELKKA----EEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAA 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 317 ISLNQQENEIKNKEFELTAIEKDIANKQRDKDELQANIGWSET---HHDVDSSEAMKSYVSEQIKNKQEQAAyiKQLERS 393
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKDEEEKKKIAHLK--KEEEKK 1769
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613182489 394 LEENKIEDNAV-HSELDSVEEK--IVPEETFEKKKEYSQQVIELNEKENLY-SKLKERFEIEQQE 454
Cdd:PTZ00121 1770 AEEIRKEKEAViEEELDEEDEKrrMEVDKKIKDIFDNFANIIEGGKEGNLViNDSKEMEDSAIKE 1834
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-461 |
2.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 169 RKKDELYKKSGKNpiiNQQIEQLKQLESQIREEEAKLETYHRlvDDRDKSSRRLENLKHNLNQLSKMHEEKQKevalhdh 248
Cdd:PTZ00121 1444 KKADEAKKKAEEA---KKAEEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKK------- 1511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 249 SQEWKSLEQQLNIEPITFPE--KGVDRYEKARAHKQSLErdigLRNERLAQLKEEATQLEPVKQSDIDAFISLNQQENEI 326
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEeaKKADEAKKAEEKKKADE----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 327 KNKEFELTAIEKDIANKQRDK-DELQANIGWSETHHDVDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEENKIEdnAVH 405
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAE 1665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 613182489 406 SELDSVEEKIVPEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRQKL 461
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-460 |
2.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 165 EVINRKKDELYKKSGKNpiinQQIEQLKQLESQIREEEAKLETYHRLVDDRDKSS--RRLENLKhNLNQLSKMHEEK--- 239
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAK----KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELK-KAEELKKAEEKKkae 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 240 QKEVALHDHSQEWKSLEQQLNIEP--ITFPEKGVDRYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSDIDafi 317
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--- 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 318 slNQQENEIKNKEFELTAIEKDIANKQRDKDELQAnigwsethHDVDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEEN 397
Cdd:PTZ00121 1645 --EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA--------EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613182489 398 KIEDNAVHSELDsvEEKIVPEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRQK 460
Cdd:PTZ00121 1715 KKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-344 |
3.20e-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: 44.66 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 158 TEFTSMREVINRKKDELYKKSGK-NPIINQQIEQLKQLESQIREEEAKL----ETYHRLVDDRDKSSRRLENLKHNLNQL 232
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELtllnEEAANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 233 SKMHEEKQKEVALHDHSQEwkslEQQLNIEPITfpekgvDRYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSD 312
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIE----ELEELIEELE------SELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190
....*....|....*....|....*....|..
gi 613182489 313 IDAFISLNQQENEIKNKefeLTAIEKDIANKQ 344
Cdd:TIGR02168 914 RRELEELREKLAQLELR---LEGLEVRIDNLQ 942
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
159-464 |
5.13e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 159 EFTSMREVINRKKDELykkSGKNPIINQQIEQLKQLESQIREEEAKLETYHR-----LVDDRDKSSRRLENLKHNLNQLS 233
Cdd:PRK01156 406 AIKKELNEINVKLQDI---SSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgTTLGEEKSNHIINHYNEKKSRLE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 234 KMHEEKQKEV-ALHDHSQEWKSLEQQLNiepitfpEKGVDRYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQSD 312
Cdd:PRK01156 483 EKIREIEIEVkDIDEKIVDLKKRKEYLE-------SEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 313 IDAFIS-LNQQENEIKNKEFELTAIEKDIANKQRDKDELQANIGWSETHHDVDSSEAMKSYVSEQIKNKQEQAAYIKQLE 391
Cdd:PRK01156 556 KSLKLEdLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613182489 392 RSLEENKIEDNAVHSELDSVEEKIVPEETFEK-KKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRQKLLRT 464
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPdLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-460 |
6.42e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 272 DRYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPVKQsDIDAfiSLNQQENEIKNKEFELTAIEKDIANKQRDKDELQ 351
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALER--RIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 352 ANIGWSETH-----------------------HDVDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEENKIEDNAVHSEL 408
Cdd:COG4942 97 AELEAQKEElaellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613182489 409 DSVEEKIVpeetfEKKKEYSQQVielNEKENLYSKLKERFEIEQQEKQKRQK 460
Cdd:COG4942 177 EALLAELE-----EERAALEALK---AERQKLLARLEKELAELAAELAELQQ 220
|
|
| DUF3784 |
pfam12650 |
Domain of unknown function (DUF3784); This family of proteins is functionally uncharacterized. ... |
451-504 |
7.77e-04 |
|
Domain of unknown function (DUF3784); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 96 and 110 amino acids in length.
Pssm-ID: 463655 Cd Length: 94 Bit Score: 39.50 E-value: 7.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 613182489 451 EQQEKQKRQKLLRTTFILLTLVGIGLTAFSFISN--NMLFGIIFAVLTLVFVIGII 504
Cdd:pfam12650 32 EEKEKYDEKKLCRFMGILLLLIGILFLLLGLLSAfgSEAFLIIAIIAIIIIVIYII 87
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
139-485 |
1.17e-03 |
|
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: 43.04 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 139 NLNEKQLQDYLLQAGALGSTEFTSMREVINRKKDELYKKSGKNPIINQQIEQLKQLESQIREEEAKletyHRLVDDRDKS 218
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK----SRLKKEEKEE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 219 SRRLENLKHNLNQLSKMHEEKQKEVALHDHSQEWKSLEQQLNIEPITFPEKGVDRYEKARAHKQSLERDIGLRNERLAQL 298
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 299 KEEATQLEPVKQSDIDAFISLNQQENEIKNKEFELTAIEKDIANKQRDKDELQANIGWS-ETHHDVDSSEAMKSYVSEQI 377
Cdd:pfam02463 845 EQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeESQKLNLLEEKENEIEERIK 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 378 KNKQEQAAYIKQLERSLEENKIEDNAVHSELDSVEEKIVPEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQK 457
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
330 340
....*....|....*....|....*...
gi 613182489 458 RQKLLRTTFILLTLVGIGLTAFSFISNN 485
Cdd:pfam02463 1005 KKLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-76 |
1.32e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.91 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613182489 1 MIIKSLEIYGYGQFVQRKIEFN--KNFTEIFGENEAGKSTIQAFIHSILFGFPTKKSKEPRLEPRLGN-QYGGKLVLIL 76
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDnpPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNgEFGDSAKLIL 79
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
186-468 |
1.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 186 QQIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMHEEKQKEVAlhdhsqEWKSLEQQLNIEPIT 265
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE------EKRERAEELRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 266 FPEKGVDRYEKARAHKQSLER---DIGLRNERLAQLKEEATQLEPVK--QSDIDAFISLNQQENEIKNKEFELTAIEKD- 339
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESLERIRtlLAAIADAEDEIERLREKREALAELNDERREr 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 340 IANKQRDKDELqanigwsETHHDVDSSEAMKSyvseqikNKQEQAAYIKQLERSLEENKIEDN-------AVHSELDSVE 412
Cdd:PRK02224 629 LAEKRERKREL-------EAEFDEARIEEARE-------DKERAEEYLEQVEEKLDELREERDdlqaeigAVENELEELE 694
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 613182489 413 EKIVPEETFEKKKEYSQQVI-ELNEKENLYSKLkeRFEIEQQEKQKRQKLLRTTFIL 468
Cdd:PRK02224 695 ELRERREALENRVEALEALYdEAEELESMYGDL--RAELRQRNVETLERMLNETFDL 749
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-460 |
3.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 162 SMREVINRKKD---ELYKKSGKNPIINQQIEQLKQLEsQIREEEAKLEtyhRLVDDRDKSSRRLENLKHNLNQLSKMHEE 238
Cdd:PRK03918 416 ELKKEIKELKKaieELKKAKGKCPVCGRELTEEHRKE-LLEEYTAELK---RIEKELKEIEEKERKLRKELRELEKVLKK 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 239 KQKEVALHDHSQEWKSLEQQLNIEPITFPEKGVDRYEKARahkqslERDIGLRNErLAQLKEEATQLEPVKQSdidafis 318
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK------EKLIKLKGE-IKSLKKELEKLEELKKK------- 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 319 LNQQENEIKNKEFELTAIEKDIANKQ-RDKDELQANIGWSETHHD----VDSSEAMKSYVSEQIKNKQEQA----AYIKQ 389
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNeyleLKDAEKELEREEKELKKLEEELdkafEELAE 637
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613182489 390 LERSLEENKIEDNAVHSELDSVEEKIVPEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRQK 460
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-39 |
3.90e-03 |
|
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: 40.76 E-value: 3.90e-03
10 20 30
....*....|....*....|....*....|....*....
gi 613182489 1 MIIKSLEIYGYGQFVQRKIEFNKNFTEIFGENEAGKSTI 39
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSI 39
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-48 |
3.92e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.76 E-value: 3.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 613182489 3 IKSLEIYGYGQFVQR-KIEFNKNFTEIFGENEAGKSTIqafIHSILF 48
Cdd:cd03278 1 LKKLELKGFKSFADKtTIPFPPGLTAIVGPNGSGKSNI---IDAIRW 44
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
159-847 |
4.46e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 159 EFTSMREVINRKKDELYKKSGKNPIINQQIEQLKQLESQIRE-EEAKLEtyhRLVDDRDKSSRRLENLKHNLNQLSKMHE 237
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAlKSRKKQ---MEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 238 EKQKEV-----ALHDHSQEWKSLEQQ---LNIEPITFP-EKGVDRYEKARAHKQSLERDIgLRNERLAQLKEEATQLEPV 308
Cdd:TIGR00606 309 NHQRTVrekerELVDCQRELEKLNKErrlLNQEKTELLvEQGRLQLQADRHQEHIRARDS-LIQSLATRLELDGFERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 309 KQSDIDAFISL--NQQENEIKNKEFELTAIEKDIANKQRDKDELQANIgwSETHHDVDSSEAMKSYVSEQIKNKQEQaay 386
Cdd:TIGR00606 388 SERQIKNFHTLviERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEK--KGLGRTIELKKEILEKKQEELKFVIKE--- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 387 IKQLERSLEEN-KIEDNAVHSELD-SVEEKIVPEETFEKKKEYSQqvielNEKENLYSKLkeRFEIEQQEKQKRQKLLRT 464
Cdd:TIGR00606 463 LQQLEGSSDRIlELDQELRKAERElSKAEKNSLTETLKKEVKSLQ-----NEKADLDRKL--RKLDQEMEQLNHHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 465 TFILLTlvGIGLTAFSFISNNMLFGiifaVLTLVFVIGIIMSKSKEVDYSEAITDEIEEIKAQLAildenyDLDFDLDEQ 544
Cdd:TIGR00606 536 QMEMLT--KDKMDKDEQIRKIKSRH----SDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLA------KLNKELASL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 545 YRIRDHWQQALKNKdilEEKRQYIEGRLNDAKGRHDElQSTVENVKDELYLSSKisndlivDSISTMANIKALDQHISDL 624
Cdd:TIGR00606 604 EQNKNHINNELESK---EEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQL 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 625 NQQRQQLVQELDTFYNHAEAVTKSQFVYFNKLSLFHDVQQWLKSAEDTNEKWR--------INAENTKLVTNELNHLNAQ 696
Cdd:TIGR00606 673 TDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglapGRQSIIDLKEKEIPELRNK 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 697 LEENNKEITALFDFIN-----VGTEEDFYQHHEDYQTYTSNLSRFNDLTKYLENQ--NYSYELSSSLSEKTTAQLEEEDH 769
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEeqetlLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKiaQQAAKLQGSDLDRTVQQVNQEKQ 832
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613182489 770 LLATQVDEYNEQYLEMQAQVSDLSAQINHMEtdTTLANLRHEYHSLKNQLNDIAKDWASLSYLQSLVDEHIKQIKDKR 847
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIQHLK--SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAK 908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-345 |
4.99e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 159 EFTSMREVINRKKDELYKKSGK--NPIINQQIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMH 236
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAEllKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 237 EEkqkevaLHDHSQEWKSLEQQLNIEPITFPEkgvDRYEKARAHKQSLERdiglrneRLAQLKEEATQLEPVKQSDIDAF 316
Cdd:PRK03918 633 EE------LAETEKRLEELRKELEELEKKYSE---EEYEELREEYLELSR-------ELAGLRAELEELEKRREEIKKTL 696
|
170 180
....*....|....*....|....*....
gi 613182489 317 ISLNQQENEIKNKEFELTAIEKDIANKQR 345
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
296-465 |
6.97e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 296 AQLKEEATQLEPVKQSDIDAFISLNQQENEIKNKEFELTAIEKDIANKQRDKDelQANIGWSETHHDVDSSEAMKSYVSE 375
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARR--QAQQERDELADEIASGASGKSALQD 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 376 QiknKQEQAAYIKQLERSLEENKIEDNAVH-------SELDSVEEKIVPEETFEKKKEYSQQVIELNEKE---------- 438
Cdd:pfam01576 883 E---KRRLEARIAQLEEELEEEQSNTELLNdrlrkstLQVEQLTTELAAERSTSQKSESARQQLERQNKElkaklqemeg 959
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613182489 439 -----------NLYSK---LKERFEIEQQEKQKRQKLLRTT 465
Cdd:pfam01576 960 tvkskfkssiaALEAKiaqLEEQLEQESRERQAANKLVRRT 1000
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-460 |
7.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 165 EVINRKKDELYKKSGknpiinqqiEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMHEEKQKEVA 244
Cdd:PTZ00121 1325 EEAKKKADAAKKKAE---------EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 245 LHDHSQEWKSLEQQLniepitfpEKGVDRYEKARAHKQSLERDigLRNERLAQLKEEATQLEPVKQSDIDAfislNQQEN 324
Cdd:PTZ00121 1396 AKKKAEEDKKKADEL--------KKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEA----KKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 325 EIKNKEFELTAIE-KDIANKQRDKDELQANigwsethhdvdSSEAMKSyvSEQIKNKQEQAAYIKQLERSLEENKIEdna 403
Cdd:PTZ00121 1462 AKKKAEEAKKADEaKKKAEEAKKADEAKKK-----------AEEAKKK--ADEAKKAAEAKKKADEAKKAEEAKKAD--- 1525
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 613182489 404 vhsELDSVEEKIVPEETfeKKKEYSQQVIELNEKENLySKLKERFEIEQQEKQKRQK 460
Cdd:PTZ00121 1526 ---EAKKAEEAKKADEA--KKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDK 1576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-396 |
7.95e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 185 NQQIEQLKQLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHNLNQLSKMHEEKQKEVAlhDHSQEWKSLEQQLNIEPI 264
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 265 TFPEKGVDRYEKARAHKQSLERdiglRNERLAQLKEEATQLEPVKQsdidafiSLNQQENEIKNKEFELTAIEKDIANKQ 344
Cdd:COG4942 126 LSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRA-------ELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613182489 345 RDKDELQANIgwsethhdvdssEAMKSYVSEQIKNKQEQAAYIKQLERSLEE 396
Cdd:COG4942 195 AERQKLLARL------------EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-456 |
8.47e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 167 INRKKDELYKKSGKNPIINQQIEQLK------------------QLESQIREEEAKLETYHRLVDDRDKSSRRLENLKHN 228
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEnelnllekeklniqknidKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 229 LNQLSKMHEEKQKEvaLHDHSQEWKSLEQQLNiEPITFPEKGVDRYEKARAHKQSLERDIGLRNERLAQLKEEATQLEPV 308
Cdd:TIGR04523 227 NNQLKDNIEKKQQE--INEKTTEISNTQTQLN-QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 309 KQSDIDafislNQQENEIKNKEFELTAIEKDIANKQRDKDELQANIgwSETHHDVDSSEAMKSYVSEQIKNKQEQaayIK 388
Cdd:TIGR04523 304 KEQDWN-----KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI--SQLKKELTNSESENSEKQRELEEKQNE---IE 373
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 389 QLERSLEENKIEDNAVHSELDSVEEKIVPEETFEKKKEYSQQVI--ELNEKENLYSKLKErfEIEQQEKQ 456
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLqqEKELLEKEIERLKE--TIIKNNSE 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-593 |
9.72e-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: 40.04 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 321 QQENEIKNKEFELTAIEKDIANKQRDKDEL--QANIGWSETHHDVDSSEAMKSYVSEQIKNKQEQAAYIKQLERSLEENK 398
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELrkELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 399 IEDNAVHSELDSVEEKIvpEETFEKKKEYSQQVIELNEKENLYSKLKERFEIEQQEKQKRqkllrttfilLTLVGIGLTA 478
Cdd:TIGR02168 754 KELTELEAEIEELEERL--EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE----------LTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613182489 479 FSFISNNMLFGIIFAVLTLVFVIGIIMSKSKEVdysEAITDEIEEIKAQLAILDEnyDLDFDLDEQYRIRDHWQQALKNK 558
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDI---ESLAAEIEELEELIEELES--ELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....*
gi 613182489 559 DILEEKRQYIEGRLNDAKGRHDELQSTVENVKDEL 593
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
|