|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-250 |
1.59e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.65 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 29 DDRLLQAVEQNDPEKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQP 108
Cdd:COG0666 54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 109 DCLKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPN 188
Cdd:COG0666 134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207163335 189 LQDNQGRSALMFSCESDSMETVEMLLKGGTNPHLTDALGHNSTHYSITAGNHSITQLLQNLG 250
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-250 |
4.47e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.33 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 17 YGVITSQDWSKTDDRLLQAVEQNDPEKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGF 96
Cdd:COG0666 9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 97 NALHLAAKNGQPDCLKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIEL 176
Cdd:COG0666 89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 177 CAFLLERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGGTNPHLTDALGHNSTHYSITAGNHSITQLLQNLG 250
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
42-250 |
6.98e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 114.67 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 42 EKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDCLKRLLQERMPV 121
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 122 DSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFS 201
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207163335 202 CESDSMETVEMLLKGGTNPHLTDALGHNSTHYSITAGNHSITQLLQNLG 250
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
32-198 |
1.41e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 99.26 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPEkVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDCL 111
Cdd:COG0666 124 LHLAAYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 112 KRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQD 191
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 1207163335 192 NQGRSAL 198
Cdd:COG0666 283 LDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
66-158 |
3.95e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 66 FHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDCLKRLLqERMPVDSTDSfGRTSLHHAAVSGCLSCTE 145
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1207163335 146 ILWDFKANLDAQD 158
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
47-256 |
1.36e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 89.67 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 47 LLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIG-VTDGTGFNALHLAAKNGQPDCLKRLLQERMPVD--S 123
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDipN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 124 TDSFgrTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSALM-FSC 202
Cdd:PHA02875 133 TDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 203 ESDSMETVEMLLKGGTNPHLTdalghnsthYSITAGNHSITQLLQNLGVTTAAE 256
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM---------FMIEGEECTILDMICNMCTNLESE 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-1029 |
2.25e-17 |
|
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: 87.80 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 340 EEIRKLRLE--RGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAErdrllveLEELRAAqvsgvtcdsedaedsdd 417
Cdd:TIGR02168 220 AELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQELEEK-------LEELRLE----------------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 418 mlDFPGAEKLLSRQSRGLDANlpaEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTDMQssgpdfv 497
Cdd:TIGR02168 276 --VSELEEEIEELQKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 498 ptAQYESLRREFEELQEKYSRAQASTEASSIAEdpgcEEKEEKHQkALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKP 577
Cdd:TIGR02168 344 --EKLEELKEELESLEAELEELEAELEELESRL----EELEEQLE-TLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 578 EKSSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVNLKKQVEE 657
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 658 LGKALE-LSKAAGKKEGEGAPLNGLQARVEELeqelkESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLNQALLELERL 736
Cdd:TIGR02168 497 LQENLEgFSEGVKALLKNQSGLSGILGVLSEL-----ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 737 R---------PPSHIDEDEEDDEPSESSEVSIASDHSLHMSPGGRTLEA----------IKEELEVARQEAAQA----LD 793
Cdd:TIGR02168 572 RvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddLDNALELAKKLRPGYrivtLD 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 794 --------SLCAERESRAQDVLQLRDAvpLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSV 865
Cdd:TIGR02168 652 gdlvrpggVITGGSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 866 SKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEqglvsKEDHEAQRLSLQAEINTLTAQLADLARK 945
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE-----LAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 946 HEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAE----STHIQQLHQDIQHSQGLIKEKDRKITELSKEVFR 1021
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
....*...
gi 1207163335 1022 LKEALGAL 1029
Cdd:TIGR02168 885 LEEALALL 892
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
132-224 |
3.78e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 132 LHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERgANPNLQDNqGRSALMFSCESDSMETVE 211
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1207163335 212 MLLKGGTNPHLTD 224
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
340-942 |
8.15e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 340 EEIRKLRLERgrLLQKIKVLEQQQSSATTALEELsslKERLSEAEAERDRLLVELEELRAAQvsgvtcdsedaedsddml 419
Cdd:COG1196 220 EELKELEAEL--LLLKLRELEAELEELEAELEEL---EAELEELEAELAELEAELEELRLEL------------------ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 420 dfpGAEKLLSRQSRGLDANLPAEQGEGISQENPAMvEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTDMQssgpdfvpt 499
Cdd:COG1196 277 ---EELELELEEAQAEEYELLAELARLEQDIARLE-ERRRELEERLEELEEELAELEEELEELEEELEELE--------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 500 AQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEK 579
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 580 SSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVNLKKQVEEL- 658
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADy 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 659 ------GKALELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLnqaLLE 732
Cdd:COG1196 504 egflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL---PLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 733 LERLRPPSHIDEDEEDDEPSESSEVSIASDHSLHMSPGGRTLEAikEELEVARQEAAQALDslcAERESRAQDVLQLRDA 812
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRA---VTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 813 VplvkhQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSVSKEEHDKiKADLERSLEDSRQIAAAAQ 892
Cdd:COG1196 656 G-----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA-EAEEERLEEELEEEALEEQ 729
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1207163335 893 ESLSEKETELKDLRSQKALEQGLVSKEDHEAQRLSLQAEINTLTAQLADL 942
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
329-1018 |
1.16e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 329 SENLTEDEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATTA-----LEELSSLKERLSEAEAERDRLLVELEELRAAQVS 403
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAeearkAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 404 GVTCDSEDAEDSDDMLDFPGAEKLL-SRQSRGLDANLPAEQGEGISQ----ENPAMVEQLRRkVEEL--TSQNADLVLKV 476
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRkAEDARKAEAARKAEEERKAEEarkaEDAKKAEAVKK-AEEAkkDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 477 QMLEMFEKDDTDMQSSGPDFVPTAQYESlRREFEELQ--EKYSRAQASTEASSIAEDPGCEEKEEKHQKA--LEKKLSQA 552
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 553 QAELEELKEQMRLGVYSVEDAEEKPEKSSVEggdLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELE 632
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 633 AALQDREKEGEENETVVNLKKQVEELGKALELSKAAGKKEgegaplnglqaRVEELEQELKEsvpRGQFEEvqvtlglql 712
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK-----------KADEAKKKAEE---AKKAEE--------- 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 713 nqlAQERAEVAARLNQALLELERLRPPSHIDEDEEDDEPSESSEVSIASDHSlhMSPGGRTLEAIKEELEVARQEAAQAL 792
Cdd:PTZ00121 1462 ---AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKA 1536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 793 DSLCAERESRAQDvlQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERA-----LREHAQTELSRLEIELKAAQKDSVSK 867
Cdd:PTZ00121 1537 DEAKKAEEKKKAD--ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeeakkAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 868 EEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRsqKALEQGLVSKEDheaqrLSLQAEINTLTAQLADLARKHE 947
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK--KAEEENKIKAAE-----EAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207163335 948 KTCLEvfQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHIQQLHQDIQHSQglikEKDRKITELSKE 1018
Cdd:PTZ00121 1688 KKAAE--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE----EDKKKAEEAKKD 1752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
500-1029 |
5.87e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 500 AQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEK 579
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 580 SSVEggdLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENEtvvNLKKQVEELG 659
Cdd:COG1196 354 EEAE---AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE---RLEEELEELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 660 KALELSkaagkkegegaplngLQARVEELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLNQALLELERLRPP 739
Cdd:COG1196 428 EALAEL---------------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 740 SHIDEDEEDDEPSEssevsiasdhslhmspggrtLEAIKEELEVARQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQ 819
Cdd:COG1196 493 LLLLLEAEADYEGF--------------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 820 ESLSAVAQQLAQTEKELQAERA---------LREHAQTELSRLEIELKAAQKDSVSKEEHDKIKADLERSLEDSRQIAAA 890
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRAtflpldkirARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 891 AQESLSEKETELKDLRSQKALE---QGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSER 967
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEggsAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207163335 968 QVAESQLETVKKQLTDLQAESTHIQQLHQDIQHSQ-----GLIKEKDRKITELSKEVFRLKEALGAL 1029
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELleeeaLEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-1063 |
4.82e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 340 EEIRKLRLERGRLLQKIKV----LEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELRAAQvsgvtcdsedaeds 415
Cdd:TIGR02168 302 QQKQILRERLANLERQLEEleaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-------------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 416 ddmldfpgaeKLLSRQSRGLDANLpaeqgegisqenpamvEQLRRKVEELTSQNADLVLKVQMLEmfekddTDMQSSgpd 495
Cdd:TIGR02168 368 ----------EELESRLEELEEQL----------------ETLRSKVAQLELQIASLNNEIERLE------ARLERL--- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 496 fvpTAQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQMRlgvysveDAEE 575
Cdd:TIGR02168 413 ---EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD-------AAER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 576 kpekssveggdlETHQLKARVQELEAELVSKKTDGEGLSEDDNN------TMQQLKERVK-------ELEAALQDR---- 638
Cdd:TIGR02168 483 ------------ELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglsgILGVLSELISvdegyeaAIEAALGGRlqav 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 639 --EKEGEENETVVNLKKqvEELGKA--LELSKAAGKK-EGEGAPLNGLQARVEELEQELKESVPrgqfeEVQVTLGLQLN 713
Cdd:TIGR02168 551 vvENLNAAKKAIAFLKQ--NELGRVtfLPLDSIKGTEiQGNDREILKNIEGFLGVAKDLVKFDP-----KLRKALSYLLG 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 714 QLAqeraeVAARLNQALLELERLRPPSHIdeDEEDDEPSESSEVSIASDHSLHMSPGGR-----TLEAIKEELEVARQEA 788
Cdd:TIGR02168 624 GVL-----VVDDLDNALELAKKLRPGYRI--VTLDGDLVRPGGVITGGSAKTNSSILERrreieELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 789 AQALDSLCAERESRAQDVLQLRDAvpLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKD----S 864
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKE--LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaE 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 865 VSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRS--------QKALEQGLVSKEDhEAQRLSLQAEINTLT 936
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlrerLESLERRIAATER-RLEDLEEQIEELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 937 AQLADLARKHEKTCLEVFQVQREALFNksERQVAESQLETVKKQLTDLQAE----STHIQQLHQDIQHSQGLIKEKDRKI 1012
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLN--ERASLEEALALLRSELEELSEElrelESKRSELRRELEELREKLAQLELRL 931
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1207163335 1013 TELSKEVFRLKEALGALTPPLGRSPSPPSSGIPGQQLALQNRVTSLTQQLQ 1063
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
774-1095 |
8.07e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 774 LEAIKEELEVARQEAAQALDSLCAERESRaqdvlqlrdavplvkhQESLSAVAQQLAQTEKELQAERALREHAQTELSRL 853
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEA----------------QAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 854 EIELKAAQKDsvsKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRS-----QKALEQGLVSKEDHEAQRLSL 928
Cdd:COG1196 322 EEELAELEEE---LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAelaeaEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 929 QAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAEsthIQQLHQDIQHSQGLIKEK 1008
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE---EEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 1009 DRKITELSKEVFRLKEALGALTPPLGRSPSPPSSGIPGQQLALQNRVTSLTQQLQDWERKHKAVVSIYRSHLLAAVQGRM 1088
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
....*..
gi 1207163335 1089 DEEVQAL 1095
Cdd:COG1196 556 DEVAAAA 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-942 |
3.01e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 334 EDEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELRAAQVSgvtcdsedae 413
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 414 dsddmldfpgAEKLLSRQSRGLDANLPAEQGEGISQEnpamvEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTDMQSsg 493
Cdd:COG1196 310 ----------RRRELEERLEELEEELAELEEELEELE-----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 494 pdfvptaqyESLRREFEELQEKYSRAQASTEASSIAEDpgcEEKEEKHQKALEKKLSQAQAELEELKEQMRLgvysvEDA 573
Cdd:COG1196 373 ---------ELAEAEEELEELAEELLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAE-----LEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 574 EEKPEKSSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVNLKK 653
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 654 QVEELGKALELSKAAGKKEGEGAPL-----NGLQARVEELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLNQ 728
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALeaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 729 ALLELERLRPPSHIDEDEEDDEPSESSEVSIASDHSLHMspGGRTLEAIKEELEVARQEAAQALDSLCAERESRAQDVLQ 808
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA--ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 809 LRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSVSKEEHDKIKADLERSLEDSRQIA 888
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 889 AAAQE--SLSEKETELKDLRSQ-KALEQ-GLVSKEDHEAqrlsLQAEINTLTAQLADL 942
Cdd:COG1196 754 EELPEppDLEELERELERLEREiEALGPvNLLAIEEYEE----LEERYDFLSEQREDL 807
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
32-125 |
4.96e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPEKVaTLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHgVDIGVTDGtGFNALHLAAKNGQPDCL 111
Cdd:pfam12796 1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1207163335 112 KRLLQERMPVDSTD 125
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
32-252 |
7.71e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.01 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPEKVATLLvKKGLCPSKLDAEGKSAFHLCA-----SRGRLDCLEVILSHGVDIGVTDGTGFNALHLAA--K 104
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 105 NGQPDCLKRLLQERMPVDSTDSFGRTSLHhAAVSGCLSCTEI---LWDFKANLDAQDgdgstplilaaqmsRIELcafLL 181
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLH-LYLESNKIDLKIlklLIDKGVDINAKN--------------RVNY---LL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207163335 182 ERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGGTNPHLTDALGHNSTHYSITAGNHSITQLLQNLGVT 252
Cdd:PHA03100 180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
42-220 |
4.21e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.67 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 42 EKVATLLVKKGLCPSKLDAEGKSAFHLCASRGR--LDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPD--CLKRLLQE 117
Cdd:PHA03095 132 PKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 118 RMPVDSTDSFGRTSLHHAAVSGclSCTEILWDF----KANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQDNQ 193
Cdd:PHA03095 212 GCDPAATDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289
|
170 180
....*....|....*....|....*..
gi 1207163335 194 GRSALMFSCESDSMETVEMLLKggTNP 220
Cdd:PHA03095 290 GNTPLSLMVRNNNGRAVRAALA--KNP 314
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
62-236 |
5.05e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 66.20 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 62 GKSAFHLCASRGRLDCLEVI---LSHGVDIGVTDGTGFNALHLAAKNGQ-PDCLKRLLQERMPVDSTDSFGRTSLHhaav 137
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVKDIVrllLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLH---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 138 sGCLS--CT-----EILWDFKANLDAQDGDGSTPliLAAQMSR----IELCAFLLERGANPNLQDNQGRSALMFSCES-- 204
Cdd:PHA03095 123 -VYLSgfNInpkviRLLLRKGADVNALDLYGMTP--LAVLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfk 199
|
170 180 190
....*....|....*....|....*....|..
gi 1207163335 205 DSMETVEMLLKGGTNPHLTDALGHNSTHYSIT 236
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
70-217 |
5.20e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 70 ASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDCLKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWD 149
Cdd:PLN03192 533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 150 FKANLDAQdgDGSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGG 217
Cdd:PLN03192 613 FASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
64-115 |
8.92e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 8.92e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1207163335 64 SAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDCLKRLL 115
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
536-1029 |
1.15e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 536 EKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVEGGDLEthQLKARVQELEAELVSKKTDGEGLSE 615
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE--ELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 616 DDNNTMQQLKERVKELEAaLQDREKEGEE----NETVVNLKKQVEELGKAL-ELSKAAGKKEGEgapLNGLQARVEELEq 690
Cdd:PRK03918 260 KIRELEERIEELKKEIEE-LEEKVKELKElkekAEEYIKLSEFYEEYLDELrEIEKRLSRLEEE---INGIEERIKELE- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 691 ELKESVprGQFEEVQVTLGLQLNQLaQERAEVAARLNQALLELERLRPpshidedeeddepsessevsiasdhslhmSPG 770
Cdd:PRK03918 335 EKEERL--EELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKK-----------------------------RLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 771 GRTLEAIK---EELEVARQEAAQALDSLCAERESRAQDVLQLRDAV---------------PLVKHQES--LSAVAQQLA 830
Cdd:PRK03918 383 GLTPEKLEkelEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrELTEEHRKelLEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 831 QTEKELQAERALREHAQTELSRLEIELKAAQKDSVSKEEHDKIKAdLERSLE--DSRQIAAAAQESLSEKETELKDLRSQ 908
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE-LEEKLKkyNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 909 KALEQGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQ-----------VQREALFNKSERQVAESQLETV 977
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeleerlkelepFYNEYLELKDAEKELEREEKEL 621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 978 KKQLTDLQAESTHIQQLHQDIQHSQGLIKE------------KDRKITELSKEVFRLKEALGAL 1029
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEElekkyseeeyeeLREEYLELSRELAGLRAELEEL 685
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-255 |
1.88e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.08 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 31 RLLQAVEQNDPEKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDC 110
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 111 LKRLLQERMPVDSTDsfgrTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRI-ELCAFLLERGANPNL 189
Cdd:PHA02876 227 IKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 190 QDNQGRSALMFSCESD-SMETVEMLLKGGTNPHLTDALGHNSTHYSITAG-NHSITQLLQNLGVTTAA 255
Cdd:PHA02876 303 KNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNA 370
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
32-248 |
5.61e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.06 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPeKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVtdgtgfnalhLAAKNGQPDCL 111
Cdd:PHA02874 39 LIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 112 KRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQD 191
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207163335 192 NQGRSALMFSCESDSMETVEMLLKGGTNPHLTDALGHNSTHYSITAgNHSITQLLQN 248
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN 243
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
165-251 |
2.11e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.51 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 165 LILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGGTnphlTDALGHNST--HYSITAGNHSI 242
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNGRTalHYAARSGHLEI 76
|
....*....
gi 1207163335 243 TQLLQNLGV 251
Cdd:pfam12796 77 VKLLLEKGA 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
499-1068 |
3.48e-09 |
|
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: 61.23 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 499 TAQYESLRREFEELQEKYSRAQaSTEASSIAEDPGCEEKEEKHQKA---LEKKLSQAQAELEELKE-----QMRLGVYSV 570
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAE-EELEELTAELQELEEKLEELRLEvseLEEEIEELQKELYALANeisrlEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 571 EDAEEKPEKSSVEGgdlETHQLKARVQELEAELVSKKTDGEGLSEDdnntMQQLKERVKELEAALQDREKEGEENETVV- 649
Cdd:TIGR02168 310 RLANLERQLEELEA---QLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELEAELEELESRLEELEEQLe 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 650 NLKKQVEELGkaLELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQvTLGLQLNQLAQERAEVAARLNQA 729
Cdd:TIGR02168 383 TLRSKVAQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 730 LLELERLRppshidedeeddepsessevsiasdhslhmspggRTLEAIKEELEVARQEAAQaLDSLCAERESRAQDVLQL 809
Cdd:TIGR02168 460 EEALEELR----------------------------------EELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 810 RDAVP-LVKHQESLSAVAQQLAQ---TEKELQA--ERALREHAQTELSRleiELKAAQKDSVSKEEHDKIKAD-LERSLE 882
Cdd:TIGR02168 505 SEGVKaLLKNQSGLSGILGVLSElisVDEGYEAaiEAALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTfLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 883 DSRQIAAAAQESLSEKE---TELKDLRSQKALEQGLVS-------------KEDHEAQRLSLQAEINTLTAQLAD----L 942
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEgflGVAKDLVKFDPKLRKALSyllggvlvvddldNALELAKKLRPGYRIVTLDGDLVRpggvI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 943 ARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAEsthIQQLHQDIQHSQGLIKEKDRKITELSKEVFRL 1022
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE---LEELEEELEQLRKELEELSRQISALRKDLARL 738
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1207163335 1023 KEALGALTpPLGRSPSPPSSGIPGQQLALQNRVTSLTQQLQDWERK 1068
Cdd:TIGR02168 739 EAEVEQLE-ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
42-250 |
3.75e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.42 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 42 EKVATLLVKKGLCPSKLDAEGKSAFHLCASRG-RLDCLEVILSHGVDIGVTDGTGFNALH--LAAKNGQPDCLKRLLQER 118
Cdd:PHA03095 63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 119 MPVDSTDSFGRTSLHHAAVSG--CLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAF--LLERGANPNLQDNQG 194
Cdd:PHA03095 143 ADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLG 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 195 RSAL----MFSCESDSMetVEMLLKGGTNPHLTDALGHNSTHYSITAGNHSITQLLQNLG 250
Cdd:PHA03095 223 NTPLhsmaTGSSCKRSL--VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
128-181 |
3.93e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 3.93e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 128 GRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLL 181
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
330-1020 |
8.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 330 ENLTEDEEVFEEIRK--LRLER-----GRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELR---- 398
Cdd:PRK03918 138 DAILESDESREKVVRqiLGLDDyenayKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselp 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 399 --AAQVSGVTCDSedaedsddmldfpgaEKLLSRQSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKV 476
Cdd:PRK03918 218 elREELEKLEKEV---------------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 477 QMLEMFEKDDTdmqssgpdfvptaQYESLRREFEELQEKYSR-----AQASTEASSIAEDPGCEEKEEKHQKALEKKLSQ 551
Cdd:PRK03918 283 KELKELKEKAE-------------EYIKLSEFYEEYLDELREiekrlSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 552 AQAELEELKEQMRLgvysVEDAEEKPEkssveggdlETHQLKARVQELEAELVSKKtdgeglseddnntMQQLKERVKEL 631
Cdd:PRK03918 350 LEKRLEELEERHEL----YEEAKAKKE---------ELERLKKRLTGLTPEKLEKE-------------LEELEKAKEEI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 632 EaalqdrEKEGEENETVVNLKKQVEELGKAL-ELSKAAGKKEGEGAPLNglqarvEELEQELKESVPrgqfeevqvtlgL 710
Cdd:PRK03918 404 E------EEISKITARIGELKKEIKELKKAIeELKKAKGKCPVCGRELT------EEHRKELLEEYT------------A 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 711 QLNQLAQERAEVAARLNQALLELERLRPPSHIDEDEEDDEPSESSEVSIASDHSLHmspGGRTLEAIKEELEVARQEaaq 790
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY---NLEELEKKAEEYEKLKEK--- 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 791 aLDSLCAERESRAQDVLQLRDAvplvkhQESLSAVAQQLAQTEKEL-QAERALREHAQTELSRLEI---ELKAAQKDSVS 866
Cdd:PRK03918 534 -LIKLKGEIKSLKKELEKLEEL------KKKLAELEKKLDELEEELaELLKELEELGFESVEELEErlkELEPFYNEYLE 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 867 KEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQGLVSKEDHEAQR---LSLQAEINTLTAQLADLA 943
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELReeyLELSRELAGLRAELEELE 686
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 944 RKHEKTclevfqvqrEALFNKSERQVAEsqLETVKKQLTDLQAESTHIQQLHQDIQHSQGLIKEKD-RKITELSKEVF 1020
Cdd:PRK03918 687 KRREEI---------KKTLEKLKEELEE--REKAKKELEKLEKALERVEELREKVKKYKALLKERAlSKVGEIASEIF 753
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
835-1090 |
8.91e-09 |
|
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: 60.07 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 835 ELQAERALREHA-QTELSRLEIELKAAQKdsvsKEEHDKIKAdLERSLEDSRQIAAAAQESLSEKETELKDLRsqkaLEQ 913
Cdd:TIGR02168 206 ERQAEKAERYKElKAELRELELALLVLRL----EELREELEE-LQEELKEAEEELEELTAELQELEEKLEELR----LEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 914 GLVSKEDHEAQR--LSLQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHI 991
Cdd:TIGR02168 277 SELEEEIEELQKelYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 992 QQ----LHQDIQHSQGLIKEKDRKITELSKEVFRLKEalgaltpplgrspsppssgipgQQLALQNRVTSLTQQLQDWER 1067
Cdd:TIGR02168 357 EAeleeLEAELEELESRLEELEEQLETLRSKVAQLEL----------------------QIASLNNEIERLEARLERLED 414
|
250 260
....*....|....*....|...
gi 1207163335 1068 KHKAVVSIYRSHLLAAVQGRMDE 1090
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKE 437
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
32-198 |
9.79e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPEKVATLLvKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKNGQPDCL 111
Cdd:PHA02874 128 LHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 112 KRLLQERMPVDSTDSFGRTSLHHAAVSGcLSCTEILWDfKANLDAQDGDGSTPLILAAQMS-RIELCAFLLERGANPNLQ 190
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284
|
....*...
gi 1207163335 191 DNQGRSAL 198
Cdd:PHA02874 285 DNKGENPI 292
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
48-139 |
1.28e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.11 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 48 LVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTG---------------FNALH------------ 100
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGntalwnaisakhhkiFRILYhfasisdphaag 623
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207163335 101 ----LAAKNGQPDCLKRLLQERMPVDSTDSFGRTSLHHAAVSG 139
Cdd:PLN03192 624 dllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-986 |
1.80e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 334 EDEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELRAaqvsgvtcdsedae 413
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE-------------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 414 dsddmlDFPGAEKllsrqsrgldanlpaeQGEGISQEnpamVEQLRRKVEELTSQNADLVLKvqmLEMFEKDDTDMQSSG 493
Cdd:PRK02224 266 ------TIAETER----------------EREELAEE----VRDLRERLEELEEERDDLLAE---AGLDDADAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 494 PDFvpTAQYESLRREFEElqEKYSRAQASTEASSIAEDPGC--EEKEEKHQKA--LEKKLSQAQAELEELKEQMRLGVYS 569
Cdd:PRK02224 317 EEL--EDRDEELRDRLEE--CRVAAQAHNEEAESLREDADDleERAEELREEAaeLESELEEAREAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 570 VEDAEEKPEKSSVEGGDLETHQlkarvQELEAELvskktdgeglseddnntmQQLKERVKELEAALQDREKEGEENETVV 649
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFL-----EELREER------------------DELREREAELEATLRTARERVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 650 nlkkqveelgkalelskAAGKKEGEGAPLNGlQARVEELEQElkesvpRGQFEEvqvtLGLQLNQLAQERAEVAARLNQA 729
Cdd:PRK02224 450 -----------------EAGKCPECGQPVEG-SPHVETIEED------RERVEE----LEAELEDLEEEVEEVEERLERA 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 730 --LLELERlrppshideDEEDDEPSESSEVSIASDHSlhmspggRTLEAIKEELEVARqEAAQALDSLCAERESRAQDVL 807
Cdd:PRK02224 502 edLVEAED---------RIERLEERREDLEELIAERR-------ETIEEKRERAEELR-ERAAELEAEAEEKREAAAEAE 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 808 QLRDavplvKHQESLSAVAQQLAQTEKELQAER------ALREHAQTELSRLeiELKAAQKDSVSKEEHDKIKADLERsl 881
Cdd:PRK02224 565 EEAE-----EAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERL--REKREALAELNDERRERLAEKRER-- 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 882 edSRQIAAAAQESLSEKETELKDlRSQKALEQGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKtclevfqvqREAL 961
Cdd:PRK02224 636 --KRELEAEFDEARIEEAREDKE-RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER---------REAL 703
|
650 660
....*....|....*....|....*
gi 1207163335 962 FNKSERqvaesqLETVKKQLTDLQA 986
Cdd:PRK02224 704 ENRVEA------LEALYDEAEELES 722
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
32-250 |
2.10e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 58.54 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPEKVATLLVKKGLCPSKLDAEGKSAFHLCASRG-RLDCLEVILSHGVDIGVTDGTGFNALHLAAK-NGQPD 109
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 110 CLKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCA-FLLERGANPN 188
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVkTLIDRGANVN 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207163335 189 LQDNQGRSALMFSCESD-SMETVEMLLKGGTNPHLTDAlgHNSTHYSITAGNHSITQLLQNLG 250
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI--QNQYPLLIALEYHGIVNILLHYG 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
612-984 |
3.02e-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: 58.14 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 612 GLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVN-LKKQVEELGKalELSKAAGKKEGEGAPLNGLQARVEELEQ 690
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAeLRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 691 ElkesvpRGQFEEVQVTLGLQLNQLAQERAEVAARLNQALLELERLRppSHIDEDEEDDEPSESSEVSIASDHSlhmspg 770
Cdd:TIGR02168 741 E------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKALREALD------ 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 771 grTLEAIKEELEVARQEAAQALDSLCAERESRaqdvlqlrdavplvkhQESLSAVAQQLAQTEKELQAERALREHAQTEL 850
Cdd:TIGR02168 807 --ELRAELTLLNEEAANLRERLESLERRIAAT----------------ERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 851 SRLEIELKAAQKDSVSKEEHdkikadlERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQglvskEDHEAQRLSLQA 930
Cdd:TIGR02168 869 EELESELEALLNERASLEEA-------LALLRSELEELSEELRELESKRSELRRELEELREKL-----AQLELRLEGLEV 936
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 931 EINTLTAQLADLARkhektcLEVFQVQREALFNKSERQVAESQLETVKKQLTDL 984
Cdd:TIGR02168 937 RIDNLQERLSEEYS------LTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
111-232 |
3.45e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.34 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 111 LKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEI---LWDFKANLDAQDGDGSTPLILAAQMS-RIELCAFLLERGAN 186
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGAD 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207163335 187 PNLQDNQGRSALMFSCESDSM--ETVEMLLKGGTNPHLTDALGHNSTH 232
Cdd:PHA03095 110 VNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLA 157
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
621-998 |
7.23e-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: 56.99 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 621 MQQLKERVKELEAALQDREKEGEENETVVNLKKQVEELGKALelskaagkkegegaplngLQARVEELEQELKEsvprgq 700
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELAL------------------LVLRLEELREELEE------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 701 feevqvtLGLQLNQLAQERAEVAARLNQALLELERLRppshidedeeddepsessevsiasdhsLHMSPGGRTLEAIKEE 780
Cdd:TIGR02168 244 -------LQEELKEAEEELEELTAELQELEEKLEELR---------------------------LEVSELEEEIEELQKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 781 LEVARQEAAQALDSLCAERESRAQDVLQL-RDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKA 859
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLeELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 860 AQKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQGLVSKEDHEAQRLSLQAEINTLTAQL 939
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207163335 940 ADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHIQQLHQDI 998
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
780-988 |
7.86e-08 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 55.15 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 780 ELEVARQEAaqalDSLCAERESRAQDVLQLRDAVPLV--KHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIEL 857
Cdd:pfam09787 48 ELEELRQER----DLLREEIQKLRGQIQQLRTELQELeaQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 858 KAAqkdsvskeehdkikadlersLEDSRQIAAAAQESLSEKETELKDLRSQkaleqgLVSKEDHEAQRLSLQAEINTLTA 937
Cdd:pfam09787 124 RYL--------------------EEELRRSKATLQSRIKDREAEIEKLRNQ------LTSKSQSSSSQSELENRLHQLTE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207163335 938 QLAdlarkhEKtclevfQVQREALfnKSERQVAESQLETVKKQLTDLQAES 988
Cdd:pfam09787 178 TLI------QK------QTMLEAL--STEKNSLVLQLERMEQQIKELQGEG 214
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
539-732 |
8.33e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 539 EKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVEGG----DLETHQLKARVQELEAELVSKKTDGEGLS 614
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQlaeaRAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 615 EDDnnTMQQLKERVKELEAALQD-REKEGEENETVVNLKKQVEELGKAL--ELSKAAGKKEGEgapLNGLQARVEELEQE 691
Cdd:COG3206 261 QSP--VIQQLRAQLAELEAELAElSARYTPNHPDVIALRAQIAALRAQLqqEAQRILASLEAE---LEALQAREASLQAQ 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207163335 692 LKESvpRGQFEEVQvTLGLQLNQLAQErAEVAARLNQALLE 732
Cdd:COG3206 336 LAQL--EARLAELP-ELEAELRRLERE-VEVARELYESLLQ 372
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
81-135 |
9.78e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 49.65 E-value: 9.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207163335 81 ILSHG-VDIGVTDGTGFNALHLAAKNGQPDCLKRLLQERMPVDSTDSFGRTSLHHA 135
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
161-214 |
1.15e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.15e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 161 GSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFSCESDSMETVEMLL 214
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-1067 |
1.66e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 535 EEKEEKHQKALEKKLSQAQAELEELKEQmrLGVYSVEDAEEKPEKSSVEGgDLEthQLKARVQELEAELVSKKTDGEGLS 614
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEE--LKEAEEELEELTAELQELEE-KLE--ELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 615 EDDNNTMQQLKERVKELEAALQDREKEGEENEtvvNLKKQVEELGKALELSKAagKKEGEGAPLNGLQARVEELEQELKE 694
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLE---ELESKLDELAEELAELEE--KLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 695 SVPRGQFEEVQVT--------LGLQLNQLAQERAEVAARLNQALLELERLRPPSHIDEDEEDDEPSESSEVSIAS----- 761
Cdd:TIGR02168 370 LESRLEELEEQLEtlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEleeel 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 762 -DHSLHMSPGGRTLEAIKEELEVARQE---AAQALDSLCAERESRAQDVLQL----RDAVPLVKHQESLSAVAQQLAQ-- 831
Cdd:TIGR02168 450 eELQEELERLEEALEELREELEEAEQAldaAERELAQLQARLDSLERLQENLegfsEGVKALLKNQSGLSGILGVLSEli 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 832 -TEKELQA--ERALREHAQTELSR----------------------LEIELKAAQKDSVSKEEHDK-------------- 872
Cdd:TIGR02168 530 sVDEGYEAaiEAALGGRLQAVVVEnlnaakkaiaflkqnelgrvtfLPLDSIKGTEIQGNDREILKniegflgvakdlvk 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 873 -----------------IKADLERSLEDSRQI-----------------------AAAAQESLSEKETELKDLRSQKALE 912
Cdd:TIGR02168 610 fdpklrkalsyllggvlVVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 913 QGLVskEDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAEsthIQ 992
Cdd:TIGR02168 690 EEKI--AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IE 764
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207163335 993 QLHQDIQHSQGLIKEKDRKITELSKEVFRLKEALGALTPPLGRSPSPPSSGIPGQQlALQNRVTSLTQQLQDWER 1067
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA-NLRERLESLERRIAATER 838
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
547-1095 |
2.07e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 547 KKLSQAQAELEELKEQMR-LGVysVEDAEEKPEKSSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEDdnntMQQLK 625
Cdd:COG4913 235 DDLERAHEALEDAREQIElLEP--IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE----LARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 626 ERVKELEAALQDREKEgeenetVVNLKKQVEELGkalelskaagkkegeGAPLNGLQARVEELEQELKE-SVPRGQFEEV 704
Cdd:COG4913 309 AELERLEARLDALREE------LDELEAQIRGNG---------------GDRLEQLEREIERLERELEErERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 705 QVTLGLQLNQLAQERAEVAARLNQALLELERLRppshidedeeddepsessevsiasdhslhmspggRTLEAIKEELEVA 784
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEEL----------------------------------EALEEALAEAEAA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 785 RQEAAQALDSLCAERESRAQ-------DVLQLRDavplvkhqeslsAVAQQLAQTEKELQ------------------AE 839
Cdd:COG4913 414 LRDLRRELRELEAEIASLERrksnipaRLLALRD------------ALAEALGLDEAELPfvgelievrpeeerwrgaIE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 840 RALREHAQTELSRLEIELKAAQK-DSVSKEEHdkIKADLERSLEDSRQIAAAAQESLSEK-------------------- 898
Cdd:COG4913 482 RVLGGFALTLLVPPEHYAAALRWvNRLHLRGR--LVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleaelgrrf 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 899 -------ETELKdlRSQKAL-EQGLVS-------KEDH--------------------EAQRLSLQAEINTLTAQLADLA 943
Cdd:COG4913 560 dyvcvdsPEELR--RHPRAItRAGQVKgngtrheKDDRrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEALE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 944 RKHE--KTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHIQQLHQDIQHSQGLIKEKDRKITELSKEVFR 1021
Cdd:COG4913 638 AELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 1022 LKEALGALTPPLGRSPSPPSSGIPGQQLALQNRVTSLTQQLQDwERKHKAVVSIYRSHlLAAVQGRMDEEVQAL 1095
Cdd:COG4913 718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG-DAVERELRENLEER-IDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
817-1026 |
3.12e-07 |
|
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: 54.00 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 817 KHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDsVSKEEHDkiKADLERSLEDSRQIAAAAQESLS 896
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQE--LAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 897 EKETELKDL------RSQKALEQGLVSKEDhEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVA 970
Cdd:COG4942 101 AQKEELAELlralyrLGRQPPLALLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207163335 971 ESQLETVKKQLTDLQAESTH-IQQLHQDIQHSQGLIKEKDRKITELSKEVFRLKEAL 1026
Cdd:COG4942 180 LAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
334-656 |
3.34e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 334 EDEEVFEEIRKLRlERGRLLQKIKVLEQQQSSATTALEELSSLKER-----LSEAEAERDRLLVELEELRAAQvsgvtcd 408
Cdd:PTZ00121 1519 EEAKKADEAKKAE-EAKKADEAKKAEEKKKADELKKAEELKKAEEKkkaeeAKKAEEDKNMALRKAEEAKKAE------- 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 409 seDAEDSDDMLDFPGAEKLLSRQSRgldanlpAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTd 488
Cdd:PTZ00121 1591 --EARIEEVMKLYEEEKKMKAEEAK-------KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK- 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 489 mqssgpdfvptAQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQ-KALEKKLSQAQAELEELKEQMRLGV 567
Cdd:PTZ00121 1661 -----------IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaEELKKKEAEEKKKAEELKKAEEENK 1729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 568 YSVEDAEE-------KPEKSSVEGGDLETHQLKARVQELEAELVSKKTDG---EGLSEDDNNTMQQLKERVKELEAALQD 637
Cdd:PTZ00121 1730 IKAEEAKKeaeedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
330
....*....|....*....
gi 1207163335 638 REKEGEENETVVNLKKQVE 656
Cdd:PTZ00121 1810 IIEGGKEGNLVINDSKEME 1828
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
132-227 |
6.51e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 132 LHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFSCESDSMETVE 211
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 1207163335 212 MLLKGGTNPHLTDALG 227
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
535-1029 |
7.69e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 535 EEKEEK--HQK--ALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVEGGDLEThqLKARVQELEAELVSKKTDG 610
Cdd:PRK02224 197 EEKEEKdlHERlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET--LEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 611 EGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVV----NLKKQVEELGKALE---LSKAAGKKEGEGAPLNG--L 681
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEarreELEDRDEELRDRLEecrVAAQAHNEEAESLREDAddL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 682 QARVEELEQELKESVPRGQFEEVQVTLGL-QLNQLAQERAEVAARLNQALLELERLrppshidedeeddepsESSEVSIA 760
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRReEIEELEEEIEELRERFGDAPVDLGNA----------------EDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 761 SDHS-LHMSPGgrTLEAIKEELEVARQEAAQALDS---------------LCAERESRAQ------DVLQLRDAVPLVkh 818
Cdd:PRK02224 419 EERDeLREREA--ELEATLRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERveeleaELEDLEEEVEEV-- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 819 qESLSAVAQQLAQTEKELQAeraLREHAQTELSRLEIELKAAQKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEK 898
Cdd:PRK02224 495 -EERLERAEDLVEAEDRIER---LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 899 ETELKDLRSQKA-----------LEQGLVSKEDHEAQ------RLSLQAEINTLTAQLADLARKHEKTCLEVFQVQR-EA 960
Cdd:PRK02224 571 REEVAELNSKLAelkerieslerIRTLLAAIADAEDEierlreKREALAELNDERRERLAEKRERKRELEAEFDEARiEE 650
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207163335 961 LfnKSERQVAESQLETVKKQLTDLQAESThiqqlhqDIQHSQGLIKEKDRKITELSKEVFRLKEALGAL 1029
Cdd:PRK02224 651 A--REDKERAEEYLEQVEEKLDELREERD-------DLQAEIGAVENELEELEELRERREALENRVEAL 710
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
347-1029 |
7.93e-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: 53.53 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 347 LERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELRAAQVSgvtcDSEDAEDSDDMLDFPGaeK 426
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK----AERYQALLKEKREYEG--Y 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 427 LLSRQSRGLDANLPAEQGEGISQEnpAMVEQLRRKVEELtsqNADLVLKVQMLEMFEKDDTDMQSSGPDFVP------TA 500
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLE--EELEKLTEEISEL---EKRLEEIEQLLEELNKKIKDLGEEEQLRVKekigelEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 501 QYESLRREFEELQEKYSRAQAsTEASSIAEDPGCEEKEEKHQKALE---KKLSQAQAELEELKEQMRLGVYSVEDAEEKP 577
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEE-RLAKLEAEIDKLLAEIEELEREIEeerKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 578 EKSSVEGGDLET--HQLKARVQELEAELVSKKTDGEGLSE---DDNNTMQQLKERVKELEAALQDREKEGEENETvvNLK 652
Cdd:TIGR02169 381 AETRDELKDYREklEKLKREINELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINELEEEKEDKALEIKKQEW--KLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 653 KQVEELGKA-LELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPR-------------------------GQFEE--- 703
Cdd:TIGR02169 459 QLAADLSKYeQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggraveevlkasiqgvhgtvaqlGSVGErya 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 704 --VQVTLGLQLNQLAQERAEVAARLNQAL----------LELERLRPPShidedEEDDEPSESSEVSIASD--------H 763
Cdd:TIGR02169 539 taIEVAAGNRLNNVVVEDDAVAKEAIELLkrrkagratfLPLNKMRDER-----RDLSILSEDGVIGFAVDlvefdpkyE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 764 SLHMSPGGRTLeaIKEELEVARQEAAQA----LDSLCAERE------SRAQDVLQLRdavplvkhQESLSAVAQQLAQTE 833
Cdd:TIGR02169 614 PAFKYVFGDTL--VVEDIEAARRLMGKYrmvtLEGELFEKSgamtggSRAPRGGILF--------SRSEPAELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 834 KELQAEralREHAQTELSRLEIELKAA-QKDSVSKEEHDKIKADLERSLEDsrqiAAAAQESLSEKETELKDLrsQKALE 912
Cdd:TIGR02169 684 EGLKRE---LSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEEDLSSL--EQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 913 QGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTclEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESthiQ 992
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK---E 829
|
730 740 750
....*....|....*....|....*....|....*..
gi 1207163335 993 QLHQDIQHSQGLIKEKDRKITELSKEVFRLKEALGAL 1029
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
499-945 |
8.82e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 499 TAQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEekhQKALEKKLSQAQAELEELKEQMRlgvySVEDAEEKPE 578
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE---LEALEAELAELPERLEELEERLE----ELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 579 kssveggdlethQLKARVQELEAELVSKKtdgEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVN-LKKQVEE 657
Cdd:COG4717 167 ------------ELEAELAELQEELEELL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEeLEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 658 LGKALELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLNQALLELERLR 737
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 738 PPSHIDEDEEDdepsessevSIASDHSLHMSPGGRTLEAIKEELEVARQEAAQALDslcAERESRAQDVLQLRDAVPLVK 817
Cdd:COG4717 312 ALEELEEEELE---------ELLAALGLPPDLSPEELLELLDRIEELQELLREAEE---LEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 818 HQESLSAVAQQLAQTEkELQAERALREHAQTELSRLEIELKAAQKDSVSKEEHDKIkADLERSLEDSRQIAAAAQESLSE 897
Cdd:COG4717 380 GVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL-EELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1207163335 898 KETELKDLRSQKALEQglvskedheaqrlsLQAEINTLTAQLADLARK 945
Cdd:COG4717 458 LEAELEQLEEDGELAE--------------LLQELEELKAELRELAEE 491
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
97-147 |
1.28e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 1.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1207163335 97 NALHLAAKNGQPDCLKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEIL 147
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-659 |
1.32e-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: 52.75 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 341 EIRKLRLERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVEL-EELRAAQVSGVTCDSEDAEDSDDML 419
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 420 DFpgAEKLLSRQSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQML-EMFEKDDTDMQSSgpdfvp 498
Cdd:TIGR02168 758 EL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLnEEAANLRERLESL------ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 499 TAQYESLRREFEELQEKYSRAQAStEASSIAEDPGCEEKEEKHQKALEKKL---SQAQAELEELKEQMRLGVYSVEDAEE 575
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 576 KPEKSSVEGGDLETH--QLKARVQELEAELVSKKtdgEGLSEDDNNTMQQLKERVKELEAALQDREKEgeenetVVNLKK 653
Cdd:TIGR02168 909 KRSELRRELEELREKlaQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENKIEDDEEEARRR------LKRLEN 979
|
....*.
gi 1207163335 654 QVEELG 659
Cdd:TIGR02168 980 KIKELG 985
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
505-947 |
2.30e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 505 LRREFEELQEKYSRAQASTEASSIAEDPGCEEkEEKHQKALEKKLSQAQAELEELKEQMrlgvysvEDAEEKPEKSSVEg 584
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEE-ELKEAEEKEEEYAELQEELEELEEEL-------EELEAELEELREE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 585 gdLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERvKELEAALQDREKEGEENETVVNLKKQVEELGKALEL 664
Cdd:COG4717 118 --LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 665 SKAAGKkegegapLNGLQARVEELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLNQALLELERLRPPSHIDE 744
Cdd:COG4717 195 QDLAEE-------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 745 DEEDDEPSESSEVSIASDHSLHMSPGGRTLEAIKEELEvaRQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSA 824
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE--ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 825 VAQ-QLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSVSK--EEHDKIKADLERSLEDSRQIAAAAQESLSEKETE 901
Cdd:COG4717 346 IEElQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1207163335 902 LKDlRSQKALEQGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHE 947
Cdd:COG4717 426 DEE-ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
500-999 |
3.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 500 AQYESLRREfEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQmrlgvysVEDAEEkpek 579
Cdd:COG4913 249 EQIELLEPI-RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE-------LERLEA---- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 580 ssveggdlETHQLKARVQELEAELvskktdgeglSEDDNNTMQQLKERVKELEAALQDREKEGEEnetvvnLKKQVEELG 659
Cdd:COG4913 317 --------RLDALREELDELEAQI----------RGNGGDRLEQLEREIERLERELEERERRRAR------LEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 660 KALELSKAAgkkegegapLNGLQARVEELEQELKESvpRGQFEEVQVTLGLQLNQLAQERAEVAARLNQalLELERLRPP 739
Cdd:COG4913 373 LPLPASAEE---------FAALRAEAAALLEALEEE--LEALEEALAEAEAALRDLRRELRELEAEIAS--LERRKSNIP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 740 SHIDEDEEDdepsessevsIASDHSLHMSPggrtLEAIKEELEVARQEAA-----------QALDSLCAER-ESRAQDV- 806
Cdd:COG4913 440 ARLLALRDA----------LAEALGLDEAE----LPFVGELIEVRPEEERwrgaiervlggFALTLLVPPEhYAAALRWv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 807 --------LQLRDAVPLVKHQESLSAVAQQLAqtEKELQAERALREHAQTELSRL--------EIELKAAQ--------- 861
Cdd:COG4913 506 nrlhlrgrLVYERVRTGLPDPERPRLDPDSLA--GKLDFKPHPFRAWLEAELGRRfdyvcvdsPEELRRHPraitragqv 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 862 KDSVSKEEHD-----------------KIKAdLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQGLVSKEDHEAQ 924
Cdd:COG4913 584 KGNGTRHEKDdrrrirsryvlgfdnraKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207163335 925 RLSLQAEINTLTAQLADLarkhEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHIQQLHQDIQ 999
Cdd:COG4913 663 VASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-1029 |
5.20e-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: 50.84 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 336 EEVFEEIRKLRLERGRLLQ-KIKVLEQQQSSATTALE----ELSSLKERLSEAEAERDRLLVELEELRAAQvsgvtcdse 410
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAekerELEDAEERLAKLEAEIDKLLAEIEELEREI--------- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 411 daeDSDDMLDFPGAEKLLSRQSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQ----NADLVLKVQMLEMFEKDD 486
Cdd:TIGR02169 346 ---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinelKRELDRLQEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 487 TDMQSSGPDFVptAQYESLRREFEELQEKYSraQASTEASSIAEDPGCEEKE----EKHQKALEKKLSQAQAELEELKEQ 562
Cdd:TIGR02169 423 ADLNAAIAGIE--AKINELEEEKEDKALEIK--KQEWKLEQLAADLSKYEQElydlKEEYDRVEKELSKLQRELAEAEAQ 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 563 MRLGVYSVED--AEEKPEKSSVEGgdlethqlkarVQELEAELVSKKtdgeglseddnntmqqlKERVKELEAALQDR-- 638
Cdd:TIGR02169 499 ARASEERVRGgrAVEEVLKASIQG-----------VHGTVAQLGSVG-----------------ERYATAIEVAAGNRln 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 639 ----EKEGEENETVVNLKKqvEELGKA--LELSK--------AAGKKEG------------------------------- 673
Cdd:TIGR02169 551 nvvvEDDAVAKEAIELLKR--RKAGRAtfLPLNKmrderrdlSILSEDGvigfavdlvefdpkyepafkyvfgdtlvved 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 674 -EGAPLNGLQARVEELEQELKE---SVPRGQFEEVqvtlGLQLNQlAQERAEVaARLNQALLELERLRppSHIDEDEEDD 749
Cdd:TIGR02169 629 iEAARRLMGKYRMVTLEGELFEksgAMTGGSRAPR----GGILFS-RSEPAEL-QRLRERLEGLKREL--SSLQSELRRI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 750 EPSESSEVSIASDHSLHMSPGGRTLEAIKEELEVARQEAAQALDSLCAERESRAQDvlqlrdavplvkhQESLSAVAQQL 829
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-------------KSELKELEARI 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 830 AQTEKELQAERALREHAQTELSRLEIELKAAQKDSVsKEEHDKIKA---DLERSLEDSRQIAAAAQESLSEKETELKDLR 906
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKL-EEEVSRIEArlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 907 SQKA-----LEQGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQL 981
Cdd:TIGR02169 847 EQIKsiekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1207163335 982 TDLQAESTHIQQLHQDIQHsqglIKEKDRKITELSKEVFRLKEALGAL 1029
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEE----IPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
61-183 |
5.34e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 50.56 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 61 EGKSAFHLCASRGRLDCLEVILSHGVDI-----GV-----TDGTGF----NALHLAAKNGQPDCLKRLLQ-ERMPVD--S 123
Cdd:cd22193 75 EGQTALHIAIERRQGDIVALLVENGADVhahakGRffqpkYQGEGFyfgeLPLSLAACTNQPDIVQYLLEnEHQPADieA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 124 TDSFGRTSLHhaavsgclSCTEILWDFKANLD------------------------AQDGDGSTPLILAAQMSRIELCAF 179
Cdd:cd22193 155 QDSRGNTVLH--------ALVTVADNTKENTKfvtrmydmilirgaklcptveleeIRNNDGLTPLQLAAKMGKIEILKY 226
|
....
gi 1207163335 180 LLER 183
Cdd:cd22193 227 ILQR 230
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
29-191 |
6.06e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 50.26 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 29 DDRLLQAVEQNDP--EKVATLLVKKGLCPSKLDAE-GKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLAAKN 105
Cdd:PHA02878 132 DLVYIDKKSKDDIieAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 106 GQPDCLKRLLQERMPVDSTDSFGRTSLHHaAVSGCLSCT--EILWDFKANLDAQDG-DGSTPLILAAQMSRIelCAFLLE 182
Cdd:PHA02878 212 YNKPIVHILLENGASTDARDKCGNTPLHI-SVGYCKDYDilKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLE 288
|
....*....
gi 1207163335 183 RGANPNLQD 191
Cdd:PHA02878 289 YGADINSLN 297
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
152-198 |
7.77e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 7.77e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1207163335 152 ANLDAQDGDGSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSAL 198
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
329-893 |
7.82e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 329 SENLTEDEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATTALEElssLKERLSEAEaERDRLLVELEELRAAQVSGVTCD 408
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE-EKVKELKELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 409 SEDAEDSDDMldfpgaEKLLSRQSrgldanlpaEQGEGIsQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEKddtd 488
Cdd:PRK03918 303 EEYLDELREI------EKRLSRLE---------EEINGI-EERIKELEEKEERLEELKKKLKELEKRLEELEERHE---- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 489 mqssgpdfvptaQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALeKKLSQAQAELEELKEQMRLGVY 568
Cdd:PRK03918 363 ------------LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI-SKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 569 SVEDAEekpEKSSVEGGDLETHQLKARVQELEAELvskktdgeglsEDDNNTMQQLKERVKELEAALQDREKEGEENETV 648
Cdd:PRK03918 430 ELKKAK---GKCPVCGRELTEEHRKELLEEYTAEL-----------KRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 649 VNLKK---QVEELGKAL------ELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPrgqFEEVQVTLGLQLNQLAQER 719
Cdd:PRK03918 496 IKLKElaeQLKELEEKLkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE---LKKKLAELEKKLDELEEEL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 720 AEVAARLNQALLE--------LERLRPPshidedeeddepsessevsiaSDHSLHMSPGGRTLEAIKEELEVARQEAAQA 791
Cdd:PRK03918 573 AELLKELEELGFEsveeleerLKELEPF---------------------YNEYLELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 792 LDSL------CAERESRAQDVLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSV 865
Cdd:PRK03918 632 FEELaetekrLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580
....*....|....*....|....*...
gi 1207163335 866 SKEEHDKIKADLERSLEDSRQIAAAAQE 893
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
355-1008 |
1.32e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 355 KIKVLEQQQSSATTALEELSSLKERLS---EAEAERDRLLVELEELRAaQVSGVTCDSEDAEDSDDMLDF-PGAEKLLSR 430
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTqkrEAQEEQLKKQQLLKQLRA-RIEELRAQEAVLEETQERINRaRKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 431 QSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEkddtdmqssgpdfvptAQYESLRREFE 510
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH----------------SQEIHIRDAHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 511 elQEKYSRAQASteassiaedpgceekeekHQKALEKKLSQAQAELEELKEQMRLGvySVEDAEEKPEKSSVEGGDLETH 590
Cdd:TIGR00618 363 --VATSIREISC------------------QQHTLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 591 QLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVNLKKQVEElgkalelskaagK 670
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR------------K 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 671 KEGEGAPLNGLQarveELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAARLNQALLELErlrppsHIDEDEEDDE 750
Cdd:TIGR00618 489 KAVVLARLLELQ----EEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY------HQLTSERKQR 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 751 PSESSEVSIASDHSLHMSpggRTLEAIKEELEVARQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSAVAQQLA 830
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILT---QCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 831 QTEKELQAERALREHAQTELSRLEIELKAAqKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQka 910
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHAL-SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH-- 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 911 leQGLVSKEDHEAQRL--SLQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETvkkQLTDLQAES 988
Cdd:TIGR00618 713 --IEEYDREFNEIENAssSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA---ELSHLAAEI 787
|
650 660
....*....|....*....|
gi 1207163335 989 THIQQLHQDIQHSQGLIKEK 1008
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAE 807
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
773-999 |
1.46e-05 |
|
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: 48.61 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 773 TLEAIKEELEVARQEAAQALDSLCAERESRAQDVLQLRDAvplvkhQESLSAVAQQLAQTEKELQAERALREHAQTELSR 852
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL------ERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 853 LEIELkAAQKDSVSK--------EEHDKIK--------ADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKAleqglv 916
Cdd:COG4942 95 LRAEL-EAQKEELAEllralyrlGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 917 skeDHEAQRLSLQAEINTLTAQLADLARKhektclevfQVQREALFNKSERQVAESQletvkKQLTDLQAESTHIQQLHQ 996
Cdd:COG4942 168 ---ELEAERAELEALLAELEEERAALEAL---------KAERQKLLARLEKELAELA-----AELAELQQEAEELEALIA 230
|
...
gi 1207163335 997 DIQ 999
Cdd:COG4942 231 RLE 233
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
17-194 |
1.89e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 48.72 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 17 YGVITSQDWSKTDDRLLQAVEQNDPEKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGF 96
Cdd:PHA02878 156 YGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 97 NALHLAAKNGQP-DCLKRLLQERMPVDSTDSF-GRTSLHHAAVSGclSCTEILWDFKANLDAQDGDGSTPLILAA-QMSR 173
Cdd:PHA02878 236 TPLHISVGYCKDyDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkQYLC 313
|
170 180
....*....|....*....|....*.
gi 1207163335 174 IELCAFL-----LERGANPNLQDNQG 194
Cdd:PHA02878 314 INIGRILisnicLLKRIKPDIKNSEG 339
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
346-735 |
2.53e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 346 RLERGRLLQKIKVLEQQQSSAttalEELSSLKERLSEAEAERDRLLVELEELRAAqVSGVTCDSEDAEDSDDMLDfpGAE 425
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLR----ERLEGLKRELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLE--QEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 426 KLLSRQSRGLDANLPAEQGEgiSQENPAMVEQLRRKVEELTSQNADLVLKVQMLEmfekddtdmQSSGPDFVPTaqyesL 505
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQE--IENVKSELKELEARIEELEEDLHKLEEALNDLE---------ARLSHSRIPE-----I 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 506 RREFEELQEKYSRAQASTEASsiaedpgceekeEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVEGG 585
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREI------------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 586 DLETH--QLKARVQELEAELVSKKTDGEGLSEDdnntMQQLKERVKELEAALQD-REKEGEENETVVNLKKQVEELGKAl 662
Cdd:TIGR02169 865 ELEEEleELEAALRDLESRLGDLKKERDELEAQ----LRELERKIEELEAQIEKkRKRLSELKAKLEALEEELSEIEDP- 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 663 elsKAAGKKE-GEGAPLNGLQARVEELEQELKesvprgQFEEVqvtlglqlNQLA-QERAEVAARLN-----QALLELER 735
Cdd:TIGR02169 940 ---KGEDEEIpEEELSLEDVQAELQRVEEEIR------ALEPV--------NMLAiQEYEEVLKRLDelkekRAKLEEER 1002
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
480-737 |
2.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 480 EMFEKDDTDMQSSGP--DFVPTAQYESLRREFEELQEKYSRAQASTEASsiaedpgceekeEKHQKALEKKLSQAQAeLE 557
Cdd:COG4913 588 TRHEKDDRRRIRSRYvlGFDNRAKLAALEAELAELEEELAEAEERLEAL------------EAELDALQERREALQR-LA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 558 ELKEQmrlgvysvedaeekpekssveggDLETHQLKARVQELEAELvskktdgEGLsEDDNNTMQQLKERVKELEAALQD 637
Cdd:COG4913 655 EYSWD-----------------------EIDVASAEREIAELEAEL-------ERL-DASSDDLAALEEQLEELEAELEE 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 638 -REKEGEENETVVNLKKQVEELGKALELSKAAgkkeGEGAPLNGLQARVEELEQELKESVPRGQFEEVQvtlglqlNQLA 716
Cdd:COG4913 704 lEEELDELKGEIGRLEKELEQAEEELDELQDR----LEAAEDLARLELRALLEERFAAALGDAVERELR-------ENLE 772
|
250 260
....*....|....*....|.
gi 1207163335 717 QERAEVAARLNQALLELERLR 737
Cdd:COG4913 773 ERIDALRARLNRAEEELERAM 793
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
336-993 |
3.23e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 336 EEVFEEIRKLRLERGRLLQKIKVLEQQQSSattaleELSSLKERLSEAEAERDRLLVELEELRAAQVSGVTCDSEDAEDS 415
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIAS------RQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 416 DDMLDFPGAEKLLSRQSRGLDANLPAEQGEGISQEnpamVEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTDMQSSGPD 495
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSE----LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 496 FVPTAQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEK---KLSQAQAElEELKEQMRLGVYSVED 572
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGElklRLNQATAT-PELLLQLENFDERIER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 573 AEEKPEKSSVEGGDLETHQLKARvqeleaelvskktdgeGLSEDDNNTMQQLKERVKELEAALQDREKEgeenetvvnLK 652
Cdd:pfam12128 476 AREEQEAANAEVERLQSELRQAR----------------KRRDQASEALRQASRRLEERQSALDELELQ---------LF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 653 KQVEELGKALElSKAAGKKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQVTLglqlnqlaqeraevaarlnqallE 732
Cdd:pfam12128 531 PQAGTLLHFLR-KEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL-----------------------D 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 733 LERLRPPSHIDEDEEDDEPSESSEVSIASDHSLH------MSPGGRTLEAIKEELEVARQEAAQALDSLcaERESRAQDV 806
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQaaaeeqLVQANGELEKASREETFARTALKNARLDL--RRLFDEKQS 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 807 LQLRDAVPLVKHQ----ESLSAVAQQLAQTEKELQAeraLREHAQTELSRLEIELKAAQKDSVS--KEEHDKIKADLers 880
Cdd:pfam12128 665 EKDKKNKALAERKdsanERLNSLEAQLKQLDKKHQA---WLEEQKEQKREARTEKQAYWQVVEGalDAQLALLKAAI--- 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 881 leDSRQIAAAAQeslseketeLKDLRSQKALEqgLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTcLEVFQVQREA 960
Cdd:pfam12128 739 --AARRSGAKAE---------LKALETWYKRD--LASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV-LRYFDWYQET 804
|
650 660 670
....*....|....*....|....*....|...
gi 1207163335 961 LfnKSERQVAESQLETVKKQLTDLQAESTHIQQ 993
Cdd:pfam12128 805 W--LQRRPRLATQLSNIERAISELQQQLARLIA 835
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
777-999 |
3.24e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 777 IKEELEVARQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIE 856
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 857 LKAaqkdsvskeehdkikadLERSLEDSRQIAAAAQES--LSEKETELKDLRSQKAlEQGLVSKEDHEaQRLSLQAEINT 934
Cdd:COG3206 242 LAA-----------------LRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELA-ELSARYTPNHP-DVIALRAQIAA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207163335 935 LTAQLADLARKhektCLEVFQVQREALfnKSERQVAESQLETVKKQLTDLQAESTHIQQLHQDIQ 999
Cdd:COG3206 303 LRAQLQQEAQR----ILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
61-183 |
3.37e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 47.83 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 61 EGKSAFHLCASRGRLDCLEVILSHGVDIGV-TDGTGFN-------------ALHLAAKNGQPDCLKRLL-QERMPVDSTD 125
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhAKGVFFNpkykhegfyfgetPLALAACTNQPEIVQLLMeKESTDITSQD 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207163335 126 SFGRTSLHHAAVSGCLSCTEIlwDF-------------KANLDA-QDGDGSTPLILAAQMSRIELCAFLLER 183
Cdd:cd22194 220 SRGNTVLHALVTVAEDSKTQN--DFvkrmydmillkseNKNLETiRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
160-192 |
4.81e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.51 E-value: 4.81e-05
10 20 30
....*....|....*....|....*....|....
gi 1207163335 160 DGSTPLILAA-QMSRIELCAFLLERGANPNLQDN 192
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
622-1029 |
6.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 622 QQLKERVKELEAALQDREKEGEEnetvvnLKKQVEELGKALELSKAAGKKEGEGAPLNGLQARVEELEQELKEsvprgqf 701
Cdd:COG4717 91 AELQEELEELEEELEELEAELEE------LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 702 eevqvtlglqLNQLAQERAEVAARLNQALLELERLRppshidedeeddepsessevsiaSDHSLHMSPGGRTLEAIKEEL 781
Cdd:COG4717 158 ----------LRELEEELEELEAELAELQEELEELL-----------------------EQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 782 EVARQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEI------ 855
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 856 ------ELKAAQKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKE--TELKDLRSQKALEQGLVSKEDHEAQRLS 927
Cdd:COG4717 285 llallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 928 LQAEINTLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLqAESTHIQQLHQDIQHSQGLIKE 1007
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|..
gi 1207163335 1008 KDRKITELSKEVFRLKEALGAL 1029
Cdd:COG4717 444 LEEELEELREELAELEAELEQL 465
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
329-980 |
7.21e-05 |
|
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: 46.96 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 329 SENLTEDEEVFEEIRKLRLERGRLLQ-KIKVLEQQQssattalEELSSLKERLSEAEAERDRLLVELEELRAAQV----- 402
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLGRTIElKKEILEKKQ-------EELKFVIKELQQLEGSSDRILELDQELRKAERelska 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 403 ---SGVTCDSEDAED-SDDMLDFPGAEKLLSRQSRGLDANLPA-EQGEGISQENPAMVEQLR----RKVEELTSQNADLV 473
Cdd:TIGR00606 491 eknSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQLNHHTTTrTQMEMLTKDKMDKDEQIRkiksRHSDELTSLLGYFP 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 474 LKVQMLEMFEKDDTDMQSSGPDF----VPTAQYESLRREFEElQEKYSRAQASTEASSIAEDPGCEEKEEKHQKaLEKKL 549
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDRLaklnKELASLEQNKNHINN-ELESKEEQLSSYEDKLFDVCGSQDEESDLER-LKEEI 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 550 SQAQAELEELKEQMrlGVYSVEDAEEKPEKSSVEGGDLETHQLKARVQELEAELVSKktdgeglseddnntMQQLKERVK 629
Cdd:TIGR00606 649 EKSSKQRAMLAGAT--AVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSK--------------LRLAPDKLK 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 630 ELEAALQDREKEGEENETVVNLKKQVEELgKALELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQVTLG 709
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDL-KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 710 LQLNQLAQERAEVAARLNQALLELERLRPPSHIDEDEEDDEPSESSEVSIASDHSLH------MSPGGRTLEAIKEELEV 783
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNrkliqdQQEQIQHLKSKTNELKS 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 784 AR---QEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAA 860
Cdd:TIGR00606 872 EKlqiGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 861 QKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQGLVSKEDHEAQRLSLQAEINTLTAQLA 940
Cdd:TIGR00606 952 NIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELK 1031
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1207163335 941 DLARKHEKTCLEVFQVQreALFNKSERQVAESQLETVKKQ 980
Cdd:TIGR00606 1032 EVEEELKQHLKEMGQMQ--VLQMKQEHQKLEENIDLIKRN 1069
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-1015 |
7.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 501 QYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQmrlgvysVEDAEEkpEKS 580
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE-------LDELEA--QIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 581 SVEGGDLEthQLKARVQELEAELVSKKTDGE-------GLSEDDNNTMQQLKERVKELEAALQD-REKEGEENETVVNLK 652
Cdd:COG4913 334 GNGGDRLE--QLEREIERLERELEERERRRArleallaALGLPLPASAEEFAALRAEAAALLEAlEEELEALEEALAEAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 653 KQVEELGKALElskaagKKEGEgapLNGLQARV-----------EELEQELKESVPRGQF--EEVQVTLGLQLNQLAQER 719
Cdd:COG4913 412 AALRDLRRELR------ELEAE---IASLERRKsniparllalrDALAEALGLDEAELPFvgELIEVRPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 720 AEVAARLN---------QALLELERLRPPSHIDEDEEDDEPSESSEVSIASDhslhmspggrtleAIKEELEVARQEAAQ 790
Cdd:COG4913 483 VLGGFALTllvppehyaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD-------------SLAGKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 791 ALDSLCAERESRAQ--DVLQLRD---AVP---LVKHQESLSA----------------VAQQLAQTEKELQAERALREHA 846
Cdd:COG4913 550 WLEAELGRRFDYVCvdSPEELRRhprAITragQVKGNGTRHEkddrrrirsryvlgfdNRAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 847 QTELSRLEIELKAAQKdsvSKEEHDKIKADLERSLEdsrqiAAAAQESLSEKETELKDLR-SQKALEQgLvskedhEAQR 925
Cdd:COG4913 630 EERLEALEAELDALQE---RREALQRLAEYSWDEID-----VASAEREIAELEAELERLDaSSDDLAA-L------EEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 926 LSLQAEINTLTAQLADLARKHEK--TCLEVFQVQREAL------FNKSERQVAESQLETVKKQLTDLQAESTHIQQLHQD 997
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRleKELEQAEEELDELqdrleaAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
570
....*....|....*...
gi 1207163335 998 IQHSQGLIKEKDRKITEL 1015
Cdd:COG4913 775 IDALRARLNRAEEELERA 792
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
774-1030 |
8.06e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 774 LEAIKEELEVARQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRL 853
Cdd:PRK11281 82 TEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 854 EIELKAAQKDSvskeehDKIKADLERSLEDSRQIAAAAQESLsekETELKDLRSQKALeqglvskedheaQRLSLQAeiN 933
Cdd:PRK11281 162 QAALYANSQRL------QQIRNLLKGGKVGGKALRPSQRVLL---QAEQALLNAQNDL------------QRKSLEG--N 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 934 TltaQLADLARK-HEKTCLEVFQVQREALFNK---SERQVAESQlETVKKQLTdlQAESTHIQ-------QLHQDIQHSQ 1002
Cdd:PRK11281 219 T---QLQDLLQKqRDYLTARIQRLEHQLQLLQeaiNSKRLTLSE-KTVQEAQS--QDEAARIQanplvaqELEINLQLSQ 292
|
250 260
....*....|....*....|....*...
gi 1207163335 1003 GLIKEKDRkITELSKEVFRLKEALGALT 1030
Cdd:PRK11281 293 RLLKATEK-LNTLTQQNLRVKNWLDRLT 319
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
149-246 |
8.32e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.78 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 149 DFKANLDAQDGDGSTP--LILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGGTNPHLTDAL 226
Cdd:PLN03192 511 DLLGDNGGEHDDPNMAsnLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
90 100
....*....|....*....|
gi 1207163335 227 GHNSTHYSITAGNHSITQLL 246
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRIL 610
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
144-258 |
1.13e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.03 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 144 TEILWDFKANLDAQDGD-GSTPLILAAQMSRIELCAFLLERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGGTNPHL 222
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207163335 223 TDALGHNSTHYSITA-GNHSITQLLQNLGVTTAAEGS 258
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSY 266
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
114-168 |
1.27e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207163335 114 LLQER-MPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILA 168
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
335-695 |
1.58e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 335 DEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELraaqvsgvtcdsedaed 414
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL----------------- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 415 sddmldfpgaEKLLSRQSRGLdANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEKDDtdmqssgp 494
Cdd:TIGR02169 764 ----------EARIEELEEDL-HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL-------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 495 dfvpTAQYESLRREFEELQEK--YSRAQASTEASSIAEDPG----CEEKEEKHQKA---LEKKLSQAQAELEELKEQMRL 565
Cdd:TIGR02169 825 ----TLEKEYLEKEIQELQEQriDLKEQIKSIEKEIENLNGkkeeLEEELEELEAAlrdLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 566 GVYSVEDAEEKPEKSSVEGGdlethQLKARVQELEAELVSKKTDGEGLSEDDNNTM--QQLKERVKELEAALQDREKege 643
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLS-----ELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRALEP--- 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1207163335 644 enetvVNLK--KQVEELGKAL-ELSKAAGKKEGEGAplnGLQARVEELEQELKES 695
Cdd:TIGR02169 973 -----VNMLaiQEYEEVLKRLdELKEKRAKLEEERK---AILERIEEYEKKKREV 1019
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
597-988 |
1.83e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 597 QELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENETVVNLKKQVEELGKALELskAAGKKEGega 676
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEE--ADEQQEE--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 677 plngLQARVEELEQELKESvpRGQFEEVQVTLGLQlnqlaQERAevaARLNQALLELERLR----PPSHIDEDEEDDEPS 752
Cdd:PRK04863 381 ----NEARAEAAEEEVDEL--KSQLADYQQALDVQ-----QTRA---IQYQQAVQALERAKqlcgLPDLTADNAEDWLEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 753 ESSEVSIASDHSLHMSPGGRTLEAIKEELEvarqEAAQALDSLCAERE-SRAQDVlqlrdAVPLVKHQESLSAVAQQLAQ 831
Cdd:PRK04863 447 FQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSrSEAWDV-----ARELLRRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 832 TEKELQA-ERALREHAQTELSRLEIElKAAQKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQ-K 909
Cdd:PRK04863 518 LRMRLSElEQRLRQQQRAERLLAEFC-KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARiQ 596
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207163335 910 ALEQglvskedHEAQRLSLQAEINTLTAQLADlarkHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLtDLQAES 988
Cdd:PRK04863 597 RLAA-------RAPAWLAAQDALARLREQSGE----EFEDSQDVTEYMQQLLERERELTVERDELAARKQAL-DEEIER 663
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
622-905 |
2.04e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 622 QQLKERVKELEAALQDREKEGEEnetvvnLKKQVEELgKALELskaagkKEGEgaplnglqarVEELEQELKesvpR-GQ 700
Cdd:COG0497 168 RALKKELEELRADEAERARELDL------LRFQLEEL-EAAAL------QPGE----------EEELEEERR----RlSN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 701 FEEVQVTLGLQLNQLAQERAEVAARLNQALLELERLrppshidedeeddepsessevsiaSDHSLHMSPGGRTLEAIKEE 780
Cdd:COG0497 221 AEKLREALQEALEALSGGEGGALDLLGQALRALERL------------------------AEYDPSLAELAERLESALIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 781 LEVARQEAAQALDSLCA--ER----ESRAQDVLQL-RdavplvKHQESLSAVAQQLAQTEKELQAEralrEHAQTELSRL 853
Cdd:COG0497 277 LEEAASELRRYLDSLEFdpERleevEERLALLRRLaR------KYGVTVEELLAYAEELRAELAEL----ENSDERLEEL 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207163335 854 EIELKAAQKDSvskeehdkikADLERSLEDSRQIAAAAqesLSEK-ETELKDL 905
Cdd:COG0497 347 EAELAEAEAEL----------LEAAEKLSAARKKAAKK---LEKAvTAELADL 386
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
99-232 |
3.85e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 44.62 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 99 LHLAAKNGQPDCLKRLLQErmpvDSTDSF-----GRTSLHHAAVSGCLSCTEILWDFKANL--DAQDGD---GSTPLILA 168
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKC----PSCDLFqrgalGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 169 AQMSRIELCAFLLERGA---NPNL--------QDNQ---GRSALMFSCESDSMETVEMLLKGGTNPHLTDALGHNSTH 232
Cdd:cd22192 97 VVNQNLNLVRELIARGAdvvSPRAtgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
340-563 |
6.41e-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: 43.60 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 340 EEIRKLRLERGRLLQKIKVLEQQQSSATTAL----EELSSLKERLSEAEAERDRLLVELEELRAAqvsgvtcdSEDAEDS 415
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIraleQELAALEAELAELEKEIAELRAELEAQKEE--------LAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 416 DDMLDFPGAEKLLSRQSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEkddtdmqssgpd 495
Cdd:COG4942 113 LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL------------ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 496 fvptAQYESLRREFEELQEKYSRAQASTEaSSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQM 563
Cdd:COG4942 181 ----AELEEERAALEALKAERQKLLARLE-KELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
48-102 |
7.44e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 7.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207163335 48 LVKKGLC-PSKLDAEGKSAFHLCASRGRLDCLEVILSHGVDIGVTDGTGFNALHLA 102
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-740 |
8.80e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 330 ENLTEDEEVFEEIRKLRLE-RGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELRAAQVSgvtcd 408
Cdd:COG1196 365 EALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE----- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 409 sedaedsddmldfpGAEKLLSRQSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTD 488
Cdd:COG1196 440 --------------EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 489 MQSSGPDFVPTAQYESLRREFEELQ---EKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELkEQMRL 565
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIgveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL-DKIRA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 566 GVYSVEDAEEKPEKSSVEGGDLETHQLKARVQELEAELVSkKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEEN 645
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG-RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 646 ETVVNLKKQVEELGKALELSKAAGKKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQVTLGLQLNQLAQERAEVAAR 725
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
410
....*....|....*
gi 1207163335 726 LNQALLELERLRPPS 740
Cdd:COG1196 744 EEELLEEEALEELPE 758
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
62-183 |
9.29e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 43.26 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 62 GKSAFHLCASRGRLDCLEVILSHGVDIG----------VTDGTGFN----ALHLAAKNGQPDCLKRLLQ---ERMPVDST 124
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkKKGGPGFYfgelPLSLAACTNQLDIVKFLLEnphSPADISAR 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207163335 125 DSFGRTSLHH--AAVSGCLSCT--------EIL-----WDFKANLDA-QDGDGSTPLILAAQMSRIELCAFLLER 183
Cdd:cd22196 174 DSMGNTVLHAlvEVADNTPENTkfvtkmynEILilgakIRPLLKLEEiTNKKGLTPLKLAAKTGKIGIFAYILGR 248
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
503-694 |
9.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 503 ESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSV 582
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 583 EGGDL----ETHQLKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEENetvvnlKKQVEEL 658
Cdd:PTZ00121 1676 KAEEAkkaeEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED------KKKAEEA 1749
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207163335 659 GKALELSK--AAGKKEGEGAPLNGLQARVEELEQELKE 694
Cdd:PTZ00121 1750 KKDEEEKKkiAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
324-1024 |
1.15e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 324 TQHPPSENLTEDEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATtalEELSSLKERLSEAEAERDRLLVELEELRAAqvs 403
Cdd:TIGR00618 216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ---QLLKQLRARIEELRAQEAVLEETQERINRA--- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 404 gvtcdsedaedsddmldfPGAEKLLSRQSRGLDANLPAEQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFE 483
Cdd:TIGR00618 290 ------------------RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 484 KDDTDMQSSGPdfVPTAQYESLRREFEELQEKYSRAQ-----------ASTEASSIAEDPG------CEEKEEKHQKALE 546
Cdd:TIGR00618 352 SQEIHIRDAHE--VATSIREISCQQHTLTQHIHTLQQqkttltqklqsLCKELDILQREQAtidtrtSAFRDLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 547 KKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEDDNNTmQQLKE 626
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP-CPLCG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 627 RVKELEAALQDREKEGEENETVVNLKKQVEELGKALElskaagKKEGEGAPLNGLQARVEELEQELKESvprgqfeevqv 706
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE------DVYHQLTSERKQRASLKEQMQEIQQS----------- 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 707 tlglqLNQLAQERAEVAARLNQALLELERLRPPSHIDEDEEDDEPSESSEVSIASDHSLHmspggrtLEAIKEELEVARQ 786
Cdd:TIGR00618 572 -----FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD-------LQDVRLHLQQCSQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 787 EAAQALDSLCAERESRAQDvlQLRDAVPLVKHQEslsavAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSVS 866
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQE--RVREHALSIRVLP-----KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 867 KEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQglvsKEDHEAQRLSLQAEINTLTaQLADLARKh 946
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKAR----TEAHFNNNEEVTAALQTGA-ELSHLAAE- 786
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 947 ektcLEVFQVQREALFNkserQVAESQLETVKKQLTDLQAESTHIQQLHQDIQHSQGLIKEKDRKITELSKEVFRLKE 1024
Cdd:TIGR00618 787 ----IQFFNRLREEDTH----LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
32-198 |
1.48e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 42.69 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 32 LLQAVEQNDPEKVATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVILSHG---VDIGVTDG--TGFNALHLAAKNG 106
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 107 QPDCLKRLLQERMPVDS---TDSF---GRTSLHH--------AAVSGCLSCTEILWDFKANLDAQDGDGSTPL-ILAAQM 171
Cdd:cd22192 101 NLNLVRELIARGADVVSpraTGTFfrpGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhILVLQP 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207163335 172 SRIELCA---FLLERGANPN------LQDNQGRSAL 198
Cdd:cd22192 181 NKTFACQmydLILSYDKEDDlqpldlVPNNQGLTPF 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
348-737 |
1.57e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 348 ERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELRAAQvsgvtcdsedaedsdDMLDFPGAEKL 427
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL---------------QLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 428 LSRQSRGLDANLPAEQgegisqenpAMVEQLRRKVEELTSQNADLV-LKVQMLEMFEKDDTDMQSSGPDFVptAQYESLR 506
Cdd:COG4717 137 LEAELAELPERLEELE---------ERLEELRELEEELEELEAELAeLQEELEELLEQLSLATEEELQDLA--EELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 507 REFEELQEKYSRAQASTEASSIAEDpgcEEKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAE------------ 574
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELE---QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 575 ---------EKPEKSSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEDDNNT--------MQQLKERVKELEAALQD 637
Cdd:COG4717 283 lgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 638 REKEGEENETVVNLKKQ----VEELGKALELSKAAGKKEGEgapLNGLQARVEELEQELKESVPRGQFEEVQvtlgLQLN 713
Cdd:COG4717 363 LQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEE---LEELEEQLEELLGELEELLEALDEEELE----EELE 435
|
410 420
....*....|....*....|....
gi 1207163335 714 QLAQERAEVAARLNQALLELERLR 737
Cdd:COG4717 436 ELEEELEELEEELEELREELAELE 459
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
169-246 |
1.72e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 169 AQMSRIELCAF-----------LLERGANPNLQDNQGRSALMFSCESDSMETVEMLLKGGTNPHLTDALGHNSTHYSITA 237
Cdd:PTZ00322 79 AHMLTVELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
....*....
gi 1207163335 238 GNHSITQLL 246
Cdd:PTZ00322 159 GFREVVQLL 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
712-988 |
1.77e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 712 LNQLAQERAEVAARLNQALLELERLRppshidedeeddepSESSEVSIASDHSLHMSpggrTLEAIKEELEVARQEAAQA 791
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFR--------------QKNGLVDLSEEAKLLLQ----QLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 792 ldslcaerESRAQDVLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERAlrehaqTELSRLeielkaaqkdsvsKEEHD 871
Cdd:COG3206 239 --------EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA------ELSARY-------------TPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 872 KIKAdLERSLEDSR-QIAAAAQESLSEKETELKDLRSQKAleqglvskedheaqrlSLQAEINTLTAQLADLARKhektc 950
Cdd:COG3206 292 DVIA-LRAQIAALRaQLQQEAQRILASLEAELEALQAREA----------------SLQAQLAQLEARLAELPEL----- 349
|
250 260 270
....*....|....*....|....*....|....*...
gi 1207163335 951 levfQVQREALfnKSERQVAESQLETVKKQLTDLQAES 988
Cdd:COG3206 350 ----EAELRRL--EREVEVARELYESLLQRLEEARLAE 381
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
459-696 |
1.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 459 RRKVEELTSQNADLVL---KVQMLEMFEKDDTDMQSSGPDFVPTAQYESLRREFEELQEKYSRAQASTEASSIAEDPGCE 535
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 536 EKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDA--EEKPEKSSVEGGDLETHQLKA--RVQELEAELVSKKTDGE 611
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELK 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 612 GLSEDDNNTMQQLKERVKELEAALQDREKEGEEnetvvnlKKQVEELGKALELSKAAGKKEGEGAPLNGLQARVEELEQE 691
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-------KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
....*
gi 1207163335 692 LKESV 696
Cdd:PTZ00121 1796 VDKKI 1800
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
591-867 |
1.83e-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: 42.06 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 591 QLKARVQELEAELVSKKTDGEGLSEDDNNT---MQQLKERVKELEAALQDREKEgeenetVVNLKKQVEELGKALELSKA 667
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAE------LAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 668 AGKKEGEGAPLNGLQARVEELeqelkesVPRGQFEEVQVTLGLqLNQLAQERAEVAARLNQALLELERLRppshidedee 747
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 748 ddepsessevsiasdhslhmspggRTLEAIKEELEVARQEAAQALDSLCAERESRaqdvlqlrdavplvkhQESLSAVAQ 827
Cdd:COG4942 167 ------------------------AELEAERAELEALLAELEEERAALEALKAER----------------QKLLARLEK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1207163335 828 QLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSVSK 867
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
500-959 |
1.84e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 500 AQYESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQ------KALEKKLSQAQAELEELKEQMRLGVYSVEDA 573
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQelqkriRLLEKREAEAEEALREQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 574 EEKP-EKSSVEGGDLETHQ-LKARVQELEAELvsKKTDGEgLSEdDNNTMQQLKERVKELEAALQDREKEGEENETVVNL 651
Cdd:pfam05557 89 NKKLnEKESQLADAREVIScLKNELSELRRQI--QRAELE-LQS-TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 652 KKQVEELGKALE--LSKAAGKKEgEGAPLNGLQARVEELEQELKESVPR-GQFEEVQVTLGLqlnqLAQERAEVAARLNQ 728
Cdd:pfam05557 165 LAEAEQRIKELEfeIQSQEQDSE-IVKNSKSELARIPELEKELERLREHnKHLNENIENKLL----LKEEVEDLKRKLER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 729 --------ALLELERLRppshidedeedDEPSESSEVSIASDHSLHMspggRTLEAIKEELEVARQEAAqaldSLCAERE 800
Cdd:pfam05557 240 eekyreeaATLELEKEK-----------LEQELQSWVKLAQDTGLNL----RSPEDLSRRIEQLQQREI----VLKEENS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 801 SRAQDVLQLRDAVPLVkhQESLSAVAQQLAQTEKELQAERALREHAQTELSRL--EIELKAAQKDSVSKE----EHDKIK 874
Cdd:pfam05557 301 SLTSSARQLEKARREL--EQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLtkERDGYRAILESYDKEltmsNYSPQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 875 ADLERSLED------------SRQIAAAAQESLSEK------ETELKDLRSQKALEQGLVSKEDHEaqrlSLQAEINTLT 936
Cdd:pfam05557 379 LERIEEAEDmtqkmqahneemEAQLSVAEEELGGYKqqaqtlERELQALRQQESLADPSYSKEEVD----SLRRKLETLE 454
|
490 500
....*....|....*....|...
gi 1207163335 937 AQLADLARkhEKTCLEVFQVQRE 959
Cdd:pfam05557 455 LERQRLRE--QKNELEMELERRC 475
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
815-974 |
1.87e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 815 LVKHQES-LSAVAQQ---LAQTEKELQAERALREHaqtELSRLE------IELKAAQ---------------KDSVSKEE 869
Cdd:PRK05771 87 LIKDVEEeLEKIEKEikeLEEEISELENEIKELEQ---EIERLEpwgnfdLDLSLLLgfkyvsvfvgtvpedKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 870 HDKIKADLERSLEDSRQIAAA-AQESLSEKETELK--DLRSQKALEQGLVSK--EDHEAQRLSLQAEINTLTAQLADLAR 944
Cdd:PRK05771 164 SDVENVEYISTDKGYVYVVVVvLKELSDEVEEELKklGFERLELEEEGTPSEliREIKEELEEIEKERESLLEELKELAK 243
|
170 180 190
....*....|....*....|....*....|
gi 1207163335 945 KHEKTCLevfqVQREALFNKSERQVAESQL 974
Cdd:PRK05771 244 KYLEELL----ALYEYLEIELERAEALSKF 269
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
888-1099 |
1.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 888 AAAAQES---LSEKETELKDLRSQKALEQGLVskeDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQVQREALfnK 964
Cdd:COG4913 227 ADALVEHfddLERAHEALEDAREQIELLEPIR---ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL--R 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 965 SERQVAESQLETVKKQLTDLQAESTHIQQLH-----QDIQHSQGLIKEKDRKITELSKEVFRLKEALGALT--------- 1030
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaee 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 1031 -PPLGRSPSPPSSGIPGQQLALQNRVTSLTQQLQDWERKHKAVVSIYRShlLAAVQGRMDEEVQALLLQI 1099
Cdd:COG4913 382 fAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS--LERRKSNIPARLLALRDAL 449
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
44-250 |
2.01e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.13 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 44 VATLLVKKGLCPSKLDAEGKSAFHLCASRGRLDCLEVIL---SHGVDIGVTDGTGFNALHLAAKNG---QPDCLKRLLQE 117
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 118 RMPVDS-TDSFGRTSLHhaavsgCLscteilwdFKANLDAQDGDgstplilaaqmsrieLCAFLLERGANPNLQDNQGRS 196
Cdd:PHA02798 171 GVDINThNNKEKYDTLH------CY--------FKYNIDRIDAD---------------ILKLFVDNGFIINKENKSHKK 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207163335 197 ALMFSCES---DSM----ETVEMLLKgGTNPHLTDALGHNSTHYSITAGNHSITQLLQNLG 250
Cdd:PHA02798 222 KFMEYLNSllyDNKrfkkNILDFIFS-YIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLG 281
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
100-181 |
2.19e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 100 HLAAkNGQPDCLKRLLQERMPVDSTDSFGRTSLHHAAVSGCLSCTEILWDFKANLDAQDGDGSTPLILAAQMSRIELCAF 179
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
..
gi 1207163335 180 LL 181
Cdd:PTZ00322 167 LS 168
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
503-735 |
2.26e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 503 ESLRREFEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKALEKKLSQAQAELEELKEQMRLGVYSVEDAEE--KPEKS 580
Cdd:COG5185 285 NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEaiKEEIE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 581 SVEGgdlethqlKARVQELEAELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKEGEEN--ETVVNLKKQVEEL 658
Cdd:COG5185 365 NIVG--------EVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQieELQRQIEQATSSN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 659 GKALELSKAAGKKegegapLNGLQARVEELEQELKESVPRGQFEEVQVTLG---LQLNQLAQERAEVAARLNQALLELER 735
Cdd:COG5185 437 EEVSKLLNELISE------LNKVMREADEESQSRLEEAYDEINRSVRSKKEdlnEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
774-1025 |
2.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 774 LEAIKEELEVARQEAAQALDSLCAERESraqdvlqlrdavpLVKHQESLSAVAQQLAQTEKELQAERALREHAQTELSRL 853
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEE-------------LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 854 EIELKAAQKDsvsKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKALEQGLVSKEDHEAQRLSLQAEIN 933
Cdd:COG4372 107 QEEAEELQEE---LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 934 TLTAQLADLARKHEKTCLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHIQQLHQDIQHSQGLIKEKDRKIT 1013
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250
....*....|..
gi 1207163335 1014 ELSKEVFRLKEA 1025
Cdd:COG4372 264 ELAILVEKDTEE 275
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
73-198 |
3.17e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 41.40 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 73 GRLDCLEVILShgvDIGVTDG-TGFNALHLAA---KNGQPDCLKRLLQERMPVDS---------TDSF--GRTSLHHAAV 137
Cdd:cd21882 6 GLLECLRWYLT---DSAYQRGaTGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNpkelvnapcTDEFyqGQTALHIAIE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207163335 138 SGCLSCTEILWDFKANLDAQ-DGD------------GSTPLILAAQMSRIELCAFLLERGANP---NLQDNQGRSAL 198
Cdd:cd21882 83 NRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVL 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
544-737 |
3.30e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 544 ALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVEGGDLETH--QLKARVQELEAELVSKKTDGEGLSEDDNNTM 621
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 622 QQLKERVKELEAALQDREKEGEENETVVNLKKQ-VEELGKALELSKAAGKK-EGEGAPLNGLQARVEELEQELKESvpRG 699
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAELEAE--RA 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207163335 700 QFEEVQVTLGLQLNQLAQERAEVAARLNQALLELERLR 737
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
340-718 |
3.57e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 340 EEIRKLRLERGRL-LQKIKV------LEQQQSSATTALEELSSLKERLSEAEAERDRLLVE-------LEELRAAQVsgv 405
Cdd:pfam05622 173 EELKKANALRGQLeTYKRQVqelhgkLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIErdtlretNEELRCAQL--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 406 tcdsedaedsddmldfpgaekllsrQSRGLDANLPAEQGEGISQENPA---MVEQLRRKVEELTSQNADLVLKvqmlemf 482
Cdd:pfam05622 250 -------------------------QQAELSQADALLSPSSDPGDNLAaeiMPAEIREKLIRLQHENKMLRLG------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 483 ekddtdmqssgpdfvptaQYESLRREFEELQEKYSRAQASteassiaedpgCEEKEEKHQKALEkKLSQAQAELEELKEQ 562
Cdd:pfam05622 298 ------------------QEGSYRERLTELQQLLEDANRR-----------KNELETQNRLANQ-RILELQQQVEELQKA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 563 MrlgvysvEDAEEKPEKSSVEGGDLETHQLKARvqELEAELVSKKtdgEGLSEDDNNTMQQLKERVKELEAALQDREKEG 642
Cdd:pfam05622 348 L-------QEQGSKAEDSSLLKQKLEEHLEKLH--EAQSELQKKK---EQIEELEPKQDSNLAQKIDELQEALRKKDEDM 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 643 EENEtvVNLKKQVEelgKALELSKAAGKKEGEGAPL------NGLQ---ARVEELEQELKESVPRGQFEEVQVT-----L 708
Cdd:pfam05622 416 KAME--ERYKKYVE---KAKSVIKTLDPKQNPASPPeiqalkNQLLekdKKIEHLERDFEKSKLQREQEEKLIVtawynM 490
|
410
....*....|
gi 1207163335 709 GLQLNQLAQE 718
Cdd:pfam05622 491 GMALHRKAIE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
819-1068 |
3.61e-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: 41.70 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 819 QESLSAVAQQLAQTEKELQAERALREHAQT-------ELSRLEIELK------AAQKDSVSKEEHDKikADLERSLEDS- 884
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESERAARNKAEKqrrdlgeELEALKTELEdtldttAAQQELRSKREQEV--TELKKALEEEt 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 885 ----------RQIAAAAQESLSEKETELKdlRSQKALEQglvSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVF 954
Cdd:pfam01576 341 rsheaqlqemRQKHTQALEELTEQLEQAK--RNKANLEK---AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 955 QVQreALFNKSERQVAE---------SQLETVKKQLTDLQAESTHIQ----QLHQDIQHSQGLIKEKDRKITELSKEVFR 1021
Cdd:pfam01576 416 ELQ--ARLSESERQRAElaeklsklqSELESVSSLLNEAEGKNIKLSkdvsSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1207163335 1022 LKEALGALTPPLGRSPSPPSsgipgqqlALQNRVTSLTQQLQDWERK 1068
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKR--------NVERQLSTLQAQLSDMKKK 532
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
830-992 |
3.68e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 830 AQTEKELQAERALREHAQTELSRLEIELKAAQK----DSVSKEEHDKIKADLeRSLEDSRQIAAAAQESLSEKETELKDL 905
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQAleseLAISRQDYDGATAQL-RAAQAAVKAAQAQLAQAQIDLARRRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 906 rsqkaLEQGLVSKEDHEAQRLSLQAEINTLTAQLADLARKHEKTCLEVFQVQREAlfnKSERQVAESQLETVKKQLTDLQ 985
Cdd:pfam00529 133 -----APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEV---RSELSGAQLQIAEAEAELKLAK 204
|
....*..
gi 1207163335 986 AESTHIQ 992
Cdd:pfam00529 205 LDLERTE 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
442-1023 |
4.48e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 442 EQGEGISQENPAMVEQLRRKVEELTSQNADLVLKVQMlEMFEKDDTDMQSSGPDFV-------------PTAQYESLRRE 508
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE-EIQENKDLIKENNATRHLcnllketcarsaeKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 509 ------------------FEELQEKYSRAQASTEASSIAEDPGCEEKEEKHQKAL---EKKLSQAQAELEELKEQMRLGV 567
Cdd:pfam05483 181 trqvymdlnnniekmilaFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKENKMKDLT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 568 YSVEDAEEKPEKSSvEGGDLETHQLKarvqeleaELVSKKTDGEGLSEDDNNTMQQLKERVKELEAALQDREKE----GE 643
Cdd:pfam05483 261 FLLEESRDKANQLE-EKTKLQDENLK--------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTicqlTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 644 ENETvvnlkkQVEELGKAlelskaagkKEGEGAPLNGLQARVEELEQELKESVPRGQFEEVQVT-LGLQLNQLAQERAEV 722
Cdd:pfam05483 332 EKEA------QMEELNKA---------KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 723 AARLNQALLELERLRppshidedeeddepsesseVSIASDHSLHMSpgGRTLEAIKEELEVARQEaaqaLDSLCAERESR 802
Cdd:pfam05483 397 TKFKNNKEVELEELK-------------------KILAEDEKLLDE--KKQFEKIAEELKGKEQE----LIFLLQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 803 AQDvLQLRDAVPLVKHQESLSAVAQQLAQTEKELQAERALREHAQ----------TELSRLEIELKAAQKDSVS--KEEH 870
Cdd:pfam05483 452 IHD-LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllenkeltQEASDMTLELKKHQEDIINckKQEE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 871 DKIKA--DLERSLEDSRQIAAAAQESLSEKETELKDL--RSQKALEQGLVSKEDHEAQRLSLQAEINTLTAQLADLARKh 946
Cdd:pfam05483 531 RMLKQieNLEEKEMNLRDELESVREEFIQKGDEVKCKldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN- 609
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207163335 947 ektcLEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHiQQLHQDIQHSQGLIKEKDRKITELSKEVFRLK 1023
Cdd:pfam05483 610 ----IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
160-189 |
4.53e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.53e-03
10 20 30
....*....|....*....|....*....|
gi 1207163335 160 DGSTPLILAAQMSRIELCAFLLERGANPNL 189
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
820-935 |
4.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 820 ESLSAVAQQLAQTEKELQAERALREHAQTELSRLEIELKAAQKDSVSKEE-HDKIKADLERSLEDSRQIAAAAQESLSEk 898
Cdd:pfam02841 190 EAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERsYQEHVKQLIEKMEAEREQLLAEQERMLE- 268
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207163335 899 etelkdlrsQKALEQGLVSKEDHEAQRLSLQAEINTL 935
Cdd:pfam02841 269 ---------HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
774-1061 |
4.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 774 LEAIKEELEVARQEAAQALDSLCAERESRAQDVLQLRDAvpLVKHQESLSAVAQQLAQTEKELQAERALREhAQTELSRL 853
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--LQQTQQSHAYLTQKREAQEEQLKKQQLLKQ-LRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 854 EIELKAAqkdsvskeEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQKA-LEQGLVSKEDHEAQRLSLQAEI 932
Cdd:TIGR00618 273 RAQEAVL--------EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRsRAKLLMKRAAHVKQQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 933 NTLTaqladlarkhektclevfQVQREALFNKSERQVAESQLETVKKQLTDLQaestHIQQLHQDIQH----SQGLIKEK 1008
Cdd:TIGR00618 345 RLLQ------------------TLHSQEIHIRDAHEVATSIREISCQQHTLTQ----HIHTLQQQKTTltqkLQSLCKEL 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207163335 1009 DRKITELSKEVFRLKE--ALGALTPPLGRSPSPPSSGIPGQQLALQNRVTSLTQQ 1061
Cdd:TIGR00618 403 DILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
488-698 |
4.70e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 488 DMQSSGPDFVPTAQYESlrrEFEELQEKYSRAQastEASSIAEDPGCEEKEEKHQKALEKKLSQA------QAELEELKE 561
Cdd:PLN03229 420 NMKKREAVKTPVRELEG---EVEKLKEQILKAK---ESSSKPSELALNEMIEKLKKEIDLEYTEAviamglQERLENLRE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 562 QM-----------RLGVYSVEDAEEKPEKSSVEGGDLEThqLKARVQELEA-----ELVSKKTDGEGLSEDDNNTMQQ-- 623
Cdd:PLN03229 494 EFskansqdqlmhPVLMEKIEKLKDEFNKRLSRAPNYLS--LKYKLDMLNEfsrakALSEKKSKAEKLKAEINKKFKEvm 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 624 ----LKERVKELEAALQDRE--KEGEEN----ETVVNLKKQVE-ELGKALELS-------KAAGKKEGEGAPLNGLQARV 685
Cdd:PLN03229 572 drpeIKEKMEALKAEVASSGasSGDELDddlkEKVEKMKKEIElELAGVLKSMglevigvTKKNKDTAEQTPPPNLQEKI 651
|
250
....*....|...
gi 1207163335 686 EELEQELKESVPR 698
Cdd:PLN03229 652 ESLNEEINKKIER 664
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
782-996 |
5.76e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 782 EVARQEAAQALDSLCA-----EReSRAQDVlqlrdAVPLVKHQESLSAVAQQLAQTEKEL-QAERalREHAQTELSRLEI 855
Cdd:COG3096 468 DAARRQFEKAYELVCKiagevER-SQAWQT-----ARELLRRYRSQQALAQRLQQLRAQLaELEQ--RLRQQQNAERLLE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 856 EL-KAAQKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETELKDLRSQ-KALEQglvskedHEAQRLSLQAEIN 933
Cdd:COG3096 540 EFcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARiKELAA-------RAPAWLAAQDALE 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 934 TLTAQL-ADLARKHEKTCLEVFQVQREALFNKSERQVAEsqletvKKQLTDLQAEsthiqQLHQ 996
Cdd:COG3096 613 RLREQSgEALADSQEVTAAMQQLLEREREATVERDELAA------RKQALESQIE-----RLSQ 665
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
916-1026 |
6.10e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 916 VSKEDHEAQRLSLQAEINTLTAQLADLARkhektclEVFQVQREALFNKSERQVAESQLETVKKQLTDLQAESTHIQQLH 995
Cdd:PRK11448 135 VPPEDPENLLHALQQEVLTLKQQLELQAR-------EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKA 207
|
90 100 110
....*....|....*....|....*....|.
gi 1207163335 996 QDIQHSQgliKEKDRKITELSKEVFRLKEAL 1026
Cdd:PRK11448 208 AETSQER---KQKRKEITDQAAKRLELSEEE 235
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
95-117 |
6.14e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 6.14e-03
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
542-904 |
6.74e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 542 QKALEKKLSQAQAELEELKEQMRLGVYSVEDAEEKPEKSSVeggdlETHQLKARVQELEAELVSKKtdgeglSEDDNNTM 621
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD-----EKQSEKDKKNKALAERKDSA------NERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 622 QQLKERVKELEAALQDREKEGEENETVVNLKKQV--EELGKALELSKAAGKKEGEGAplnglQARVEELEQELKESVP-R 698
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVveGALDAQLALLKAAIAARRSGA-----KAELKALETWYKRDLAsL 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 699 GQFEEVQVTLGLQLNQLAQeRAEVAARLNQALLELERLRPPSHIDEDEEDDEPSESSEvsiasdhslhmspggRTLEAIK 778
Cdd:pfam12128 764 GVDPDVIAKLKREIRTLER-KIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIE---------------RAISELQ 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 779 EELevARQEAAQALDSLCAERESRAQDVLQLRDAVPLVKHQESLSAVAQqlaqtekelqaeraLREHAQTELSRLEIELK 858
Cdd:pfam12128 828 QQL--ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT--------------LKEDANSEQAQGSIGER 891
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1207163335 859 AAQKDSVsKEEHDKIKADLERSLEDSRQIAAAAQ--------ESLSEKETELKD 904
Cdd:pfam12128 892 LAQLEDL-KLKRDYLSESVKKYVEHFKNVIADHSgsglaetwESLREEDHYQND 944
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
456-737 |
7.14e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 456 EQLRRKVEELTSqnadlvlKVQMLEMFEKDDTDMQSSgpdfvptaqyeslrrefeeLQEKYSRAQAS-TEASSIAEDPGC 534
Cdd:pfam15921 475 EMLRKVVEELTA-------KKMTLESSERTVSDLTAS-------------------LQEKERAIEATnAEITKLRSRVDL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 535 EEKEEKHQKALEKKLSQAQAELEELKEQM--------------------------RLGVYSVEDAEEKPE---------- 578
Cdd:pfam15921 529 KLQELQHLKNEGDHLRNVQTECEALKLQMaekdkvieilrqqienmtqlvgqhgrTAGAMQVEKAQLEKEindrrlelqe 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 579 -KSSVEGGDLETHQLKARVQELEAELVSKKTDG-------EGLSEDDNNTMQQLKERVKELEAALQDRE-------KEGE 643
Cdd:pfam15921 609 fKILKDKKDAKIRELEARVSDLELEKVKLVNAGserlravKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkrnfrNKSE 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 644 ENETVVN-LKKQVEELGKALELSKAAgKKEGEGA--------------------PLNGLQARVEELEQELKESVPRGQFe 702
Cdd:pfam15921 689 EMETTTNkLKMQLKSAQSELEQTRNT-LKSMEGSdghamkvamgmqkqitakrgQIDALQSKIQFLEEAMTNANKEKHF- 766
|
330 340 350
....*....|....*....|....*....|....*
gi 1207163335 703 evqvtLGLQLNQLAQERAEVAARLNQALLELERLR 737
Cdd:pfam15921 767 -----LKEEKNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
456-902 |
7.29e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 456 EQLRRKVEELTSQNADLvlkvqmlemfekdDTDMQSSGP--DFVPTA--QYESLRREFEELQEKYSRAQASTEASSIAEd 531
Cdd:PRK04863 310 VEMARELAELNEAESDL-------------EQDYQAASDhlNLVQTAlrQQEKIERYQADLEELEERLEEQNEVVEEAD- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 532 pgcEEKEEkhqkaLEKKLSQAQAELEELKEQM------------RLGVY--SVEDAEEKpeKSSVEGGDLETHQLKARVQ 597
Cdd:PRK04863 376 ---EQQEE-----NEARAEAAEEEVDELKSQLadyqqaldvqqtRAIQYqqAVQALERA--KQLCGLPDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 598 ELEAELvskktdgeglseddnntmQQLKERVKELEAALQDREKEGEENETVVNLkkqVEELGKALELSKA---AGKKEGE 674
Cdd:PRK04863 446 EFQAKE------------------QEATEELLSLEQKLSVAQAAHSQFEQAYQL---VRKIAGEVSRSEAwdvARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 675 GAPLNGLQARVEELEQELKEsvprgqfeevqvtlglqLNQLAQERAEVAARLNQALLELerlrppshidedeeddepses 754
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSE-----------------LEQRLRQQQRAERLLAEFCKRL--------------------- 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 755 sevsiasdhslhmspgGRTLEAIkEELEVARQEAAQALDSLCAERESRAQDVLQLRDavplvkHQESLSAVAQQLAQTEK 834
Cdd:PRK04863 547 ----------------GKNLDDE-DELEQLQEELEARLESLSESVSEARERRMALRQ------QLEQLQARIQRLAARAP 603
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207163335 835 ELQAeralrehAQTELSRLEIELKAAQKDSVSKEEHDKIKADLERSLEDSRQIAAAAQESLSEKETEL 902
Cdd:PRK04863 604 AWLA-------AQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
331-610 |
7.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 331 NLTEDEEVFEEIRKLRLERGRLLQKIKVLEQQQSSATTALEELSSLKERLSEAEAERDRLLVELEELraaqvsGVTCDSE 410
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL------GFESVEE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 411 DAEDSDDMldfpgaEKLLSRQSRGLDAnlpaeqgegiSQENPAMVEQLRRKVEELTSQNADLVLKVQMLEMFEKDDTDMQ 490
Cdd:PRK03918 590 LEERLKEL------EPFYNEYLELKDA----------EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 491 SSGPDfvptAQYESLRREFEELQEKYSRAQASTEassiaedpGCEEKEEKHQKALEkKLSQAQAELEELKEQMRLGVYSV 570
Cdd:PRK03918 654 KKYSE----EEYEELREEYLELSRELAGLRAELE--------ELEKRREEIKKTLE-KLKEELEEREKAKKELEKLEKAL 720
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1207163335 571 EDAEEKPEKSSVEGGDLETHQLKaRVQELEAELVSKKTDG 610
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERALS-KVGEIASEIFEELTEG 759
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
575-920 |
7.57e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.22 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 575 EKPEKSSVEGGDLETHQLKARVQELEAELVSKKTDGEGLSEddnnTMQQLKERVkeleaalqdrEKEGEENETVVNLKKQ 654
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNE----MIEKLKKEI----------DLEYTEAVIAMGLQER 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 655 VEELgkALELSKAAGKKEgegaPLN-GLQARVEELEQELKESVPR-GQFEEVQVTLGLqLNQLAqeRAEVAARLNQALLE 732
Cdd:PLN03229 488 LENL--REEFSKANSQDQ----LMHpVLMEKIEKLKDEFNKRLSRaPNYLSLKYKLDM-LNEFS--RAKALSEKKSKAEK 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 733 LeRLRPPSHIDEDEEDDEPSESSEVSIASDHSLHMSPGGRTLEAIKEELEVARQEA----AQALDSLCAERESRAQDVLQ 808
Cdd:PLN03229 559 L-KAEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIelelAGVLKSMGLEVIGVTKKNKD 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207163335 809 LRDAVPLVKHQESLSAVAQQLAQtekelQAERALRE---HAQTELSRLEIELKAAQKDSVSKEEHDKIKADLERSLEDSR 885
Cdd:PLN03229 638 TAEQTPPPNLQEKIESLNEEINK-----KIERVIRSsdlKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL 712
|
330 340 350
....*....|....*....|....*....|....*
gi 1207163335 886 QiAAAAQESLSEKETELKDLRSQKALEQGLVSKED 920
Cdd:PLN03229 713 N-SSELKEKFEELEAELAAARETAAESNGSLKNDD 746
|
|
| |
