|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1112-1632 |
1.33e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1112 IRAEQQTALQRLREEAETLQKAERASLEQKSRRA------LEQLREQL-----EAEERSAQAALRAEKEAEKEATLLQLR 1180
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAellllkLRELEAELeeleaELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1181 EQLE--GERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEgaQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1258
Cdd:COG1196 274 LELEelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1259 ELSSLLRDKRQEVEREHErkmDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELEsvRQEQDQQL 1338
Cdd:COG1196 352 ELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--LEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1339 EDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEH--- 1415
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegf 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1416 ------THLLESKQQLRRAIDDLRVRRVELESQ---------VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1480
Cdd:COG1196 507 legvkaALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1481 PPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVR-------QTRSMRRRQT 1553
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVtlegeggSAGGSLTGGS 666
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1554 ALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDED 1632
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1119-1473 |
2.87e-18 |
|
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: 92.04 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1119 ALQRLREEAETLQKAERA---------SLEQKSRRAlEQLREqLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERRE 1189
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIlnelerqlkSLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1190 avaglEKKHSTELEQLCSSLEAkHREVISNLQKKIEGAQQKeeaqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRD-KR 1268
Cdd:TIGR02168 255 -----LEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE--------LYALANEISRLEQQKQILRERLANLERQlEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1269 QEVEREH-ERKMDKMKEEhwqemaeareryEAEERKQRADLLGHLTGELERLRRAHE--RELESVRQEQDQQLEDLRRRH 1345
Cdd:TIGR02168 321 LEAQLEElESKLDELAEE------------LAELEEKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1346 RDQERKLQDLEAELSSrtkdVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK--EEATATRRHLEEAKKEHTHLLESKQ 1423
Cdd:TIGR02168 389 AQLELQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1424 QLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1473
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1092-1628 |
3.58e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.54 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERA-SLEQKSRRALEQLREQLEAEERS--AQAALRAEK 1168
Cdd:COG1196 260 AELAELEAELEELRLELE-ELELELEEAQAEEYELLAELARLEQDiARLEERRRELEERLEELEEELAEleEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1169 EAEKEATLLQLREQLEG--ERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEgaQQKEEAQLQESLGRAEQRT 1246
Cdd:COG1196 339 LEELEEELEEAEEELEEaeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE--LAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1247 HQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERE 1326
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1327 LESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARL---AQLNVQEENMRKEKqlllDAQRQAALEKEEAtA 1403
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaaLAAALQNIVVEDDE----VAAAAIEYLKAAK-A 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1404 TRRHLEEAKKEHTHLLESKQQLRRAIDDlrvRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAaetnapph 1483
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGA---AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV-------- 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1484 pepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWR 1563
Cdd:COG1196 641 ---TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1564 HELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL--LEEV 1628
Cdd:COG1196 718 EEELEEEALEEQL--EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIeaLGPV 782
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1112-1648 |
4.57e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.74 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1112 IRAEQQTALQRLREeAETLQKAERASLEQKSRRAlEQLREQLEaEERSAQAALRAEKEAEKEATLLQLREQLEGERREAV 1191
Cdd:PTZ00121 1272 IKAEEARKADELKK-AEEKKKADEAKKAEEKKKA-DEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1192 AGLEKKHSTELEQLCSSLEAKHREViSNLQKKIEGAQQK-EEAQLQESLGRAEQRTHQKVHQVIEYEQElssllRDKRQE 1270
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKK-EEAKKKADAAKKKaEEKKKADEAKKKAEEDKKKADELKKAAAA-----KKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1271 VER--EHERKMDKMKEEHwQEMAEARERYEAEERKQRADllgHLTGELERLRRAHERELESvrqEQDQQLEDLRRRHRDQ 1348
Cdd:PTZ00121 1423 AKKkaEEKKKADEAKKKA-EEAKKADEAKKKAEEAKKAE---EAKKKAEEAKKADEAKKKA---EEAKKADEAKKKAEEA 1495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1349 ERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKqqlRRA 1428
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA---KKA 1572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1429 IDD--LRVRRVELESQVDQLQTQS-QRLQKHVSSLEAEVQRKQNILKEMAAETNAPphpepglhiEDLRK---SLGTNEN 1502
Cdd:PTZ00121 1573 EEDknMALRKAEEAKKAEEARIEEvMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---------EEEKKkveQLKKKEA 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1503 QEVSSSLSLSKEGIDLSMDSVRHFLSAE-----GVAVRSAKEFLVRQTRSMRRRQTALKAAQQ---HWRHELASAQEV-- 1572
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkKEAEEKKKAEELkk 1723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1573 DEDLPGTKVlENVRKNLDEETKHLDEMK-------SAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKVTFD 1645
Cdd:PTZ00121 1724 AEEENKIKA-EEAKKEAEEDKKKAEEAKkdeeekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
...
gi 1958798733 1646 LSD 1648
Cdd:PTZ00121 1803 IFD 1805
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1098-1627 |
5.16e-18 |
|
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: 91.18 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1098 RAQVQSSTEAFENQIRAEQQTALQRLREEAEtlqkaeraSLEQKSRRalEQLREQLEAEERSAQAalraekeaeKEATLL 1177
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKRE--------AQEEQLKK--QQLLKQLRARIEELRA---------QEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1178 QLREQLEGERREAVAGLEKKHSTELEQ----LCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQkvHQV 1253
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQqaqrIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI--HIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1254 IEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQ---------RADLLGHL----TGELERLR 1320
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQatidtrtsaFRDLQGQLahakKQQELQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1321 RAHERELESVRQEQDQQLE-----DLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMR--KEKQLLLDAQRQ 1393
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEkihlqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCplCGSCIHPNPARQ 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1394 AALEKEeatATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1473
Cdd:TIGR00618 519 DIDNPG---PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1474 MAAETNAPPHPE---------------PGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHflsaegvAVRSAK 1538
Cdd:TIGR00618 596 LQDLTEKLSEAEdmlaceqhallrklqPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE-------HALSIR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1539 EFlvrQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDeetKHLDEMKSAMRKGHDLLKKKEEKLN 1618
Cdd:TIGR00618 669 VL---PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD---REFNEIENASSSLGSDLAAREDALN 742
|
....*....
gi 1958798733 1619 QLESSLLEE 1627
Cdd:TIGR00618 743 QSLKELMHQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1111-1480 |
3.57e-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: 88.19 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1111 QIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERsaqaaLRAEKEAEKEATLLQLrEQLEGERREA 1190
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEE-----ELEELTAELQELEEKL-EELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1191 vaglekkhSTELEQLCSSLEAKHREvISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSlLRDKRQE 1270
Cdd:TIGR02168 280 --------EEEIEELQKELYALANE-ISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAE-LEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1271 VEREHERKMDKMKEEhwqemaeareryeaeerkqradllghltgelerlrRAHERELESVRQEQDQQLEDLRRRHRDQER 1350
Cdd:TIGR02168 349 LKEELESLEAELEEL-----------------------------------EAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1351 KLQDLEAELSSrtkdVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKeeataTRRHLEEAKKEHTHLLESKQQLRRAID 1430
Cdd:TIGR02168 394 QIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKE-----LQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1431 DLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1480
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1109-1641 |
9.01e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLREeAETLQKAERASLEQKSRRAlEQLREQLEA----EERSAQAALRAE---------KEAEKEAT 1175
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRK-AEELRKAEDARKAEAARKA-EEERKAEEArkaeDAKKAEAVKKAEeakkdaeeaKKAEEERN 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1176 LLQLREQLEGE------RREAVAGLEKKHSTEL---EQLCSSLEAKHREVIsnlqKKIEGAQQK-EEAQLQESLGRAEQR 1245
Cdd:PTZ00121 1251 NEEIRKFEEARmahfarRQAAIKAEEARKADELkkaEEKKKADEAKKAEEK----KKADEAKKKaEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1246 THQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgelERLRRAHer 1325
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA----------EEKKKAD-- 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1326 ELESVRQEQDQQLEDLRRrhRDQERKLQDleaELSSRTKDVKaRLAQLNVQEENMRKEKQLlldaqRQAALEKEEATATR 1405
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKK--AAAAKKKAD---EAKKKAEEKK-KADEAKKKAEEAKKADEA-----KKKAEEAKKAEEAK 1463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1406 RHLEEAKKEHThlLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILK--EMAAETNAPPH 1483
Cdd:PTZ00121 1464 KKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKkaEEAKKADEAKK 1541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1484 PEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRhflsAEgvAVRSAKEFLVRQTRSMRRRQTALKAAQ-QHW 1562
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK----AE--EAKKAEEARIEEVMKLYEEEKKMKAEEaKKA 1615
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1563 RHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMksamrkghdllkKKEEKLNQLESSLLEEVSDEDTLKGSSIKK 1641
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL------------KKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1091-1464 |
1.46e-16 |
|
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: 86.26 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVqsstEAFENQIRaEQQTALQRLREEAETLQKAerasleqksrraLEQLREQLEAEER-SAQAALRAEKE 1169
Cdd:TIGR02168 676 RREIEELEEKI----EELEEKIA-ELEKALAELRKELEELEEE------------LEQLRKELEELSRqISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1170 AEKEATLLQLREQLEGERREAVAGLEKKHStELEQLCSSLEAkHREVISNLQKKIEgaQQKEEAQLQESLGRAEQ----R 1245
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAE-AEAEIEELEAQIE--QLKEELKALREALDELRaeltL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1246 THQKVHQVIEYEQELSSLLRDKRQEVEREHERKmdKMKEEHWQEMAEARERYEAEERKQRADLLGHLtgeleRLRRAHER 1325
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1326 ELESVRQEqdqqLEDLRRRHRDQERKLQDLEAELSSRTK---DVKARLAQLNVQEEN----MRKEKQLLLD-AQRQAALE 1397
Cdd:TIGR02168 888 ALALLRSE----LEELSEELRELESKRSELRRELEELREklaQLELRLEGLEVRIDNlqerLSEEYSLTLEeAEALENKI 963
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1398 KEEATATRRHLEEAKKEHTHL----LESKQQLRraidDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEV 1464
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELgpvnLAAIEEYE----ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1115-1485 |
2.58e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.35 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQkAERASLEQKsRRALEQLREQLEAEERSAQAALRAEKEAEKEAtLLQLREQLEGERREAvagl 1194
Cdd:COG4913 285 FAQRRLELLEAELEELR-AELARLEAE-LERLEARLDALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEER---- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1195 eKKHSTELEQLCSSLEAK---HREVISNLQKKIEGAQQK---EEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR--- 1265
Cdd:COG4913 358 -ERRRARLEALLAALGLPlpaSAEEFAALRAEAAALLEAleeELEALEEALAEAEAALRDLRRELRELEAEIASLERrks 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1266 --DKRQ-------------------------EVEREHE----------------------------RKMDKMKEEH---W 1287
Cdd:COG4913 437 niPARLlalrdalaealgldeaelpfvgeliEVRPEEErwrgaiervlggfaltllvppehyaaalRWVNRLHLRGrlvY 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1288 QEMAEARERYEAEERKQRA-----------------DLLGHL--------TGELERLRRA--------HERELesvRQEQ 1334
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSlagkldfkphpfrawleAELGRRfdyvcvdsPEELRRHPRAitragqvkGNGTR---HEKD 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1335 DQQleDLRRRH---RDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEeATATRRHL 1408
Cdd:COG4913 594 DRR--RIRSRYvlgFDNRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1409 EEAKKEHTHLLESK---QQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1485
Cdd:COG4913 671 AELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1079-1523 |
5.01e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1079 EKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaEER 1158
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE-EAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1159 SAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQlcsSLEAKHREVIsnlqKKIEGAQQKEEAQLQES 1238
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---AEEAKKADEA----KKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1239 LGRAEQRthQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELER 1318
Cdd:PTZ00121 1557 LKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1319 LRRAHERELESVRQ-EQDQQLEDLRRRHRDQERKLQDLEA----ELSSRTKDVKARLAQLNVQEENMRKEKQLlldaQRQ 1393
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKaEELKKAEEENKIKAAEEAKKAEEDKkkaeEAKKAEEDEKKAAEALKKEAEEAKKAEEL----KKK 1710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1394 AALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVElESQVDQLQTQSQRlqkhvsSLEAEVQRKQNILKE 1473
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEK------KAEEIRKEKEAVIEE 1783
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1474 MAAETNAPPHPEPGLHIEDLRKSL-----GTNENQEVsssLSLSKEGIDLSMDSV 1523
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFaniieGGKEGNLV---INDSKEMEDSAIKEV 1835
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1087-1432 |
5.34e-16 |
|
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: 84.34 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1087 REEESQRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASlEQKSRRALEQLREQLEAEERSAQAALRA 1166
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1167 EKEAEKEATLLQLREQLEGErreaVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQ--QKEEAQLQESLGRAEQ 1244
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQ----IEQLKEELKALREAL-DELRAELTLLNEEAANLRERLEslERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1245 RTHQKVHQVIEYEQELSSlLRDKRQEVEREHERKmDKMKEEHWQEMAEARERYEAEERKQRADL--LGHLTGELERLRR- 1321
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEE-LEELIEELESELEAL-LNERASLEEALALLRSELEELSEELRELEskRSELRRELEELREk 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1322 --AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqeENMRKEkqllLDAQRQAALEKE 1399
Cdd:TIGR02168 924 laQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL----ENKIKE----LGPVNLAAIEEY 995
|
330 340 350
....*....|....*....|....*....|...
gi 1958798733 1400 EATATRRhlEEAKKEHTHLLESKQQLRRAIDDL 1432
Cdd:TIGR02168 996 EELKERY--DFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1316-1635 |
7.11e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1316 LERLRRAHER--ELESVRQEQDQQLEDLRR------RHRDQERKLQDLEAELSS-RTKDVKARLAQLNVQEENMRKEKQL 1386
Cdd:COG1196 178 ERKLEATEENleRLEDILGELERQLEPLERqaekaeRYRELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1387 LLDAQRQAALEKEEATAT----RRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1462
Cdd:COG1196 258 LEAELAELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1463 EVQRKQNILKEMAAEtnapphpepglhIEDLRKSLgTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLV 1542
Cdd:COG1196 338 ELEELEEELEEAEEE------------LEEAEAEL-AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1543 RQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLES 1622
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330
....*....|...
gi 1958798733 1623 SLLEEVSDEDTLK 1635
Cdd:COG1196 485 ELAEAAARLLLLL 497
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1102-1626 |
3.92e-15 |
|
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: 81.55 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1102 QSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRA---LEQLREQLEAEERSAQAALRAEKEAEKEATLLQ 1178
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGkaeLLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1179 LREQLEgERREAVAGLEKKHstELEQLCSSLEAKHREVISNLQKKieGAQQKEEAQLQESLGRAEQRTHQKVHQ--VIEY 1256
Cdd:TIGR00618 231 LREALQ-QTQQSHAYLTQKR--EAQEEQLKKQQLLKQLRARIEEL--RAQEAVLEETQERINRARKAAPLAAHIkaVTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1257 EQelssllrdKRQEVEREHERKMDKMKEEHwqeMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELeSVRQEQDQ 1336
Cdd:TIGR00618 306 EQ--------QAQRIHTELQSKMRSRAKLL---MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT-SIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1337 QLEDLRRRHRDQERK--LQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEE---- 1410
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKttLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqc 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1411 AKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHI 1490
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1491 EDLRKSLGTnenqevssslslskegidlSMDSVRHFLSAEGVAVRSAKEflvrqtRSMRRRQTALKAAQQHwrhelasaQ 1570
Cdd:TIGR00618 534 EQTYAQLET-------------------SEEDVYHQLTSERKQRASLKE------QMQEIQQSFSILTQCD--------N 580
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1571 EVDEDLPG-TKVLENVRKNLDEETKHLDEMKSAMrkgHDLLKKKEEKLNQLESSLLE 1626
Cdd:TIGR00618 581 RSKEDIPNlQNITVRLQDLTEKLSEAEDMLACEQ---HALLRKLQPEQDLQDVRLHL 634
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1070-1469 |
4.01e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1070 QLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQL 1149
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1150 REQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGErrEAVAGLEKKHSTELEQlcsSLEAKHREVIsnlqKKIEGAQQ 1229
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD--EAKKAEEAKKADEAKK---AEEKKKADEL----KKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1230 KEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLL 1309
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1310 GHLTGEL---ERLRRAHER------ELESVRQEQDQQLEDLRRRHRDQERKLQDL--EAELSSRTKDVKARLAQLNVQEE 1378
Cdd:PTZ00121 1640 KKEAEEKkkaEELKKAEEEnkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKEAEEKKKAE 1719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1379 NMRKEKQL----LLDAQRQAALEKEEATATRRHLEEAKK-EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRL 1453
Cdd:PTZ00121 1720 ELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
410
....*....|....*.
gi 1958798733 1454 QKHVSSLEAEVQRKQN 1469
Cdd:PTZ00121 1800 IKDIFDNFANIIEGGK 1815
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1124-1480 |
4.37e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.94 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1124 REEAETLQKAERASLEQKSRRALEQL--REQLEAEERSAQAALraekeaEKEATLLQLREQLEGERREavaglekkhstE 1201
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEM------DRQAAIYAEQERMAMERER-----------E 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1202 LEQLcsSLEAKHREVISNLQKKIegAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQEVEREHERKMDK 1281
Cdd:pfam17380 350 LERI--RQEERKRELERIRQEEI--AMEISRMRELERLQMERQQKNERVRQELEAARKVK-ILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1282 MKEEhwQEmaeareryeaeERKQRadllghltgELERLRRAHERELESVRQEQ---DQQLEDLRRRHRDQERKLQDLEAE 1358
Cdd:pfam17380 425 IRAE--QE-----------EARQR---------EVRRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1359 lssrtkdvkarlaqlnvqeenmrKEKQLLLDAQRQAALEKEEATATRRHLEEAKK--------EHTHLLESKQQLRRAID 1430
Cdd:pfam17380 483 -----------------------KRDRKRAEEQRRKILEKELEERKQAMIEEERKrkllekemEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1431 DLRVRRVELESQvDQLQTQSQRLQKHVSSLEAeVQRKQNILKEMAAETNA 1480
Cdd:pfam17380 540 EERRKQQEMEER-RRIQEQMRKATEERSRLEA-MEREREMMRQIVESEKA 587
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1099-1444 |
1.87e-14 |
|
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: 79.34 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1099 AQVQSSTEAFENQIRaEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREqLEAEERSAQAALRAEKEAEKEatLLQ 1178
Cdd:TIGR02169 180 EEVEENIERLDLIID-EKRQQLERLRREREKAERYQALLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEE--LEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1179 LREQLEgERREAVAGLEKKhsteLEQLCSSLEAKHREVISNLQKKIeGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1258
Cdd:TIGR02169 256 LTEEIS-ELEKRLEEIEQL----LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1259 ELSSLLRDKRqEVEREHERKmdKMKEEHWQEMAEARERYEAEERKQRADL---LGHLTGELERLRRAHE---RELESVRQ 1332
Cdd:TIGR02169 330 EIDKLLAEIE-ELEREIEEE--RKRRDKLTEEYAELKEELEDLRAELEEVdkeFAETRDELKDYREKLEklkREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1333 EQDQQLEDLRRRHRDQER---KLQDLEA---ELSSRTKDVKARLAQlnvQEENMRKEKQLLLDAQRQAALEKEEATATRR 1406
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADlnaAIAGIEAkinELEEEKEDKALEIKK---QEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958798733 1407 HLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1444
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1100-1478 |
4.02e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1100 QVQSSTEAFENQIRAEQQTAL------QRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAEE-------------- 1157
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADdleeraEELREEAAELESELEEAREAveDRREEIEELEEEIEELRerfgdapvdlgnae 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1158 ------RSAQAALRaEKEAEKEATLLQLREQLE---------------------------GERREAVAGLEkkhsTELEQ 1204
Cdd:PRK02224 412 dfleelREERDELR-EREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELE----AELED 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1205 LcssleakhREVISNLQKKIEGAQQKEEAQ-----LQESLGRAEQRTHQKvHQVIEYEQELSSLLRDKRQEVEREHERKM 1279
Cdd:PRK02224 487 L--------EEEVEEVEERLERAEDLVEAEdrierLEERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKR 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1280 DKMKEEHwqEMAEARERYEAEERKQRADLlghlTGELERLRRAheRELESVRQEQDQQLEDLRRRHRD-QERKLQDLE-- 1356
Cdd:PRK02224 558 EAAAEAE--EEAEEAREEVAELNSKLAEL----KERIESLERI--RTLLAAIADAEDEIERLREKREAlAELNDERRErl 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1357 AELSSRTKDVKARLAQLNVQEenMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESkqqlrraIDDLRVRR 1436
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-------LEELRERR 700
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958798733 1437 VELESQVDQLQT---QSQRLQKHVSSLEAEVqRKQNI--LKEMAAET 1478
Cdd:PRK02224 701 EALENRVEALEAlydEAEELESMYGDLRAEL-RQRNVetLERMLNET 746
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1097-1460 |
4.42e-14 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 78.46 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAfenqiRAEQQTALQRLREEAETLqKAERASLEQksrrALEQLREQLEaeerSAQAALR-AEKEAEKEAT 1175
Cdd:PRK04863 291 LRRELYTSRRQ-----LAAEQYRLVEMARELAEL-NEAESDLEQ----DYQAASDHLN----LVQTALRqQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1176 LLQLREQLEgERREAVAGL--------EKKHSTELEQLCSsleakhREVISNLQKKIEgAQQKEEAQLQES---LGRAEQ 1244
Cdd:PRK04863 357 LEELEERLE-EQNEVVEEAdeqqeeneARAEAAEEEVDEL------KSQLADYQQALD-VQQTRAIQYQQAvqaLERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1245 RTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELER 1318
Cdd:PRK04863 429 LCGLpdlTADNAEDWLEEF----QAKEQEATeelLSLEQKLSVAQAAHSQ-------------FEQAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1319 ----------LRRAHERELESVRQEQ-DQQLEDLRRRHRDQER--------------------KLQDLEAELSSRTKDVK 1367
Cdd:PRK04863 492 seawdvarelLRRLREQRHLAEQLQQlRMRLSELEQRLRQQQRaerllaefckrlgknlddedELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1368 ARLAQLNVQEENMR-KEKQLLLDAQRQAALEKE--EATATRRHLEEAKKEHthlLESKQQLRRAIDDLRVRRVELESQVD 1444
Cdd:PRK04863 572 ESVSEARERRMALRqQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEE---FEDSQDVTEYMQQLLERERELTVERD 648
|
410
....*....|....*.
gi 1958798733 1445 QLQTQSQRLQKHVSSL 1460
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1134-1627 |
4.93e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1134 ERAS--------LEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEATllQLREQLEGERREAVAGLEK------KH 1198
Cdd:PRK02224 169 ERASdarlgverVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELD--EEIERYEEQREQARETRDEadevleEH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1199 STELEQLcSSLEAKhrevISNLQKKIEGAQQKEEAQLQESLGRAEQRthqkvhqvieyeQELSSLLRDKRQEVERehERK 1278
Cdd:PRK02224 247 EERREEL-ETLEAE----IEDLRETIAETEREREELAEEVRDLRERL------------EELEEERDDLLAEAGL--DDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1279 MDKMKEEHWQEMAEARERYEAEERKQRADlLGHLTGELERLR----RAHER--ELESVRQEQDQQLEDLRRRHRDQERKL 1352
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVA-AQAHNEEAESLRedadDLEERaeELREEAAELESELEEAREAVEDRREEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1353 QDLEAELssrtKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLES------KQQLR 1426
Cdd:PRK02224 387 EELEEEI----EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1427 -----RAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLE--AEVQRKQNILKEMAAETNApphpepglHIEDLRKslGT 1499
Cdd:PRK02224 463 gsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLEERREDLEE--------LIAERRE--TI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1500 NENQEVSSSLSLSKEGIDLSMDSVRhflsAEGVAVRSAKEFLVRQTRSMRRRQTALKAaqqhwrhELASAQEVDEDLPGT 1579
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKR----EAAAEAEEEAEEAREEVAELNSKLAELKE-------RIESLERIRTLLAAI 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1958798733 1580 KVLENVRKNLDEETKHLDEMKSAMRkghDLLKKKEEKLNQLESSLLEE 1627
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNDERR---ERLAEKRERKRELEAEFDEA 646
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1181-1694 |
7.04e-14 |
|
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: 77.47 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1181 EQLEGERREAVAGLEKKHSTELEQLCSsleaKHREVISNLQKKIEGAQQKE---EAQLQESLGRAEQRTHQKVHQVIEYE 1257
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLIS----EHEVEITGLTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1258 QELSSLlRDKRQEVEREHERKMDKMKEEhwQEMAEARERYEAEERKQRADLLGHLTGELERL-RRAHERELE-SVRQEQD 1335
Cdd:pfam15921 324 STVSQL-RSELREAKRMYEDKIEELEKQ--LVLANSELTEARTERDQFSQESGNLDDQLQKLlADLHKREKElSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1336 QQLED-----------LRRRHRDQERKLQDLEAELSSRTKDVKARLAQ--LNVQEENMRKEKQLLLDAQRQAALEK---- 1398
Cdd:pfam15921 401 KRLWDrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1399 -EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaEVQRKQNILKEMAAE 1477
Cdd:pfam15921 481 vEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1478 TNAPphpepglhIEDLRKSLG-----TNENQEVSSSLSLSKEGIDLSMDSVRHFLSaEGVAVRSAKEFLVRQTRSM---- 1548
Cdd:pfam15921 560 KDKV--------IEILRQQIEnmtqlVGQHGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIRELEARvsdl 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1549 -RRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHL--------DEMKSAMRKGHDLLKKKEEKLNQ 1619
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrnksEEMETTTNKLKMQLKSAQSELEQ 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1620 LESSLLE-EVSDEDTLKGS--SIKKVTFDLSDMDDLSSEsfescpLLHITPTPNSADPNKiHYLSSSLQRISSELNGV 1694
Cdd:pfam15921 711 TRNTLKSmEGSDGHAMKVAmgMQKQITAKRGQIDALQSK------IQFLEEAMTNANKEK-HFLKEEKNKLSQELSTV 781
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1215-1627 |
7.35e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.41 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1215 EVISNLQKKIEGAQQ--KEEAQLQESLGRAEQRTHQKVHQVieyeQELSSLLRDKRQEVE--REHERKMDKMKEEhwqem 1290
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEklEKEVKELEELKEE----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1291 aeareryEAEERKQRADLLGHLTGELERLR---------RAHERELESVRQEQDQ---------QLEDLRRRHRDQERKL 1352
Cdd:PRK03918 240 -------IEELEKELESLEGSKRKLEEKIReleerieelKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1353 QDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR------------------QAALEKEEATATRRHLEEAKKE 1414
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerhelyeeakakKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1415 HTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH-----VSSLEAEVQRKQNILKEMAAEtnapphpepglh 1489
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAE------------ 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1490 IEDLRKSLGTNENQEvsSSLSLSKEGIDLSMDSVRHFLSAEGVA--VRSAKEFLvrqtrsmrrRQTALKAAQQHWRhela 1567
Cdd:PRK03918 461 LKRIEKELKEIEEKE--RKLRKELRELEKVLKKESELIKLKELAeqLKELEEKL---------KKYNLEELEKKAE---- 525
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1568 SAQEVDEDLPGtkvLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1627
Cdd:PRK03918 526 EYEKLKEKLIK---LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1136-1478 |
1.43e-13 |
|
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: 76.65 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1136 ASLEQKSRRALEQLREqleAEERSAQAALraekeaeKEATLLQLREQLEGERREAV---AGLEKKHSTELEQLCSSLEAk 1212
Cdd:TIGR02169 166 AEFDRKKEKALEELEE---VEENIERLDL-------IIDEKRQQLERLRREREKAEryqALLKEKREYEGYELLKEKEA- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1213 HREVISNLQKKIEGaQQKEEAQLQESLGRAEQRTHqkvhqvieyeqELSSLLRDKRQEVEREHERKMDKMKEEhwqemae 1292
Cdd:TIGR02169 235 LERQKEAIERQLAS-LEEELEKLTEEISELEKRLE-----------EIEQLLEELNKKIKDLGEEEQLRVKEK------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1293 areryeaeerkqradlLGHLTGELERLRRAherelesvrqeqdqqLEDLRRRHRDQERKLQDLEAELSSrtkdVKARLAQ 1372
Cdd:TIGR02169 296 ----------------IGELEAEIASLERS---------------IAEKERELEDAEERLAKLEAEIDK----LLAEIEE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1373 LNVQEENMRKEKQLLLDaqRQAALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQR 1452
Cdd:TIGR02169 341 LEREIEEERKRRDKLTE--EYAELKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340
....*....|....*....|....*.
gi 1958798733 1453 LQKHVSSLEAEVQRKQNILKEMAAET 1478
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEK 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1243-1482 |
1.56e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1243 EQRTHQKVHQVIEYEQELSSLlrdkRQEVEREhERKMDKMK--EEHWQEMAEARERYEAEerKQRADLLGHLTGELE-RL 1319
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERA----HEALEDA-REQIELLEpiRELAERYAAARERLAEL--EYLRAALRLWFAQRRlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1320 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALE-K 1398
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1399 EEATATRRHLEEAKKEHTHLLES----KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqnILKEM 1474
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA---LRDAL 449
|
....*...
gi 1958798733 1475 AAETNAPP 1482
Cdd:COG4913 450 AEALGLDE 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1106-1652 |
3.47e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRAEQQTALQRLREEAETLQKAeRASLEQKSRRALEQLREQLEAEE-RSAQAALRAEkEAEK--EATLLQLREQ 1182
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETG-KAEEARKAEEAKKKAEDARKAEEaRKAEDARKAE-EARKaeDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1183 LEGERREAVAgLEKKHSTELEQLCSSLEAKHREVIsnlqKKIEGAQQKEEAQLQESLGRAEQrthqkvhqVIEYEQELSS 1262
Cdd:PTZ00121 1160 AEDARKAEEA-RKAEDAKKAEAARKAEEVRKAEEL----RKAEDARKAEAARKAEEERKAEE--------ARKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1263 LLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHE-RELESVRQ-EQDQQLED 1340
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkKKADEAKKaEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1341 LRRRhrdqerklqdleAELSSRTKDVKARLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLE 1420
Cdd:PTZ00121 1307 AKKK------------AEEAKKADEAKKKAEEAKKKADAAKKKAE---EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1421 SKQQLRRAIDDLRvRRVELESQVDQLQTQSQrlqkhvssleaEVQRKQNILKEMAAETNAPphpepglhiEDLRKslgtn 1500
Cdd:PTZ00121 1372 KKEEAKKKADAAK-KKAEEKKKADEAKKKAE-----------EDKKKADELKKAAAAKKKA---------DEAKK----- 1425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1501 ENQEVSSSLSLSKEgidlsmdsvrhflsAEgvAVRSAKEfLVRQTRSMRRRQTALKAAQqhwrhELASAQEVDEDLPGTK 1580
Cdd:PTZ00121 1426 KAEEKKKADEAKKK--------------AE--EAKKADE-AKKKAEEAKKAEEAKKKAE-----EAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1581 VLENVRKNLDEETKHLDEMKSAM--RKGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKVTFDLSDMDDL 1652
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAeaKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1114-1432 |
4.48e-13 |
|
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: 75.10 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1114 AEQQTALQRLREEAETLqKAERASLEQKSRRaLEQLREQLEAEERSAQAALRaekEAEKEATLLQLREQLEGERREAVAG 1193
Cdd:TIGR02169 670 RSEPAELQRLRERLEGL-KRELSSLQSELRR-IENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1194 LEKKHSTELEQLCSSLeAKHREVISNLQKKIEgAQQKEEAQLQESLG-------RAEQRTHQKVHQ-----VIEYEQELS 1261
Cdd:TIGR02169 745 DLSSLEQEIENVKSEL-KELEARIEELEEDLH-KLEEALNDLEARLShsripeiQAELSKLEEEVSriearLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1262 SL------LRDKRQEVER-----EHERKMDKMKEEHWQEMAEARERYEAEERKQRADL---LGHLTGELERLRrAHEREL 1327
Cdd:TIGR02169 823 RLtlekeyLEKEIQELQEqridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrLGDLKKERDELE-AQLREL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1328 ESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA-------RLAQLNVQEENMRKEKQLL-LDAQRQAALEKE 1399
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeELSLEDVQAELQRVEEEIRaLEPVNMLAIQEY 981
|
330 340 350
....*....|....*....|....*....|...
gi 1958798733 1400 EATATRrhLEEAKKEHTHLLESKQQLRRAIDDL 1432
Cdd:TIGR02169 982 EEVLKR--LDELKEKRAKLEEERKAILERIEEY 1012
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1060-1477 |
4.64e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.42 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1060 LSFLQSLLKTQLQKAAEEEEKEEETQIREEEsQRLACLRAQVQSSTEafENQIRAEQQTALQRLREEAETLQkAERASLE 1139
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNL-KELKELEEELKEAEE--KEEEYAELQEELEELEEELEELE-AELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1140 QKSRR------ALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKH 1213
Cdd:COG4717 116 EELEKlekllqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-----AELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1214 REVISNLQKKIEGAQQkEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLlrDKRQEVEREH------------------ 1275
Cdd:COG4717 191 EEELQDLAEELEELQQ-RLAELEEELEEAQEELEELEEELEQLENELEAA--ALEERLKEARlllliaaallallglggs 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1276 ----------------------ERKMDKMKEEHWQEMAEARERYEAEERKQRAdllghLTGELERLRRAHERELESV--- 1330
Cdd:COG4717 268 llsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEE-----LEELLAALGLPPDLSPEELlel 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1331 -RQEQDQQLEDLRRRHRDQERKLQDLEAELSS-----RTKDVKARLAQLNVQEENMRKEKQL-LLDAQRQAALEKEEATA 1403
Cdd:COG4717 343 lDRIEELQELLREAEELEEELQLEELEQEIAAllaeaGVEDEEELRAALEQAEEYQELKEELeELEEQLEELLGELEELL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1404 TRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQrlqkhVSSLEAEVQRKQNILKEMAAE 1477
Cdd:COG4717 423 EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1060-1432 |
8.54e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1060 LSFLQSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAfENQIRAEQQTALQRLREEAETLQKAERASLE 1139
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1140 QKSRRAlEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSL---EAKHREV 1216
Cdd:COG1196 461 LLELLA-ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigvEAAYEAA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1217 I---------SNLQKKIEGAQQKEEAQLQESLGRAE---------QRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERK 1278
Cdd:COG1196 540 LeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1279 MDKMKEEHWQEMAEARERYEAEERKQRADLLGHLT-----GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQ 1353
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1354 DLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEAT---------------ATRRHLEEAKKE---- 1414
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeeealeelpeppdleELERELERLEREieal 779
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958798733 1415 ------------------------HTHLLESKQQLRRAIDDL 1432
Cdd:COG1196 780 gpvnllaieeyeeleerydflseqREDLEEARETLEEAIEEI 821
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1315-1578 |
1.09e-12 |
|
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: 73.55 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAHERELesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV----------KARLAQLN-----VQEEN 1379
Cdd:TIGR02168 250 EAEEELEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqilRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1380 MRKEKQLLLDAQRQAALEKEEATATRRH------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRL 1453
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1454 QKHVSSLEAEVQRKQNIlkemaaetnapphpepglhIEDLRKSLGTNENQEVSSSLSLSKEGIdlsmdsvrHFLSAEGVA 1533
Cdd:TIGR02168 406 EARLERLEDRRERLQQE-------------------IEELLKKLEEAELKELQAELEELEEEL--------EELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798733 1534 VRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPG 1578
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1127-1641 |
2.69e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 72.31 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1127 AETLQKAERASLEQKSRRALEQLrEQLEAEERSAQAALRAEKE-AEKEATLLQLREQLEGERREAVAGLEKKHSTELEQL 1205
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENL-AELIIDLEELKLQELKLKEqAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1206 CSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVH--QVIEYEQELSSLLRDKRQEVEREHERKmdkmk 1283
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEElkLLAKEEEELKSELLKLERRKVDDEEKL----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1284 eEHWQEMAEARERYEAEERKQRADLLghltGELERLRRAHERELESVRQEQDQQLEDLRRRHRDqERKLQDLEAELSSRT 1363
Cdd:pfam02463 317 -KESEKEKKKAEKELKKEKEEIEELE----KELKELEIKREAEEEEEEELEKLQEKLEQLEEEL-LAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1364 KDVKARLAQLNVQEENMRKEKQLlldAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQV 1443
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLEL---ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1444 DQ-----------LQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHI--EDLRKSLGTnenqevssSLS 1510
Cdd:pfam02463 468 KKsedllketqlvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIsaHGRLGDLGV--------AVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1511 LSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRH--ELASAQEVDEDLPGTKVLENVRKN 1588
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSiaVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1589 LDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKK 1641
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1122-1632 |
2.93e-12 |
|
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: 72.06 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1122 RLREEAETLQK---AERASLEQKSRRaLEQLREQLEAEERSAQaalraEKEAEKEATLLQLREQLEGERREAVAGLEKKH 1198
Cdd:pfam05483 82 KLYKEAEKIKKwkvSIEAELKQKENK-LQENRKIIEAQRKAIQ-----ELQFENEKVSLKLEEEIQENKDLIKENNATRH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1199 STEL-EQLCSSLEAKH----------REVISNLQKKIEGAQQK-EEAQLQESLGRAE-----QRTHQKVHQVieyEQELS 1261
Cdd:pfam05483 156 LCNLlKETCARSAEKTkkyeyereetRQVYMDLNNNIEKMILAfEELRVQAENARLEmhfklKEDHEKIQHL---EEEYK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1262 SLLRDKRQEVE------REHERKMDKMK---EEHWQEMAEARERYEAEER--KQRADLLGHLTGELERLRRAHERELESV 1330
Cdd:pfam05483 233 KEINDKEKQVSllliqiTEKENKMKDLTfllEESRDKANQLEEKTKLQDEnlKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1331 RQ-EQDQQL--EDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAAL----------E 1397
Cdd:pfam05483 313 KAlEEDLQIatKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIitmelqkkssE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1398 KEEATATRRH----LEEAKK---EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1470
Cdd:pfam05483 393 LEEMTKFKNNkeveLEELKKilaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1471 LKEMAAEtnapphpepgLHIEDLRKS-LGTNENQEVSSSLSLSKEGIDLSMDSVRHflSAEGVAVRSAKEFLVRQTRSMR 1549
Cdd:pfam05483 473 VEDLKTE----------LEKEKLKNIeLTAHCDKLLLENKELTQEASDMTLELKKH--QEDIINCKKQEERMLKQIENLE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1550 RRQTALKAAQQHWRHELasAQEVDE-DLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKlnqleSSLLEEV 1628
Cdd:pfam05483 541 EKEMNLRDELESVREEF--IQKGDEvKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK-----NKNIEEL 613
|
....
gi 1958798733 1629 SDED 1632
Cdd:pfam05483 614 HQEN 617
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1303-1642 |
4.34e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 69.93 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1303 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1382
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1462
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1463 EVQR-----KQNILKEMAAETN-APPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRS 1536
Cdd:COG4372 172 ELQAlseaeAEQALDELLKEANrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1537 AKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEK 1616
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340
....*....|....*....|....*.
gi 1958798733 1617 LNQLESSLLEEVSDEDTLKGSSIKKV 1642
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLE 357
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1097-1513 |
6.16e-12 |
|
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: 71.02 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQ-KAERASLEQKSRRALEQLREQLEAEE------RSAQAALRAEKE 1169
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLENFDerieraREEQEAANAEVE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1170 AEKEAtLLQLR----EQLEGERREAVAGLEKKhsTELEQLCSSLEAKHREVISNLQKkiegaqqkEEAQLQESLGR---A 1242
Cdd:pfam12128 489 RLQSE-LRQARkrrdQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRK--------EAPDWEQSIGKvisP 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1243 EQRTHQKVHQVIEYEQELSSL------LRDKRQEV------EREHERKMDKMKEehwqemaeaRERYEAEERKQRADLLG 1310
Cdd:pfam12128 558 ELLHRTDLDPEVWDGSVGGELnlygvkLDLKRIDVpewaasEEELRERLDKAEE---------ALQSAREKQAAAEEQLV 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1311 HLTGELERLRRAHERELESV--------------RQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQ 1376
Cdd:pfam12128 629 QANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQ 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1377 EENMRKEKQLLLD----------AQRQAALEKEEaTATRRHLEEAKKEHTHLLESK--------------QQLRRAIDDL 1432
Cdd:pfam12128 709 KREARTEKQAYWQvvegaldaqlALLKAAIAARR-SGAKAELKALETWYKRDLASLgvdpdviaklkreiRTLERKIERI 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1433 RVRRVELESQVDQLQT----QSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphpepgLHIEDLRKSLGTNENQEVSSS 1508
Cdd:pfam12128 788 AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLARLIADTK--------LRRAKLEMERKASEKQQVRLS 859
|
....*
gi 1958798733 1509 LSLSK 1513
Cdd:pfam12128 860 ENLRG 864
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1315-1477 |
7.31e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 67.26 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAHERELESVRQEQD---QQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLlldaq 1391
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAaleARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRNNKEY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1392 rqAALEKEEATATRRhLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQtqsQRLQKHVSSLEAEVQRKQNIL 1471
Cdd:COG1579 92 --EALQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAER 165
|
....*.
gi 1958798733 1472 KEMAAE 1477
Cdd:COG1579 166 EELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1306-1645 |
7.66e-12 |
|
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: 70.87 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1306 ADLLGHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRK 1382
Cdd:TIGR02169 680 RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLD--AQRQAALEKEEAtatrrhlEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSL 1460
Cdd:TIGR02169 759 ELKELEAriEELEEDLHKLEE-------ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1461 EAEVQRKQNILKEMAAETNapphpEPGLHIEDLRKSLGTNENQEVSSSLS---LSKEGIDLSMDsvRHFLSAEGVAVRSA 1537
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIK-----SIEKEIENLNGKKEELEEELEELEAAlrdLESRLGDLKKE--RDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1538 KEFLVRQTRSMRRRQTALKAAQQHWRHELAS----AQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSA-MR-------- 1604
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEiedpKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnMLaiqeyeev 984
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958798733 1605 -KGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKvTFD 1645
Cdd:TIGR02169 985 lKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME-AFE 1025
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1194-1642 |
8.44e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1194 LEKKHsTELEQLCSSLEAKHREVISNLQKKiegaqQKEEAQLQESLgraeQRTHQKVHQVIEYEQELSSLLRDKRQEVER 1273
Cdd:TIGR04523 209 KIQKN-KSLESQISELKKQNNQLKDNIEKK-----QQEINEKTTEI----SNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1274 eHERKMDkmkeehwqemaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQL-EDLRRRHRDQERKL 1352
Cdd:TIGR04523 279 -NNKKIK----------------------------------ELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1353 QDLEAELSSRTKdvkaRLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDL 1432
Cdd:TIGR04523 324 EEIQNQISQNNK----IISQLNEQISQLKKELT---NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1433 RVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqniLKEMAAETNApphpepglHIEDLrkslgTNENqevsSSLSLS 1512
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNS--------EIKDL-----TNQD----SVKELI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1513 KEGIDLSMDSVRHFLSAegvavrsakeflvrQTRSMRRRQTALKAAQqhwrhelasaQEVDEDLPGTKVLENVRKNLDEE 1592
Cdd:TIGR04523 456 IKNLDNTRESLETQLKV--------------LSRSINKIKQNLEQKQ----------KELKSKEKELKKLNEEKKELEEK 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1593 TKHL----DEMKSAMRKGHDLLKKKEEKLNQLESSLLEevsDEDTLKGSSIKKV 1642
Cdd:TIGR04523 512 VKDLtkkiSSLKEKIEKLESEKKEKESKISDLEDELNK---DDFELKKENLEKE 562
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1111-1651 |
8.48e-12 |
|
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: 70.59 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1111 QIRAEQQTALQRLREEAETLQKAERASleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEatLLQLREQLEgERREA 1190
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQL--STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE--LEALTQQLE-EKAAA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1191 VAGLEKKHS---TELEQLCSSLEaKHREVISNLQKKIEGAQQ--KEE----AQLQESLGRAEQRTHQKVHQVIEYEQELS 1261
Cdd:pfam01576 568 YDKLEKTKNrlqQELDDLLVDLD-HQRQLVSNLEKKQKKFDQmlAEEkaisARYAEERDRAEAEAREKETRALSLARALE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1262 SLLrDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERELESVRqEQDQQLED- 1340
Cdd:pfam01576 647 EAL-EAKEELERTNKQLRAEMED-----------------LVSSKDDVGKNVHELERSKRALEQQVEEMK-TQLEELEDe 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1341 --------LRRRHRDQ------ERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEA----T 1402
Cdd:pfam01576 708 lqatedakLRLEVNMQalkaqfERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELeaqiD 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1403 ATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRvelesqvDQLQTQSQRLQKHVSSLEAEVQRKQNILK---------- 1472
Cdd:pfam01576 788 AANKGREEAVKQLKKLQAQMKDLQRELEEARASR-------DEILAQSKESEKKLKNLEAELLQLQEDLAaserarrqaq 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1473 ----EMAAETNAPPHPEPGLHIE----DLRKSLGTNENQEVSSSLSLSKE---GIDLSMDSVRHFLSAEGVA---VRSAK 1538
Cdd:pfam01576 861 qerdELADEIASGASGKSALQDEkrrlEARIAQLEEELEEEQSNTELLNDrlrKSTLQVEQLTTELAAERSTsqkSESAR 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1539 EFLVRQTRSMRRR--------QTALKAAQQHWRHELASA-----QEVDEDLPGTKVLENVRKNL-------DEETKHLDE 1598
Cdd:pfam01576 941 QQLERQNKELKAKlqemegtvKSKFKSSIAALEAKIAQLeeqleQESRERQAANKLVRRTEKKLkevllqvEDERRHADQ 1020
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1599 MKSAMRKGHDLLKkkeeklnQLESSlLEEVSDEDTLKGSSIKKVTFDLSDMDD 1651
Cdd:pfam01576 1021 YKDQAEKGNSRMK-------QLKRQ-LEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1140-1449 |
9.75e-12 |
|
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: 70.15 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1140 QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATL---LQLREQLEGERREA------VAGLEKKHSTELEQLCS--- 1207
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDRNQELqkrIRLLEKREAEAEEAlreqaeLNRLKKKYLEALNKKLNeke 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1208 SLEAKHREVISNLQKKI-EGAQQKEEAQLQESLGRAEQRTHQKVHQVI-----EYEQELSSLlrDKRQEVEREHERKMDK 1281
Cdd:pfam05557 97 SQLADAREVISCLKNELsELRRQIQRAELELQSTNSELEELQERLDLLkakasEAEQLRQNL--EKQQSSLAEAEQRIKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1282 M-----KEEHWQEMaeareryeAEERKQRADLLGHLTGELERLRR--AHERELESVRQEQDQQLEDLRRRHRDQER---- 1350
Cdd:pfam05557 175 LefeiqSQEQDSEI--------VKNSKSELARIPELEKELERLREhnKHLNENIENKLLLKEEVEDLKRKLEREEKyree 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1351 ------KLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLldaQRQAALEKEEATATR--RHLEEAKKEhthLLESK 1422
Cdd:pfam05557 247 aatlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQ---QREIVLKEENSSLTSsaRQLEKARRE---LEQEL 320
|
330 340
....*....|....*....|....*..
gi 1958798733 1423 QQLRRAIDDLRVRRVELESQVDQLQTQ 1449
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1207-1477 |
9.99e-12 |
|
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: 70.47 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1207 SSLEAKHREvISNLQKKIEGAQQKEeAQLQESLGRAEQrthqkvhQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEH 1286
Cdd:TIGR02168 670 SSILERRRE-IEELEEKIEELEEKI-AELEKALAELRK-------ELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1287 WQEmaeareryeaeerkQRADLLGHLTGELErlrraherELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV 1366
Cdd:TIGR02168 741 EVE--------------QLEERIAQLSKELT--------ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1367 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL 1446
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270
....*....|....*....|....*....|.
gi 1958798733 1447 QTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1477
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESK 909
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1118-1630 |
1.22e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1118 TALQRLREEAETLQKAERASLE-QKSRRALEQLREQLE-----AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAV 1191
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDaREQIELLEPIRELAEryaaaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1192 AGLEKKHStELEQLCSSLEAKHREvisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLlrdkrqEV 1271
Cdd:COG4913 305 ARLEAELE-RLEARLDALREELDE----LEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL------GL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1272 EREHERKMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgELERLRRAHERELESVRQEqdqqLEDLRRRH----RD 1347
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALA--------EAEAALRDLRRELRELEAE----IASLERRKsnipAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1348 QERKLQDLEAELSSRTKDVK--ARLAQLNVQEENMRK--EKQL------LL--DAQRQAALEKEEATATRRHL--EEAK- 1412
Cdd:COG4913 442 LLALRDALAEALGLDEAELPfvGELIEVRPEEERWRGaiERVLggfaltLLvpPEHYAAALRWVNRLHLRGRLvyERVRt 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1413 ---------------------KEHT------HLL---------ESKQQLR---RAI----------------DDLRVRRV 1437
Cdd:COG4913 522 glpdperprldpdslagkldfKPHPfrawleAELgrrfdyvcvDSPEELRrhpRAItragqvkgngtrhekdDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1438 ------------ELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILkemAAETNAPPHPEPGLHIEDLRKSLGTNENQev 1505
Cdd:COG4913 602 yvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERR---EALQRLAEYSWDEIDVASAEREIAELEAE-- 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1506 ssslslsKEGIDLSMDSVRHfLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLEnV 1585
Cdd:COG4913 677 -------LERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-L 747
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1958798733 1586 RKNLDE--ETKHLDEMKSAMRKG-HDLLKKKEEKLNQLESSLLEEVSD 1630
Cdd:COG4913 748 RALLEErfAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1146-1655 |
1.81e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1146 LEQLREQLEAEERSAQAALRAEK-EAEKEATLLQLREQLEGerreavaglekKHSTELEQLCSSLEAKHREV---ISNLQ 1221
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERvLSDQRGSLDQLKAQIEE-----------KEEKDLHERLNGLESELAELdeeIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1222 KKIEGAQQKEEAqLQESLGRAEQRthqkvhqvieyEQELSSLLR--DKRQEVEREHERKMDKMKEEhwqemaeareryEA 1299
Cdd:PRK02224 227 EQREQARETRDE-ADEVLEEHEER-----------REELETLEAeiEDLRETIAETEREREELAEE------------VR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1300 EERKQRADLLGHLTGELER--LRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlaqlnvQE 1377
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEagLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL------EE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1378 ENMrkekqlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHV 1457
Cdd:PRK02224 357 RAE--------ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1458 SSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSA 1537
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1538 KEFlvrqTRSMRRRQTALKAAQQHwrhelasAQEVDEDlpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKL 1617
Cdd:PRK02224 509 DRI----ERLEERREDLEELIAER-------RETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958798733 1618 NQLESSLLEEVSDEDTLkgssiKKVTFDLSDMDDLSSE 1655
Cdd:PRK02224 575 AELNSKLAELKERIESL-----ERIRTLLAAIADAEDE 607
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1109-1474 |
3.92e-11 |
|
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: 68.66 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLREEAETLQKaERASLEQKsrraLEQLREQLEAEERSAQAAL-RAEKEA-----------EKEATL 1176
Cdd:pfam01576 199 EEKGRQELEKAKRKLEGESTDLQE-QIAELQAQ----IAELRAQLAKKEEELQAALaRLEEETaqknnalkkirELEAQI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1177 LQLREQLEGER--REAVAGLEKKHSTELEQLCSSLE-------------AKHREVISNLQKKIEGAQQKEEAQLQEslgr 1241
Cdd:pfam01576 274 SELQEDLESERaaRNKAEKQRRDLGEELEALKTELEdtldttaaqqelrSKREQEVTELKKALEEETRSHEAQLQE---- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1242 aeqrTHQKVHQVIEYEQELSSLLRDKRQEVEreherKMDKMKEEHWQEmaeareryeaeerkqradllghLTGELERLRR 1321
Cdd:pfam01576 350 ----MRQKHTQALEELTEQLEQAKRNKANLE-----KAKQALESENAE----------------------LQAELRTLQQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1322 AhERELESVRQEQDQQLEDLRRRHRDQER-------KLQDLEAELSSRT--------------KDVKARLAQLN-----V 1375
Cdd:pfam01576 399 A-KQDSEHKRKKLEGQLQELQARLSESERqraelaeKLSKLQSELESVSsllneaegkniklsKDVSSLESQLQdtqelL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1376 QEENMRK-----------------EKQLLLDAQRQAALEKEEATA------TRRHLEEAKKEHTHLLESKQQLRRAIDDL 1432
Cdd:pfam01576 478 QEETRQKlnlstrlrqledernslQEQLEEEEEAKRNVERQLSTLqaqlsdMKKKLEEDAGTLEALEEGKKRLQRELEAL 557
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958798733 1433 RVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEM 1474
Cdd:pfam01576 558 TQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL 599
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1103-1630 |
4.31e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 68.24 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1103 SSTEAFENQIRAEQQTALQRLREEAETLQKAeraSLEQKSRraleqlreqLEAEERSAQAALRAEKEAEKEATLLQ---- 1178
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRET---SLQQKMR---------LEAQAMELDALAVAEKAGQAEAEGLRaala 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1179 ----LREQL-EGERREavagLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQK----------EEAQLQESLGRAE 1243
Cdd:pfam07111 126 gaemVRKNLeEGSQRE----LEEIQRLHQEQL-SSLTQAHEEALSSLTSKAEGLEKSlnsletkragEAKQLAEAQKEAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1244 QRTHQ--KVHQVIEYEQELSSLLRD----------KRQEVEREHERKMDKMKeeHWQEMAEARERYEAEERKQRADLLGH 1311
Cdd:pfam07111 201 LLRKQlsKTQEELEAQVTLVESLRKyvgeqvppevHSQTWELERQELLDTMQ--HLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1312 LTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQ------ERKLQDLEAelSSRTKDVKARLAQLNVQEENMRKEKQ 1385
Cdd:pfam07111 279 LALQEEELTRKIQ-PSDSLEPEFPKKCRSLLNRWREKvfalmvQLKAQDLEH--RDSVKQLRGQVAELQEQVTSQSQEQA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1386 LLLDA--QRQAALEKEEATATRRHLE-----EAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHV 1457
Cdd:pfam07111 356 ILQRAlqDKAAEVEVERMSAKGLQMElsraqEARRRQQQQTASaEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1458 SSLEAEVQRKQNI---------LKEMAAETNAPPHPEP------GLHIEDLRKslgtnENQEVSSSLSLSKEGIDLSMDS 1522
Cdd:pfam07111 436 NRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAPpvdadlSLELEQLRE-----ERNRLDAELQLSAHLIQQEVGR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1523 VRHFLSAEgvavrsakeflvrqtrsmrrRQTALKAAQQhWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSA 1602
Cdd:pfam07111 511 AREQGEAE--------------------RQQLSEVAQQ-LEQELQRAQESLASV--GQQLEVARQGQQESTEEAASLRQE 567
|
570 580
....*....|....*....|....*....
gi 1958798733 1603 MRKGHDLLKKK-EEKLNQLESSLLEEVSD 1630
Cdd:pfam07111 568 LTQQQEIYGQAlQEKVAEVETRLREQLSD 596
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1091-1624 |
4.97e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAER-ASLEQKsrraLEQLREQLEAEErsAQAALRAEKE 1169
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElAELEEK----LEELKEELESLE--AELEELEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1170 AEKEATLLQLREQLEGERREaVAGLEKK---HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE---SLGRAE 1243
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSK-VAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaELEELE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1244 QRTHQKVHQVIEYEQELSSL------LRDKRQEVEREHERK------MDKMKEEH------------------------- 1286
Cdd:TIGR02168 447 EELEELQEELERLEEALEELreeleeAEQALDAAERELAQLqarldsLERLQENLegfsegvkallknqsglsgilgvls 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1287 ------------------------------------------------WQEMAEARERYEAEERKQR------------- 1305
Cdd:TIGR02168 527 elisvdegyeaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtFLPLDSIKGTEIQGNDREIlkniegflgvakd 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1306 ------------ADLLGH------LTGELERLRRAHEREL----------------------ESVRQEQDQQLEDLRRRH 1345
Cdd:TIGR02168 607 lvkfdpklrkalSYLLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKI 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1346 RDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEE----AKKEHTHLLES 1421
Cdd:TIGR02168 687 EELEEKIAELEKAL----AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqLSKELTELEAE 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1422 KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEM---------AAETNAPPHPEPGLHIED 1492
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlreRLESLERRIAATERRLED 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1493 LRKSLGTNENQEVSSSLSLSKEGIDL--------SMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRH 1564
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIeeleseleALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798733 1565 ELASAQevdEDLPGTKV-LENVRKNLDEETK-HLDEMKSAMRKGHDLLKKKEEKLNQLESSL 1624
Cdd:TIGR02168 923 KLAQLE---LRLEGLEVrIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1106-1370 |
8.26e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 65.71 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLE-----------AEERSAQAALRAEKEAEKEA 1174
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEderileylkekAEREEEREAEREEIEEEKER 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1175 TLLQLREQLEGERReavaglEKKHSTEL--EQLCSSLEAKHRevisnlQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQ 1252
Cdd:pfam13868 185 EIARLRAQQEKAQD------EKAERDELraKLYQEEQERKER------QKEREEAEKKARQRQELQQAREEQIELKERRL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1253 VIEYEQElssllrdkrqevEREHERKMDKMKEEHWQEMaeareryeAEERKQRadllghltgeleRLRRAHERELESVRQ 1332
Cdd:pfam13868 253 AEEAERE------------EEEFERMLRKQAEDEEIEQ--------EEAEKRR------------MKRLEHRRELEKQIE 300
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958798733 1333 EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARL 1370
Cdd:pfam13868 301 EREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1106-1465 |
2.44e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRaEQQTALQRLREEAETLqkAERASLEQKSRRALEQLREQLEAEERSAQAALR----AEKEAEKEATLL---- 1177
Cdd:PRK02224 275 EELAEEVR-DLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLreda 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1178 -QLREQLEgERREAVAGLEkkhsTELEQLCSSLEaKHREVISNLQKKIEGAQqKEEAQLQESLGRAEQR------THQKV 1250
Cdd:PRK02224 352 dDLEERAE-ELREEAAELE----SELEEAREAVE-DRREEIEELEEEIEELR-ERFGDAPVDLGNAEDFleelreERDEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1251 HqviEYEQELSSLLRDKRQEVErEHERKMDKMK-EEHWQEMAEARERYEAEERKQRADllgHLTGELERLRRAHER---E 1326
Cdd:PRK02224 425 R---EREAELEATLRTARERVE-EAEALLEAGKcPECGQPVEGSPHVETIEEDRERVE---ELEAELEDLEEEVEEveeR 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1327 LESVRQ--EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKdvkaRLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATAT 1404
Cdd:PRK02224 498 LERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRE----RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1405 RRHLEEAKKEHTHLLESKQQLR----------RAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQ 1465
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRtllaaiadaeDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1091-1457 |
2.51e-10 |
|
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: 66.13 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVQSSTEafenqIRAEQQTALQRLREEAETLQKAERAsLEQKSRRALEQLREqleaeersAQAALR-AEKE 1169
Cdd:COG3096 284 SERALELRRELFGARR-----QLAEEQYRLVEMARELEELSARESD-LEQDYQAASDHLNL--------VQTALRqQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1170 AEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCSSlEAKHREVISNL---QKKIEgAQQKEEAQLQ---ESLGRAE 1243
Cdd:COG3096 350 ERYQEDLEELTERLE-EQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLadyQQALD-VQQTRAIQYQqavQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1244 QRTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELE 1317
Cdd:COG3096 427 ALCGLpdlTPENAEDYLAAF----RAKEQQATeevLELEQKLSVADAARRQ-------------FEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1318 RLRrAHERELESVR-----QEQDQQLEDLRRRHRDQERKLQdleaelssRTKDVKARLAQLNVQEenmrkekQLLLDAQR 1392
Cdd:COG3096 490 RSQ-AWQTARELLRryrsqQALAQRLQQLRAQLAELEQRLR--------QQQNAERLLEEFCQRI-------GQQLDAAE 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1393 QAALEKEEATATRRHLEEAKKEHThllESKQQLRRAIDDLRVRRVELESQVD---QLQTQSQRLQKHV 1457
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLEQLRARIKELAARAPawlAAQDALERLREQS 618
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
994-1478 |
2.60e-10 |
|
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: 65.76 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 994 QGLGQEEQDDSRSSRSEpQSKHTQVSEREQP-------RSTLHSQATEEGPLRTLEGQPEG--QPGKDSVASPAPLSFLQ 1064
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLL-QTLHSQEIHIRDAhevatsiREISCQQHTLTQHIHTLQQQKTTltQKLQSLCKELDILQREQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1065 SLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRR 1144
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1145 ALEQLREQLEAEersaQAALRAEKEAEKEATLLQLREqLEGERREAVAGLE--KKHSTELEQLCSSLEAKhREVISNLQK 1222
Cdd:TIGR00618 490 AVVLARLLELQE----EPCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQtyAQLETSEEDVYHQLTSE-RKQRASLKE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1223 KIEGAQQKEE--AQLQESLGRAEQRTHQKVHQVIEYEQELSsllRDKRQEVEREHERKMDKMKEEHWQEMaearERYEAE 1300
Cdd:TIGR00618 564 QMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLS---EAEDMLACEQHALLRKLQPEQDLQDV----RLHLQQ 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1301 ERKQRADLLGHLTGELERLrrAHERELESVRQEQDQQLEDLRRRhrdqERKLQDLEAELSSRTKDvKARLAQLNvqeENM 1380
Cdd:TIGR00618 637 CSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASR----QLALQKMQSEKEQLTYW-KEMLAQCQ---TLL 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1381 RKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIddLRVRRVELESQVDQLQTQSQRLQKhVSSL 1460
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV--LKARTEAHFNNNEEVTAALQTGAE-LSHL 783
|
490
....*....|....*...
gi 1958798733 1461 EAEVQRKQNILKEMAAET 1478
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLL 801
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1114-1620 |
5.21e-10 |
|
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: 64.75 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1114 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleAEERSAQAALRAEKEAEKEatllQLREQLEGERREAVAG 1193
Cdd:pfam15921 84 SHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM--QMERDAMADIRRRESQSQE----DLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1194 ------LEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQKEEAQLQE----------SLGRAEQRTHQKVHQVIEY- 1256
Cdd:pfam15921 158 kclkedMLEDSNTQIEQL-RKMMLSHEGVLQEIRSILVDFEEASGKKIYEhdsmstmhfrSLGSAISKILRELDTEISYl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1257 -------EQELSSLLRDKRQEVE---REHERKMDKMKEEHWQEmaeareryeaeerkqradllghLTGELERLRRAhere 1326
Cdd:pfam15921 237 kgrifpvEDQLEALKSESQNKIElllQQHQDRIEQLISEHEVE----------------------ITGLTEKASSA---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1327 lESVRQEQDQQLEDLRRRHRDQE----RKLQDLEAELSSRTKDVKarlaqlnvqeENMRKEKQLLLDAQRQAALEKEEAT 1402
Cdd:pfam15921 291 -RSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELR----------EAKRMYEDKIEELEKQLVLANSELT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1403 ATRRHLEEAKKEHTHLlesKQQLRRAIDDLRVRRVELESQVDQLQTQSQR----------LQKHVSSLEAEVQRKQNILK 1472
Cdd:pfam15921 360 EARTERDQFSQESGNL---DDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitidhLRRELDDRNMEVQRLEALLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1473 EMAAETNapphpepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQ 1552
Cdd:pfam15921 437 AMKSECQ-------GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798733 1553 TALKAAQQhwrhELASAQ-EVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMR---KGHDLLKKKEEKLNQL 1620
Cdd:pfam15921 510 RAIEATNA----EITKLRsRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAekdKVIEILRQQIENMTQL 577
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1175-1623 |
5.55e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1175 TLLQ-----LREQLEGERREAVAGLEKKHST------ELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAE 1243
Cdd:COG4717 38 TLLAfiramLLERLEKEADELFKPQGRKPELnlkelkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1244 QRTHQKVHQVIEYEQELSSLlRDKRQEVEREHERKMDKMKEehWQEMAEAREryeaeerkqradllgHLTGELERLRRAH 1323
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEE--LRELEEELE---------------ELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1324 ERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALE------ 1397
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARllllia 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1398 ---------KEEATATRRHLEEA---------------KKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRL 1453
Cdd:COG4717 256 aallallglGGSLLSLILTIAGVlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1454 QKHVSSLEAEVQRKQNILKEmaaetnapphpepglhIEDLRKSLGTNENQEVSSSLslskegidlsmdsvrhflsAEGVA 1533
Cdd:COG4717 336 PEELLELLDRIEELQELLRE----------------AEELEEELQLEELEQEIAAL-------------------LAEAG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1534 VRSAKEFLVRQTRSmrRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKK 1613
Cdd:COG4717 381 VEDEEELRAALEQA--EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
490
....*....|
gi 1958798733 1614 EEKLNQLESS 1623
Cdd:COG4717 459 EAELEQLEED 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1315-1477 |
5.60e-10 |
|
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: 63.63 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAhERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK------------ 1382
Cdd:COG4942 42 ELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLL------DAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH 1456
Cdd:COG4942 121 PLALLLspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180
....*....|....*....|.
gi 1958798733 1457 VSSLEAEVQRKQNILKEMAAE 1477
Cdd:COG4942 201 LARLEKELAELAAELAELQQE 221
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1113-1414 |
6.79e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.01 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1113 RAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAAlRAEKEAEKEATLLQLREQLEGERREAVA 1192
Cdd:pfam13868 44 RLDEMMEEERERALEEEEEKEEE--RKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVERIQEEDQAEAEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1193 GLEKKHSTELE-QLCSSLEAKHREvisnlQKKIEgaQQKEEAQLQESLG----RAEQRTHQKVHQVIEYEQELSSLLrdK 1267
Cdd:pfam13868 121 KLEKQRQLREEiDEFNEEQAEWKE-----LEKEE--EREEDERILEYLKekaeREEEREAEREEIEEEKEREIARLR--A 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1268 RQEVEREHERKMDKMKEEHWQE-----MAEARERYEAEERKQRADLLGHLT--GELERLRRAHERELESVRQEQ--DQQL 1338
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEeqerkERQKEREEAEKKARQRQELQQAREeqIELKERRLAEEAEREEEEFERmlRKQA 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798733 1339 EDLRRRHRDQERKlqdleaelssRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKE 1414
Cdd:pfam13868 272 EDEEIEQEEAEKR----------RMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1115-1475 |
9.41e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQKAeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE-ATLLQLREQLE---GERREA 1190
Cdd:PRK03918 349 ELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARIGELKkeiKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1191 VAGLEKKHST------EL-EQLCSSLEAKHREVISNLQKKIEGAQQKEEaQLQESLGRAEQ---------RTHQKVHQVI 1254
Cdd:PRK03918 428 IEELKKAKGKcpvcgrELtEEHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELEKvlkkeseliKLKELAEQLK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1255 EYEQELSSLLRDKRQEVEREHErkmdKMKEEhwqemaeareryeaeerkqradlLGHLTGELERLrrahERELESVrQEQ 1334
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYE----KLKEK-----------------------LIKLKGEIKSL----KKELEKL-EEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1335 DQQLEDLRRRHRDQERKLQDLEAELSSR----TKDVKARLAQL-----------NVQEENMRKEKQL------LLDAQRQ 1393
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELepfyneylelkDAEKELEREEKELkkleeeLDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1394 AALEKEEATATRRHLEEAKK-----EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQ 1468
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
....*..
gi 1958798733 1469 NILKEMA 1475
Cdd:PRK03918 715 KLEKALE 721
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1103-1546 |
9.97e-10 |
|
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: 63.59 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1103 SSTEAFENQIRAEQQTALQrLREEAETlQKAEraslEQKSRRALEQLREQLEAEERSAQAALRAEKEA----EKEATLLQ 1178
Cdd:pfam05483 310 STQKALEEDLQIATKTICQ-LTEEKEA-QMEE----LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRleknEDQLKIIT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1179 LREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQ-KKIEGAQQKEEAQLQESLGRAEQRTHQ---KVHQVI 1254
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDleiQLTAIK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1255 EYEQELSSLLRDKRQEVEREHERKM------DKMKEEHwQEMAEARERYEAEERKQRADLLGHLTGElERLRRAHER--- 1325
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIeltahcDKLLLEN-KELTQEASDMTLELKKHQEDIINCKKQE-ERMLKQIENlee 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1326 -------ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK 1398
Cdd:pfam05483 542 kemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1399 EEATATRRHLE----EAKKEHTHLLESKQQLRRAID----DLRVRRVELESQVDQLQtQSQRLQKHVSSLEAEV-QRKQN 1469
Cdd:pfam05483 622 KKGSAENKQLNayeiKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVE-KAKAIADEAVKLQKEIdKRCQH 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1470 ILKEMAAETNAPPHPEPGLhIEDLRKSLG--TNENQEVSS---SLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQ 1544
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKI-IEERDSELGlyKNKEQEQSSakaALEIELSNIKAELLSLKKQLEIE----KEEKEKLKME 775
|
..
gi 1958798733 1545 TR 1546
Cdd:pfam05483 776 AK 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1098-1415 |
1.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1098 RAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLE--QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAT 1175
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEelEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1176 LLQL----------------------------------------REQLEGERREAVAGLEKKHSTELEQLCSSLEAKHre 1215
Cdd:COG4717 252 LLIAaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1216 VISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQkvHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEehWQEMAEARE 1295
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEQAEE--YQELKEELE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1296 RYeaeerkqRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDvkARLAQLNV 1375
Cdd:COG4717 406 EL-------EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798733 1376 QEENMRKEKQLLldAQRQAALEkeeatATRRHLEEAKKEH 1415
Cdd:COG4717 477 ELEELKAELREL--AEEWAALK-----LALELLEEAREEY 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1099-1480 |
1.74e-09 |
|
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: 63.06 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1099 AQVQSSTEAFENQIRAEQQTaLQRLREEAETLQKAERAsLEQKSRRALEQLrEQLEAEERSAQAALRAEKEAEKEATLLQ 1178
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSI-LTQCDNRSKEDI-PNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1179 LREQLEGERREA---VAGLEKKHSTELEQLcssLEAKHREVISNLQKKIE---GAQQKEEAQLQESLGRAEQRTHQKVHQ 1252
Cdd:TIGR00618 615 HALLRKLQPEQDlqdVRLHLQQCSQELALK---LTALHALQLTLTQERVRehaLSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1253 VIEYEQELSSLLRDKRQEveREHERKMDKMKEEhWQemaeARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQ 1332
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLREL--ETHIEEYDREFNE-IE----NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1333 EQDQQLedLRRRHRDQErkLQDLEAELSSRTKDVKAR---LAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRrhLE 1409
Cdd:TIGR00618 765 NNNEEV--TAALQTGAE--LSHLAAEIQFFNRLREEDthlLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR--LE 838
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1410 EakkEHTHLLESKQQLRRAIDDLRvrrvelesQVDQLQTQSQRLQKHVSSLEA----EVQRKQNILKEMAAETNA 1480
Cdd:TIGR00618 839 E---KSATLGEITHQLLKYEECSK--------QLAQLTQEQAKIIQLSDKLNGinqiKIQFDGDALIKFLHEITL 902
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1305-1634 |
2.12e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1305 RADLLGHLTGELERLRRAHERELESV---RQEQDQQLEDLRRRHRDQERKLQDLEaELSSRTKDVKARLAQLNVQEENMR 1381
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlkeLKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1382 KEKQLLLDAQRQAALEKEEATATRR--HLEEAKKEHTHLLESKQQLRRAIDDLRVRRVE------------LESQVDQLQ 1447
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEElleqlslateeeLQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1448 TQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTnenqeVSSSLSLSKEGIDLSMDSVRHF- 1526
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI-----AAALLALLGLGGSLLSLILTIAg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1527 -------LSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRknldeetkHLDEM 1599
Cdd:COG4717 278 vlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD--------RIEEL 349
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958798733 1600 KSAMRKGHDLLKKKEEKLNQLE-SSLLEE--VSDEDTL 1634
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEiAALLAEagVEDEEEL 387
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1100-1431 |
3.05e-09 |
|
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: 62.50 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1100 QVQSSTEAFENQIrAEQQTALQRLREEaetLQKAERASL------------------------EQKSRRALEQLRE---Q 1152
Cdd:pfam01576 682 ELERSKRALEQQV-EEMKTQLEELEDE---LQATEDAKLrlevnmqalkaqferdlqardeqgEEKRRQLVKQVREleaE 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1153 LEAEERSAQAALRAEKEAEKEatLLQLREQLEGE---RREAVAGLeKKHSTELEQLCSSLEAKH--REVISNLQKKIEGA 1227
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELD--LKELEAQIDAAnkgREEAVKQL-KKLQAQMKDLQRELEEARasRDEILAQSKESEKK 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1228 QQKEEA---QLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKR--QEVEREHERKMDKMKEEHWQEMA--EARERYEAE 1300
Cdd:pfam01576 835 LKNLEAellQLQEDLAASERARRQAQQERDELADEIASGASGKSalQDEKRRLEARIAQLEEELEEEQSntELLNDRLRK 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1301 ERKQRADLLGHLTGElerlrRAHERELESVRQEQDQQLEDLRRrhrdqerKLQDLEAELSSRTKD----VKARLAQLNVQ 1376
Cdd:pfam01576 915 STLQVEQLTTELAAE-----RSTSQKSESARQQLERQNKELKA-------KLQEMEGTVKSKFKSsiaaLEAKIAQLEEQ 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1377 EENMRKEKQ---------------LLL---DAQRQAALEKEEATAT-------RRHLEEAKKEHTHLLESKQQLRRAIDD 1431
Cdd:pfam01576 983 LEQESRERQaanklvrrtekklkeVLLqveDERRHADQYKDQAEKGnsrmkqlKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1115-1467 |
3.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQK--AERASLEQKSRRaLEQLREQLEAEERSAQAALraEKEAEKEATLLQLREQLEGERREaVA 1192
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKlsEFYEEYLDELRE-IEKRLSRLEEEINGIEERI--KELEEKEERLEELKKKLKELEKR-LE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1193 GLEKKHST---------ELEQLCSSLEAKHREVISNLQKKIEGAQ---QKEEAQLQESLGRAEQRTHQKVHQVIEYE--- 1257
Cdd:PRK03918 356 ELEERHELyeeakakkeELERLKKRLTGLTPEKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELKKAIEELKkak 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1258 -------QELSSllrDKRQEVEREHERKMDKMKEEhwqemaeareryeaeeRKQRADLLGHLTGELERLR--RAHERELE 1328
Cdd:PRK03918 436 gkcpvcgRELTE---EHRKELLEEYTAELKRIEKE----------------LKEIEEKERKLRKELRELEkvLKKESELI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1329 SVRQEQDQ-----------QLEDLRRRHRDQE---RKLQDLEAELSS------RTKDVKARLAQLNVQEENMRKEKQLLL 1388
Cdd:PRK03918 497 KLKELAEQlkeleeklkkyNLEELEKKAEEYEklkEKLIKLKGEIKSlkkeleKLEELKKKLAELEKKLDELEEELAELL 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1389 DAQRQAALEKEEATATR-RHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaEVQRK 1467
Cdd:PRK03918 577 KELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-ELEKK 655
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1123-1634 |
3.52e-09 |
|
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: 62.11 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1123 LREEAETLQKA-ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATllQLREQLEGERreavaglekkhsTE 1201
Cdd:pfam01576 7 MQAKEEELQKVkERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE--EMRARLAARK------------QE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1202 LEQLCSSLEAKHRE------VISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKV----------HQVIEYEQELSSLLR 1265
Cdd:pfam01576 73 LEEILHELESRLEEeeersqQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVtteakikkleEDILLLEDQNSKLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1266 DKRQEVER---------EHERK---MDKMKEEHwQEMAEARERYEAEERKQRAdllghltgELERLRRAHERELESVRQ- 1332
Cdd:pfam01576 153 ERKLLEERiseftsnlaEEEEKaksLSKLKNKH-EAMISDLEERLKKEEKGRQ--------ELEKAKRKLEGESTDLQEq 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1333 --EQDQQLEDLRRRHRDQERKLQDLEAELSSRT-------KDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATA 1403
Cdd:pfam01576 224 iaELQAQIAELRAQLAKKEEELQAALARLEEETaqknnalKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1404 TRRHLEE------AKKEhthlLESKQ-----QLRRAID-----------DLRVRR----VELESQVDQLQTQSQRLQKHV 1457
Cdd:pfam01576 304 LKTELEDtldttaAQQE----LRSKReqevtELKKALEeetrsheaqlqEMRQKHtqalEELTEQLEQAKRNKANLEKAK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1458 SSLEAEVQRKQNILKEMAAETNAPPHPEPGL--HIEDLRKSLGTNENQEVSSSLSLSKegIDLSMDSVRHFLS-AEGVAV 1534
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLegQLQELQARLSESERQRAELAEKLSK--LQSELESVSSLLNeAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1535 RSAK-------------EFLVRQTR---SMRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDE 1598
Cdd:pfam01576 458 KLSKdvsslesqlqdtqELLQEETRqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNV--ERQLSTLQAQLSDMKKKLEE 535
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958798733 1599 MKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTL 1634
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1110-1464 |
3.67e-09 |
|
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: 62.11 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALQRLREEAEtlqKAERASLEQKSR-----RALEQLREQLEAEERsAQAALRAEKEA---EKEATLLQLRE 1181
Cdd:pfam01576 607 DQMLAEEKAISARYAEERD---RAEAEAREKETRalslaRALEEALEAKEELER-TNKQLRAEMEDlvsSKDDVGKNVHE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1182 qLEGERREAVAGLE--KKHSTELE-QLCSSLEAKHRevisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1258
Cdd:pfam01576 683 -LERSKRALEQQVEemKTQLEELEdELQATEDAKLR-----LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1259 ELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLR----------RAHERELE 1328
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilaqsKESEKKLK 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1329 SVRQEQDQQLEDL-----RRRHRDQERklQDLEAELSSRTKD----------VKARLAQLNVQEENMRKEKQLLLDAQRQ 1393
Cdd:pfam01576 837 NLEAELLQLQEDLaaserARRQAQQER--DELADEIASGASGksalqdekrrLEARIAQLEEELEEEQSNTELLNDRLRK 914
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1394 AALEKE----EATATRRHLEEAKKehthlleSKQQLRRAIDDLRVRRVELESQVDQLQTQSqrlqkhVSSLEAEV 1464
Cdd:pfam01576 915 STLQVEqlttELAAERSTSQKSES-------ARQQLERQNKELKAKLQEMEGTVKSKFKSS------IAALEAKI 976
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1125-1635 |
3.91e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1125 EEAETLQKAERASLEQKSRR------ALEQLREQLEAEERSAQaalRAEKEAEKEATLLQLREQLEGErreaVAGLEKKh 1198
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREineissELPELREELEKLEKEVK---ELEELKEEIEELEKELESLEGS----KRKLEEK- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1199 steLEQLCSSLEAKhREVISNLQKKIEGAQQ-KEEAQLQESLGRAEQRTHQKVHQVieyEQELSSlLRDKRQEVEREHEr 1277
Cdd:PRK03918 261 ---IRELEERIEEL-KKEIEELEEKVKELKElKEKAEEYIKLSEFYEEYLDELREI---EKRLSR-LEEEINGIEERIK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1278 KMDKMKEEhwqemaeareryeaeerkqradlLGHLTGELERLRRAHE------RELESVRQEQDqQLEDLRRRHRDQ--- 1348
Cdd:PRK03918 332 ELEEKEER-----------------------LEELKKKLKELEKRLEeleerhELYEEAKAKKE-ELERLKKRLTGLtpe 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1349 --ERKLQDLE---AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRH--LEEAKKEHTHLLES 1421
Cdd:PRK03918 388 klEKELEELEkakEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1422 KQQLRRAIDDLRVRRVELESQ-------------VDQLQTQSQRLQKH-VSSLEAEvQRKQNILKEMAAETNApphpepg 1487
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVlkkeseliklkelAEQLKELEEKLKKYnLEELEKK-AEEYEKLKEKLIKLKG------- 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1488 lHIEDLRKSLgtNENQEVSSSLSLSKEGID---LSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRH 1564
Cdd:PRK03918 540 -EIKSLKKEL--EKLEELKKKLAELEKKLDeleEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1565 ELAS-------AQEVDEDLPGT-KVLENVRKNLDEETKHLDE-----MKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDE 1631
Cdd:PRK03918 617 EEKElkkleeeLDKAFEELAETeKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
....
gi 1958798733 1632 DTLK 1635
Cdd:PRK03918 697 EKLK 700
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1159-1404 |
5.31e-09 |
|
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: 60.55 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1159 SAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQES 1238
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-AALERR----IAALARRIR-ALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1239 LGRAEQRTHQKVHQVIEYEQELSSLLRdkRQEVEREHERKMDKMKEEHWQEMAEARE--RYEAEERKQRADLLGHLTGEL 1316
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1317 ERLRRAHERE---LESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRtkdvKARLAQLNVQEENMRKekqlLLDAQRQ 1393
Cdd:COG4942 163 AALRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEA----LIARLEA 234
|
250
....*....|.
gi 1958798733 1394 AALEKEEATAT 1404
Cdd:COG4942 235 EAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1129-1478 |
5.32e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1129 TLQKAERASLEQKSRRALEQL------------REQLEAEERSAQAALRAEKEAEKEATLLQLREQLE------GERREA 1190
Cdd:COG4717 38 TLLAFIRAMLLERLEKEADELfkpqgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEeleaelEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1191 VAGLEKKHS------------TELEQLCSSLEA--KHREVISNLQKKIEGAQQ---KEEAQLQESLGRAEQRTHQKVHQV 1253
Cdd:COG4717 118 LEKLEKLLQllplyqelealeAELAELPERLEEleERLEELRELEEELEELEAelaELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1254 IEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRAD-------------------------- 1307
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiag 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1308 -------LLGHLTGELERLRRAHERELESVR-QEQDQQLEDLR-RRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEE 1378
Cdd:COG4717 278 vlflvlgLLALLFLLLAREKASLGKEAEELQaLPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1379 NMRKEKQLLLDAQRQAAL-------EKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR-----RVELESQVDQL 1446
Cdd:COG4717 358 ELEEELQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdEEELEEELEEL 437
|
410 420 430
....*....|....*....|....*....|..
gi 1958798733 1447 QTQSQRLQKHVSSLEAEVQRKQNILKEMAAET 1478
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1115-1441 |
5.52e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQKAERASlEQKSRRALEQLREQLEAEeRSAQAALRAEKE---AEKEATLLQLREQ-----LEGE 1186
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAR-EVERRRKLEEAEKARQAE-MDRQAAIYAEQErmaMERERELERIRQEerkreLERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1187 RREAVAgLEKKHSTELEQLCSSLEAKHREVISNL-------------QKKI-------EGAQQKEEAQLQESLGRAEQRT 1246
Cdd:pfam17380 366 RQEEIA-MEISRMRELERLQMERQQKNERVRQELeaarkvkileeerQRKIqqqkvemEQIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1247 HQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeERKQRADllghltgelerlrrahere 1326
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK---------------RDRKRAE------------------- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1327 lESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVkARLAQLNVQEENMRKEKQllLDAQRQAALEKEEATATRR 1406
Cdd:pfam17380 491 -EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAI-YEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERS 566
|
330 340 350
....*....|....*....|....*....|....*
gi 1958798733 1407 HLEEAKKEhthlleskQQLRRAIDDLRVRRVELES 1441
Cdd:pfam17380 567 RLEAMERE--------REMMRQIVESEKARAEYEA 593
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1098-1266 |
6.19e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1098 RAQVQSSTEAFENQIR------AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAE 1171
Cdd:COG3206 170 REEARKALEFLEEQLPelrkelEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1172 KE-----------ATLLQLREQ---LEGERREAVAGLEKKHST------ELEQLCSSLEAKHREVISNLQKKIEGAQQkE 1231
Cdd:COG3206 250 GSgpdalpellqsPVIQQLRAQlaeLEAELAELSARYTPNHPDvialraQIAALRAQLQQEAQRILASLEAELEALQA-R 328
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798733 1232 EAQLQESLGRAEQRthqkVHQVIEYEQELSSLLRD 1266
Cdd:COG3206 329 EASLQAQLAQLEAR----LAELPELEAELRRLERE 359
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1111-1417 |
7.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1111 QIRAEQQTALQRLREeAETLQKAERASLEQKSRRALEQLR---EQL--EAEERSAQAALRAEKEAEKEATLLQLREQLEG 1185
Cdd:PTZ00121 1568 EAKKAEEDKNMALRK-AEEAKKAEEARIEEVMKLYEEEKKmkaEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1186 ERREAVAGLEKKHSTELEQLCSSLEAKHREViSNLQKKIEGAQQKEEAQLQEslgrAEQRthQKVHQVIEYEQELssllR 1265
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKA-EEAKKAEEDEKKAAEALKKE----AEEA--KKAEELKKKEAEE----K 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1266 DKRQEVEREHERKMDKMKEehwqemaeaRERyEAEERKQRADLLGHLTGE---LERLRRAHERELESVRQEQDQQLEDlR 1342
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEE---------AKK-EAEEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEE-E 1784
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1343 RRHRDQERKLqdleaELSSRTKDVKARLAqlNVQEENmrKEKQLLLDAQRQAALE--KEEATATRRHLEEAKKEHTH 1417
Cdd:PTZ00121 1785 LDEEDEKRRM-----EVDKKIKDIFDNFA--NIIEGG--KEGNLVINDSKEMEDSaiKEVADSKNMQLEEADAFEKH 1852
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1113-1454 |
9.78e-09 |
|
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: 60.57 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1113 RAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE--------ATLLQLREQLE 1184
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEnaelqaelRTLQQAKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1185 GERREAVAGLEK--------------------KHSTELEQLCSSLEAKHREVIsNLQKKIEGAqqkeEAQLQESLGRAEQ 1244
Cdd:pfam01576 405 HKRKKLEGQLQElqarlseserqraelaeklsKLQSELESVSSLLNEAEGKNI-KLSKDVSSL----ESQLQDTQELLQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1245 RTHQKV---HQVIEYEQELSSLLrdKRQEVEREHERKMDKMKEEHWQEMaeareryeAEERKQRADLLGHLTGeLERLRR 1321
Cdd:pfam01576 480 ETRQKLnlsTRLRQLEDERNSLQ--EQLEEEEEAKRNVERQLSTLQAQL--------SDMKKKLEEDAGTLEA-LEEGKK 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1322 AHERELESVRQ---EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------RLAQLNVQEENMRKEKQLLLDAQR 1392
Cdd:pfam01576 549 RLQRELEALTQqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNlekkqkKFDQMLAEEKAISARYAEERDRAE 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1393 QAALEKE-EATATRRHLEEAKKEHTHLLESKQQLRRAIDDL---------------RVRRVeLESQVDQLQTQSQRLQ 1454
Cdd:pfam01576 629 AEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvgknvheleRSKRA-LEQQVEEMKTQLEELE 705
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1092-1480 |
1.06e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 59.92 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETlqkaerasleQKSRRALEQLREQLEAEERSAQAALRAEKEAE 1171
Cdd:COG5278 107 ARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRS----------GEGKALMDEIRARLLLLALALAALLLAAAALL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1172 KEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVH 1251
Cdd:COG5278 177 LLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1252 QVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVR 1331
Cdd:COG5278 257 LALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1332 QEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEA 1411
Cdd:COG5278 337 LAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAA 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1412 KKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1480
Cdd:COG5278 417 SAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1190-1469 |
1.25e-08 |
|
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: 59.39 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1190 AVAGLEKKHSTELEQLcssleakhREVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQ 1269
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1270 EVEREhERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAheRELESVRQEQDQQLEDLRRRhrdqe 1349
Cdd:COG4942 87 ELEKE-IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRAD----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1350 rklqdleaelssrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAalekeeatatRRHLEEAKKEHTHLLESkqqlrrai 1429
Cdd:COG4942 159 -----------------LAELAALRAELEAERAELEALLAELEEE----------RAALEALKAERQKLLAR-------- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798733 1430 ddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQN 1469
Cdd:COG4942 204 --LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1092-1374 |
1.54e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFE--NQIRAEQQTALQRLREEAETLQKAERASLEQKS----RRALEQLREQLEAEERSAQAALR 1165
Cdd:COG4913 610 AKLAALEAELAELEEELAeaEERLEALEAELDALQERREALQRLAEYSWDEIDvasaEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1166 AEKEAEK-EATLLQLREQLEgERREAVAGLEKKHsTELEQLCSSLEAKhrevisnLQKKIEGAQQKEEAQLQESLGRAEQ 1244
Cdd:COG4913 690 LEEQLEElEAELEELEEELD-ELKGEIGRLEKEL-EQAEEELDELQDR-------LEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1245 RTHQKvhqviEYEQELSSLLRDKRQEVEREHERKMDKMKE--EHWQemaeareryeaeerkqraDLLGHLTGELERLrRA 1322
Cdd:COG4913 761 DAVER-----ELRENLEERIDALRARLNRAEEELERAMRAfnREWP------------------AETADLDADLESL-PE 816
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1323 HERELESVRQEQDQQLED--LRRRHRDQERKLQDLEAELSSRTKDVKARLAQLN 1374
Cdd:COG4913 817 YLALLDRLEEDGLPEYEErfKELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1108-1635 |
1.74e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 59.99 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1108 FENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEATLLQLREQLEGE 1186
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1187 RREAVAGLEKKHSTELEQLCSSLEAKHREVI-SNLQKKIEGAQQKEEAQLQESLgRAEQRTHQKVHQVIEYEQELSSLLR 1265
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKElKELEIKREAEEEEEEELEKLQE-KLEQLEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1266 DKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELER---LRRAHERELESVRQEQDQQLEDL- 1341
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkltEEKEELEKQELKLLKDELELKKSe 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1342 RRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEK--------QLLLDAQRQAALEKEEATATRRHL----- 1408
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAlikdgvggRIISAHGRLGDLGVAVENYKVAIStaviv 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1409 EEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSL------EAEVQRKQNILKEMAAETNAPP 1482
Cdd:pfam02463 552 EVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILnlaqldKATLEADEDDKRAKVVEGILKD 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1483 HPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEgvaVRSAKEFLVRQTRSMRRRQTALKAAQQHW 1562
Cdd:pfam02463 632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---ELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1563 RHELASAQEVDEDLPGTKVLENVRKN----LDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLK 1635
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKIneelKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1332-1480 |
2.29e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1332 QEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKqllldAQRQAALEKEEATATR--RHLE 1409
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEI-----KRLELEIEEVEARIKKyeEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1410 EAK--KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1480
Cdd:COG1579 84 NVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1060-1437 |
2.31e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1060 LSFLQSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLE 1139
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1140 -QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVA------------GLEKKHSTELEQLC 1206
Cdd:COG4717 201 lEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaaallallglggSLLSLILTIAGVLF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1207 SSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELS-SLLRDKRQEVE--REHERKMDKMK 1283
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEelQELLREAEELE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1284 EEHWQEmaeareryeaEERKQRADLLGHLTGE-LERLRRAHERELEsvRQEQDQQLEDLRRRHRDQERKLQDLEAELSsr 1362
Cdd:COG4717 361 EELQLE----------ELEQEIAALLAEAGVEdEEELRAALEQAEE--YQELKEELEELEEQLEELLGELEELLEALD-- 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798733 1363 TKDVKARLAQLNVQEENMRKEKQLLLdaQRQAALEKE-EATATRRHLEEAKKEHTHLlesKQQLRRAIDDLRVRRV 1437
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELR--EELAELEAElEQLEEDGELAELLQELEEL---KAELRELAEEWAALKL 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1100-1631 |
2.54e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1100 QVQSSTEAFENQiraEQQTALQRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAeersaqaaLRAEKEaEKEATLL 1177
Cdd:TIGR04523 292 QLKSEISDLNNQ---KEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQ--------LKKELT-NSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1178 QLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQESLgraeqRTHQKVHQVIEYE 1257
Cdd:TIGR04523 360 EKQRELE-EKQNEIEKLKKENQSYKQEI-KNLESQ----INDLESKIQ-NQEKLNQQKDEQI-----KKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1258 QE-LSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghltgelerlrraheRELESVRQEQDQ 1336
Cdd:TIGR04523 428 IErLKETIIKNNSEIKDLTNQDSVKELII---------------------------------------KNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1337 QLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaQLNVQEENMrKEKQLLLDAQRQAALEKEEAtatrrhLEEAKKEht 1416
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELK----KLNEEKKEL-EEKVKDLTKKISSLKEKIEK------LESEKKE-- 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1417 hlLESK-QQLRRAI--DDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDL 1493
Cdd:TIGR04523 536 --KESKiSDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE------------KKDL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1494 RKSLGTNEnqevSSSLSLSKEgIDLSMDSVRHfLSAEGVAVRSAKEFLVRQTRSMrrrQTALKAAQQHWRHELASAQEVD 1573
Cdd:TIGR04523 602 IKEIEEKE----KKISSLEKE-LEKAKKENEK-LSSIIKNIKSKKNKLKQEVKQI---KETIKEIRNKWPEIIKKIKESK 672
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1574 EDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLN-QLESSLLEEVSDE 1631
Cdd:TIGR04523 673 TKI--DDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEiEKELKKLDEFSKE 729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1121-1462 |
2.89e-08 |
|
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: 59.20 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1121 QRLREEAETLQKAERASLEQksrRALEQLR---------------EQLEAEERSA-------QAALR-AEKEAEKEATLL 1177
Cdd:COG3096 281 RELSERALELRRELFGARRQ---LAEEQYRlvemareleelsareSDLEQDYQAAsdhlnlvQTALRqQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1178 QLREQLEgERREAVAGLEKKHSTELEQLCSSlEAKHREVISNL---QKKIEgAQQKEEAQLQ---ESLGRAEQRTHQ--- 1248
Cdd:COG3096 358 ELTERLE-EQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLadyQQALD-VQQTRAIQYQqavQALEKARALCGLpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1249 KVHQVIEYEQElsslLRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELER------- 1318
Cdd:COG3096 435 TPENAEDYLAA----FRAKEQQATeevLELEQKLSVADAARRQ-------------FEKAYELVCKIAGEVERsqawqta 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1319 ---LRRAHERELESVRQEQ-DQQLEDLRRRHRDQeRKLQDLEAELSSRTKDVKARLAQLnvqEENMRKEKQLLLDAQRQA 1394
Cdd:COG3096 498 relLRRYRSQQALAQRLQQlRAQLAELEQRLRQQ-QNAERLLEEFCQRIGQQLDAAEEL---EELLAELEAQLEELEEQA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1395 ALEKEEATATRRHLEEAKKEHTHL------------------------LESKQQLRRAIDDLRVRRVELESQVDQLQTQS 1450
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELaarapawlaaqdalerlreqsgeaLADSQEVTAAMQQLLEREREATVERDELAARK 653
|
410
....*....|..
gi 1958798733 1451 QRLQKHVSSLEA 1462
Cdd:COG3096 654 QALESQIERLSQ 665
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1109-1452 |
3.99e-08 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 57.74 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEkeaEKEATLLQLREQLEGERR 1188
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGRE---ERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1189 EAvAGLEKKHSTELEQL-CSSLEAKHR--EVISNLQKKIEGAQ---QKEEAQLQESLGRAEQRTHQKVHQVIEYEQE--L 1260
Cdd:pfam15558 96 WR-EQAEDQENQRQEKLeRARQEAEQRkqCQEQRLKEKEEELQalrEQNSLQLQERLEEACHKRQLKEREEQKKVQEnnL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1261 SSLLRDKRQEVEREHERKMDK--------MKEEHWQEMAEARERYEAEERKQRAdllghlTGELERLRRAHERELESvRQ 1332
Cdd:pfam15558 175 SELLNHQARKVLVDCQAKAEEllrrlsleQSLQRSQENYEQLVEERHRELREKA------QKEEEQFQRAKWRAEEK-EE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1333 EQDQQLEDLRrrhRDQERKLQDLEAELSSRTKDVKARLAQLNVQEEnmRKEKQLLLDAQRQAALEKEEATAT-------R 1405
Cdd:pfam15558 248 ERQEHKEALA---ELADRKIQQARQVAHKTVQDKAQRARELNLERE--KNHHILKLKVEKEEKCHREGIKEAikkkeqrS 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958798733 1406 RHLEEAKKEHthlLESKQQLRRAIDDLR--VRRVELESQVDQLQTQSQR 1452
Cdd:pfam15558 323 EQISREKEAT---LEEARKTARASFHMRekVREETNNRTFDKMALEAQL 368
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1109-1626 |
4.58e-08 |
|
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: 58.52 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLREEAETLQK--AERASLEQKSRRALEQLREQLEAEERSAQaaLRAEKEAEKEATLLQLREQLEge 1186
Cdd:TIGR00606 389 ERQIKNFHTLVIERQEDEAKTAAQlcADLQSKERLKQEQADEIRDEKKGLGRTIE--LKKEILEKKQEELKFVIKELQ-- 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1187 rrEAVAGLEK--KHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLL 1264
Cdd:TIGR00606 465 --QLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LT 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1265 RDKRQEVEReherkMDKMKEEHWQEMAEARERYEAEerKQRADLLGHLTGELERLRRaherELESVRQEQdQQLEDLRRR 1344
Cdd:TIGR00606 542 KDKMDKDEQ-----IRKIKSRHSDELTSLLGYFPNK--KQLEDWLHSKSKEINQTRD----RLAKLNKEL-ASLEQNKNH 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1345 HRDQERKLQDLEAELSSRTKDVKARLAqLNVQEENMRKEkqlLLDAQRQAALEKEEATATRRHLEEAKKEHT-------H 1417
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEE---IEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqR 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1418 LLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLRksl 1497
Cdd:TIGR00606 686 VFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE------------IPELR--- 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1498 gtNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQTrSMRRRQTALKAAQQHWRHELASAQEVDEDLP 1577
Cdd:TIGR00606 751 --NKLQKVNRDIQRLKNDIEEQETLLGTIMPEE----ESAKVCLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDLDRT 823
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958798733 1578 GTKVlenvRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLE 1626
Cdd:TIGR00606 824 VQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1123-1400 |
4.91e-08 |
|
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: 58.19 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1123 LREEAETLQKAERASLEQKSRRalEQLREQLEAEERS-AQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEK----- 1196
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQ--EDIINCKKQEERMlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKseena 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1197 -----------KHSTELEQLCSSLeakhREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVhQVIEYEQELSSLlR 1265
Cdd:pfam05483 576 rsieyevlkkeKQMKILENKCNNL----KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI-KVNKLELELASA-K 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1266 DKRQEVEREHERKMD--KMKEEHWQEMAEARERYEAEERKQRADL---LGHLTGELERLRRAHERELESVRQEQDQQLED 1340
Cdd:pfam05483 650 QKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADEAVKLQKEIdkrCQHKIAEMVALMEKHKHQYDKIIEERDSELGL 729
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1341 LRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEEnmRKEKqLLLDAQRQAALEKEE 1400
Cdd:pfam05483 730 YKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKE--EKEK-LKMEAKENTAILKDK 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1324-1477 |
6.40e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1324 ERELESVRQEQDQ---QLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEkQLLLDAQ-------RQ 1393
Cdd:COG3883 43 QAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL-DVLLGSEsfsdfldRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1394 AALEKEeATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1473
Cdd:COG3883 122 SALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
....
gi 1958798733 1474 MAAE 1477
Cdd:COG3883 201 LEAE 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1097-1475 |
1.02e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENqIRAEQQTALQRLREeAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRA-------EK 1168
Cdd:PRK01156 303 YKNDIENKKQILSN-IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDdLNNQILELEGYEMDYNSYLKSieslkkkIE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1169 EAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQR--- 1245
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK----VSSLNQRIRALRENLD-ELSRNMEMLNGQsvc 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1246 ----TH---QKVHQVIEYEQELSSLLRDKRQEVERE------HERKMDKMKEEHWQEMAEARERYEAEERKQRADLlGHL 1312
Cdd:PRK01156 456 pvcgTTlgeEKSNHIINHYNEKKSRLEEKIREIEIEvkdideKIVDLKKRKEYLESEEINKSINEYNKIESARADL-EDI 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1313 TGELERLRRAHERELESVRQEQDQQLEDLRRRHRD-----QERKLQDLEA------ELSSRTKDVKARLAQLNVQEE--- 1378
Cdd:PRK01156 535 KIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalAVISLIDIETnrsrsnEIKKQLNDLESRLQEIEIGFPddk 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1379 ---------------------NMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHT-HLLESK---QQLRRAIDDLR 1433
Cdd:PRK01156 615 syidksireieneannlnnkyNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITsRINDIEdnlKKSRKALDDAK 694
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958798733 1434 VRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMA 1475
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1086-1467 |
1.20e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.70 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1086 IreeesqrlaclraqvqssteafenQIRAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAAlR 1165
Cdd:pfam13868 41 E------------------------ERRLDEMMEEERERALEEEEEKEEE--RKEERKRYRQELEEQIEEREQKRQEE-Y 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1166 AEKEAEKEATLLQLREQLEGERREAVAGLEKKhsteleqlcsslEAKHREVI-SNLQKKIEGAQQKEEAQLQESlgraeq 1244
Cdd:pfam13868 94 EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ------------RQLREEIDeFNEEQAEWKELEKEEEREEDE------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1245 rthqkvhQVIEYEQELssllrdKRQEVEREHERKMDKMKEEHWQEMaeareryeaeerkqradllghLTGELERLRRaHE 1324
Cdd:pfam13868 156 -------RILEYLKEK------AEREEEREAEREEIEEEKEREIAR---------------------LRAQQEKAQD-EK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1325 RELESVRQE--QDQQLEDLRRRHRDQERKLQDLEAELS-SRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQA-ALEKEE 1400
Cdd:pfam13868 201 AERDELRAKlyQEEQERKERQKEREEAEKKARQRQELQqAREEQIELKERRLAEEAEREEEEFERMLRKQAEDeEIEQEE 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1401 ATATRRHLEEAKKEHTHLLESKQQLRRAiddlrVRRVELESQVDQLQTQSQRLQKhvssLEAEVQRK 1467
Cdd:pfam13868 281 AEKRRMKRLEHRRELEKQIEEREEQRAA-----EREEELEEGERLREEEAERRER----IEEERQKK 338
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1100-1466 |
1.73e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.60 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1100 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAerasleQKSRRALE-------QLREQLEAEERSAQAALRAEKEAEK 1172
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEERKGSLERA------KQYQQVIDnfpklsaELRQQLNNERDEPRSVPPNMSTDAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1173 EATLLQLREQLEGERREAVAGLEKKH--STELEQLCSSLEAKHR---EVISNLQKKIEGAQQKEEAQLqeSLGRAEQRTH 1247
Cdd:PRK10929 108 EQEILQVSSQLLEKSRQAQQEQDRAReiSDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQL--TALQAESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1248 Q-KVHqvieyEQELSSLLRDKRQEVEReherkmdkMKEEHWQEmaeareryeaeeRKQRADL-LGHLTGELERLR-RAHE 1324
Cdd:PRK10929 186 KaLVD-----ELELAQLSANNRQELAR--------LRSELAKK------------RSQQLDAyLQALRNQLNSQRqREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1325 RELESVRQEQDQQlEDLRRRHRDQERKLQDLEAElssrtkdvkarlaqLNVQEENMrkekQLLLDAQRQAA---LEKEEA 1401
Cdd:PRK10929 241 RALESTELLAEQS-GDLPKSIVAQFKINRELSQA--------------LNQQAQRM----DLIASQQRQAAsqtLQVRQA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1402 TATRRHLEEAKKEHTHLLES-------------KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1466
Cdd:PRK10929 302 LNTLREQSQWLGVSNALGEAlraqvarlpempkPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNR 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1316-1477 |
1.86e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1316 LERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE-----LSSRTKDVKARLAQLNVQeenmrkekqlLLDA 1390
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQ----------LAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1391 QRQAALEKEEATATRRHLEEAKKEHTHLLESK--QQLRRAIDDLRVRR--------------VELESQVDQLQTQ-SQRL 1453
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELaelsarytpnhpdvIALRAQIAALRAQlQQEA 311
|
170 180
....*....|....*....|....
gi 1958798733 1454 QKHVSSLEAEVQRKQNILKEMAAE 1477
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQ 335
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1099-1411 |
2.09e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.92 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1099 AQVQSSTEAFENQIRAEQ---QTALQRLREEAETLQK---AERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK 1172
Cdd:pfam09731 161 AHTDSLKEASDTAEISREkatDSALQKAEALAEKLKEvinLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQS 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1173 EATLL-QLREQLEGERREAVAGLEKKH---STELEQLCSSLEAK--------HREvISNLQKKIEGAQQKEEAQLQESLG 1240
Cdd:pfam09731 241 LAKLVdQYKELVASERIVFQQELVSIFpdiIPVLKEDNLLSNDDlnsliahaHRE-IDQLSKKLAELKKREEKHIERALE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1241 --RAEQRThQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghLTGELER 1318
Cdd:pfam09731 320 kqKEELDK-LAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--------------------------LRTELER 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1319 LRRAHERELESVRQEQDQQLEdlRRRHRD------QERKLQDLE-AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQ 1391
Cdd:pfam09731 373 QAEAHEEHLKDVLVEQEIELQ--REFLQDikekveEERAGRLLKlNELLANLKGLEKATSSHSEVEDENRKAQQLWLAVE 450
|
330 340
....*....|....*....|.
gi 1958798733 1392 R-QAALEKEEATATRRHLEEA 1411
Cdd:pfam09731 451 AlRSTLEDGSADSRPRPLVRE 471
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1390-1638 |
2.32e-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: 55.16 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1390 AQRQAALE--KEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRK 1467
Cdd:COG4942 23 AEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1468 QNILKEMAAE---TNAPPHPEPGLHIEDLrkslgtnenQEVSSSLSLskegidlsMDSVRHFLSAEGVAVRSAKEFLVRQ 1544
Cdd:COG4942 103 KEELAELLRAlyrLGRQPPLALLLSPEDF---------LDAVRRLQY--------LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1545 TRS---MRRRQTALKAAQQHWRHELASAQEVDEDLpgtkvLENVRKNLDEETKHLDEmksamrkghdlLKKKEEKLNQLE 1621
Cdd:COG4942 166 RAEleaERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAE-----------LQQEAEELEALI 229
|
250
....*....|....*..
gi 1958798733 1622 SSLLEEVSDEDTLKGSS 1638
Cdd:COG4942 230 ARLEAEAAAAAERTPAA 246
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1117-1504 |
2.77e-07 |
|
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: 55.73 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1117 QTALQRLREEAETLQKAERASleqKSRRALEQLREQLEAEERSAQAALRAEKEAEKEatlLQLREQLEGERREAVAGLEK 1196
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTV---NSIKESETGNLGSESTLLEKAKEIINIEEALKG---FQDPESELEDLAQTSDKLEK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1197 --KHSTELEQ--LCSSLEAKHR--EVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsllrdkrqE 1270
Cdd:COG5185 258 lvEQNTDLRLekLGENAESSKRlnENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELE--------E 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1271 VEREHERKMDKMKEEHWQEmaeaRERYEAEERKQRADLlGHLTGElERLRRAhERELESVRQEQDQQLEDLRRRHRDQER 1350
Cdd:COG5185 330 SKRETETGIQNLTAEIEQG----QESLTENLEAIKEEI-ENIVGE-VELSKS-SEELDSFKDTIESTKESLDEIPQNQRG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1351 KLQDLEAELSSRTKDVKARLAQLNVQ--------EENMRKEKQLLLDAQRQAALEKEEATAtrrHLEEAKKEHthllesK 1422
Cdd:COG5185 403 YAQEILATLEDTLKAADRQIEELQRQieqatssnEEVSKLLNELISELNKVMREADEESQS---RLEEAYDEI------N 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1423 QQLRRAIDDLRVRRVELESQVDQLQTQsqrLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHI---EDLRKSLGT 1499
Cdd:COG5185 474 RSVRSKKEDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIlalENLIPASEL 550
|
....*
gi 1958798733 1500 NENQE 1504
Cdd:COG5185 551 IQASN 555
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1110-1403 |
2.89e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEA--EERSAQAALRAEKEAEKEATLLQLREQLEGEr 1187
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1188 reaVAGLEKkhstELEQLcSSLEAKHREVISNLQKKiegaqqkeEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL---- 1263
Cdd:PRK03918 541 ---IKSLKK----ELEKL-EELKKKLAELEKKLDEL--------EEELAELLKELEELGFESVEELEERLKELEPFyney 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1264 --LRDKRQEVEREhERKMDKMKEEHWQ--EMAEARERYEAEERKQRADLLGHLTGE-LERLRRAH---ERELESVRQEqd 1335
Cdd:PRK03918 605 leLKDAEKELERE-EKELKKLEEELDKafEELAETEKRLEELRKELEELEKKYSEEeYEELREEYlelSRELAGLRAE-- 681
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1336 qqLEDLRRRHRDQERKLQDLEAELSSRTK------DVKARLAQLNVQEENMRKEKQLLldaqRQAALEKEEATA 1403
Cdd:PRK03918 682 --LEELEKRREEIKKTLEKLKEELEEREKakkeleKLEKALERVEELREKVKKYKALL----KERALSKVGEIA 749
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1110-1547 |
3.46e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.30 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALQRLRE--EAETLQKAERASLEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEATLLQLREQLEGE 1186
Cdd:COG5278 82 EEARAEIDELLAELRSltADNPEQQARLDELEALIDQWLAELEQVIALrRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1187 RREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD 1266
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1267 KRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHR 1346
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1347 DQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLR 1426
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1427 RAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVS 1506
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958798733 1507 SSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRS 1547
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1317-1480 |
3.73e-07 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 52.76 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1317 ERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKdvKARLAqLNVQEENMRKEKqllldAQRQAAL 1396
Cdd:pfam04012 24 EKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE--KAQAA-LTKGNEELAREA-----LAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1397 EKeeatatrrHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL--QTQSQRLQKHV---------SSLEAEVQ 1465
Cdd:pfam04012 96 EK--------QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkaRLKAAKAQEAVqtslgslstSSATDSFE 167
|
170
....*....|....*
gi 1958798733 1466 RKQNILKEMAAETNA 1480
Cdd:pfam04012 168 RIEEKIEEREARADA 182
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1308-1480 |
3.80e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.69 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1308 LLGHLTGELERLRRAHER--ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK-----------------DVKA 1368
Cdd:pfam19220 32 LIEPIEAILRELPQAKSRllELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVArlakleaalreaeaakeELRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1369 RLAQLNVQEENMrkEKQLLLDAQRQAALEKE------EATATRRHLEEAKKEhthLLESKQQLRRAIDDLRVRRVELESQ 1442
Cdd:pfam19220 112 ELRDKTAQAEAL--ERQLAAETEQNRALEEEnkalreEAQAAEKALQRAEGE---LATARERLALLEQENRRLQALSEEQ 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958798733 1443 VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1480
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEGQLAAEQAE 224
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1097-1450 |
5.23e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.22 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSS-----TEAFEnQIRAEQQTALQRLREEAETLQKAeRASLEQKSRRALEQLREQL-EAEERSAQA---ALRAE 1167
Cdd:NF041483 682 VRAEAAAAaervgTEAAE-ALAAAQEEAARRRREAEETLGSA-RAEADQERERAREQSEELLaSARKRVEEAqaeAQRLV 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1168 KEAEKEAT-LLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEA---------------------KHRE--------VI 1217
Cdd:NF041483 760 EEADRRATeLVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHaaertrteaqeeadrvrsdayAERErasedanrLR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1218 SNLQKKIEGAQQKEEAQLQESLGRAEQ-RThqkvhQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemaeaRER 1296
Cdd:NF041483 840 REAQEETEAAKALAERTVSEAIAEAERlRS-----DASEYAQRVRTEASDTLASAEQDAARTRADARED--------ANR 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1297 YEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLqdleaelssrtkdvkarLAQLNVQ 1376
Cdd:NF041483 907 IRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL-----------------IAEATGE 969
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1377 EENMRKEKQLLLDAQRQAAlEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRV----RRVELESQVDQLQTQS 1450
Cdd:NF041483 970 AERLRAEAAETVGSAQQHA-ERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKdankRRSEAAEQADTLITEA 1046
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1315-1417 |
5.36e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDL---EAELSSRTKDVKARLAQLNVQEENM-RKEKQLLLDA 1390
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLekrEEELEKKEKELEQKQQELEKKEEELeELIEEQLQEL 144
|
90 100
....*....|....*....|....*..
gi 1958798733 1391 QRQAALEKEEATAtrRHLEEAKKEHTH 1417
Cdd:PRK12704 145 ERISGLTAEEAKE--ILLEKVEEEARH 169
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1094-1476 |
6.36e-07 |
|
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: 54.96 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1094 LACLRAQVQSSTEAFENQIraEQQTALQRLREEAETLQK--AERASLEQKSRRALEQLREQLEAEERSAQA-------AL 1164
Cdd:COG3096 559 LAELEAQLEELEEQAAEAV--EQRSELRQQLEQLRARIKelAARAPAWLAAQDALERLREQSGEALADSQEvtaamqqLL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1165 RAEKEAEKEATLLQLR-EQLEGERRE--AVAGLEkkhSTELEQLCSSL-------------------------EAKHREV 1216
Cdd:COG3096 637 EREREATVERDELAARkQALESQIERlsQPGGAE---DPRLLALAERLggvllseiyddvtledapyfsalygPARHAIV 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1217 ISNLQ--KK--------------IEG-----------AQQKEEA--------QLQES-------LGRAE----------- 1243
Cdd:COG3096 714 VPDLSavKEqlagledcpedlylIEGdpdsfddsvfdAEELEDAvvvklsdrQWRYSrfpevplFGRAArekrleelrae 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1244 ------------------QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERKMDKMKeeHWQEmaeare 1295
Cdd:COG3096 794 rdelaeqyakasfdvqklQRLHQAFSQFVgghlavafapDPEAELA-ALRQRRSELERELAQHRAQEQ--QLRQ------ 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1296 ryEAEERKQRADLLGHLTGELERLRRA-HERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKAR 1369
Cdd:COG3096 865 --QLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLVAVLQSDPEQfeqLQAD 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1370 LAQLNVQEENMRKEKQLLLD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQ 1447
Cdd:COG3096 943 YLQAKEQQRRLKQQIFALSEvVQRRPHFSYEDA-------VGLLGENSDLNEKlRARLEQAEEARREAREQLRQAQAQYS 1015
|
490 500
....*....|....*....|....*....
gi 1958798733 1448 TQSQRLQKHVSSLEAEVQRKQNILKEMAA 1476
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1263-1477 |
1.45e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1263 LLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTG-ELERLRRAHERELES------VRQEQD 1335
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEErEQKRQEEYEEKLQEReqmdeiVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1336 QQLEDLRRRHRDQERKLQDLEaelssRTKDVKARLAQLNVQEEnmRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEH 1415
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEID-----EFNEEQAEWKELEKEEE--REEDERILEYLKEKAEREEEREAEREEIEEEKERE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1416 T----HLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHV-------SSLEAEVQRKQNILKEMAAE 1477
Cdd:pfam13868 186 IarlrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKArqrqelqQAREEQIELKERRLAEEAER 258
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1092-1485 |
2.12e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.91 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTE---AFENQIRAEQQTALQRL----REEAETLQKAERASLEqksrRALEQLREQLEAEERSAQAA- 1163
Cdd:NF041483 134 QELAERRQTVESHVNenvAWAEQLRARTESQARRLldesRAEAEQALAAARAEAE----RLAEEARQRLGSEAESARAEa 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1164 ----LRAEKEAEK----------EAT--LLQLREQLEGERREAvagleKKHSTEL----EQLCSSLEAKHREVISNLQKK 1223
Cdd:NF041483 210 eailRRARKDAERllnaastqaqEATdhAEQLRSSTAAESDQA-----RRQAAELsraaEQRMQEAEEALREARAEAEKV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1224 IEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER-------EHERKMDKMKEEHWQEMAEARER 1296
Cdd:NF041483 285 VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQaladaraEAEKLVAEAAEKARTVAAEDTAA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1297 YEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQErklQDLEAELSSRTKDVKARLAQLNVQ 1376
Cdd:NF041483 365 QLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQA---EQLKGAAKDDTKEYRAKTVELQEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1377 EENMRKEKQLLL------------DAQRQAALEKEEATATRRHL----------------EEAKKEHTHLLESKQQLRRA 1428
Cdd:NF041483 442 ARRLRGEAEQLRaeavaegerirgEARREAVQQIEEAARTAEELltkakadadelrstatAESERVRTEAIERATTLRRQ 521
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1429 IDDL--RVR------RVELESQVDQLQTQSQRlqkHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1485
Cdd:NF041483 522 AEETleRTRaeaerlRAEAEEQAEEVRAAAER---AARELREETERAIAARQAEAAEELTRLHTE 583
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1140-1406 |
2.17e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1140 QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQlreqlegERREAVAGLEKKHSTELEqlcssLEAKHREvISN 1219
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQRLAEYSWDEID-----VASAERE-IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1220 LQKKIEGAQQ--KEEAQLQESLGRAEQRthqkvhqvieyEQELSSLLRDKRQEvEREHERKMDKMKEEHWQEMAEARERY 1297
Cdd:COG4913 673 LEAELERLDAssDDLAALEEQLEELEAE-----------LEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1298 EAEERKQRADLlghltgeLERLRRAHERELES-VRQEQDQQLEDLRRRHRDQERKL---------------QDLEAELSS 1361
Cdd:COG4913 741 DLARLELRALL-------EERFAAALGDAVEReLRENLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1362 RTkDVKARLAQLnVQEENMRKE---KQLLLDAQRQ------AALEKEEATATRR 1406
Cdd:COG4913 814 LP-EYLALLDRL-EEDGLPEYEerfKELLNENSIEfvadllSKLRRAIREIKER 865
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1110-1469 |
2.38e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaeersaqaalraEKEAEKEATLLQLREQLEgERre 1189
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEE------------ERKEERKRYRQELEEQIE-ER-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1190 avaglEKKHSTELEQlcsslEAKHREVISNLQKKIegaqQKEEAQLQESLGRAEQRTHQKVHQVIEyeqelsslLRDKRQ 1269
Cdd:pfam13868 86 -----EQKRQEEYEE-----KLQEREQMDEIVERI----QEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1270 EVEREHERKMDKMKEEHWQEMAeareryeaeerKQRADLlghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQe 1349
Cdd:pfam13868 144 ELEKEEEREEDERILEYLKEKA-----------EREEER------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1350 rklqdleaelssrtkdvkarLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEhthlleskqqlrrai 1429
Cdd:pfam13868 206 --------------------LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER--------------- 250
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798733 1430 ddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQN 1469
Cdd:pfam13868 251 --RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1313-1473 |
2.64e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 50.15 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1313 TGELERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQeenMRKEKQLLldaQR 1392
Cdd:pfam14988 49 TAELQTQLLQKEKEQASLKKEL-QALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDREAHLQ---FLKEKALL---EK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1393 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaevQRKQNILK 1472
Cdd:pfam14988 122 QLQELRILELGERATRELKRKAQALKLAAKQALSEFCRSIKRENRQLQKELLQLIQETQALEAIKSKLE---NRKQRLKE 198
|
.
gi 1958798733 1473 E 1473
Cdd:pfam14988 199 E 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1092-1473 |
4.06e-06 |
|
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: 51.97 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSStEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSrraLEQLREQLEaEERSAQAALraekeAE 1171
Cdd:TIGR00606 591 DRLAKLNKELASL-EQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD---LERLKEEIE-KSSKQRAML-----AG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1172 KEATLLQLREQLEGERREAVAGLEKKHST--ELEQLCSSLEAKHReVISNLQKKIEGAQQKEEAQLQESLGRAEQRthQK 1249
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTeaELQEFISDLQSKLR-LAPDKLKSTESELKKKEKRRDEMLGLAPGR--QS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1250 VHQVIEyeQELSSLlRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHEReles 1329
Cdd:TIGR00606 738 IIDLKE--KEIPEL-RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ---- 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1330 vrQEQDQQLEDLRRRHRDQERKLQDLEAELssRTKDVKARLAQLNVQEENMRKEK-QLLLDAQRQAALEKEEATATRRHL 1408
Cdd:TIGR00606 811 --QAAKLQGSDLDRTVQQVNQEKQEKQHEL--DTVVSKIELNRKLIQDQQEQIQHlKSKTNELKSEKLQIGTNLQRRQQF 886
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1409 EEAKKEhthLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1473
Cdd:TIGR00606 887 EEQLVE---LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1314-1478 |
4.91e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1314 GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV---KARLAQLNVQEENMRKEKQLLLDA 1390
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHeelEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1391 -----QRQAALEKEEATATRRHLEeakkEHTHLLESKQQLRRAIDDLRvrrvELESQVDQLQTQSQRLQKHVSSLEAEVQ 1465
Cdd:pfam07888 124 raaheARIRELEEDIKTLTQRVLE----RETELERMKERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170
....*....|...
gi 1958798733 1466 RKQNILKEMAAET 1478
Cdd:pfam07888 196 ELRNSLAQRDTQV 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1097-1373 |
5.18e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQI--RAEQQTALQRLREEAETLQKaERASLeQKSRRALEQLREQLEAEERSAQAALraekeAEKEA 1174
Cdd:COG4372 78 LEEELEELNEQLQAAQaeLAQAQEELESLQEEAEELQE-ELEEL-QKERQDLEQQRKQLEAQIAELQSEI-----AEREE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1175 TLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQkEEAQLQESLGRAEQRTHQKVHQVI 1254
Cdd:COG4372 151 ELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA-EKLIESLPRELAEELLEAKDSLEA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1255 EYEQELSSLLRDKRQEVEREHERKMDKMKEehwqemAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQ 1334
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKE------IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLN 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958798733 1335 DQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQL 1373
Cdd:COG4372 304 LAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1304-1642 |
5.20e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1304 QRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQL--------NV 1375
Cdd:pfam02463 184 NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIesskqeieKE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1376 QEENMRKEKQLLLDAQRQAALEKEEAtatrrhleeakkehtHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQK 1455
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELK---------------LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1456 HVSSLEAEVQRKQNILKEMAAETNapphpEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEgVAVR 1535
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKRE-----AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-LKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1536 SAKEFLVRQTRSmRRRQTALKAAQQHWRHELASAQEVDEDLPGTkvLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEE 1615
Cdd:pfam02463 403 EEKEAQLLLELA-RQLEDLLKEEKKEELEILEEEEESIELKQGK--LTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
330 340
....*....|....*....|....*..
gi 1958798733 1616 KLNQLESSLLEEVSDEDTLKGSSIKKV 1642
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1143-1473 |
6.18e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1143 RRALEQLREQLEAE-----ERSAQAALRAEK--------------------EAEKEATLLQLREQLeGERREAVAGLEKK 1197
Cdd:PRK04863 781 RAAREKRIEQLRAEreelaERYATLSFDVQKlqrlhqafsrfigshlavafEADPEAELRQLNRRR-VELERALADHESQ 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1198 HSTELEQLcssleAKHREVISNLQKKI-------EGAQQKEEAQLQESLGRAEQ-----RTHQKvhQVIEYEQELSSLlr 1265
Cdd:PRK04863 860 EQQQRSQL-----EQAKEGLSALNRLLprlnllaDETLADRVEEIREQLDEAEEakrfvQQHGN--ALAQLEPIVSVL-- 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1266 dkrqeveREHERKMDKMKEEHWQemaearERYEAEERKQRADLLGHLtgeleRLRRAHERELESVR-QEQDQQL-EDLRR 1343
Cdd:PRK04863 931 -------QSDPEQFEQLKQDYQQ------AQQTQRDAKQQAFALTEV-----VQRRAHFSYEDAAEmLAKNSDLnEKLRQ 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1344 RHRDQERKLQDLEAELssrtKDVKARLAQLNvqeenmrkekqllldaQRQAALeKEEATATRRHLEEAKKEHTHL----- 1418
Cdd:PRK04863 993 RLEQAEQERTRAREQL----RQAQAQLAQYN----------------QVLASL-KSSYDAKRQMLQELKQELQDLgvpad 1051
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1419 --LESKqqlrraiddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1473
Cdd:PRK04863 1052 sgAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1097-1640 |
6.45e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQTaLQRLREEAETLQKaeraslEQKSRRALEQLREQleaeERSAQAALRAEKEAEKEATL 1176
Cdd:pfam10174 47 LRKEEAARISVLKEQYRVTQEE-NQHLQLTIQALQD------ELRAQRDLNQLLQQ----DFTTSPVDGEDKFSTPELTE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1177 LQ-LREQLEGERreavaglekkHSTELEQLCSSLEakHREVISNLQKKIEGAQQKEEAQLQESL------GRAEQRTHQK 1249
Cdd:pfam10174 116 ENfRRLQSEHER----------QAKELFLLRKTLE--EMELRIETQKQTLGARDESIKKLLEMLqskglpKKSGEEDWER 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1250 VHQVIEYE---QELSSLLRDKRQEvereherkMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERE 1326
Cdd:pfam10174 184 TRRIAEAEmqlGHLEVLLDQKEKE--------NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1327 LESV----------RQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA---RLAQLNVQEENMRKEKQLL---LDA 1390
Cdd:pfam10174 256 VQMLktngllhtedREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLAlqtKLETLTNQNSDCKQHIEVLkesLTA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1391 QRQ-AALEKEEATATRRHLEEakKEhTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQR---LQKHVSSLEAEVQR 1466
Cdd:pfam10174 336 KEQrAAILQTEVDALRLRLEE--KE-SFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKinvLQKKIENLQEQLRD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1467 KQNILKEM----------------AAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDL--SMDSVRHFLS 1528
Cdd:pfam10174 413 KDKQLAGLkervkslqtdssntdtALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLkeKVSALQPELT 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1529 AEGVAVRSAKEFLVRQTRSMRRRQTALK----AAQQHWR------------HELASAQEVDEDLPG-TKVLEN-VRKNLD 1590
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKsleiAVEQKKEecsklenqlkkaHNAEEAVRTNPEINDrIRLLEQeVARYKE 572
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1591 EETK---HLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEdTLKGSSIK 1640
Cdd:pfam10174 573 ESGKaqaEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQ-NKKVANIK 624
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1097-1285 |
6.99e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.13 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSR-----RALEQLREQLEAEERSAQAALRAEKEaE 1171
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERleeeiTKEELLQELLLKEEELEEQKLKDELE-S 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1172 KEATLLQLREQLEGERREAVAGLEKKhstELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVH 1251
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKE---NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
170 180 190
....*....|....*....|....*....|....
gi 1958798733 1252 QVIEYEQELSSLLRDKRQEVEREHERKMDKMKEE 1285
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1114-1393 |
7.58e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1114 AEQQTALQRLREEAETLQKAERASLEQkSRRALEQLREQLEAeersaqaaLRAEKeAEKEATLLQLREQLEGERREAVAG 1193
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELES-LKKENKDLKEKVSA--------LQPEL-TEKESSLIDLKEHASSLASSGLKK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1194 LEKKHSTELE-----QLCSSLEAKHREV----------------ISNLQKkiEGAQQKEEA--------QLQESLGRAEQ 1244
Cdd:pfam10174 516 DSKLKSLEIAveqkkEECSKLENQLKKAhnaeeavrtnpeindrIRLLEQ--EVARYKEESgkaqaeveRLLGILREVEN 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1245 RTHQKVHQVIEYEQELSSLLRDKRQEVeREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRR--- 1321
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKV-ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQeld 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1322 AHERELESVRQ---EQDQQLEDLRRRHRDQ-----ERKLQDLEAELSSrtKDVKARLAQLN------VQEENM--RKEKQ 1385
Cdd:pfam10174 673 ATKARLSSTQQslaEKDGHLTNLRAERRKQleeilEMKQEALLAAISE--KDANIALLELSsskkkkTQEEVMalKREKD 750
|
....*...
gi 1958798733 1386 LLLDAQRQ 1393
Cdd:pfam10174 751 RLVHQLKQ 758
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1119-1633 |
7.98e-06 |
|
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: 51.20 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1119 ALQRLREEAETLQK------AERASLEQKSRRALEqLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVA 1192
Cdd:TIGR00606 187 ALETLRQVRQTQGQkvqehqMELKYLKQYKEKACE-IRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1193 GLE------KKHSTELEQLCSSLEAKHREVISNLQKkiegaQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD 1266
Cdd:TIGR00606 266 KLDneikalKSRKKQMEKDNSELELKMEKVFQGTDE-----QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1267 KRQEVEREHERKMDKMKEEHWQEMAEAReryeaeerkQRADLLGHLtgELERLRRAHERELESvrqeqDQQLEDLRRRHR 1346
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHIRARDS---------LIQSLATRL--ELDGFERGPFSERQI-----KNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1347 DQERKLQDLEAELSSrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAALEKE--EATATRRHLEEAKKEHTHLLESKQQ 1424
Cdd:TIGR00606 405 DEAKTAAQLCADLQS-----KERLKQEQADEIRDEKKGLGRTIELKKEILEKKqeELKFVIKELQQLEGSSDRILELDQE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1425 LRRAIDDLrvRRVELESQVDQLQTQSQRLQKHvsslEAEVQRKQNILKEMAAETNAppHPEPGLHIEDLRKSLGTNENQE 1504
Cdd:TIGR00606 480 LRKAEREL--SKAEKNSLTETLKKEVKSLQNE----KADLDRKLRKLDQEMEQLNH--HTTTRTQMEMLTKDKMDKDEQI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1505 VSSSLSLSKEGIDLSMD-SVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEvdEDLPGTKVLE 1583
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE--QLSSYEDKLF 629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1584 NVRKNLDEETKhLDEMKSAMRKGHDLLKKKEEKLNqLESSLLEEVSDEDT 1633
Cdd:TIGR00606 630 DVCGSQDEESD-LERLKEEIEKSSKQRAMLAGATA-VYSQFITQLTDENQ 677
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1110-1398 |
8.66e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 50.04 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALQRLREEAETLQKAERASLEQKSR------------RALEQLREQ--LEAEERSAQAA---LRAEKEAEK 1172
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLERARQEAEQRkqcqeqrlkekeEELQALREQnsLQLQERLEEAChkrQLKEREEQK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1173 EATLLQLREQLEGERREAvaGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE-------GAQQKEEAQLQESLGRAEQR 1245
Cdd:pfam15558 168 KVQENNLSELLNHQARKV--LVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEerhrelrEKAQKEEEQFQRAKWRAEEK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1246 THQ-KVHQvieyeqELSSLLRDKRQEVEREHERKMDKMKEEHWQEmaeareryeAEERKQRADLLghLTGELERLRRAHE 1324
Cdd:pfam15558 246 EEErQEHK------EALAELADRKIQQARQVAHKTVQDKAQRARE---------LNLEREKNHHI--LKLKVEKEEKCHR 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1325 RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaqlnvQEENMRKEKQLLLDAQRQAALEK 1398
Cdd:pfam15558 309 EGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVR--------EETNNRTFDKMALEAQLHASLQR 374
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1097-1253 |
9.93e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.67 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQTalqrLREEAETLQKAERASLEQK-SRRALEQLREQLEAE----ERSAQAALRAEKE-- 1169
Cdd:COG1842 10 IRANINALLDKAEDPEKMLDQA----IRDMEEDLVEARQALAQVIaNQKRLERQLEELEAEaekwEEKARLALEKGREdl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1170 ----AEKEATLLQLREQLEgerreavaglekkhsTELEQLcSSLEAKHREVISNLQKKIEGA-QQKEEAQLQESLGRAEQ 1244
Cdd:COG1842 86 areaLERKAELEAQAEALE---------------AQLAQL-EEQVEKLKEALRQLESKLEELkAKKDTLKARAKAAKAQE 149
|
....*....
gi 1958798733 1245 RTHQKVHQV 1253
Cdd:COG1842 150 KVNEALSGI 158
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1115-1275 |
1.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQK-AERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLL--QLREQLEGERREAV 1191
Cdd:COG4717 344 DRIEELQELLREAEELEEeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELLE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1192 AGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQE------LSSLLR 1265
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEwaalklALELLE 503
|
170
....*....|
gi 1958798733 1266 DKRQEVEREH 1275
Cdd:COG4717 504 EAREEYREER 513
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1316-1470 |
1.28e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1316 LERLRRAHERELESVRQEqDQQLedlrrrhRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRqAA 1395
Cdd:smart00787 142 LEGLKEGLDENLEGLKED-YKLL-------MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK-EK 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1396 LEKEEatatrRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH----VSSLEAEVQRKQNI 1470
Cdd:smart00787 213 LKKLL-----QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtfkeIEKLKEQLKLLQSL 286
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.40e-05 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 43.26 E-value: 1.40e-05
10 20 30
....*....|....*....|....*....|
gi 1958798733 58 LPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1243-1470 |
1.42e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1243 EQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHW----QEMAEARERYEAEERKQRADLLGHLTgELER 1318
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQLAEARAELA-EAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1319 LRRAHERELESVRQE-----QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKE-KQLLLDAQR 1392
Cdd:COG3206 241 RLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1393 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRraiddlRVRRvELESQVDQLQTQSQRLQkhvsslEAEVQRKQNI 1470
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELR------RLER-EVEVARELYESLLQRLE------EARLAEALTV 385
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1116-1641 |
1.57e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1116 QQTALQRLREEAETLQKAErasleQKSRRALEQLREQLEAEERSAqAALRAEKEA------EKEATLLQLREQLE--GER 1187
Cdd:pfam10174 301 KESELLALQTKLETLTNQN-----SDCKQHIEVLKESLTAKEQRA-AILQTEVDAlrlrleEKESFLNKKTKQLQdlTEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1188 REAVAGlekkhstELEQLCSSLEAKHREvISNLQKKIEgaqqkeeaqlqeslgraeqrthqkvhqvieyeqELSSLLRDK 1267
Cdd:pfam10174 375 KSTLAG-------EIRDLKDMLDVKERK-INVLQKKIE---------------------------------NLQEQLRDK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1268 RQEVEREHERkMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgeLERLRRAHERElesvRQEQDQQLEDLRRRHRD 1347
Cdd:pfam10174 414 DKQLAGLKER-VKSLQTDSSNTDTALTTLEEALSEKERI---------IERLKEQRERE----DRERLEELESLKKENKD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1348 QERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAkkehtHLLESKQQLRR 1427
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA-----HNAEEAVRTNP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1428 AIDDlRVRrvELESQVDQLQTQSQRLQkhvssleAEVQRKQNILKEMAAETNapphpepglhieDLRKSLGTNENQEVSS 1507
Cdd:pfam10174 555 EIND-RIR--LLEQEVARYKEESGKAQ-------AEVERLLGILREVENEKN------------DKDKKIAELESLTLRQ 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1508 SLSLSKEGIDLSmdsvrhflSAEGVAVRSAKEFLVRQtrsmRRRQTALKAAQQHWRHE--LASAQEVDEDLPGTKV-LEN 1584
Cdd:pfam10174 613 MKEQNKKVANIK--------HGQQEMKKKGAQLLEEA----RRREDNLADNSQQLQLEelMGALEKTRQELDATKArLSS 680
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1585 VRKNLDEETKHLDEMKSAMRkghdllKKKEEKLNQLESSLLEEVSDEDT----LKGSSIKK 1641
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERR------KQLEEILEMKQEALLAAISEKDAnialLELSSSKK 735
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1092-1469 |
1.83e-05 |
|
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: 49.95 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFEnQIRaEQQTALQRLREEA-----ETLQ------KAERASLEQKSR------RALEQLREQLE 1154
Cdd:COG3096 850 RELAQHRAQEQQLRQQLD-QLK-EQLQLLNKLLPQAnlladETLAdrleelREELDAAQEAQAfiqqhgKALAQLEPLVA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1155 AEERSAQ--AALRAEKEAEKEaTLLQLREQLEG-----ERREAVAglekkHSTELEQLCSSleakhreviSNLQKKIEga 1227
Cdd:COG3096 928 VLQSDPEqfEQLQADYLQAKE-QQRRLKQQIFAlsevvQRRPHFS-----YEDAVGLLGEN---------SDLNEKLR-- 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1228 QQKEEAQLQESlgRAEQRTHQKVHQVIEYEQELSSLL--RDKRQEVEREHERKMdkmkeehwQEMAEARERYEAEERKQR 1305
Cdd:COG3096 991 ARLEQAEEARR--EAREQLRQAQAQYSQYNQVLASLKssRDAKQQTLQELEQEL--------EELGVQADAEAEERARIR 1060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1306 ADllgHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELS------------SRTKDVKARLA-- 1371
Cdd:COG3096 1061 RD---ELHEELSQNR-SRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcavlrlARDNDVERRLHrr 1136
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1372 QLNVQE-ENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHL---LESKQQLRRAI-------DD----LRVRR 1436
Cdd:COG3096 1137 ELAYLSaDELRSMSDKALGALRLAVADNEHLRDALRLSEDPRRPERKVqfyIAVYQHLRERIrqdiirtDDpveaIEQME 1216
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958798733 1437 VELESQVDQLQTQSQRLQkhVSS------LEAEVQRKQN 1469
Cdd:COG3096 1217 IELARLTEELTSREQKLA--ISSesvaniIRKTIQREQN 1253
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1091-1235 |
2.06e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAE-----ERSAQAALR 1165
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEER-LVQKEEQLDARaekldNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1166 AEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELeqLCSSLEAKhreviSNLQKKIEGAQQKEEAQL 1235
Cdd:PRK12705 111 EKALSARELELEELEKQLD-NELYRVAGLTPEQARKL--LLKLLDAE-----LEEEKAQRVKKIEEEADL 172
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1265-1574 |
2.18e-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: 49.84 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1265 RDKRQEVE---REHERKMDKMKEEH----WQEmaeareryeaeERKQRADLLGHLTGeLERLRRAHERELESVRQEQDQQ 1337
Cdd:pfam12128 217 RLNRQQVEhwiRDIQAIAGIMKIRPeftkLQQ-----------EFNTLESAELRLSH-LHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1338 LEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQ-RQAALEKEEATATRRHLEEAKKEHT 1416
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1417 HLLESKQQLRRAIDDLRVRRVE-----LESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIE 1491
Cdd:pfam12128 365 ALTGKHQDVTAKYNRRRSKIKEqnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1492 DLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLvRQTRSmrRRQTALKAAQQHWRHELASAQE 1571
Cdd:pfam12128 445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSEL-RQARK--RRDQASEALRQASRRLEERQSA 521
|
...
gi 1958798733 1572 VDE 1574
Cdd:pfam12128 522 LDE 524
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1306-1500 |
2.33e-05 |
|
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: 48.60 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1306 ADLLGHLTGELERLRRAHERELESVRQEQDQQ---LEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqEENMRK 1382
Cdd:pfam09787 28 ASLKEGSGVEGLDSSTALTLELEELRQERDLLreeIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQEL---EEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDAQRQAALEKEEataTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR----------RVELESQVDQL------ 1446
Cdd:pfam09787 105 ERSARREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQltsksqssssQSELENRLHQLtetliq 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1447 -QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphPEPGLHIEDLRKSLGTN 1500
Cdd:pfam09787 182 kQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS----NGTSINMEGISDGEGTR 232
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1324-1478 |
2.74e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1324 ERELESVRQEQDQQLEDlrrrhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLlldaqrqaaLEKEEata 1403
Cdd:PRK12704 48 KKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL---------LEKRE--- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1404 trRHLEEAKKEHTHLLESKQQLRRAIDDLRvrrvelESQVDQLQtqsqrlqkHVSSLEAEvQRKQNILKEMAAET 1478
Cdd:PRK12704 110 --EELEKKEKELEQKQQELEKKEEELEELI------EEQLQELE--------RISGLTAE-EAKEILLEKVEEEA 167
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1106-1278 |
3.45e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAEERSAQaalRAEKEAE-KEATLLQLREQLE 1184
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLDRKLELLE---KREEELEkKEKELEQKQQELE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1185 gERREAVAGLEKKHSTELEQlcssleakhrevISNLqkkiegaqQKEEAQlQESLGRAEQrthqkvhqviEYEQELSSLL 1264
Cdd:PRK12704 128 -KKEEELEELIEEQLQELER------------ISGL--------TAEEAK-EILLEKVEE----------EARHEAAVLI 175
|
170
....*....|....
gi 1958798733 1265 RDKRQEVEREHERK 1278
Cdd:PRK12704 176 KEIEEEAKEEADKK 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1127-1411 |
3.50e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1127 AETLQKAERASLEQKSRRALEQLREQLEaeerSAQAALRaekeaEKEATLLQLREQlegerrEAVAGLEKKHSTELEQLc 1206
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLP----ELRKELE-----EAEAALEEFRQK------NGLVDLSEEAKLLLQQL- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1207 SSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQRTHQKVhqvieyEQELSSLLRDKRQEVEREHERKMDKMKEEH 1286
Cdd:COG3206 222 SELESQ----LAEARAELAEAEARLA-ALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1287 wQEMAEareryeaeerkqradllghLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELsSRTKDV 1366
Cdd:COG3206 291 -PDVIA-------------------LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPEL 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798733 1367 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEA 1411
Cdd:COG3206 350 EAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1320-1626 |
4.76e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1320 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEEN-------MRKEKQLLLDAQR 1392
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnrasmQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1393 QAALEKEEATATRRhLEEakkehthLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILK 1472
Cdd:PLN02939 116 QTNSKDGEQLSDFQ-LED-------LVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1473 eMAAETNAppHPE-PGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVR-----HFLSAEGVAVRSAKEFLVRqtr 1546
Cdd:PLN02939 188 -LAAQEKI--HVEiLEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLlkddiQFLKAELIEVAETEERVFK--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1547 sMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKV------LENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEklnqL 1620
Cdd:PLN02939 262 -LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYdcwwekVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK----L 336
|
....*.
gi 1958798733 1621 ESSLLE 1626
Cdd:PLN02939 337 EASLKE 342
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1091-1260 |
5.15e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.72 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKA---ERASLEQKSRRALEQLREQLEAEERSAQAALRAE 1167
Cdd:pfam01442 10 STYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKlepYLEELQAKLGQNVEELRQRLEPYTEELRKRLNAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1168 KEaekeatllQLREQLEgerrEAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTH 1247
Cdd:pfam01442 90 AE--------ELQEKLA----PYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQ 157
|
170
....*....|...
gi 1958798733 1248 QKVHQVIEYEQEL 1260
Cdd:pfam01442 158 ELREKLEPQAEDL 170
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
5.16e-05 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 41.74 E-value: 5.16e-05
10 20 30
....*....|....*....|....*....|.
gi 1958798733 59 PKGWKPCQNITGDLYYFNFDTGQSIWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1380-1636 |
6.35e-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: 47.45 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1380 MRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1459
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1460 LEAEVQRKQNilkemaaetnapphpepglHIEDLRKSLGTNENQEVSSSLSLSKEGidlSMDSVRHFLSAEGV--AVRSA 1537
Cdd:COG4942 81 LEAELAELEK-------------------EIAELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFldAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1538 K------EFLVRQTRSMRRRQTALKAAQQhwrhELASAQevdedlpgtKVLENVRKNLDEETKHLDEMKSAMRKghdLLK 1611
Cdd:COG4942 139 QylkylaPARREQAEELRADLAELAALRA----ELEAER---------AELEALLAELEEERAALEALKAERQK---LLA 202
|
250 260
....*....|....*....|....*
gi 1958798733 1612 KKEEKLNQLESSLLEEVSDEDTLKG 1636
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEA 227
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1109-1236 |
7.05e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAE---QQTALQRLREEAETLQKAERASL---EQKSRRALEQLREQLEAEersaqaalRAEKEAEKEATLLQLREQ 1182
Cdd:COG2268 205 EAEAEREteiAIAQANREAEEAELEQEREIETAriaEAEAELAKKKAEERREAE--------TARAEAEAAYEIAEANAE 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1183 LEGERREAVAglEKKHSTELEQlcSSLEAKHREVISNLQKKIEG----AQQKEEAQLQ 1236
Cdd:COG2268 277 REVQRQLEIA--EREREIELQE--KEAEREEAELEADVRKPAEAekqaAEAEAEAEAE 330
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1227-1459 |
7.41e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1227 AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--EHERKMD---KMKEEHWQEMAEARERYEAEE 1301
Cdd:PRK10929 20 ATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERakQYQQVIDnfpKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1302 RKQRADllghltgELE-RLRRAHERELESVR---QEQD-------------QQLEDLRRRHRDQERKLQDL--------E 1356
Cdd:PRK10929 100 PNMSTD-------ALEqEILQVSSQLLEKSRqaqQEQDrareisdslsqlpQQQTEARRQLNEIERRLQTLgtpntplaQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1357 AELSSRTKDVKARLAQLNvqeenmrkekQLLLdAQRQAALEKEEAtatRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRR 1436
Cdd:PRK10929 173 AQLTALQAESAALKALVD----------ELEL-AQLSANNRQELA---RLRSELAKKRSQQLDAYLQALRNQLNSQRQRE 238
|
250 260
....*....|....*....|....*
gi 1958798733 1437 VE--LESqVDQLQTQSQRLQKHVSS 1459
Cdd:PRK10929 239 AEraLES-TELLAEQSGDLPKSIVA 262
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1320-1616 |
9.47e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1320 RRAHERELESVRQEQDQQLEDLRRRhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKE 1399
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRRR--DQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1400 EATAT---------RRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1470
Cdd:pfam15558 94 SRWREqaedqenqrQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1471 LKEMAaetnapphpepgLHieDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFL---SAEGVAVRSAKEflvrQTRS 1547
Cdd:pfam15558 174 LSELL------------NH--QARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLveeRHRELREKAQKE----EEQF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1548 MRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEK 1616
Cdd:pfam15558 236 QRAKWRAEEKEEERQEHKEALAELADRKI--QQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEK 302
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1091-1365 |
1.01e-04 |
|
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: 47.66 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleaEERSAQAALRAEKEA 1170
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL---PKELLASRQLALQKM 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1171 EKEatllqlREQLEGERREAVAGLEKKHSTELEQLCSSleaKHREVISNLQKKIEGAQQKEEAQLQESLGRAE-QRTHQK 1249
Cdd:TIGR00618 686 QSE------KEQLTYWKEMLAQCQTLLRELETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMhQARTVL 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1250 VHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHE----- 1324
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsr 836
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958798733 1325 -RELESVRQEQDQQLEDLRRRHRDQERKLQDlEAELSSRTKD 1365
Cdd:TIGR00618 837 lEEKSATLGEITHQLLKYEECSKQLAQLTQE-QAKIIQLSDK 877
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1106-1201 |
1.23e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRAEQQTALQRLREEAETLQKAERASLE-----QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLR 1180
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREVQRQLEIAEREreielQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAK 335
|
90 100
....*....|....*....|.
gi 1958798733 1181 EQLEGERREAVAGLEKKHSTE 1201
Cdd:COG2268 336 GLAEAEGKRALAEAWNKLGDA 356
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1082-1440 |
1.28e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1082 EETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTAlQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERS-- 1159
Cdd:COG3064 32 EQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAA-ELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAaa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1160 --------AQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKE 1231
Cdd:COG3064 111 ekaaaaaeKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1232 EAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--------EHERKMDKMKEEHWQEMAEARERYEAEERK 1303
Cdd:COG3064 191 EAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAalaaveatEEAALGGAEEAADLAAVGVLGAALAAAAAG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1304 QRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAElSSRTKDVKARLAQLNVQEENMRKE 1383
Cdd:COG3064 271 AAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG-ALVVRGGGAASLEAALSLLAAGAA 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1384 KQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELE 1440
Cdd:COG3064 350 AAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLD 406
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1102-1385 |
1.42e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1102 QSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKsRRALEQLREQLEAEERSAQAALRAEKEAEKEATL--LQL 1179
Cdd:pfam02029 22 QKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEE-EAFLDRTAKREERRQKRLQEALERQKEFDPTIADekESV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1180 REQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQE 1259
Cdd:pfam02029 101 AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1260 LSSLLRDKRQEVEREH---------ERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGE----LERLRR----A 1322
Cdd:pfam02029 181 DEKIKKEKKVKYESKVfldqkrghpEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRRrrqeK 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798733 1323 HERELESVRQEQ---DQQLEDLRRRhRDQERKLqdLEAELSSRTKDVKARLAQLnvqEENMRKEKQ 1385
Cdd:pfam02029 261 ESEEFEKLRQKQqeaELELEELKKK-REERRKL--LEEEEQRRKQEEAERKLRE---EEEKRRMKE 320
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1098-1277 |
1.46e-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: 46.30 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1098 RAQVQSSTEAFENQIRAEQQtALQRLREEAETLQKaERASLEQKSRRALEQLRE-------------QLEAEERSAQAAL 1164
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEK-ELAALKKEEKALLK-QLAALERRIAALARRIRAleqelaaleaelaELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1165 RAEKEAEKE--------------------------ATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSLEAKHREVIS 1218
Cdd:COG4942 100 EAQKEELAEllralyrlgrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1219 NLQKKIE-----GAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHER 1277
Cdd:COG4942 179 LLAELEEeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1092-1285 |
1.70e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFEN------QIRAEQQTALQRLREEAETLQKAerasleQKSRRALEQLREQLEAEERSAQAALr 1165
Cdd:COG4372 45 EELEQLREELEQAREELEQleeeleQARSELEQLEEELEELNEQLQAA------QAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1166 aeKEAEKE-ATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQ 1244
Cdd:COG4372 118 --EELQKErQDLEQQRKQLEAQIAELQSEIAER-EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958798733 1245 RthqKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEE 1285
Cdd:COG4372 195 N---AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1104-1225 |
1.97e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1104 STEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRaekeaekeatllQLREQ 1182
Cdd:cd16269 178 SKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEqQRELEQKLEDQERSYEEHLR------------QLKEK 245
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798733 1183 LEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE 1225
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1208-1373 |
2.14e-04 |
|
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: 45.52 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1208 SLEAKHREVISNLQKKIEGAQQKEE--AQLQES---------------LGRAEQRTHQKVHQVIEYEQELSSLlRDKRQE 1270
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKliASLKEGsgvegldsstaltleLEELRQERDLLREEIQKLRGQIQQL-RTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1271 VEREHERKMDKMKEehwqemaeareryeaeerkQRADLLGHLTGElERLRRAHERELESVRQEQDQQLEDLRR------- 1343
Cdd:pfam09787 80 LEAQQQEEAESSRE-------------------QLQELEEQLATE-RSARREAEAELERLQEELRYLEEELRRskatlqs 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958798733 1344 RHRDQERKLQDLEAELSSRT------KDVKARLAQL 1373
Cdd:pfam09787 140 RIKDREAEIEKLRNQLTSKSqssssqSELENRLHQL 175
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1097-1341 |
2.20e-04 |
|
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: 46.48 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQtaLQRLREEAETL-------QKA-----ERASLEQKSRRALEQLREQLEAEERSA---- 1160
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEAR--LEAAEEEVDSLksqladyQQAldvqqTRAIQYQQAVQALEKARALCGLPDLTPenae 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1161 --QAALRAeKEAEKEATLLQLREQLE------GERREAVAGLEK---------KHSTELEQLCSSLEAKHR-EVISNLQK 1222
Cdd:COG3096 441 dyLAAFRA-KEQQATEEVLELEQKLSvadaarRQFEKAYELVCKiageversqAWQTARELLRRYRSQQALaQRLQQLRA 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1223 KIEGAQQKEEAQ-----LQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMD---------------KM 1282
Cdd:COG3096 520 QLAELEQRLRQQqnaerLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSElrqqleqlrarikelAA 599
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1283 KEEHW---QEMAEARERYEAEERKQRADLLGHLTGELERLRRA--HERELESVRQEQDQQLEDL 1341
Cdd:COG3096 600 RAPAWlaaQDALERLREQSGEALADSQEVTAAMQQLLEREREAtvERDELAARKQALESQIERL 663
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1109-1196 |
2.44e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.81 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTAlQRLREEAETLQK---AERASLEQKSRRALEQLREqlEAEERSAQAALRAEKEAEKEatLLQLREQLEG 1185
Cdd:cd06503 32 EEKIAESLEEA-EKAKEEAEELLAeyeEKLAEARAEAQEIIEEARK--EAEKIKEEILAEAKEEAERI--LEQAKAEIEQ 106
|
90
....*....|.
gi 1958798733 1186 ERREAVAGLEK 1196
Cdd:cd06503 107 EKEKALAELRK 117
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1124-1197 |
2.67e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 43.23 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1124 REE--AETLQKAERASLEQKsrRALEQLREQL------------EAEERSAQ--AALRAEKEAEKEATLLQLREQLEGER 1187
Cdd:PRK05759 36 RQKkiADGLAAAERAKKELE--LAQAKYEAQLaearaeaaeiieQAKKRAAQiiEEAKAEAEAEAARIKAQAQAEIEQER 113
|
90
....*....|
gi 1958798733 1188 REAVAGLEKK 1197
Cdd:PRK05759 114 KRAREELRKQ 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1092-1233 |
2.67e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEErsaqaalRAEKEAE 1171
Cdd:COG1579 38 DELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLK-------RRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798733 1172 KEatLLQLREQLEgERREAVAGLEKKHStELEQLCSSLEAKHREVISNLQKKIEGAQQKEEA 1233
Cdd:COG1579 110 DE--ILELMERIE-ELEEELAELEAELA-ELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1315-1442 |
2.76e-04 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 43.16 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSR--------------TKDVKARLAQLNVQEENM 1380
Cdd:pfam07321 3 RLLRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEeqrlyaeiqgklvlLKELEKVKQQVALLRENE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798733 1381 RKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1442
Cdd:pfam07321 83 ADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELE 144
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
2.89e-04 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 39.89 E-value: 2.89e-04
10 20 30
....*....|....*....|....*....|.
gi 1958798733 57 PLPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1311-1445 |
3.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1311 HLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER--------KLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1382
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRqearrereELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDA-------QRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIddlRVRRVELESQVDQ 1445
Cdd:PRK12705 110 REKALSAReleleelEKQLDNELYRVAGLTP--EQARKLLLKLLDAELEEEKAQ---RVKKIEEEADLEA 174
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1320-1477 |
3.80e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 45.42 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1320 RRAHERELESVRQEQDQQLEDLRRRhrDQERK-LQDLEAELSSRTKDVKARlaqlnvQEENMRKEKQLLLDAQRQAAL-- 1396
Cdd:pfam10168 556 REEIQKRVKLLKLQKEQQLQELQSL--EEERKsLSERAEKLAEKYEEIKDK------QEKLMRRCKKVLQRLNSQLPVls 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1397 --EKEEatatrrhleeaKKEHTHLLESKQQLRRAIDDLRVRrveLESQVDQLQTQSQRLQKHVSSLEAEvQRK--QNILK 1472
Cdd:pfam10168 628 daEREM-----------KKELETINEQLKHLANAIKQAKKK---MNYQRYQIAKSQSIRKKSSLSLSEK-QRKtiKEILK 692
|
....*
gi 1958798733 1473 EMAAE 1477
Cdd:pfam10168 693 QLGSE 697
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1118-1466 |
3.91e-04 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 45.57 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1118 TALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKK 1197
Cdd:COG2203 342 IAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1198 HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR------DKRQEV 1271
Cdd:COG2203 422 LLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLllllllALLALS 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1272 EREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERK 1351
Cdd:COG2203 502 ALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELAL 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1352 LQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDD 1431
Cdd:COG2203 582 ALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLA 661
|
330 340 350
....*....|....*....|....*....|....*
gi 1958798733 1432 LRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1466
Cdd:COG2203 662 TELDLILDSSLLLGLLLLGALLLLGGGLALLLSIG 696
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1244-1477 |
4.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1244 QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERkmdkmkeehwQEMAEARERYEAEERKQRADLLGHLT 1313
Cdd:PRK04863 813 QRLHQAFSRFIgshlavafeaDPEAELR-QLNRRRVELERALAD----------HESQEQQQRSQLEQAKEGLSALNRLL 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1314 GELERLRR-AHERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKARLAQLNVQEENMRKEKQLL 1387
Cdd:PRK04863 882 PRLNLLADeTLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFAL 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1388 LD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQkhvsSLEAEVQ 1465
Cdd:PRK04863 962 TEvVQRRAHFSYEDA-------AEMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLA----SLKSSYD 1030
|
250
....*....|..
gi 1958798733 1466 RKQNILKEMAAE 1477
Cdd:PRK04863 1031 AKRQMLQELKQE 1042
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1098-1192 |
4.22e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1098 RAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEersAQAALrAEKEAEKEATLL 1177
Cdd:COG2268 259 TARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAE---KQAAE-AEAEAEAEAIRA 334
|
90
....*....|....*
gi 1958798733 1178 QLREQLEGERREAVA 1192
Cdd:COG2268 335 KGLAEAEGKRALAEA 349
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1111-1224 |
4.38e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1111 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLegeRREA 1190
Cdd:COG0711 52 AALAEYEEKLAEARAEAAEI----IAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV---ADLA 124
|
90 100 110
....*....|....*....|....*....|....
gi 1958798733 1191 VAGLEKKHSTELEqlcsslEAKHREVISNLQKKI 1224
Cdd:COG0711 125 VAIAEKILGKELD------AAAQAALVDRFIAEL 152
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1038-1462 |
4.43e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1038 LRTLEGQPEGQPGKDSVASPAPLS-FLQSLLKTQLQKAAE-EEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIrAE 1115
Cdd:pfam07888 6 LVTLEEESHGEEGGTDMLLVVPRAeLLQNRLEECLQERAElLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1116 QQTALQRLREEAETLQKAERAslEQKSRRALEQLREQLEAEERSAQAALR---------AEKEAEKEATLLQLREqlege 1186
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKE--LSASSEELSEEKDALLAQRAAHEARIReleediktlTQRVLERETELERMKE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1187 RREAVAGLEKKHSTELEQLCSSLEAKHREV--ISNLQKKIEGAQQKEEAQLQEsLGRAEQRTHQKVHQVIEYEQELSSLL 1264
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELrsLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1265 RDKRQEVEREHerkmdkmkeehwqemaeareryeaeERKQRADLLGHLTGELERLRRAHERELESVRQEQDQ---QLEDL 1341
Cdd:pfam07888 237 EELRSLQERLN-------------------------ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQltlQLADA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1342 RRRHR-DQERKLQDLEAELSSRTKDvKARLAQLNvqEENMRKEKQLLLDAQRQAALEKE---EATATRRHLEEAKKEHTH 1417
Cdd:pfam07888 292 SLALReGRARWAQERETLQQSAEAD-KDRIEKLS--AELQRLEERLQEERMEREKLEVElgrEKDCNRVQLSESRRELQE 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958798733 1418 LLESkqqlrraiddLRVRRVELEsqvdQLQTQSQRLQKHVSSLEA 1462
Cdd:pfam07888 369 LKAS----------LRVAQKEKE----QLQAEKQELLEYIRQLEQ 399
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1114-1240 |
4.73e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.51 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1114 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeAEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAG 1193
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEEL-AREALAEKKSLEKQAEALETQLAQQRSAVE-QLRKQLAA 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798733 1194 LEKKhsteLEQlcssLEAKHREVISNLQkkiegaQQKEEAQLQESLG 1240
Cdd:pfam04012 123 LETK----IQQ----LKAKKNLLKARLK------AAKAQEAVQTSLG 155
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1111-1196 |
4.83e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.91 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1111 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGerrEA 1190
Cdd:pfam00430 51 AALAEAEQQLKEARAEAQEI----IENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVA---LA 123
|
....*.
gi 1958798733 1191 VAGLEK 1196
Cdd:pfam00430 124 VQIAEK 129
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
1175-1280 |
5.10e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 42.20 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1175 TLLQLREQLEGERREAVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGA-------------QQKEEA--QLQESL 1239
Cdd:COG2882 9 TLLDLAEKEEDEAARELGQAQQALEQAEEQL-EQLEQYREEYEQRLQQKLQQGlsaaqlrnyqqfiARLDEAieQQQQQV 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798733 1240 GRAEQRTHQKVHQVIEYEQELSSL--LRDKRQEVEREHERKMD 1280
Cdd:COG2882 88 AQAEQQVEQARQAWLEARQERKALekLKERRREEERQEENRRE 130
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1405-1635 |
5.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1405 RRHLEEA--------KKEhthllESKQQLRRAIDDL-RVR--RVELESQVDQLQTQSQRLQKHVsSLEAEVQRKQNILKe 1473
Cdd:COG1196 158 RAIIEEAagiskykeRKE-----EAERKLEATEENLeRLEdiLGELERQLEPLERQAEKAERYR-ELKEELKELEAELL- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1474 maaetnapphpepGLHIEDLRKSLGT-----NENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSM 1548
Cdd:COG1196 231 -------------LLKLRELEAELEEleaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1549 RRRQTALKAAQQHWRHELASAQEVDEDLP-GTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1627
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
....*...
gi 1958798733 1628 VSDEDTLK 1635
Cdd:COG1196 378 EEELEELA 385
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1288-1433 |
5.23e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1288 QEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER---KLQDLEAELSSRTK 1364
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1365 DVKARLAQLNVQEENMRKEkqllldAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLR 1433
Cdd:PRK12705 113 ALSARELELEELEKQLDNE------LYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1100-1237 |
5.80e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1100 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQL 1179
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ--LEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798733 1180 REQLEGERREAVAGL----EKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE 1237
Cdd:PRK09510 148 KAEAEAKRAAAAAKKaaaeAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1171-1475 |
5.82e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1171 EKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEaqlqeslgraeqrthqKV 1250
Cdd:COG1340 8 SSLEELEEKIEELREEIEEL-----KEKRDELNEELKELAEKRDELNAQVKELREEAQELRE----------------KR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1251 HQVIEYEQELssllRDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERElesv 1330
Cdd:COG1340 67 DELNEKVKEL----KEERDELNEKLNELREELDE-----------------LRKELAELNKAGGSIDKLRKEIERL---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1331 rqEQDQQLEDLRRrhrDQERKLQDLEAELSSRTKDVKarlaQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRrhlEE 1410
Cdd:COG1340 122 --EWRQQTEVLSP---EEEKELVEKIKELEKELEKAK----KALEKNEKLKELRAELKELRKEAEEIHKKIKELA---EE 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798733 1411 AKKEHTHLLESKQQ---LRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMA 1475
Cdd:COG1340 190 AQELHEEMIELYKEadeLRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1337-1482 |
5.83e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1337 QLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAqrqaaleKEEATATRRHLEEAKK 1413
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQEnkrLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-------KARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798733 1414 EHTHLLESKQQLRRAIDDLRVRrveLESQVDQLQtqsQR-------LQKHVSSLEAEVQRKQNILKEMAAETNAPP 1482
Cdd:pfam13851 107 EHEVLEQRFEKVERERDELYDK---FEAAIQDVQ---QKtglknllLEKKLQALGETLEKKEAQLNEVLAAANLDP 176
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1315-1419 |
5.94e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 41.78 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAHERELESVRQEQDQQLEDLRRRHR-DQERKLQDLEAELSSRTKDVKA---RLAQLNVQEE-NMRKEKQLLLD 1389
Cdd:pfam12474 26 ELEQLERQQKQQIEKLEQRQTQELRRLPKRIRaEQKKRLKMFRESLKQEKKELKQeveKLPKFQRKEAkRQRKEELELEQ 105
|
90 100 110
....*....|....*....|....*....|
gi 1958798733 1390 AQRQAALEKEEATATRRHLEEAKKEHTHLL 1419
Cdd:pfam12474 106 KHEELEFLQAQSEALERELQQLQNEKRKEL 135
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1364-1464 |
6.71e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1364 KDVKARLAQLNVQEENMRKEKQLLlDAQRQAALEKEEATATRRH--LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELES 1441
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEA-SFERLAELRDELAELEEELeaLKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100
....*....|....*....|...
gi 1958798733 1442 QVDQLQtqsQRLQKHVSSLEAEV 1464
Cdd:COG0542 493 ELAELE---EELAELAPLLREEV 512
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1092-1175 |
7.52e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 1171
Cdd:COG0711 59 EKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV-----ADLAVAIAEKILG 133
|
....
gi 1958798733 1172 KEAT 1175
Cdd:COG0711 134 KELD 137
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1303-1474 |
7.61e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1303 KQRADLLGHLtgelerlrraherelesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTkdvkARLAQLNVQeenmRK 1382
Cdd:PRK11637 68 QQRASLLAQL-------------------KKQEEAISQASRKLRETQNTLNQLNKQIDELN----ASIAKLEQQ----QA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDAQRQAALEKEEATATRRHL--EEAKKEH------THLLESKQQlrrAIDDLRVRRVELESQVDQL---QTQSQ 1451
Cdd:PRK11637 121 AQERLLAAQLDAAFRQGEHTGLQLILsgEESQRGErilayfGYLNQARQE---TIAELKQTREELAAQKAELeekQSQQK 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958798733 1452 RL------------------QKHVSSLEAEVQRKQNILKEM 1474
Cdd:PRK11637 198 TLlyeqqaqqqkleqarnerKKTLTGLESSLQKDQQQLSEL 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1091-1398 |
8.46e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQV---QSSTEAFENQIRAEQQTAL-----QRLREEAETLQKAERA-----SLEQKSRRALEQLREQLEAEE 1157
Cdd:PRK04863 799 AERYATLSFDVqklQRLHQAFSRFIGSHLAVAFeadpeAELRQLNRRRVELERAladheSQEQQQRSQLEQAKEGLSALN 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1158 RSA-QAALRAEKEAEKEATllQLREQLEgERREAVAGLEK--KHSTELEQLCSSLEAKHREvISNLQKKIEGAQQKEEAQ 1234
Cdd:PRK04863 879 RLLpRLNLLADETLADRVE--EIREQLD-EAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ-FEQLKQDYQQAQQTQRDA 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1235 ------LQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE---EHWQEMAEARERYEAEERKQr 1305
Cdd:PRK04863 955 kqqafaLTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQaqaQLAQYNQVLASLKSSYDAKR- 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1306 aDLLGHLTGELERLR-RAHERELESVRQEQDQQLEDLR--RRHRDQ-ERKLQDLEAELSSRTKDVKA---RLAQLNVQEE 1378
Cdd:PRK04863 1034 -QMLQELKQELQDLGvPADSGAEERARARRDELHARLSanRSRRNQlEKQLTFCEAEMDNLTKKLRKlerDYHEMREQVV 1112
|
330 340
....*....|....*....|
gi 1958798733 1379 NMRKEKQLLLDAQRQAALEK 1398
Cdd:PRK04863 1113 NAKAGWCAVLRLVKDNGVER 1132
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1110-1234 |
9.01e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALqrlREEAETLQKAERASLEQKSRRALEQ-----LREQLEAEERSAQAALRAEKEAEKEATLLQLREQLE 1184
Cdd:TIGR02794 53 NRIQQQKKPAA---KKEQERQKKLEQQAEEAEKQRAAEQarqkeLEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1185 GER-------REAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQ 1234
Cdd:TIGR02794 130 AEAkakaeaeAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAE 186
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1100-1454 |
9.50e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1100 QVQSSTEAFENQIRAEQQTALQ-------RLREE--AETLQKAERASLEQKSRRAL------------EQLREQLE---- 1154
Cdd:NF041483 87 QLRADAERELRDARAQTQRILQehaehqaRLQAElhTEAVQRRQQLDQELAERRQTveshvnenvawaEQLRARTEsqar 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1155 -------AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLeKKHSTELEQLCSSLEAKHREVISNL-QKKIEG 1226
Cdd:NF041483 167 rlldesrAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAIL-RRARKDAERLLNAASTQAQEATDHAeQLRSST 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1227 AQQKEEAQLQES-LGR-AEQRThqkvhqvieyeQELSSLLRDKRQEVerehERKMDKMKEEHWQEMAEARERYEAEERKQ 1304
Cdd:NF041483 246 AAESDQARRQAAeLSRaAEQRM-----------QEAEEALREARAEA----EKVVAEAKEAAAKQLASAESANEQRTRTA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1305 RAdllghltgELERLRRAHERELESVRQEQDQQLEDLRrrhrdQERKLQDLEAELSSRTKDVKARLAQL----NVQEENM 1380
Cdd:NF041483 311 KE--------EIARLVGEATKEAEALKAEAEQALADAR-----AEAEKLVAEAAEKARTVAAEDTAAQLakaaRTAEEVL 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1381 RKEKQlllDAQRQAALEKEEATATRRHLE-EAKKEHTHLLESKQQLRRAIDD----LRVRRVELESQVDQLQTQSQRLQ 1454
Cdd:NF041483 378 TKASE---DAKATTRAAAEEAERIRREAEaEADRLRGEAADQAEQLKGAAKDdtkeYRAKTVELQEEARRLRGEAEQLR 453
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1320-1468 |
1.06e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1320 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlAQLNVQEENMRKEKQLLLDAQRQaalEKE 1399
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAE-AAYEIAEANAEREVQRQLEIAER---ERE 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1400 EAtatrrhLEEAKKEhthllESKQQLRRAIddlrVRRVELESQVDQLQTQsqrlqkhvssLEAEVQRKQ 1468
Cdd:COG2268 292 IE------LQEKEAE-----REEAELEADV----RKPAEAEKQAAEAEAE----------AEAEAIRAK 335
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1341-1624 |
1.06e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1341 LRRRHRDQERKLQDLEAELSsRTKDVKARLaqlnvqeenmrkEKQL-LLDAQRQAALEKEEATATRRHLEEA--KKEHTH 1417
Cdd:TIGR02168 170 YKERRKETERKLERTRENLD-RLEDILNEL------------ERQLkSLERQAEKAERYKELKAELRELELAllVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1418 LLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLrksl 1497
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE------------ISRL---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1498 gtnENQevssslslsKEGIDLSMDSVrhflsaegvaVRSAKEFLVRQTRSMRRRQTALKAAQQhWRHELASAQEVdedlp 1577
Cdd:TIGR02168 301 ---EQQ---------KQILRERLANL----------ERQLEELEAQLEELESKLDELAEELAE-LEEKLEELKEE----- 352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958798733 1578 gtkvLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL 1624
Cdd:TIGR02168 353 ----LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1217-1387 |
1.17e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1217 ISNLQKKIEGAQqKEEAQLQESLGRAEQRtHQKVHQVIEyeqELSSLLRDKRQEVErEHERKMDKMKEEhwqemaearer 1296
Cdd:COG1579 19 LDRLEHRLKELP-AELAELEDELAALEAR-LEAAKTELE---DLEKEIKRLELEIE-EVEARIKKYEEQ----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1297 yEAEERKQRAdlLGHLTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQ 1376
Cdd:COG1579 82 -LGNVRNNKE--YEALQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|.
gi 1958798733 1377 EENMRKEKQLL 1387
Cdd:COG1579 158 LEELEAEREEL 168
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1120-1273 |
1.22e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1120 LQRLREEAE-TLQKAER--ASLEQKSRRALEQLREQLEAEERSAQ--AALRAEKEAEKeatllqLREQLEGERreavagl 1194
Cdd:PRK00106 26 MKSAKEAAElTLLNAEQeaVNLRGKAERDAEHIKKTAKRESKALKkeLLLEAKEEARK------YREEIEQEF------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798733 1195 eKKHSTELEQLcsslEAKHREVISNLQKKIEGAQQKEEAqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER 1273
Cdd:PRK00106 93 -KSERQELKQI----ESRLTERATSLDRKDENLSSKEKT-----LESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1243-1424 |
1.36e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1243 EQRTHQKVHQVIEYEQELSSLLRDKRQEVEREherkmDKMKEEhwQEMAEARERYEAEERKQRAdllghltgELERLRRA 1322
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERA-----EKMREE--LELEQQRRFEEIRLRKQRL--------EEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1323 HE-----RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSS----RTKDVKARLAQLNVQEENMRKEKQLLLDAQRQ 1393
Cdd:pfam15709 405 EEerkqrLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEaekqRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|.
gi 1958798733 1394 AALEKEEATATRRHLEEAKKEHTHLLESKQQ 1424
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1097-1237 |
1.47e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaleqLREQLEAEERSAQAALRAEKEAEKEATL 1176
Cdd:PRK00106 58 IKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESR----LTERATSLDRKDENLSSKEKTLESKEQS 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798733 1177 LQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVI-----SNLQKKIEGAQQKEEAQLQE 1237
Cdd:PRK00106 134 LTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIIlaeteNKLTHEIATRIREAEREVKD 199
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1099-1466 |
1.48e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 43.64 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1099 AQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQ 1178
Cdd:COG2203 338 DQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1179 LREQLEGERREAVAGLEKK-----HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQV 1253
Cdd:COG2203 418 LEGLLLLDLLLLLLLLRRIlllrvLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLAL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1254 IEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQE 1333
Cdd:COG2203 498 LALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLI 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1334 QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKK 1413
Cdd:COG2203 578 ELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLR 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1414 EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1466
Cdd:COG2203 658 ALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVL 710
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1336-1477 |
1.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1336 QQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLldaqrqaaleKEEATATRRHLEEAKKEH 1415
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSEL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798733 1416 THLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1477
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1438-1627 |
1.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1438 ELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLRKSLGTNENqEVSSSLSLSKEgid 1517
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE------------LEDLEKEIKRLEL-EIEEVEARIKK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1518 lsmdsvrhfLSAEGVAVRSAKEF--LVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEETKH 1595
Cdd:COG1579 78 ---------YEEQLGNVRNNKEYeaLQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAE 146
|
170 180 190
....*....|....*....|....*....|...
gi 1958798733 1596 LDEMKSAMRKGHDLLKKKEEKL-NQLESSLLEE 1627
Cdd:COG1579 147 LDEELAELEAELEELEAEREELaAKIPPELLAL 179
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1110-1182 |
1.69e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1110 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRaekeAEKEATLLQLREQ 1182
Cdd:cd06503 50 EELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE----QEKEKALAELRKE 118
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1143-1466 |
1.91e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 43.26 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1143 RRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQK 1222
Cdd:COG2203 330 LELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1223 KIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEER 1302
Cdd:COG2203 410 ADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLL 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1303 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1382
Cdd:COG2203 490 LLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLL 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1462
Cdd:COG2203 570 LGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALA 649
|
....
gi 1958798733 1463 EVQR 1466
Cdd:COG2203 650 LASL 653
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1308-1514 |
2.00e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1308 LLGHLTGELErlrrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLL 1387
Cdd:PHA02562 189 KIDHIQQQIK----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1388 LDAQRQAALEKEEATATRRH---------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQ---- 1454
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLelkn 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798733 1455 ------KHVSSLEAEVQRKQNILKEMAAETnaPPHPEPglhIEDLRKSLgtnenQEVSSSLS-LSKE 1514
Cdd:PHA02562 345 kistnkQSLITLVDKAKKVKAAIEELQAEF--VDNAEE---LAKLQDEL-----DKIVKTKSeLVKE 401
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1110-1284 |
2.16e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.10 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1110 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEaekeatllQLREQLEgerrE 1189
Cdd:pfam01442 10 STYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVE--------ELRQRLE----P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1190 AVAGLEKKHSTELEQlcssLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKV----HQVIEYEQELSSLLR 1265
Cdd:pfam01442 78 YTEELRKRLNADAEE----LQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLeelkESLAPYAEEVQAQLS 153
|
170
....*....|....*....
gi 1958798733 1266 DKRQEVEREHERKMDKMKE 1284
Cdd:pfam01442 154 QRLQELREKLEPQAEDLRE 172
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
1115-1245 |
2.38e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLeaEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAGL 1194
Cdd:pfam12072 57 EAKEEIHKLRAEAERELKERRNELQRQERR-LLQKEETL--DRKDESLEKKEESLEKKEKELEAQQQQLE-EKEEELEEL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1195 EKKHSTELEQ------------LCSSLEAKHREVISNLQKKIEgAQQKEEAQL--QESLGRAEQR 1245
Cdd:pfam12072 133 IEEQRQELERisgltseeakeiLLDEVEEELRHEAAVMIKEIE-EEAKEEADKkaKEIIALAIQR 196
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1349-1659 |
2.43e-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: 42.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1349 ERKLQDLEAELSSRtKDVKARLAQLNVQEENMRKEKqllLDAQRQAALEKEEATA--------TRRHLEEAKKEHT---H 1417
Cdd:COG5185 235 LKGFQDPESELEDL-AQTSDKLEKLVEQNTDLRLEK---LGENAESSKRLNENANnlikqfenTKEKIAEYTKSIDikkA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1418 LLESKQQLRRA--IDDLRVRRVELESQVDQLQTQsqrLQKHVSSLEAEVQRKQNILKEMAAETNapphpepglhiedlrK 1495
Cdd:COG5185 311 TESLEEQLAAAeaEQELEESKRETETGIQNLTAE---IEQGQESLTENLEAIKEEIENIVGEVE---------------L 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1496 SLGTNENQEVSSSLSLSKEGIDLSM----DSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQE 1571
Cdd:COG5185 373 SKSSEELDSFKDTIESTKESLDEIPqnqrGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1572 VDedlpgTKVLENVRKNLDEETKHLDEMKSAMrkghdlLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKV--TFDLSDM 1649
Cdd:COG5185 453 VM-----READEESQSRLEEAYDEINRSVRSK------KEDLNEELTQIESRVSTLKATLEKLRAKLERQLegVRSKLDQ 521
|
330
....*....|
gi 1958798733 1650 DDLSSESFES 1659
Cdd:COG5185 522 VAESLKDFMR 531
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1099-1216 |
2.62e-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: 42.85 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1099 AQVQSSTEAFENQIRaEQQTALQRLREEAETLQKAERASLEQKsrraLEQLREQLEAEERSAQAALRAEKEAEKEatLLQ 1178
Cdd:pfam01576 934 QKSESARQQLERQNK-ELKAKLQEMEGTVKSKFKSSIAALEAK----IAQLEEQLEQESRERQAANKLVRRTEKK--LKE 1006
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958798733 1179 LREQLEGERREAVAGLEK--KHSTELEQLCSSLEAKHREV 1216
Cdd:pfam01576 1007 VLLQVEDERRHADQYKDQaeKGNSRMKQLKRQLEEAEEEA 1046
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1214-1414 |
2.73e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1214 REVISNLQKKIEGAQqKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD--KRQEVEREHERKMDKMKEEHWQEMA 1291
Cdd:COG3883 22 QKELSELQAELEAAQ-AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1292 EARERYEAEERKQRADLLGHLTGeLERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLA 1371
Cdd:COG3883 101 SVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958798733 1372 QLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKE 1414
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1097-1480 |
3.20e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQIRAEQQTaLQRLREEAETLQKAERasLEQKSRRALEQlREQLEAEERSAQAALRAEKEAEKEA-- 1174
Cdd:PRK10246 203 LQAQASGVALLTPEQVQSLTAS-LQVLTDEEKQLLTAQQ--QQQQSLNWLTR-LDELQQEASRRQQALQQALAAEEKAqp 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1175 -----TLLQLREQLEG--ERREavaglekKHSTELEQLcsslEAKHREVISNLQ------KKIEGAQQKEEAQLQESLGR 1241
Cdd:PRK10246 279 qlaalSLAQPARQLRPhwERIQ-------EQSAALAHT----RQQIEEVNTRLQstmalrARIRHHAAKQSAELQAQQQS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1242 AEQ--RTHQKVHQvieYEQELSSLlrdkrqeveREH--ERKMDKMKEEHWQEmaeareryEAEERKQRADLLGHLTGELE 1317
Cdd:PRK10246 348 LNTwlAEHDRFRQ---WNNELAGW---------RAQfsQQTSDREQLRQWQQ--------QLTHAEQKLNALPAITLTLT 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1318 RLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQrqAALE 1397
Cdd:PRK10246 408 ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK--TICE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1398 KEEATAT----RRHLEEAK-------KEHThLLESKQQLRraIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1466
Cdd:PRK10246 486 QEARIKDleaqRAQLQAGQpcplcgsTSHP-AVEAYQALE--PGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQR 562
|
410
....*....|....
gi 1958798733 1467 KQNILKEMAAETNA 1480
Cdd:PRK10246 563 DESEAQSLRQEEQA 576
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1118-1218 |
3.27e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1118 TALQRLREEAETLqKAERASLEQKSRRALEQLREQLEAEERSAQ---AALRAEKEAEKEAT--LLQLREQLEgERREAVA 1192
Cdd:COG0542 411 EELDELERRLEQL-EIEKEALKKEQDEASFERLAELRDELAELEeelEALKARWEAEKELIeeIQELKEELE-QRYGKIP 488
|
90 100
....*....|....*....|....*.
gi 1958798733 1193 GLEKKHsTELEQLCSSLEAKHREVIS 1218
Cdd:COG0542 489 ELEKEL-AELEEELAELAPLLREEVT 513
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1315-1410 |
3.32e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1315 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQA 1394
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90
....*....|....*.
gi 1958798733 1395 ALEKEEATATRRHLEE 1410
Cdd:COG0542 495 AELEEELAELAPLLRE 510
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1113-1290 |
3.56e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1113 RAEQ--QTALQRLREEAETLQKAERA-----SLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLlqlreqLEG 1185
Cdd:pfam00261 54 RTEErlAEALEKLEEAEKAADESERGrkvleNRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVV------VEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1186 ERREAVAGLEKKhstelEQLCSSLEAKHREVISNLQK---KIEGAQQKEEA------QLQESLGRAEQRTHQKVHQVIEY 1256
Cdd:pfam00261 128 DLERAEERAELA-----ESKIVELEEELKVVGNNLKSleaSEEKASEREDKyeeqirFLTEKLKEAETRAEFAERSVQKL 202
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798733 1257 EQELSSLlrdkrqEVEREHER-KMDKMKEEHWQEM 1290
Cdd:pfam00261 203 EKEVDRL------EDELEAEKeKYKAISEELDQTL 231
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1134-1440 |
3.60e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1134 ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKeatllqlreqLEGERREAVAglEKKHSTELEQLCSSLEAK- 1212
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHN----------SYEEDSELKP--SGQGGLDEEEAFLDRTAKr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1213 HREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHWQEMAE 1292
Cdd:pfam02029 72 EERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1293 ARERYEAEERKQRADLlghlTGELERLRRAHERELESVRQEQDQQLED---LRRRHRDQERKLQDLEAELSSRTKDVKAR 1369
Cdd:pfam02029 151 QAEEEGEEEEDKSEEA----EEVPTENFAKEEVKDEKIKKEKKVKYESkvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1370 LAQLNV-----QEENMRKEKQLLLDAQRQAALEKEEATATRRH---------LEEAKK---EHTHLLESKQQLRRAIDDL 1432
Cdd:pfam02029 227 QGGLSQsqereEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRqkqqeaeleLEELKKkreERRKLLEEEEQRRKQEEAE 306
|
....*...
gi 1958798733 1433 RVRRVELE 1440
Cdd:pfam02029 307 RKLREEEE 314
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1171-1478 |
3.64e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1171 EKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEA--KHRE--VISNLQKKIEGAQQKEeAQLQESLGRAEQRT 1246
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKErlKHKEslVAASTSSRVGGLCLKC-AQHEAVLAQTHTNV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1247 H-QKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE-EHWQEMAEARERYEAEERKQradlLGHLTGELERLRRAHE 1324
Cdd:pfam15964 298 HmQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQvKQAVQMTEEANFEKTKALIQ----CEQLKSELERQKERLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1325 RELES-----------VRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKD-------VKARLAQLNVQEENMRKEKQL 1386
Cdd:pfam15964 374 KELASqqekraqekeaLRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREknslvsqLEEAQKQLASQEMDVTKVCGE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1387 LLDAQRQAALEKEEA--------TATRRHLE----EAKKEHTHLLESKQQLRRAIDDLRVRRVELeSQVDQLQTQSQRlQ 1454
Cdd:pfam15964 454 MRYQLNQTKMKKDEAekehreyrTKTGRQLEikdqEIEKLGLELSESKQRLEQAQQDAARAREEC-LKLTELLGESEH-Q 531
|
330 340
....*....|....*....|....
gi 1958798733 1455 KHVSSLEAEvQRKQNILKEMAAET 1478
Cdd:pfam15964 532 LHLTRLEKE-SIQQSFSNEAKAQA 554
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1092-1171 |
3.98e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 1171
Cdd:pfam00430 58 QQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQV-----VALAVQIAEKLLE 132
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1333-1477 |
4.03e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1333 EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQlNVQEENMRKEKQLLLDAQRQAalekeEATATRRHLEEAK 1412
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-EQLERAEKMREELELEQQRRF-----EEIRLRKQRLEEE 399
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798733 1413 KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1477
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1128-1474 |
4.13e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1128 ETLQKAERasLEQK----SRRALEQLREQL-EAEERSAQAALRAEKEAEKEAT-LLQLREQLEGERREAVAGL---EKKH 1198
Cdd:PRK04778 61 QSEEKFEE--WRQKwdeiVTNSLPDIEEQLfEAEELNDKFRFRKAKHEINEIEsLLDLIEEDIEQILEELQELlesEEKN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1199 STELEQLcsslEAKHREV--------------ISNLQKKIEGAQQK-------------EEA-----QLQESLGRAEQrt 1246
Cdd:PRK04778 139 REEVEQL----KDLYRELrksllanrfsfgpaLDELEKQLENLEEEfsqfveltesgdyVEAreildQLEEELAALEQ-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1247 hqKVHQVIEYEQELSSLLRDKRQEVEREHerkmDKMKEEHWqemaeareryeaeerkqradLLGHLtgelerlrrAHERE 1326
Cdd:PRK04778 213 --IMEEIPELLKELQTELPDQLQELKAGY----RELVEEGY--------------------HLDHL---------DIEKE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1327 LESVRQEQDQQLEDLRRRHRDQ-ERKLQDLEAEL----SSRTKDVKARlaqlNVQEENMRKEKQLLLDAQRQAALEKEEA 1401
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLDEaEEKNEEIQERIdqlyDILEREVKAR----KYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1402 TATRR--HLEEAKKEHTHLLESK-QQLRRAIDDLRVR-----------RVELESQVDQL---QTQSQRLQKHVSSLEAEV 1464
Cdd:PRK04778 334 DRVKQsyTLNESELESVRQLEKQlESLEKQYDEITERiaeqeiayselQEELEEILKQLeeiEKEQEKLSEMLQGLRKDE 413
|
410
....*....|
gi 1958798733 1465 QRKQNILKEM 1474
Cdd:PRK04778 414 LEAREKLERY 423
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1106-1225 |
4.33e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAeersaqaaLRAEKE------AEKEATLLQL 1179
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEE-IRRLEEQVER--------LEAEVEeleaelEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1180 REQLEGERREAVAGLEK-----KHSTELEQLCSSLEAKhREVISNLQKKIE 1225
Cdd:COG2433 447 ERELSEARSEERREIRKdreisRLDREIERLERELEEE-RERIEELKRKLE 496
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1091-1197 |
4.50e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.41 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1091 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQkaeraSLEQKSRRALEQLREQLEAEERSAqAALRAEKEA 1170
Cdd:pfam15665 95 RQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALE-----ELRAKHRQEIQELLTTQRAQSASS-LAEQEKLEE 168
|
90 100 110
....*....|....*....|....*....|
gi 1958798733 1171 EKEATLLQLREQLE---GERREAVAGLEKK 1197
Cdd:pfam15665 169 LHKAELESLRKEVEdlrKEKKKLAEEYEQK 198
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1330-1444 |
4.51e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1330 VRQEQDQQLEDLRrrhrDQERKLQDLEAELSSRTKD----VKARLAQLNVQEENMRKEKQLLLDAQRQaalEKEEATATR 1405
Cdd:COG0542 402 VRMEIDSKPEELD----ELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARWEA---EKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958798733 1406 RHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1444
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1349-1477 |
4.58e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1349 ERKLQDLEAelssrtkdvkaRLAQLnvqEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRA 1428
Cdd:pfam20492 5 EREKQELEE-----------RLKQY---EEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958798733 1429 IDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1477
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1331-1477 |
4.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1331 RQEQDQQLEDLRRRHRDQERKLQDLEAEL----SSRTKDVKARLAQLNVQEENMRKEKQL--LLDAQRQAALEKEEATAT 1404
Cdd:PRK11281 75 IDRQKEETEQLKQQLAQAPAKLRQAQAELealkDDNDEETRETLSTLSLRQLESRLAQTLdqLQNAQNDLAEYNSQLVSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1405 RRHLEEAKKEHTHLLESKQQLRRAIDDLRV--------------------------RRVELE----------SQVDQLQT 1448
Cdd:PRK11281 155 QTQPERAQAALYANSQRLQQIRNLLKGGKVggkalrpsqrvllqaeqallnaqndlQRKSLEgntqlqdllqKQRDYLTA 234
|
170 180
....*....|....*....|....*....
gi 1958798733 1449 QSQRLQKHVSSLEAEVQRKQNILKEMAAE 1477
Cdd:PRK11281 235 RIQRLEHQLQLLQEAINSKRLTLSEKTVQ 263
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1109-1190 |
4.74e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSA--QAALRAEKEAEKEATLLQLREQLEGE 1186
Cdd:pfam05672 30 EEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAeeEAEEREQREQEEQERLQKQKEEAEAK 109
|
....
gi 1958798733 1187 RREA 1190
Cdd:pfam05672 110 AREE 113
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1117-1474 |
4.81e-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: 41.60 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1117 QTALQRLREE---AETLQKAERASLEQKSRRALE-QLR-EQLEAEERSAQA------ALR--AEKEAEKEATLLQLREQL 1183
Cdd:pfam05622 65 QKQLEQLQEEnfrLETARDDYRIKCEELEKEVLElQHRnEELTSLAEEAQAlkdemdILResSDKVKKLEATVETYKKKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1184 E--GERREAVAGLEKKHSTELEQLCSSLEAKHREviSNLQKKIEGAQQkeeaQLQESLGRAEQRTHQKVHQVIEY---EQ 1258
Cdd:pfam05622 145 EdlGDLRRQVKLLEERNAEYMQRTLQLEEELKKA--NALRGQLETYKR----QVQELHGKLSEESKKADKLEFEYkklEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1259 ELSSLLRDK-RQEVEREHERKMDKmkEEHWQEMAEARERYEAEERKQRADLLGHLTGEL------ERLRR-AHERELESV 1330
Cdd:pfam05622 219 KLEALQKEKeRLIIERDTLRETNE--ELRCAQLQQAELSQADALLSPSSDPGDNLAAEImpaeirEKLIRlQHENKMLRL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1331 RQEQ--DQQLEDLRRRHRDQERKLQDLEAELssrtkdvkaRLAQLNVQEenMRKEKQLLLDAQRQAALEKEEATATRRHL 1408
Cdd:pfam05622 297 GQEGsyRERLTELQQLLEDANRRKNELETQN---------RLANQRILE--LQQQVEELQKALQEQGSKAEDSSLLKQKL 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798733 1409 EEAKKEHTHLLESKQQLRRAIDDLRvrrvelesqvdqlQTQSQRLQKHVSSLEAEVQRKQNILKEM 1474
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELE-------------PKQDSNLAQKIDELQEALRKKDEDMKAM 418
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1097-1497 |
4.96e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1097 LRAQVQSSTEAFENQirAEQQTALQRLREEAETLQKAERASLE---------QKSRRALEQLREQLEAEER-------SA 1160
Cdd:pfam07111 336 LRGQVAELQEQVTSQ--SQEQAILQRALQDKAAEVEVERMSAKglqmelsraQEARRRQQQQTASAEEQLKfvvnamsST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1161 QAALRAE--KEAEKEATLLQLREQLEGERRE--AVAGL--EKKHSTELEQLCSSLEAKHREVISNLQKKIEgaqqkeeaQ 1234
Cdd:pfam07111 414 QIWLETTmtRVEQAVARIPSLSNRLSYAVRKvhTIKGLmaRKVALAQLRQESCPPPPPAPPVDADLSLELE--------Q 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1235 LQESLGRAEQRTHQKVHQVieyEQELSsllRDKRQ-EVEReheRKMDKMKEEHWQEMaeareryeaeerKQRADLLGHLT 1313
Cdd:pfam07111 486 LREERNRLDAELQLSAHLI---QQEVG---RAREQgEAER---QQLSEVAQQLEQEL------------QRAQESLASVG 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1314 GELERLRRAHERELE---SVRQEQDQQLEDLRRRHRDqerKLQDLEAELSSRTKDVKARLaqlNVQEENMRKEKQLLLDA 1390
Cdd:pfam07111 545 QQLEVARQGQQESTEeaaSLRQELTQQQEIYGQALQE---KVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQI 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1391 QRQAALEKEEATATRRHLEEAKKEhthllESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1470
Cdd:pfam07111 619 QHRATQEKERNQELRRLQDEARKE-----EGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVV 693
|
410 420
....*....|....*....|....*..
gi 1958798733 1471 LKEMAAETNAPPHPEPGLHIEDLRKSL 1497
Cdd:pfam07111 694 SSPRPECSASAPIPAAVPTRESIKGSL 720
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1092-1244 |
5.04e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFENQIRAEQQTA----LQRLREEAETLQKAERASLEQKSRRA----LEQLREQLEAEERSAQ-- 1161
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAeeaeKQRAAEQARQKELEQRAAAEKAAKQAeqaaKQAEEKQKQAEEAKAKqa 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1162 ------------------AALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhsteleqlcsslEAKHREVISNLQKK 1223
Cdd:TIGR02794 130 aeakakaeaeaerkakeeAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKA------------EAEAKAKAEEAKAK 197
|
170 180
....*....|....*....|.
gi 1958798733 1224 IEGAQQKEEAQLQEslgRAEQ 1244
Cdd:TIGR02794 198 AEAAKAKAAAEAAA---KAEA 215
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1109-1225 |
5.13e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTA-LQRLREEAETLQKaeraSLEQKsrraLEQLREQLEAE----ERSAQAALRAEKEaEKEATLLQLREQL 1183
Cdd:PRK00409 527 ELERELEQKAEeAEALLKEAEKLKE----ELEEK----KEKLQEEEDKLleeaEKEAQQAIKEAKK-EADEIIKELRQLQ 597
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958798733 1184 EGERREAVAglekkhsTELEQLCSSLEAKHREVISNLQKKIE 1225
Cdd:PRK00409 598 KGGYASVKA-------HELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1303-1385 |
5.81e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.92 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1303 KQRADLLG-HLT-GELE-RLRRAHE--RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK---DVK----ARL 1370
Cdd:pfam08614 61 QLREELAElYRSrGELAqRLVDLNEelQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKlnqDLQdelvALQ 140
|
90
....*....|....*
gi 1958798733 1371 AQLNVQEENMRKEKQ 1385
Cdd:pfam08614 141 LQLNMAEEKLRKLEK 155
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1106-1245 |
5.94e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.39 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1106 EAFENQIRAEQQTAlQRLREEAETLQKaerasleqKSRRALEQLREqlEAEERSAQAalRAEKEAEKEATLLQLREQLEG 1185
Cdd:COG0711 30 DERQEKIADGLAEA-ERAKEEAEAALA--------EYEEKLAEARA--EAAEIIAEA--RKEAEAIAEEAKAEAEAEAER 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1186 ERREAVAGLEKKHSTELEQLcssleakhREVISNLqkkiegAQQKEEAQLQESLGRAEQR 1245
Cdd:COG0711 97 IIAQAEAEIEQERAKALAEL--------RAEVADL------AVAIAEKILGKELDAAAQA 142
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1109-1197 |
6.23e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 38.83 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLrEEAETLQKAERASLEQkSRRALEQLREQLEAE-ERSAQAALrAEKEAEKEATLLQLREQLEGER 1187
Cdd:PRK07353 38 EDYIRTNRAEAKERL-AEAEKLEAQYEQQLAS-ARKQAQAVIAEAEAEaDKLAAEAL-AEAQAEAQASKEKARREIEQQK 114
|
90
....*....|
gi 1958798733 1188 REAVAGLEKK 1197
Cdd:PRK07353 115 QAALAQLEQQ 124
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1116-1244 |
6.23e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1116 QQTALQRLREEAETLQKAERAsleqksRRALEQLREQLEAE--ERSAQAALRAEKEAEKEATLLQLREQLEGERREAvag 1193
Cdd:pfam05672 21 RQAREQREREEQERLEKEEEE------RLRKEELRRRAEEEraRREEEARRLEEERRREEEERQRKAEEEAEEREQR--- 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1194 lEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQ 1244
Cdd:pfam05672 92 -EQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEE 141
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1346-1472 |
6.74e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1346 RDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKekqllLDAQRQAALEKEEatatrrhlEEAKKEhthLLESKQQL 1425
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK-----WEEKARLALEKGR--------EDLARE---ALERKAEL 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798733 1426 RRAIDDLRVRRVELESQVDQLQTQSQRLQKHVssleAEVQRKQNILK 1472
Cdd:COG1842 97 EAQAEALEAQLAQLEEQVEKLKEALRQLESKL----EELKAKKDTLK 139
|
|
| MIC19_MIC25 |
pfam05300 |
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ... |
1107-1199 |
8.21e-03 |
|
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Pssm-ID: 461615 [Multi-domain] Cd Length: 173 Bit Score: 39.29 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1107 AFENQIRAEQQTAlqRLREEAETLQKAERASLEQKSRRALeqLREQLEAEERSAQAALRAEKEAEKEATLlqlrEQLEGE 1186
Cdd:pfam05300 68 KEELYKRLEQEQA--KVQEELARLAEREREAAQESLTRAI--LRERASTEDERLKAQQLAKQLEEKEAEL----KKQDAF 139
|
90
....*....|...
gi 1958798733 1187 RREAVAGLEKKHS 1199
Cdd:pfam05300 140 YKEQLARLEEKNA 152
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1143-1466 |
8.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.38 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1143 RRALEQLREQLEAEERSAQAALRAEKEAekeatllqlreqLEGERREAVAGLEKKHSTELEQLCSSLEAKHREvisnlqk 1222
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALY------------LAGRFEEAEALLERALAARALAALAALRHGNPP------- 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1223 kiegaqqkEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEER 1302
Cdd:COG3899 790 --------ASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGL 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1303 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1382
Cdd:COG3899 862 ETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAA 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1462
Cdd:COG3899 942 AAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLA 1021
|
....
gi 1958798733 1463 EVQR 1466
Cdd:COG3899 1022 AALA 1025
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1120-1285 |
8.29e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1120 LQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKeAEKEATLLQlrEQLEGERREAVAGLEKKHS 1199
Cdd:pfam05262 183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-AQQKADFAQ--DNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1200 TELEQLCSSLEAKHReVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQElsslLRDKRQEVEREHE--- 1276
Cdd:pfam05262 260 LPKPADTSSPKEDKQ-VAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKE----AEDKELEAQKKREpva 334
|
....*....
gi 1958798733 1277 RKMDKMKEE 1285
Cdd:pfam05262 335 EDLQKTKPQ 343
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1092-1290 |
8.65e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQsstEAFENQIRAEQQT-ALQRLREEAETLQKAERASLEQKSRRALEQLREQL---EAEERSAQAALRAE 1167
Cdd:PRK04863 935 EQFEQLKQDYQ---QAQQTQRDAKQQAfALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLeqaEQERTRAREQLRQA 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1168 KE--AEKEATLLQL-------REQLEGERRE-------AVAGLEKKHSTELEQLCSSLEAkHREVISNLQKKIegaqQKE 1231
Cdd:PRK04863 1012 QAqlAQYNQVLASLkssydakRQMLQELKQElqdlgvpADSGAEERARARRDELHARLSA-NRSRRNQLEKQL----TFC 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798733 1232 EAQLQESLGR---AEQRTHQKVHQVIEYEQELSSLLR-DKRQEVEREHERKMDK-MKEEHWQEM 1290
Cdd:PRK04863 1087 EAEMDNLTKKlrkLERDYHEMREQVVNAKAGWCAVLRlVKDNGVERRLHRRELAyLSADELRSM 1150
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1115-1231 |
8.66e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1115 EQQTALQRLREEAETLQKAERA---------SLEQKSRRALEQlREQLEAEERSAQAAL-RAEKEAEKEAtllQLREQLE 1184
Cdd:pfam20492 7 EKQELEERLKQYEEETKKAQEEleeseetaeELEEERRQAEEE-AERLEQKRQEAEEEKeRLEESAEMEA---EEKEQLE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798733 1185 GERREAVAglekkhstELEQLCSSLEAKHREViSNLQKKIEGAQQKE 1231
Cdd:pfam20492 83 AELAEAQE--------EIARLEEEVERKEEEA-RRLQEELEEAREEE 120
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1109-1237 |
8.78e-03 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 38.53 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1109 ENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLR----------EQLEAEERSAQAALRAEKEAEKEATLLQ 1178
Cdd:pfam07321 12 EDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRlyaeiqgklvLLKELEKVKQQVALLRENEADLEKQVAE 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1179 LREQLEGErREAVAGLEKKHSTELEQL--CSSLEAKHREVISNLQkkiegaQQKEEAQLQE 1237
Cdd:pfam07321 92 ARQQLEAE-REALRQARQALAEARRAVekFAELVRLVQAEELRQQ------ERQEEQELEE 145
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1099-1171 |
9.05e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 40.21 E-value: 9.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798733 1099 AQVQsstEAFENQIRAeqqtalQRLREEAETLQKAERASLEQKSRRALEqlREQLEAEERSAQAALRAEKEAE 1171
Cdd:COG0330 167 EEVQ---DAMEDRMKA------EREREAAILEAEGYREAAIIRAEGEAQ--RAIIEAEAYREAQILRAEGEAE 228
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1146-1269 |
9.23e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1146 LEQLREQLE---AEERSAQAALRAEKEAEKEaTLLQLREQLEGERREAVagLEKKHSTELEQLCSSLEAKHREVISNLQK 1222
Cdd:smart00787 142 LEGLKEGLDenlEGLKEDYKLLMKELELLNS-IKPKLRDRKDALEEELR--QLKQLEDELEDCDPTELDRAKEKLKKLLQ 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798733 1223 KIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQ 1269
Cdd:smart00787 219 EIM-IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1092-1583 |
9.53e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 40.59 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1092 QRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeAEERSAQAALRAE-KEA 1170
Cdd:pfam15450 48 RELLQVRAHVQLQDSELK-QLRQEVQQAARAPEKEALEFPGPQNQNQMQALDKRLVEVREAL-TQIRRKQALQDSErKGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1171 EKEATLlqlreqlegeRREAVAGLEKKHSTELEQLCSSLeakhrevisnlQKKIEGAQQKEEAQLQESLGRAEQRTHQKV 1250
Cdd:pfam15450 126 EQEANL----------RLTKLTGKLKQEEQGREAACSAL-----------QKSQEEASQKVDHEVARMQAQVTKLGEEMS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1251 HQVIEYEQELSSLL---------RDKRQEVER-EHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLR 1320
Cdd:pfam15450 185 LRFLKREAKLCSFLqksflalekRMKASESTRlKAESSLREELEGRWQKLQELTEERLRALQGQREQEEGHLLEQCRGLD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1321 RAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEkqllldaqrqaalekee 1400
Cdd:pfam15450 265 AAVVQLTKFVRQNQVSLNRVLLAEQKARDAKGQLEESQAGELASYVQENLEAVQLAGELAQQE----------------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1401 ataTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD-QLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETN 1479
Cdd:pfam15450 328 ---TQGALELLQEKSQVLEGSVAELVRQVKDLSDHFLALSWRLDlQEQTLGLKLSEAKKEWEGAERKSLEDLAQWQKEVA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1480 ApphpepglHIEDLRKSLGTNENQ--EVSSSLSLSKEGIDLSmdsvrhfLSAEGvavrSAKEFLVrqtRSMRRRQTALka 1557
Cdd:pfam15450 405 A--------HLREVQEKVDSLPRQieAVSDKCVLHKSDSDLK-------ISAEG----KAREFEV---EAMRQELAAL-- 460
|
490 500
....*....|....*....|....*.
gi 1958798733 1558 aqqhwrheLASAQEVDEDLPGTKVLE 1583
Cdd:pfam15450 461 --------LSSVQLLKEGNPGRKIAE 478
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1114-1413 |
9.58e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1114 AEQQTALQRLREEAETLQKAerasleqksRRALEQLREQleaeersaqaalraEKEAEKEATLLqlREQLEgERREA--V 1191
Cdd:COG0497 151 AGLEELLEEYREAYRAWRAL---------KKELEELRAD--------------EAERARELDLL--RFQLE-ELEAAalQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1192 AGlekkhstELEQLcsslEAKHReVISNLQKKIEGAQQ------KEEAQLQESLGRAEQRthqkVHQVIEYE---QELSS 1262
Cdd:COG0497 205 PG-------EEEEL----EEERR-RLSNAEKLREALQEalealsGGEGGALDLLGQALRA----LERLAEYDpslAELAE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1263 LLRDKRQEVEreherkmdkmkeehwqemaeareryeaeerkqraDLLGHLTGELERLRrAHERELESVrQEQDQQLEDLR 1342
Cdd:COG0497 269 RLESALIELE----------------------------------EAASELRRYLDSLE-FDPERLEEV-EERLALLRRLA 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798733 1343 RRHRDQERKLQDLEAELssrtkdvKARLAQLNVQEENMrkekqllldaqrqAALEKEEATATRRHLEEAKK 1413
Cdd:COG0497 313 RKYGVTVEELLAYAEEL-------RAELAELENSDERL-------------EELEAELAEAEAELLEAAEK 363
|
|
| DUF1978 |
pfam09321 |
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ... |
1304-1479 |
9.63e-03 |
|
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified.
Pssm-ID: 312723 [Multi-domain] Cd Length: 244 Bit Score: 39.91 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1304 QRADLLGHLTGELERLRRAHEREleSVRQEQdQQLEDLRRRHRDQERKLQDLEAE-LSSRTKDVKARLAQLNVQEENMRK 1382
Cdd:pfam09321 66 EKKAHLKHLESLYTQARDRFEKQ--SSKKNQ-KELEEAEQEYLSSWEDVKDQEIErVQERLQALQALYPEVSVSEEETEG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798733 1383 EKQLLLDAQRQAALEKEEATaTRRHLEEA----KKEHTHLLESKQQLRRaiDDLRVRRVELESQVDQLQtqsQRLQKHVS 1458
Cdd:pfam09321 143 QETVTPTVDLETALGRIEES-YRECVRDQedywKEEESKEVEMSAEFRE--EGGKKKSEEFQEQLGSLE---RFLKEHSE 216
|
170 180
....*....|....*....|.
gi 1958798733 1459 SLEAEVQRKQNILKEMAAETN 1479
Cdd:pfam09321 217 ELEVLEKHILKHESEATAENE 237
|
|
| |
