|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
42-282 |
2.24e-119 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 374.39 E-value: 2.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 42 GGRPQRCMPEFVNAAFNVTVVATNTCGTP-PEEYCVQTGVTGVTKSCHLCDAGQQHLQHGAAFLTDYNNQADTTWWQSQT 120
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 121 MLAGVQYpnsINLTLHLGKAFDITYVRLKFHTSRPeSFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGgDEQQ 200
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 201 ALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFND-PKVLKSYYYAISDFA 279
Cdd:smart00136 156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIA 235
|
...
gi 153791270 280 VGG 282
Cdd:smart00136 236 VGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
48-282 |
3.11e-114 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 359.97 E-value: 3.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 48 CMPEFVNAAFNVTVVATNTCGT-PPEEYCVQTGVTGVtKSCHLCDAGQQHLQHGAAFLTDYNNQADTTWWQSQTMLagVQ 126
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLnGPERYCILSGLEGG-KKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 127 YPNsINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGfiRTGGDEQQALCTDE 206
Cdd:pfam00055 78 YEN-VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGP--SRGIKDDEVICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791270 207 FSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGG 282
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
551-676 |
2.89e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 551 SYFPRYFIAPVKFLGNQVLSYGQNLSFSFRVD--RRDTRLSAEDLVLEGAGLRVSVPliAQGNSYPSE-TTVKYIFRLHE 627
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHP--AEGPPLPDElTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 153791270 628 ATDYPWRPALSPfEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLQSARP 676
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
556-686 |
8.30e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 144.33 E-value: 8.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 556 YFIAPVKFLGNQVLSYGQNLSFSFRVDRRD---TRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTvKYIFRLHEATdyp 632
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPgggSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQ-TYSVRLHEEN--- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 633 WR----PALSPFEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLQSARPGP-GVPATWVE 686
Cdd:pfam00052 77 WRdsdgAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPGGsGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1033-1570 |
5.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1033 YRLVKDKVAEHRVKLQELESLIANLgtgddMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQI 1112
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1113 SRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEpnnmtlLAEEARKLAERHKQEA 1192
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1193 DDIVRVAKTANETSAEAyNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQL 1272
Cdd:COG1196 383 ELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1273 TpVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAK 1352
Cdd:COG1196 462 L-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1353 KGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAI---NRTIAEANEKTREAQLALGNAAADATEAKNKAH---- 1425
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDkirARAALAAALARGAIGAAVDLVASDLREADARYYvlgd 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1426 --EAERIASAVQKNATSTKADAERTFGEVTDLDNEVNG-----------MLRQLEEAENELKKKQDDADQDMMMAGMASQ 1492
Cdd:COG1196 621 tlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1493 AAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRkvSDLESEARKQEAAI 1570
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL--EELERELERLEREI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1070-1594 |
7.75e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLhsqiSRLQNIRNTIEETGILAERARSRVESTEQLI-EIASR 1148
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIrELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1149 ------ELEKAKmaaanvsitqpESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQ 1222
Cdd:PRK03918 268 ieelkkEIEELE-----------EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1223 TAlEIEELNRKYEQAKNISQDLEKQAaRVHEEAKRAGDKAVEIYASVAQLTPVDSEA-----------LENEANKIKKEA 1291
Cdd:PRK03918 337 EE-RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1292 ADLDRLIDQKLKDYEDLREdMRGK---------EHEVKNLLEKGKAEQQTAdqllaradaakalaeeaakkgRSTLQEAN 1362
Cdd:PRK03918 415 GELKKEIKELKKAIEELKK-AKGKcpvcgreltEEHRKELLEEYTAELKRI---------------------EKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1363 DILNNLKDFDRRVnDNKTAAEEALRRIPAINRTIAEANEKTREAqlalgnaaaDATEAKNKAHEAERI---ASAVQKNAT 1439
Cdd:PRK03918 473 EKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKY---------NLEELEKKAEEYEKLkekLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1440 STKADAERTfgevtdldNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASqaaqEAELNAR------------KAKNS 1507
Cdd:PRK03918 543 SLKKELEKL--------EELKKKLAELEKKLDELEEELAELLKELEELGFES----VEELEERlkelepfyneylELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1508 VSSLLSQLNNLLDQLGQLDTVdLNKLNEIEGSLNKAKDEMKasDLDRKVSD------------LESEARKQEAAIMDYNR 1575
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELE--ELEKKYSEeeyeelreeyleLSRELAGLRAELEELEK 687
|
570
....*....|....*....
gi 153791270 1576 DIAEIIKDIHNLEDIKKTL 1594
Cdd:PRK03918 688 RREEIKKTLEKLKEELEER 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1034-1596 |
1.16e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.72 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKLQELESLIANLGTGDDMVTDQA--FEDRLKEAEREVTDLLREAQEVKDvDQNLMDRLQRVNSSLHSQ 1111
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQA-RLDSLERLQENLEGFSEG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1112 ISRLQNIRNTIE-ETGILAERARSRvESTEQLIEIASREL------EKAKMAAANVSITQPESTGEPNNMTLLAEEARKL 1184
Cdd:TIGR02168 508 VKALLKNQSGLSgILGVLSELISVD-EGYEAAIEAALGGRlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1185 AERHKQEADDIVRVAKTANE--TSAEAYNLLLRTLAG-----EN-QTALEIEELNRKYEQ-------------------A 1237
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGgvlvvDDlDNALELAKKLRPGYRivtldgdlvrpggvitggsA 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1238 KNISQDLEKQA--ARVHEEAKRAGDKAVEIYASVAQLTpVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLR------ 1309
Cdd:TIGR02168 667 KTNSSILERRReiEELEEKIEELEEKIAELEKALAELR-KELEELEEELEQLRKELEELSRQISALRKDLARLEaeveql 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1310 -EDMRGKEHEVKNL----------LEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKdfdRRVNDN 1378
Cdd:TIGR02168 746 eERIAQLSKELTELeaeieeleerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN---EEAANL 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1379 KTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAA---DATEAKNKAHEaERIASAVQKNATSTKADAERTfgEVTDL 1455
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELES-ELEALLNERASLEEALALLRS--ELEEL 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1456 DNEVNGMLRQLEEAENELKKKQDDADQ--------DMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDT 1527
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQlelrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1528 -------VDLNKLNEIEgSLNKAKDEmkasdLDRKVSDLEsEARKQ-EAAIMDYNRDIAEIIKDIhnLEDIKKTLPT 1596
Cdd:TIGR02168 980 kikelgpVNLAAIEEYE-ELKERYDF-----LTAQKEDLT-EAKETlEEAIEEIDREARERFKDT--FDQVNENFQR 1047
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
443-490 |
2.29e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.53 E-value: 2.29e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 443 CSCDPSGS-TDECNVETGRCVCKDNVEGFNCERCKPGFFNLESSNPKGC 490
Cdd:pfam00053 1 CDCNPHGSlSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
933-978 |
3.18e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.11 E-value: 3.18e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 153791270 933 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGFGPEGC 978
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
932-979 |
1.65e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 1.65e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 932 RCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGF--GPEGCK 979
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
933-981 |
5.21e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 5.21e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 933 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGFGPEGCKPC 981
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
396-443 |
3.57e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 3.57e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 396 CHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPC 443
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
442-491 |
4.95e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 4.95e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 442 PCSCDPSGS-TDECNVETGRCVCKDNVEGFNCERCKPGFFNLeSSNPKGCT 491
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
722-761 |
5.88e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 5.88e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 153791270 722 CTCNGH---SETCDPETGVCDCRDNTAGPHCEKCSDGYYGDST 761
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
722-769 |
8.81e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 8.81e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 722 CTCNGH---SETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTLGTssDCQ 769
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
882-930 |
1.14e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.14e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 882 CACNPYGTVQqqSSCNPVTGQCQCLPHVSGRDCGTCDPGYYNLQ--SGQGC 930
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
395-441 |
1.70e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 1.70e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 395 PCHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEA--GCR 441
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
443-490 |
1.70e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 1.70e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 443 CSCDPSGS-TDECNVETGRCVCKDNVEGFNCERCKPGFFNlesSNPKGC 490
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
396-440 |
2.69e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 2.69e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 153791270 396 CHCSPVGSLSTQCDS-YGRCSCKPGVMGDKCDRCQPGFHSLTEAGC 440
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
881-931 |
3.71e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 3.71e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 153791270 881 ACACNPYGTVQQQssCNPVTGQCQCLPHVSGRDCGTCDPGYYNLQS-GQGCE 931
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1042-1325 |
1.46e-10 |
|
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: 65.92 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1042 EHRVKLQELESLIANLGTGDDMVTDQafEDRLKEAEREVTDLLREAQEVKDVDQNL--MDRLQRVNSSLHSQISRLqniR 1119
Cdd:pfam05557 143 LLKAKASEAEQLRQNLEKQQSSLAEA--EQRIKELEFEIQSQEQDSEIVKNSKSELarIPELEKELERLREHNKHL---N 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1120 NTIEETGILAERA---RSRVESTEQL-IEIASRELEKAKMAAanvSITQPESTGEPNNMTLLAEEArkLAERHKQ-EADD 1194
Cdd:pfam05557 218 ENIENKLLLKEEVedlKRKLEREEKYrEEAATLELEKEKLEQ---ELQSWVKLAQDTGLNLRSPED--LSRRIEQlQQRE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1195 IVRVA-KTANETSAEAYNLLLRTLAGENQTAL-EIEELNRKYEQAKNISQDLEKQAARVHEEakRAGDKA-VEIYasvaq 1271
Cdd:pfam05557 293 IVLKEeNSSLTSSARQLEKARRELEQELAQYLkKIEDLNKKLKRHKALVRRLQRRVLLLTKE--RDGYRAiLESY----- 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 153791270 1272 ltpvDSEALENEANKIKKEaadldrlidqKLKDYEDLREDMRGKEHEVKNLLEK 1325
Cdd:pfam05557 366 ----DKELTMSNYSPQLLE----------RIEEAEDMTQKMQAHNEEMEAQLSV 405
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
882-930 |
1.62e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 1.62e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 882 CACNPYGTVQqqSSCNPVTGQCQCLPHVSGRDCGTCDPGYYNlQSGQGC 930
Cdd:smart00180 1 CDCDPGGSAS--GTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
722-763 |
2.70e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 2.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 153791270 722 CTCNG---HSETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTLG 763
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
980-1027 |
3.09e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 3.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 980 PCDCHHEGSLSLQC-KEDGRCECREGFVGNRCDQCEENYFYNRSWP-GCQ 1027
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1089-1300 |
6.66e-10 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 61.53 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1089 EVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPEST 1168
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1169 G-----------------------EPNNMTLL-------------------AEEARKLAERHKQEADDIVRVAKTANETS 1206
Cdd:smart00283 81 SaveeleessdeigeivsviddiaDQTNLLALnaaieaarageagrgfavvADEVRKLAERSAESAKEIESLIKEIQEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1207 AEAYNLLLRTLAGENQTALEIEELNRKYE----QAKNISQDLEKQAARVHEEAKRAGD--KAVEIYASVAQLTPVDSEAL 1280
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEeivdSVEEIADLVQEIAAATDEQAAGSEEvnAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|
gi 153791270 1281 ENEANKIKKEAADLDRLIDQ 1300
Cdd:smart00283 241 SAAAEELSGLAEELDELVER 260
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
981-1026 |
1.15e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.15e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 153791270 981 CDCHHEGSLSLQC-KEDGRCECREGFVGNRCDQCEENYfYNRSWPGC 1026
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGY-YGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
826-873 |
7.63e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 153791270 826 CQCNDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKEGFFGNPLAP 873
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
981-1027 |
7.78e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.78e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 153791270 981 CDCHHEGSLSLQC-KEDGRCECREGFVGNRCDQCEENYFYNRSWPGCQ 1027
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1065-1504 |
1.16e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.22 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1065 TDQAFEDRLKEAEREVTDLLREAQEvkdvdqnlmdRLQRVNSSL---HSQISRLQniRNTIEETGIL----AERARSRVE 1137
Cdd:NF041483 562 TERAIAARQAEAAEELTRLHTEAEE----------RLTAAEEALadaRAEAERIR--REAAEETERLrteaAERIRTLQA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1138 STEQLIEIASRElekakmAAANVSITQPEstGEpNNMTLLAEEARKLAERHK---QEADDIVRV-AKTANE----TSAEA 1209
Cdd:NF041483 630 QAEQEAERLRTE------AAADASAARAE--GE-NVAVRLRSEAAAEAERLKseaQESADRVRAeAAAAAErvgtEAAEA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1210 YNLLLRTLAGENQTALEI-----EELNRKYEQAKNISQDL-----------EKQAARVHEEA-KRAGD-------KAVEI 1265
Cdd:NF041483 701 LAAAQEEAARRRREAEETlgsarAEADQERERAREQSEELlasarkrveeaQAEAQRLVEEAdRRATElvsaaeqTAQQV 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1266 YASVAQLTPVDSE-------ALENEANKIKKEAAD-LDRL-------IDQKLKDYEDLREDMRGKEHEVKNLLEKGKAE- 1329
Cdd:NF041483 781 RDSVAGLQEQAEEeiaglrsAAEHAAERTRTEAQEeADRVrsdayaeRERASEDANRLRREAQEETEAAKALAERTVSEa 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1330 --------QQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKD-----FDRRVNDNKTAAEEALRRIPA----- 1391
Cdd:NF041483 861 iaeaerlrSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSdaaaqADRLIGEATSEAERLTAEARAeaerl 940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1392 INRTIAEANEKTREAQLALGNAAADAT-EAKN-KAHEAERIASAvQKNATSTKADAERTfgeVTDLDNEVNGML------ 1463
Cdd:NF041483 941 RDEARAEAERVRADAAAQAEQLIAEATgEAERlRAEAAETVGSA-QQHAERIRTEAERV---KAEAAAEAERLRtearee 1016
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 153791270 1464 --RQLEEAENEL-KKKQDDADQ-DMMMAGMASQAAQ---EAELNARKA 1504
Cdd:NF041483 1017 adRTLDEARKDAnKRRSEAAEQaDTLITEAAAEADQltaKAQEEALRT 1064
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1070-1503 |
3.14e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.68 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQE--VKDVDQNLMDRLQRVNSSlHSQISRL-QNIRNTIEETGILAERAR--SRVEStEQLIE 1144
Cdd:NF041483 271 EEALREARAEAEKVVAEAKEaaAKQLASAESANEQRTRTA-KEEIARLvGEATKEAEALKAEAEQALadARAEA-EKLVA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1145 IASrelEKAKMAAANVSITQ---PESTGEpNNMTLLAEEARKLAERHKQEADDIVRVAKT-ANETSAEAYNLL--LRTLA 1218
Cdd:NF041483 349 EAA---EKARTVAAEDTAAQlakAARTAE-EVLTKASEDAKATTRAAAEEAERIRREAEAeADRLRGEAADQAeqLKGAA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1219 GEN------QTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQ--LTPVDSEALE------NEA 1284
Cdd:NF041483 425 KDDtkeyraKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEelLTKAKADADElrstatAES 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1285 NKIKKEAadLDRLIDQKlKDYEDLREDMRGKEHEVKNllekgKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDI 1364
Cdd:NF041483 505 ERVRTEA--IERATTLR-RQAEETLERTRAEAERLRA-----EAEEQAEEVRAAAERAARELREETERAIAARQAEAAEE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1365 LNNLK-DFDRRVndnkTAAEEAL----------RRIPA--INRTIAEANEKTR--------EAQLALGNAAADATEAKNK 1423
Cdd:NF041483 577 LTRLHtEAEERL----TAAEEALadaraeaeriRREAAeeTERLRTEAAERIRtlqaqaeqEAERLRTEAAADASAARAE 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1424 ------------AHEAERIASAVQKNATSTKAD----AERTFGEVTD-LDNEVNGMLRQLEEAENELKKKQDDADQDMmm 1486
Cdd:NF041483 653 genvavrlrseaAAEAERLKSEAQESADRVRAEaaaaAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEADQER-- 730
|
490
....*....|....*..
gi 153791270 1487 aGMASQAAQEAELNARK 1503
Cdd:NF041483 731 -ERAREQSEELLASARK 746
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1094-1569 |
4.14e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1094 DQNLMDRLQRVNSSLHSQISRLQNIRNTIE-----------------------ETGILAERARSRVES--------TEQL 1142
Cdd:NF041483 133 DQELAERRQTVESHVNENVAWAEQLRARTEsqarrlldesraeaeqalaaaraEAERLAEEARQRLGSeaesaraeAEAI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1143 IEIASRELEK--------AKMAAANVSITQPESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKT-ANETSAEAYNLL 1213
Cdd:NF041483 213 LRRARKDAERllnaastqAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAeAEKVVAEAKEAA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1214 LRTLAG-----ENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQltpvdSEALENEANKIK 1288
Cdd:NF041483 293 AKQLASaesanEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKAR-----TVAAEDTAAQLA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1289 KEAADLDRLIDqklKDYEDLREDMRGKEHEVKNLLEKGKAEqqtADQLLAradaakalaeeaakkgrstlqEANDILNNL 1368
Cdd:NF041483 368 KAARTAEEVLT---KASEDAKATTRAAAEEAERIRREAEAE---ADRLRG---------------------EAADQAEQL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1369 KDF---DRRVNDNKTA--AEEALR--------RIPAI---NRTIAEA--------NEKTREAQLALGNAAADATEAKNKA 1424
Cdd:NF041483 421 KGAakdDTKEYRAKTVelQEEARRlrgeaeqlRAEAVaegERIRGEArreavqqiEEAARTAEELLTKAKADADELRSTA 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1425 H-EAERIASAVQKNATSTKADAERTFgEVTDLDNEvngmlRQLEEAENELKKKQDDADQdmmmagMASQAAQEAE--LNA 1501
Cdd:NF041483 501 TaESERVRTEAIERATTLRRQAEETL-ERTRAEAE-----RLRAEAEEQAEEVRAAAER------AARELREETEraIAA 568
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1502 RKAKnsvssllsqlnnLLDQLGQLDTVDLNKLNEIEGSLNKAKDEmkASDLDRKVSDlESEARKQEAA 1569
Cdd:NF041483 569 RQAE------------AAEELTRLHTEAEERLTAAEEALADARAE--AERIRREAAE-ETERLRTEAA 621
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
825-874 |
5.60e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 5.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 825 PCQCNDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKEGFFGNPLAPN 874
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1067-1603 |
2.15e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.99 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1067 QAFEDRL-KEAEREVTDLL----REAQEVKDVDQNLMDRLQRvnsslhsQISRLqniRNTIEETgilAERARSrvESTEQ 1141
Cdd:NF041483 752 QAEAQRLvEEADRRATELVsaaeQTAQQVRDSVAGLQEQAEE-------EIAGL---RSAAEHA---AERTRT--EAQEE 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1142 LIEIASRELEKAKMAAANVSITQPESTGEpnnmtllAEEARKLAERHKQEA-DDIVRVAKTANETSAEAYNLLLRTLAGE 1220
Cdd:NF041483 817 ADRVRSDAYAERERASEDANRLRREAQEE-------TEAAKALAERTVSEAiAEAERLRSDASEYAQRVRTEASDTLASA 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1221 NQTALEIEELNRkyEQAKNISQDLEKQAARVHEEAKRAGDKAVEiyASVAQLTPVDSEALENEANKIKKEAADLDRLIDQ 1300
Cdd:NF041483 890 EQDAARTRADAR--EDANRIRSDAAAQADRLIGEATSEAERLTA--EARAEAERLRDEARAEAERVRADAAAQAEQLIAE 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1301 KLKDYEDLR--------------EDMRGKEHEVKNLLEkGKAEQQTADqllaradaakalaeeAAKKGRSTLQEANdiln 1366
Cdd:NF041483 966 ATGEAERLRaeaaetvgsaqqhaERIRTEAERVKAEAA-AEAERLRTE---------------AREEADRTLDEAR---- 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1367 nlKDFDRRVNDnktAAEEALRripAINRTIAEANEKTREAQLALGNAAADATEAKNKA-----HEAERIAS--AVQKNAT 1439
Cdd:NF041483 1026 --KDANKRRSE---AAEQADT---LITEAAAEADQLTAKAQEEALRTTTEAEAQADTMvgaarKEAERIVAeaTVEGNSL 1097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1440 STKA--DA----------------------ERTFGEVTDLDNevngmlRQLEEAENELKKKQDDADQdMMMAGMASQAAQ 1495
Cdd:NF041483 1098 VEKArtDAdellvgarrdataireraeelrDRITGEIEELHE------RARRESAEQMKSAGERCDA-LVKAAEEQLAEA 1170
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1496 EAelnarKAKNSVssllsqlnnlLDQLGQLDTVDLNKLNEIEGSLNKAkdEMKASDLDRKVSDLESEA-RKQEAAIMDYN 1574
Cdd:NF041483 1171 EA-----KAKELV----------SDANSEASKVRIAAVKKAEGLLKEA--EQKKAELVREAEKIKAEAeAEAKRTVEEGK 1233
|
570 580 590
....*....|....*....|....*....|....*.
gi 153791270 1575 RDI-------AEIIKDIHNLEDIKKTLPTgcFNTPS 1603
Cdd:NF041483 1234 RELdvlvrrrEDINAEISRVQDVLEALES--FEAPS 1267
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1192-1333 |
8.56e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 52.76 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1192 ADDIVRVAKTANETSAEAYNLLLRtLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKaveiYASVAQ 1271
Cdd:cd22656 75 AGDIYNYAQNAGGTIDSYYAEILE-LIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDK----LTDFEN 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1272 LTPVDSEALENEANKIKK---------EAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTA 1333
Cdd:cd22656 150 QTEKDQTALETLEKALKDlltdeggaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA 220
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-328 |
4.49e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 4.49e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 153791270 283 RCKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRPWRR 328
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
826-870 |
6.68e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 6.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 153791270 826 CQCNDniDPNAVGNCNRLTGECLkCIYNTAGFYCDRCKEGFFGNP 870
Cdd:smart00180 1 CDCDP--GGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
340-394 |
1.19e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.18 E-value: 1.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 340 CDCNGR---SQECYFdpelyrstgHGGHCTnCRDNTDGAKCERCRENFFRLGNTEACS 394
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1122-1505 |
1.27e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.13 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1122 IEETGILAER--ARSRVESTEqLIEIASRELEKAKMAAANVSIT---QPESTgepnnmtllAEEARKLAERHKQEADDIV 1196
Cdd:NF041483 475 IEEAARTAEEllTKAKADADE-LRSTATAESERVRTEAIERATTlrrQAEET---------LERTRAEAERLRAEAEEQA 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1197 RVAKTANETSA----------------EAYNLL--LRTLAGENQTALEiEELNRKYEQAKNISQDLEKQAARVH------ 1252
Cdd:NF041483 545 EEVRAAAERAArelreeteraiaarqaEAAEELtrLHTEAEERLTAAE-EALADARAEAERIRREAAEETERLRteaaer 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1253 ---------EEAKRAGDKAV-EIYASVAQLTPV----DSEAlENEANKIKKEAAD-LDRLIDQKLKDYEDL--------- 1308
Cdd:NF041483 624 irtlqaqaeQEAERLRTEAAaDASAARAEGENVavrlRSEA-AAEAERLKSEAQEsADRVRAEAAAAAERVgteaaeala 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1309 --REDMRGKEHEVKNLLEKGKAEqqtADQllaRADAAKALAEEAAKKGRSTLQEANDILNNL-KDFDRRVNDNKTAAEE- 1384
Cdd:NF041483 703 aaQEEAARRRREAEETLGSARAE---ADQ---ERERAREQSEELLASARKRVEEAQAEAQRLvEEADRRATELVSAAEQt 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1385 --------------ALRRIPAInRTIAE-ANEKTR-EAQLALGNAAADATEAKNKAHE-AERIASAVQKNATSTKADAER 1447
Cdd:NF041483 777 aqqvrdsvaglqeqAEEEIAGL-RSAAEhAAERTRtEAQEEADRVRSDAYAERERASEdANRLRREAQEETEAAKALAER 855
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1448 TFGEVtdldnevngmlrqLEEAEnelKKKQDDADQDMMMAGMASQAAQEAELNARKAK 1505
Cdd:NF041483 856 TVSEA-------------IAEAE---RLRSDASEYAQRVRTEASDTLASAEQDAARTR 897
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
770-818 |
1.53e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 770 PCPCPGGSSCAIVPKTKEVVCtHCPTGTAGKRCELCDDGYFGDPLGSNG 818
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
339-387 |
4.20e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 39.64 E-value: 4.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 153791270 339 PCDCNGR---SQECYFdpelyrstgHGGHCTnCRDNTDGAKCERCRENFFRL 387
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
284-325 |
1.36e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 153791270 284 CKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRP 325
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
284-326 |
8.39e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 35.75 E-value: 8.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 153791270 284 CKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRPW 326
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
42-282 |
2.24e-119 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 374.39 E-value: 2.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 42 GGRPQRCMPEFVNAAFNVTVVATNTCGTP-PEEYCVQTGVTGVTKSCHLCDAGQQHLQHGAAFLTDYNNQADTTWWQSQT 120
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 121 MLAGVQYpnsINLTLHLGKAFDITYVRLKFHTSRPeSFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGgDEQQ 200
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 201 ALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFND-PKVLKSYYYAISDFA 279
Cdd:smart00136 156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIA 235
|
...
gi 153791270 280 VGG 282
Cdd:smart00136 236 VGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
48-282 |
3.11e-114 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 359.97 E-value: 3.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 48 CMPEFVNAAFNVTVVATNTCGT-PPEEYCVQTGVTGVtKSCHLCDAGQQHLQHGAAFLTDYNNQADTTWWQSQTMLagVQ 126
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLnGPERYCILSGLEGG-KKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 127 YPNsINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGfiRTGGDEQQALCTDE 206
Cdd:pfam00055 78 YEN-VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGP--SRGIKDDEVICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791270 207 FSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGG 282
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
551-676 |
2.89e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 551 SYFPRYFIAPVKFLGNQVLSYGQNLSFSFRVD--RRDTRLSAEDLVLEGAGLRVSVPliAQGNSYPSE-TTVKYIFRLHE 627
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHP--AEGPPLPDElTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 153791270 628 ATDYPWRPALSPfEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLQSARP 676
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
556-686 |
8.30e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 144.33 E-value: 8.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 556 YFIAPVKFLGNQVLSYGQNLSFSFRVDRRD---TRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTvKYIFRLHEATdyp 632
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPgggSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQ-TYSVRLHEEN--- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 633 WR----PALSPFEFQKLLNNLTSIKIRGTYSERSAG-YLDDVTLQSARPGP-GVPATWVE 686
Cdd:pfam00052 77 WRdsdgAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPGGsGPPASWVE 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1033-1570 |
5.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1033 YRLVKDKVAEHRVKLQELESLIANLgtgddMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQI 1112
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1113 SRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEpnnmtlLAEEARKLAERHKQEA 1192
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1193 DDIVRVAKTANETSAEAyNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQL 1272
Cdd:COG1196 383 ELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1273 TpVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAK 1352
Cdd:COG1196 462 L-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1353 KGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAI---NRTIAEANEKTREAQLALGNAAADATEAKNKAH---- 1425
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDkirARAALAAALARGAIGAAVDLVASDLREADARYYvlgd 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1426 --EAERIASAVQKNATSTKADAERTFGEVTDLDNEVNG-----------MLRQLEEAENELKKKQDDADQDMMMAGMASQ 1492
Cdd:COG1196 621 tlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1493 AAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRkvSDLESEARKQEAAI 1570
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL--EELERELERLEREI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1070-1594 |
7.75e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLhsqiSRLQNIRNTIEETGILAERARSRVESTEQLI-EIASR 1148
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIrELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1149 ------ELEKAKmaaanvsitqpESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQ 1222
Cdd:PRK03918 268 ieelkkEIEELE-----------EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1223 TAlEIEELNRKYEQAKNISQDLEKQAaRVHEEAKRAGDKAVEIYASVAQLTPVDSEA-----------LENEANKIKKEA 1291
Cdd:PRK03918 337 EE-RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1292 ADLDRLIDQKLKDYEDLREdMRGK---------EHEVKNLLEKGKAEQQTAdqllaradaakalaeeaakkgRSTLQEAN 1362
Cdd:PRK03918 415 GELKKEIKELKKAIEELKK-AKGKcpvcgreltEEHRKELLEEYTAELKRI---------------------EKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1363 DILNNLKDFDRRVnDNKTAAEEALRRIPAINRTIAEANEKTREAqlalgnaaaDATEAKNKAHEAERI---ASAVQKNAT 1439
Cdd:PRK03918 473 EKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKY---------NLEELEKKAEEYEKLkekLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1440 STKADAERTfgevtdldNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASqaaqEAELNAR------------KAKNS 1507
Cdd:PRK03918 543 SLKKELEKL--------EELKKKLAELEKKLDELEEELAELLKELEELGFES----VEELEERlkelepfyneylELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1508 VSSLLSQLNNLLDQLGQLDTVdLNKLNEIEGSLNKAKDEMKasDLDRKVSD------------LESEARKQEAAIMDYNR 1575
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELE--ELEKKYSEeeyeelreeyleLSRELAGLRAELEELEK 687
|
570
....*....|....*....
gi 153791270 1576 DIAEIIKDIHNLEDIKKTL 1594
Cdd:PRK03918 688 RREEIKKTLEKLKEELEER 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1034-1596 |
1.16e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.72 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKLQELESLIANLGTGDDMVTDQA--FEDRLKEAEREVTDLLREAQEVKDvDQNLMDRLQRVNSSLHSQ 1111
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQA-RLDSLERLQENLEGFSEG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1112 ISRLQNIRNTIE-ETGILAERARSRvESTEQLIEIASREL------EKAKMAAANVSITQPESTGEPNNMTLLAEEARKL 1184
Cdd:TIGR02168 508 VKALLKNQSGLSgILGVLSELISVD-EGYEAAIEAALGGRlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1185 AERHKQEADDIVRVAKTANE--TSAEAYNLLLRTLAG-----EN-QTALEIEELNRKYEQ-------------------A 1237
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGgvlvvDDlDNALELAKKLRPGYRivtldgdlvrpggvitggsA 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1238 KNISQDLEKQA--ARVHEEAKRAGDKAVEIYASVAQLTpVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLR------ 1309
Cdd:TIGR02168 667 KTNSSILERRReiEELEEKIEELEEKIAELEKALAELR-KELEELEEELEQLRKELEELSRQISALRKDLARLEaeveql 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1310 -EDMRGKEHEVKNL----------LEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKdfdRRVNDN 1378
Cdd:TIGR02168 746 eERIAQLSKELTELeaeieeleerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN---EEAANL 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1379 KTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAA---DATEAKNKAHEaERIASAVQKNATSTKADAERTfgEVTDL 1455
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELES-ELEALLNERASLEEALALLRS--ELEEL 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1456 DNEVNGMLRQLEEAENELKKKQDDADQ--------DMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDT 1527
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQlelrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1528 -------VDLNKLNEIEgSLNKAKDEmkasdLDRKVSDLEsEARKQ-EAAIMDYNRDIAEIIKDIhnLEDIKKTLPT 1596
Cdd:TIGR02168 980 kikelgpVNLAAIEEYE-ELKERYDF-----LTAQKEDLT-EAKETlEEAIEEIDREARERFKDT--FDQVNENFQR 1047
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1036-1594 |
2.03e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1036 VKDKVAEHRVKLQELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQIS-- 1113
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEea 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1114 -RLQNIRNTIEETGILAERARSRVESTEQLIEI-------ASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARKL- 1184
Cdd:PTZ00121 1315 kKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAakaeaeaAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAd 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1185 -----AERHKQEADDIVRVA---KTANETSAEAYNLL----LRTLAGENQTAleiEELNRKYEQAKNiSQDLEKQA--AR 1250
Cdd:PTZ00121 1395 eakkkAEEDKKKADELKKAAaakKKADEAKKKAEEKKkadeAKKKAEEAKKA---DEAKKKAEEAKK-AEEAKKKAeeAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1251 VHEEAKRAGDKAVEiyasvaqltpvdSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQ 1330
Cdd:PTZ00121 1471 KADEAKKKAEEAKK------------ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1331 QTADQLLARADAAKALAEEAAKKGRSTLQEANdilnnlKDFDRRVNDNKTAaeEALRRIPaiNRTIAEANEKTREAQLAL 1410
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAK------KAEEDKNMALRKA--EEAKKAE--EARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1411 GNAAADATEAKNKAHEAERIASAVQKNATSTKADAE--RTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAG 1488
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1489 MASQAAQEAELNARKAKnSVSSLLSQLNNLLDQLGQLDTVDLNKLNEI----EGSLNKAKDEMKASDLDRKVSDLESEAR 1564
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEENKIKAEEAkkeaEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
570 580 590
....*....|....*....|....*....|
gi 153791270 1565 KQEAAImdyNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:PTZ00121 1768 KKAEEI---RKEKEAVIEEELDEEDEKRRM 1794
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
443-490 |
2.29e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.53 E-value: 2.29e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 443 CSCDPSGS-TDECNVETGRCVCKDNVEGFNCERCKPGFFNLESSNPKGC 490
Cdd:pfam00053 1 CDCNPHGSlSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
933-978 |
3.18e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.11 E-value: 3.18e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 153791270 933 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGFGPEGC 978
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1071-1589 |
4.49e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1071 DRLKEAE-REVTDLLREAQEVKDVDQnLMDRLQRVNSSLHSQiSRLQNIRNTIEETGILAERARSRVESTEQLIEIASRE 1149
Cdd:PTZ00121 1281 DELKKAEeKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAK-KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1150 LEKAKMAAANVSITQPESTGEPNNMTLLAEEARKL------AERHKQEADDIVRVA---KTANETSAEAYNLL----LRT 1216
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeakkkAEEDKKKADELKKAAaakKKADEAKKKAEEKKkadeAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1217 LAGENQTAleiEELNRKYEQAKNiSQDLEKQA--ARVHEEAKRAGD---KAVEIYASVAQLTPVDSEALENEANKIK--- 1288
Cdd:PTZ00121 1439 KAEEAKKA---DEAKKKAEEAKK-AEEAKKKAeeAKKADEAKKKAEeakKADEAKKKAEEAKKKADEAKKAAEAKKKade 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1289 ------KEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEAN 1362
Cdd:PTZ00121 1515 akkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1363 DILNNLKDFD--------RRVNDNKTAA------EEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAE 1428
Cdd:PTZ00121 1595 EEVMKLYEEEkkmkaeeaKKAEEAKIKAeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1429 RIASAVQKNATSTKADAERTFGEvtdldNEVNGMLRQLEEAENELKKKQDDADQ-DMMMAGMASQAAQEAELNARKA--- 1504
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKE-----AEEAKKAEELKKKEAEEKKKAEELKKaEEENKIKAEEAKKEAEEDKKKAeea 1749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1505 ------KNSVSSLLSQLNNLLDQLGQldtvdlNKLNEIEGSLNKaKDEMKASDLDRKVSDLESEArkqeAAIMDYNRDIA 1578
Cdd:PTZ00121 1750 kkdeeeKKKIAHLKKEEEKKAEEIRK------EKEAVIEEELDE-EDEKRRMEVDKKIKDIFDNF----ANIIEGGKEGN 1818
|
570
....*....|.
gi 153791270 1579 EIIKDIHNLED 1589
Cdd:PTZ00121 1819 LVINDSKEMED 1829
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
932-979 |
1.65e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 1.65e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 932 RCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGF--GPEGCK 979
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
933-981 |
5.21e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 5.21e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 933 CDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGFGPEGCKPC 981
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1065-1591 |
6.53e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1065 TDQAFEDRLKEAEREVTDLLREAQEVKDV-DQNLMDRLQRVNSSLHSQISRLQNIRNTIEETGiLAERARsRVESTEQLI 1143
Cdd:PTZ00121 1108 TGKAEEARKAEEAKKKAEDARKAEEARKAeDARKAEEARKAEDAKRVEIARKAEDARKAEEAR-KAEDAK-KAEAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1144 EI-ASRELEKAKMAAANVSITQPESTGEPNNMTLlAEEARKL-----AERHKQEADDIVRVAKTANETSAEAYNLLLRTL 1217
Cdd:PTZ00121 1186 EVrKAEELRKAEDARKAEAARKAEEERKAEEARK-AEDAKKAeavkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1218 AGENQTALEIEElNRKYEQAKNISQDLEKQAARVHEEAKRAGD---KAVEiyasvaqltPVDSEALENEANKIKKEAADL 1294
Cdd:PTZ00121 1265 FARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKADEakkKAEE---------AKKADEAKKKAEEAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1295 DRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKalaeeaakkgrstlQEANDIlNNLKDFDRR 1374
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--------------KKAEEK-KKADEAKKK 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1375 VNDNKTAAEEaLRRIPAINRTIAEANEKTREAQlalgnaaaDATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTD 1454
Cdd:PTZ00121 1400 AEEDKKKADE-LKKAAAAKKKADEAKKKAEEKK--------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1455 LDNEVNGMLRQLEEAEnELKKKQDDADQDMMMAGMASQAAQEAElNARKA---KNSVSSLLSQLNNLLDQLGQLDTVdlN 1531
Cdd:PTZ00121 1471 KADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAeeaKKADEAKKAEEAKKADEAKKAEEK--K 1546
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791270 1532 KLNEIEGS--LNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLEDIK 1591
Cdd:PTZ00121 1547 KADELKKAeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
396-443 |
3.57e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 3.57e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 396 CHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPC 443
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
442-491 |
4.95e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 4.95e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 442 PCSCDPSGS-TDECNVETGRCVCKDNVEGFNCERCKPGFFNLeSSNPKGCT 491
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
722-761 |
5.88e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 5.88e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 153791270 722 CTCNGH---SETCDPETGVCDCRDNTAGPHCEKCSDGYYGDST 761
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
722-769 |
8.81e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 8.81e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 722 CTCNGH---SETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTLGTssDCQ 769
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
882-930 |
1.14e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.14e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 882 CACNPYGTVQqqSSCNPVTGQCQCLPHVSGRDCGTCDPGYYNLQ--SGQGC 930
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1044-1594 |
1.45e-11 |
|
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: 69.71 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1044 RVKLQELESLIANLGT----------GD--DMVTDQAFEDRL--------KEAEREVTDLLREAQEVKdvdQNlMDRLQR 1103
Cdd:TIGR02169 116 RVRLSEIHDFLAAAGIypegynvvlqGDvtDFISMSPVERRKiideiagvAEFDRKKEKALEELEEVE---EN-IERLDL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1104 VNSSLHSQISRLQNIRNTIEETGILAERARsRVESTEQL--IEIASRELEK--AKMAAANVSITQPESTGEPNNMTL--L 1177
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAERYQALLKEKR-EYEGYELLkeKEALERQKEAieRQLASLEEELEKLTEEISELEKRLeeI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1178 AEEARKLAERHKQEADD-IVRVAKTANETSAE---------AYNLLLRTLAGENQTAleIEELNRKYEQAKNISQDLEKQ 1247
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEeQLRVKEKIGELEAEiaslersiaEKERELEDAEERLAKL--EAEIDKLLAEIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1248 AARVHEEAKRAGDKAVEIYASVAQLTPVDS----------------EALENEANKIKKEaadLDRLIDQKLK---DYEDL 1308
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdelkdyreklEKLKREINELKRE---LDRLQEELQRlseELADL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1309 REDMRGKEHEVKNL---LEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKD-----------FDRR 1374
Cdd:TIGR02169 426 NAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelaeaeaqaraSEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1375 VNDNKtAAEEALR-RIPAINRTIAEANEKTREAQLALGNAA------------ADATEAKN--KAHEA------------ 1427
Cdd:TIGR02169 506 VRGGR-AVEEVLKaSIQGVHGTVAQLGSVGERYATAIEVAAgnrlnnvvveddAVAKEAIEllKRRKAgratflplnkmr 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1428 -------------------------ERIASAV------------------------------------------------ 1434
Cdd:TIGR02169 585 derrdlsilsedgvigfavdlvefdPKYEPAFkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprg 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1435 -QKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKnsvsslls 1513
Cdd:TIGR02169 665 gILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK-------- 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1514 qlnnllDQLGQLDTvdlnKLNEIEGSLNKAKDEMKasDLDRKVSDLESEARKQEAAIMDYNRDIA-EIIKDIHN-LEDIK 1591
Cdd:TIGR02169 737 ------ERLEELEE----DLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLShSRIPEIQAeLSKLE 804
|
...
gi 153791270 1592 KTL 1594
Cdd:TIGR02169 805 EEV 807
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
395-441 |
1.70e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 1.70e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 395 PCHCSPVGSLSTQCDSY-GRCSCKPGVMGDKCDRCQPGFHSLTEA--GCR 441
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
443-490 |
1.70e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 1.70e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 443 CSCDPSGS-TDECNVETGRCVCKDNVEGFNCERCKPGFFNlesSNPKGC 490
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
396-440 |
2.69e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 2.69e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 153791270 396 CHCSPVGSLSTQCDS-YGRCSCKPGVMGDKCDRCQPGFHSLTEAGC 440
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
881-931 |
3.71e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 3.71e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 153791270 881 ACACNPYGTVQQQssCNPVTGQCQCLPHVSGRDCGTCDPGYYNLQS-GQGCE 931
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1202-1569 |
4.71e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1202 ANETSAEAYNLL---LRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRA-GDKAVEIYASVAQLTPVDS 1277
Cdd:PTZ00121 1089 ADEATEEAFGKAeeaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAeDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1278 EALENEANKIK--------KEAADLDRLID----QKLKDYEDLR--EDMRGKEHEvKNLLEKGKAEQQTADQLLARADAA 1343
Cdd:PTZ00121 1169 ARKAEDAKKAEaarkaeevRKAEELRKAEDarkaEAARKAEEERkaEEARKAEDA-KKAEAVKKAEEAKKDAEEAKKAEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1344 KALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALR----RIPAINRTIAEANEKTREAQlalgnaaaDATE 1419
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadeaKKAEEKKKADEAKKKAEEAK--------KADE 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1420 AKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAE---NELKKKQDDADQDMMMAGMASQAAQE 1496
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1497 AELNARKAKNsvSSLLSQLNNLLDQLGQlDTVDLNKLNEIEgslNKAKDEMKASDLDRKVsdleSEARKQEAA 1569
Cdd:PTZ00121 1400 AEEDKKKADE--LKKAAAAKKKADEAKK-KAEEKKKADEAK---KKAEEAKKADEAKKKA----EEAKKAEEA 1462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1037-1594 |
1.37e-10 |
|
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: 66.62 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1037 KDKVAEHRVKLQELESLIanlgtgddmvtdQAFEDRLKEAEREVTDLLREAQEVKDVdqnlmdrLQRVNSSLHSQISRLQ 1116
Cdd:TIGR02168 336 AEELAELEEKLEELKEEL------------ESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1117 NIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQpestgepnnmtlLAEEARKLAERHkqeaDDIV 1196
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE------------LEEELEELQEEL----ERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1197 RVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLekqAARVHEEAKRAGDKAVeiyasVAQLTPVD 1276
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV---KALLKNQSGLSGILGV-----LSELISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1277 SE---ALENEAnkikkeAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKK 1353
Cdd:TIGR02168 533 EGyeaAIEAAL------GGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1354 GRSTLQEANDILNNLkdFDR-RVNDNKTAAEEALRRIPAINR-------------TIAEANEKTREAQLALGNAAADAT- 1418
Cdd:TIGR02168 607 LVKFDPKLRKALSYL--LGGvLVVDDLDNALELAKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILERRREIEELEe 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1419 ---EAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQdmMMAGMASQAAQ 1495
Cdd:TIGR02168 685 kieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ--LSKELTELEAE 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1496 EAELNARKAKNSvssllsqlnnllDQLGQLDTvdlnKLNEIEGSLNKAKDEMKA-----SDLDRKVSDLESEARKQEAAI 1570
Cdd:TIGR02168 763 IEELEERLEEAE------------EELAEAEA----EIEELEAQIEQLKEELKAlrealDELRAELTLLNEEAANLRERL 826
|
570 580
....*....|....*....|....
gi 153791270 1571 MDYNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEEL 850
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1042-1325 |
1.46e-10 |
|
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: 65.92 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1042 EHRVKLQELESLIANLGTGDDMVTDQafEDRLKEAEREVTDLLREAQEVKDVDQNL--MDRLQRVNSSLHSQISRLqniR 1119
Cdd:pfam05557 143 LLKAKASEAEQLRQNLEKQQSSLAEA--EQRIKELEFEIQSQEQDSEIVKNSKSELarIPELEKELERLREHNKHL---N 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1120 NTIEETGILAERA---RSRVESTEQL-IEIASRELEKAKMAAanvSITQPESTGEPNNMTLLAEEArkLAERHKQ-EADD 1194
Cdd:pfam05557 218 ENIENKLLLKEEVedlKRKLEREEKYrEEAATLELEKEKLEQ---ELQSWVKLAQDTGLNLRSPED--LSRRIEQlQQRE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1195 IVRVA-KTANETSAEAYNLLLRTLAGENQTAL-EIEELNRKYEQAKNISQDLEKQAARVHEEakRAGDKA-VEIYasvaq 1271
Cdd:pfam05557 293 IVLKEeNSSLTSSARQLEKARRELEQELAQYLkKIEDLNKKLKRHKALVRRLQRRVLLLTKE--RDGYRAiLESY----- 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 153791270 1272 ltpvDSEALENEANKIKKEaadldrlidqKLKDYEDLREDMRGKEHEVKNLLEK 1325
Cdd:pfam05557 366 ----DKELTMSNYSPQLLE----------RIEEAEDMTQKMQAHNEEMEAQLSV 405
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
882-930 |
1.62e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 1.62e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 882 CACNPYGTVQqqSSCNPVTGQCQCLPHVSGRDCGTCDPGYYNlQSGQGC 930
Cdd:smart00180 1 CDCDPGGSAS--GTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1072-1594 |
1.96e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1072 RLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQlieiaSRELE 1151
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-----DIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1152 KAKMAAANVSITQpestgepnnmtlLAEEARKLAERHKQEADDIVRVAKTANETSAEaynlllrtlagENQTALEIEELN 1231
Cdd:COG1196 308 EERRRELEERLEE------------LEEELAELEEELEELEEELEELEEELEEAEEE-----------LEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1232 RKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTpVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLRED 1311
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1312 MRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRipA 1391
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--G 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1392 INRTIAEANEKTREAQLALGNAAADATEAKNKAHE---AERIASAVQKNAT------STKADAERTFGEVTDLDNEVNGM 1462
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1463 LRQLEEAENELKKKQDDADQDmmmAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNK 1542
Cdd:COG1196 602 DLVASDLREADARYYVLGDTL---LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 153791270 1543 AKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
722-763 |
2.70e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 2.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 153791270 722 CTCNG---HSETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTLG 763
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
980-1027 |
3.09e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 3.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 980 PCDCHHEGSLSLQC-KEDGRCECREGFVGNRCDQCEENYFYNRSWP-GCQ 1027
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1027-1335 |
3.39e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1027 QECPACYRLVKDKVAEHRVKLQELESLIANLGTGDDmVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVN- 1105
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQe 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1106 --SSLHSQISRLQN------IRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLL 1177
Cdd:COG4717 221 elEELEEELEQLENeleaaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1178 AEEARKLAERHKQEA------DDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQA---KNISQDLEK-- 1246
Cdd:COG4717 301 GKEAEELQALPALEEleeeelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeleQEIAALLAEag 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1247 --------QAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALEN-EANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEH 1317
Cdd:COG4717 381 vedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
330
....*....|....*...
gi 153791270 1318 EVKNLLEKGKAEQQTADQ 1335
Cdd:COG4717 461 ELEQLEEDGELAELLQEL 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1034-1508 |
4.35e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKLQELESLIANLGTGDDMVTD-QAFEDRLKEAEREVTDLlREAQEVKDVDQNLMDRLQRvnssLHSQI 1112
Cdd:COG4717 57 ELFKPQGRKPELNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEEL-EAELEELREELEKLEKLLQ----LLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1113 SRLQNIRNTIEETGILAERARSRVESTEQLI-EIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARKLAERhKQE 1191
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-LAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1192 ADDIVRVAKTANETSAEAYNLLlrtlagenQTALEIEELNRKYEQAKNISQDLekqAARVHEEAKRAGDKAVEIY----- 1266
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLIA---AALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1267 ASVAQLTPVDSEALENEANKIKKEAADLD------RLIDQKLKDY-EDLREDMRGKEHEVKNLLEKGKAEQQTADQllar 1339
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQalpaleELEEEELEELlAALGLPPDLSPEELLELLDRIEELQELLRE---- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1340 adaakalaeeaakkgRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNaaadate 1419
Cdd:COG4717 356 ---------------AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE------- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1420 aknkaHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAEL 1499
Cdd:COG4717 414 -----LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
....*....
gi 153791270 1500 NARKAKNSV 1508
Cdd:COG4717 489 AEEWAALKL 497
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1044-1501 |
5.77e-10 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 63.77 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1044 RVKLQELESLIAN--------LGTGDDmvtdqAFEDRLKEAEREVtdllreaqevkdvdQNLMDRLQRVNSSLHSQISRL 1115
Cdd:COG5278 49 LRALEELLSALLDaetgqrgyLLTGDE-----SFLEPYEEARAEI--------------DELLAELRSLTADNPEQQARL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1116 QNIRNTIEETGILAER--ARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARKLAERHKQEAD 1193
Cdd:COG5278 110 DELEALIDQWLAELEQviALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1194 DIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHE-EAKRAGDKAVEIYASVAQL 1272
Cdd:COG5278 190 ELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALlLALLAALALAALLAAALLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1273 TPVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAK 1352
Cdd:COG5278 270 LAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1353 KGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIAS 1432
Cdd:COG5278 350 LLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALA 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791270 1433 AVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNA 1501
Cdd:COG5278 430 EALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAA 498
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1089-1300 |
6.66e-10 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 61.53 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1089 EVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPEST 1168
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1169 G-----------------------EPNNMTLL-------------------AEEARKLAERHKQEADDIVRVAKTANETS 1206
Cdd:smart00283 81 SaveeleessdeigeivsviddiaDQTNLLALnaaieaarageagrgfavvADEVRKLAERSAESAKEIESLIKEIQEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1207 AEAYNLLLRTLAGENQTALEIEELNRKYE----QAKNISQDLEKQAARVHEEAKRAGD--KAVEIYASVAQLTPVDSEAL 1280
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEeivdSVEEIADLVQEIAAATDEQAAGSEEvnAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|
gi 153791270 1281 ENEANKIKKEAADLDRLIDQ 1300
Cdd:smart00283 241 SAAAEELSGLAEELDELVER 260
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1088-1594 |
8.73e-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: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1088 QE-VKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETgilAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPE 1166
Cdd:pfam05483 62 QEgLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAE---LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1167 STGEPNNMTLLAEEARKLAERHKQEAddivrvAKTANETSAEAYnlllrtlagenqtalEIEELNRKYEQAKNisqDLEK 1246
Cdd:pfam05483 139 EIQENKDLIKENNATRHLCNLLKETC------ARSAEKTKKYEY---------------EREETRQVYMDLNN---NIEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1247 QAARVHEEAKRAGDKAVEIYASVAQltpvDSEALENEANKIKKEAADLDRLI----------DQKLKDYEDLREDMRGKe 1316
Cdd:pfam05483 195 MILAFEELRVQAENARLEMHFKLKE----DHEKIQHLEEEYKKEINDKEKQVsllliqitekENKMKDLTFLLEESRDK- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1317 heVKNLLEKGKAEQQTADQLLARADAAKalaeeaakkgrstlQEANDILNNLKdfdRRVNDNKTAAEEalrrIPAINRTI 1396
Cdd:pfam05483 270 --ANQLEEKTKLQDENLKELIEKKDHLT--------------KELEDIKMSLQ---RSMSTQKALEED----LQIATKTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1397 AEANEKtREAQLALGNAAADA-----TEAKNKAHEAERIASAVQ----KNATSTK---ADAERTFGEVTDLDNEVNGMLR 1464
Cdd:pfam05483 327 CQLTEE-KEAQMEELNKAKAAhsfvvTEFEATTCSLEELLRTEQqrleKNEDQLKiitMELQKKSSELEEMTKFKNNKEV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1465 QLEEAENELKKKQDDADQDMMMAGMASQ-AAQEAEL----NARKAKN-----SVSSLLSQLNNLLDQLGQLDT-VDLNKL 1533
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQFEKIAEElKGKEQELifllQAREKEIhdleiQLTAIKTSEEHYLKEVEDLKTeLEKEKL 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1534 NEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1089-1335 |
9.95e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.47 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1089 EVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNT-IEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSitqpES 1167
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1168 TGEPNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSaEAYNLLLR-------TLAGENQTALEIEELNRKYEQAKNI 1240
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLR-KEIERLEWrqqtevlSPEEEKELVEKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1241 -------------SQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTP-VDS-----EALENEANKIKKEAADLDRLIDQK 1301
Cdd:COG1340 156 lekneklkelraeLKELRKEAEEIHKKIKELAEEAQELHEEMIELYKeADElrkeaDELHKEIVEAQEKADELHEEIIEL 235
|
250 260 270
....*....|....*....|....*....|....
gi 153791270 1302 LKDYEDLREdmrgkehEVKNLLEKGKAEQQTADQ 1335
Cdd:COG1340 236 QKELRELRK-------ELKKLRKKQRALKREKEK 262
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
981-1026 |
1.15e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.15e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 153791270 981 CDCHHEGSLSLQC-KEDGRCECREGFVGNRCDQCEENYfYNRSWPGC 1026
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGY-YGDGPPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1038-1428 |
1.49e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.84 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1038 DKVAEhRVKLQELESLIANLGTGddmVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQN 1117
Cdd:COG4372 2 DRLGE-KVGKARLSLFGLRPKTG---ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1118 IRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANvsitqpestgepnnmtlLAEEARKLAERHKQEADDIVR 1197
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-----------------LQKERQDLEQQRKQLEAQIAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1198 VAKTANETSAEaynllLRTLAGE-NQTALEIEELNRKYEQAKNisQDLEKQAARVHEEAKRAGDKAVEIY-ASVAQLTPV 1275
Cdd:COG4372 141 LQSEIAEREEE-----LKELEEQlESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAeAEKLIESLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1276 DSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGR 1355
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1356 STLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAE 1428
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1042-1594 |
1.57e-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: 62.89 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1042 EHRVKL----QELESLIANLgtgddmvtdqafEDRLKEAEREVTDLLRE----AQEVKDVDQNLMD------RLQRVNSS 1107
Cdd:pfam01576 61 EMRARLaarkQELEEILHEL------------ESRLEEEEERSQQLQNEkkkmQQHIQDLEEQLDEeeaarqKLQLEKVT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1108 LHSQISRLQNIRNTIEETGILAERARSRVEstEQLIEIASR---ELEKAKMAaaNVSITQPEStgepnnMTLLAEEARKL 1184
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSKERKLLE--ERISEFTSNlaeEEEKAKSL--SKLKNKHEA------MISDLEERLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1185 AERHKQEADDIVRvaktanETSAEAYNLllrtlagENQTA---LEIEELnrkyeQAKNISQDLEKQAA--RVHEE--AKR 1257
Cdd:pfam01576 199 EEKGRQELEKAKR------KLEGESTDL-------QEQIAelqAQIAEL-----RAQLAKKEEELQAAlaRLEEEtaQKN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1258 AGDKAV-EIYASVAQLtpvdSEALENEA---NKIKKEAADLDRLIDQKLKDYED------LREDMRGK-EHEV----KNL 1322
Cdd:pfam01576 261 NALKKIrELEAQISEL----QEDLESERaarNKAEKQRRDLGEELEALKTELEDtldttaAQQELRSKrEQEVtelkKAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1323 LEKGKA-EQQTAD--QLLARADAAKALAEEAAKKGRSTLQEANDIL----NNLKDFDRRVNDNKTAAEEALRRIPA---- 1391
Cdd:pfam01576 337 EEETRShEAQLQEmrQKHTQALEELTEQLEQAKRNKANLEKAKQALesenAELQAELRTLQQAKQDSEHKRKKLEGqlqe 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1392 -------INRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAV----------------QKNATSTKadaert 1448
Cdd:pfam01576 417 lqarlseSERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtqellqeetrQKLNLSTR------ 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1449 fgeVTDLDNEVNGMLRQLEEAE-----------------NELKKKQDDadqdmmMAGmASQAAQEAELNARKAKNSVSSL 1511
Cdd:pfam01576 491 ---LRQLEDERNSLQEQLEEEEeakrnverqlstlqaqlSDMKKKLEE------DAG-TLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1512 LSQLNNLLDQL--------GQLD--TVDLNKLNEIEGSLNKAK---DEM----------KASDLDRKvsdlESEARKQEA 1568
Cdd:pfam01576 561 LEEKAAAYDKLektknrlqQELDdlLVDLDHQRQLVSNLEKKQkkfDQMlaeekaisarYAEERDRA----EAEAREKET 636
|
650 660
....*....|....*....|....*.
gi 153791270 1569 AIMDYNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:pfam01576 637 RALSLARALEEALEAKEELERTNKQL 662
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1111-1569 |
2.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1111 QISRL-----QNIRNTIEET-GILA-----ERARSRVESTEQLIEIAS---RELEKakmaaanvsitqpestgepnNMTL 1176
Cdd:COG1196 145 MIDRIieakpEERRAIIEEAaGISKykerkEEAERKLEATEENLERLEdilGELER--------------------QLEP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1177 LAEEARKlAERHKQeaddivrVAKTANETSAEAYnlllrtlagenqtALEIEELNRKYEQAKNISQDLEKQAARVHEEAk 1256
Cdd:COG1196 205 LERQAEK-AERYRE-------LKEELKELEAELL-------------LLKLRELEAELEELEAELEELEAELEELEAEL- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1257 ragdkaveiyasvaqltpvdsEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQl 1336
Cdd:COG1196 263 ---------------------AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1337 laradaakalaeeaakkgrstLQEANDILnnlkdfdrrvndnKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAAD 1416
Cdd:COG1196 321 ---------------------LEEELAEL-------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1417 ATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQE 1496
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1497 AELNARKAKNsvssllsqlnnlldQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAA 1569
Cdd:COG1196 447 AAEEEAELEE--------------EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1037-1479 |
3.95e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1037 KDKVAEHRVKLQELESLIanlgtgDDMVTDQAFEDrlkeAEREVTDLLREaqEVKDVDQNLMDRLQRVNSSLhsqisrlQ 1116
Cdd:PRK02224 278 AEEVRDLRERLEELEEER------DDLLAEAGLDD----ADAEAVEARRE--ELEDRDEELRDRLEECRVAA-------Q 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1117 NIRNTIEEtgiLAERARSRVESTEQLIEIASrELEkAKMAAANVSITQPESTgepnnMTLLAEEARKLAERHKQEADDIV 1196
Cdd:PRK02224 339 AHNEEAES---LREDADDLEERAEELREEAA-ELE-SELEEAREAVEDRREE-----IEELEEEIEELRERFGDAPVDLG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1197 RvaktanetsAEAYNLLLRtlagenqtaleiEELNRKYEQAKNISQDLEKQAARVHE-EAKRAGDKAVEIYASVAQLTPV 1275
Cdd:PRK02224 409 N---------AEDFLEELR------------EERDELREREAELEATLRTARERVEEaEALLEAGKCPECGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1276 DS--------EALENEANKIKKEAADLDRLIDQ--KLKDYEDLREDMRGKEHEVKNLLEKGKA----EQQTADQLLARAD 1341
Cdd:PRK02224 468 ETieedrervEELEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERREtieeKRERAEELRERAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1342 AAKALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAeEALRRIPAINRTIAEA-------NEKtREAQLALGNAA 1414
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAedeierlREK-REALAELNDER 625
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1415 ADATEAKNK-------AHEAERIASAVQK--NATSTKADAERTFGEVT----DLDNEVNGMLRQLEEAEnELKKKQDD 1479
Cdd:PRK02224 626 RERLAEKRErkreleaEFDEARIEEAREDkeRAEEYLEQVEEKLDELReerdDLQAEIGAVENELEELE-ELRERREA 702
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1046-1508 |
7.30e-09 |
|
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: 60.90 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1046 KLQELESLIANLGTgDDMVTDQAFEDRLKEAER-------EVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRL--- 1115
Cdd:pfam15921 318 QLSDLESTVSQLRS-ELREAKRMYEDKIEELEKqlvlansELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1116 --QNIRNTIEETG--ILAERARS-------RVESTEQLIEIASRELE---KAKMAA---ANVSI-------TQPESTGEp 1171
Cdd:pfam15921 397 keQNKRLWDRDTGnsITIDHLRRelddrnmEVQRLEALLKAMKSECQgqmERQMAAiqgKNESLekvssltAQLESTKE- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1172 nNMTLLAEE--ARKLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTAL-EIEELNRKYEQAKNISQDLEkqA 1248
Cdd:pfam15921 476 -MLRKVVEEltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLqELQHLKNEGDHLRNVQTECE--A 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1249 ARVHEEAKragDKAVEI--------------YASVAQLTPVDSEALENEANKIKKEAADLdrlidQKLKDYEDLRedMRG 1314
Cdd:pfam15921 553 LKLQMAEK---DKVIEIlrqqienmtqlvgqHGRTAGAMQVEKAQLEKEINDRRLELQEF-----KILKDKKDAK--IRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1315 KEHEVKNL-LEKGKAEQQTADQLLARadaakalaeeaakkgRSTLQEANDILNNLKDFDRRVNdNKTAAEEALRRipAIN 1393
Cdd:pfam15921 623 LEARVSDLeLEKVKLVNAGSERLRAV---------------KDIKQERDQLLNEVKTSRNELN-SLSEDYEVLKR--NFR 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1394 RTIAEANEKTREAQLALGNAAADATEAKN--KAHE-----AERIASAVQKNATSTKadaertfGEVTDLDNEVNGMLRQL 1466
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNtlKSMEgsdghAMKVAMGMQKQITAKR-------GQIDALQSKIQFLEEAM 757
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 153791270 1467 EEAENE---LKKKQDDADQDM-MMAGMASQAAQEAEL---NARKAKNSV 1508
Cdd:pfam15921 758 TNANKEkhfLKEEKNKLSQELsTVATEKNKMAGELEVlrsQERRLKEKV 806
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
826-873 |
7.63e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 153791270 826 CQCNDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKEGFFGNPLAP 873
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
981-1027 |
7.78e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.78e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 153791270 981 CDCHHEGSLSLQC-KEDGRCECREGFVGNRCDQCEENYFYNRSWPGCQ 1027
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1065-1504 |
1.16e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.22 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1065 TDQAFEDRLKEAEREVTDLLREAQEvkdvdqnlmdRLQRVNSSL---HSQISRLQniRNTIEETGIL----AERARSRVE 1137
Cdd:NF041483 562 TERAIAARQAEAAEELTRLHTEAEE----------RLTAAEEALadaRAEAERIR--REAAEETERLrteaAERIRTLQA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1138 STEQLIEIASRElekakmAAANVSITQPEstGEpNNMTLLAEEARKLAERHK---QEADDIVRV-AKTANE----TSAEA 1209
Cdd:NF041483 630 QAEQEAERLRTE------AAADASAARAE--GE-NVAVRLRSEAAAEAERLKseaQESADRVRAeAAAAAErvgtEAAEA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1210 YNLLLRTLAGENQTALEI-----EELNRKYEQAKNISQDL-----------EKQAARVHEEA-KRAGD-------KAVEI 1265
Cdd:NF041483 701 LAAAQEEAARRRREAEETlgsarAEADQERERAREQSEELlasarkrveeaQAEAQRLVEEAdRRATElvsaaeqTAQQV 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1266 YASVAQLTPVDSE-------ALENEANKIKKEAAD-LDRL-------IDQKLKDYEDLREDMRGKEHEVKNLLEKGKAE- 1329
Cdd:NF041483 781 RDSVAGLQEQAEEeiaglrsAAEHAAERTRTEAQEeADRVrsdayaeRERASEDANRLRREAQEETEAAKALAERTVSEa 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1330 --------QQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKD-----FDRRVNDNKTAAEEALRRIPA----- 1391
Cdd:NF041483 861 iaeaerlrSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSdaaaqADRLIGEATSEAERLTAEARAeaerl 940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1392 INRTIAEANEKTREAQLALGNAAADAT-EAKN-KAHEAERIASAvQKNATSTKADAERTfgeVTDLDNEVNGML------ 1463
Cdd:NF041483 941 RDEARAEAERVRADAAAQAEQLIAEATgEAERlRAEAAETVGSA-QQHAERIRTEAERV---KAEAAAEAERLRtearee 1016
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 153791270 1464 --RQLEEAENEL-KKKQDDADQ-DMMMAGMASQAAQ---EAELNARKA 1504
Cdd:NF041483 1017 adRTLDEARKDAnKRRSEAAEQaDTLITEAAAEADQltaKAQEEALRT 1064
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1033-1470 |
1.19e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 59.54 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1033 YRLVKDKVAEHrvkLQELESLIANLGTGDDMVTD--QAFEDRLKEAEREVtDLLRE-------AQEVKDVDQNLMDRLQR 1103
Cdd:COG5278 81 YEEARAEIDEL---LAELRSLTADNPEQQARLDEleALIDQWLAELEQVI-ALRRAggleaalALVRSGEGKALMDEIRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1104 VNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARK 1183
Cdd:COG5278 157 RLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1184 LAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAV 1263
Cdd:COG5278 237 ALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1264 EIYASVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAA 1343
Cdd:COG5278 317 AAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1344 KALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNK 1423
Cdd:COG5278 397 AAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAA 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 153791270 1424 AHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAE 1470
Cdd:COG5278 477 LAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAA 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1208-1582 |
1.47e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1208 EAYNLLLRTLagENQTALE--IEELNRKYEQaknisqdLEKQAARVHE-EAKRAGDKAVEIYASVAQLTPVDSE--ALEN 1282
Cdd:TIGR02168 176 ETERKLERTR--ENLDRLEdiLNELERQLKS-------LERQAEKAERyKELKAELRELELALLVLRLEELREEleELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1283 EANKIKKEAADLDRLIDQKLKDYEDLR----EDMRGKEHEVKNLLEKgKAEQQTADQllaradaakalaeeaakkgrsTL 1358
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRlevsELEEEIEELQKELYAL-ANEISRLEQ---------------------QK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1359 QEANDILNNLKDFDRRVNdnkTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAVQKNA 1438
Cdd:TIGR02168 305 QILRERLANLERQLEELE---AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1439 TSTKADAERTFGEVTDLDNEVNGMLRQLEeaenELKKKQDDADQDMMMAGMASQAAQEAELNARKAKnsvssllsQLNNL 1518
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLE----RLEDRRERLQQEIEELLKKLEEAELKELQAELEE--------LEEEL 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791270 1519 LDQLGQLDTVDlNKLNEIEGSLNKAKDEMKA--SDLDRKVSDLESEARKQEaAIMDYNRDIAEIIK 1582
Cdd:TIGR02168 450 EELQEELERLE-EALEELREELEEAEQALDAaeRELAQLQARLDSLERLQE-NLEGFSEGVKALLK 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1037-1452 |
1.69e-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: 59.35 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1037 KDKV--AEHRVKLQ----------------ELESLIANLGTgdDMVTDQAFEDRLKEAEREVTDLL--REAQevkdvdqn 1096
Cdd:pfam05483 267 RDKAnqLEEKTKLQdenlkeliekkdhltkELEDIKMSLQR--SMSTQKALEEDLQIATKTICQLTeeKEAQ-------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1097 lMDRLQRVNSSLHSQISRLQNIRNTIEEtgiLAERARSRVESTEQLIEIASRELEKAkmaaanvSITQPESTGEPNNMTL 1176
Cdd:pfam05483 337 -MEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKK-------SSELEEMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1177 LAEEARKLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENqtalEIEELNRKYEQAKNISQDLEKQAARVHEEAK 1256
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK----EIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1257 RAGDKAVEIYASVAQLTpVDSEALENEAN----KIKKEAADL-------DRLIDQ---------KLKD-YEDLREDMRGK 1315
Cdd:pfam05483 482 KEKLKNIELTAHCDKLL-LENKELTQEASdmtlELKKHQEDIinckkqeERMLKQienleekemNLRDeLESVREEFIQK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1316 EHEVKNLLEKGKAEQQTADQLLARADAAkalaeeaakkgrstLQEANDILNNLKdfdRRVNDNKTAAEEALRRIPAINRT 1395
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQ--------------MKILENKCNNLK---KQIENKNKNIEELHQENKALKKK 623
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1396 IAEANEKTREAQLALGNAAADATEAKNKAHEaerIASAVQKNATSTKADAERTFGEV 1452
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEEKLLEEV 677
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1070-1503 |
3.14e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.68 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQE--VKDVDQNLMDRLQRVNSSlHSQISRL-QNIRNTIEETGILAERAR--SRVEStEQLIE 1144
Cdd:NF041483 271 EEALREARAEAEKVVAEAKEaaAKQLASAESANEQRTRTA-KEEIARLvGEATKEAEALKAEAEQALadARAEA-EKLVA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1145 IASrelEKAKMAAANVSITQ---PESTGEpNNMTLLAEEARKLAERHKQEADDIVRVAKT-ANETSAEAYNLL--LRTLA 1218
Cdd:NF041483 349 EAA---EKARTVAAEDTAAQlakAARTAE-EVLTKASEDAKATTRAAAEEAERIRREAEAeADRLRGEAADQAeqLKGAA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1219 GEN------QTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQ--LTPVDSEALE------NEA 1284
Cdd:NF041483 425 KDDtkeyraKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEelLTKAKADADElrstatAES 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1285 NKIKKEAadLDRLIDQKlKDYEDLREDMRGKEHEVKNllekgKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDI 1364
Cdd:NF041483 505 ERVRTEA--IERATTLR-RQAEETLERTRAEAERLRA-----EAEEQAEEVRAAAERAARELREETERAIAARQAEAAEE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1365 LNNLK-DFDRRVndnkTAAEEAL----------RRIPA--INRTIAEANEKTR--------EAQLALGNAAADATEAKNK 1423
Cdd:NF041483 577 LTRLHtEAEERL----TAAEEALadaraeaeriRREAAeeTERLRTEAAERIRtlqaqaeqEAERLRTEAAADASAARAE 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1424 ------------AHEAERIASAVQKNATSTKAD----AERTFGEVTD-LDNEVNGMLRQLEEAENELKKKQDDADQDMmm 1486
Cdd:NF041483 653 genvavrlrseaAAEAERLKSEAQESADRVRAEaaaaAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEADQER-- 730
|
490
....*....|....*..
gi 153791270 1487 aGMASQAAQEAELNARK 1503
Cdd:NF041483 731 -ERAREQSEELLASARK 746
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1049-1594 |
3.58e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1049 ELESLI-ANLGTGDDMVTD-------QAFEDRLKEAEREVTDLLREAQEVKD---------VDQNLMDRLQRVNS---SL 1108
Cdd:PRK02224 139 EVNKLInATPSDRQDMIDDllqlgklEEYRERASDARLGVERVLSDQRGSLDqlkaqieekEEKDLHERLNGLESelaEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1109 HSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAaanvsITQPESTGEPnnmtlLAEEARKLAERH 1188
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET-----IAETEREREE-----LAEEVRDLRERL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1189 KQEADDIVRVAKTANETSAEAYNLLLRTLAGENqtalEIEELNRKYEQAKNISQDLEKQAARVHEEAKRagdkaveiyas 1268
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELED----RDEELRDRLEECRVAAQAHNEEAESLREDADD----------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1269 vaqltpvdseaLENEANKIKKEAADLDrlidqklKDYEDLREDMRGKEHEVKNLlekgkaEQQTADQllaradaakalae 1348
Cdd:PRK02224 354 -----------LEERAEELREEAAELE-------SELEEAREAVEDRREEIEEL------EEEIEEL------------- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1349 eaakkgRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAinrTIAEANEKTREAQ--LALGNAAADATEAKNKAHe 1426
Cdd:PRK02224 397 ------RERFGDAPVDLGNAEDFLEELREERDELREREAELEA---TLRTARERVEEAEalLEAGKCPECGQPVEGSPH- 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1427 AERIASAVQKnatstkadaertfgeVTDLDNEvngmLRQLEEAENELKKKQDDADQdmmmagmASQAAQEAELNARKAKN 1506
Cdd:PRK02224 467 VETIEEDRER---------------VEELEAE----LEDLEEEVEEVEERLERAED-------LVEAEDRIERLEERRED 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1507 svssllsqlnnlldqLGQLDTVDLNKLNEiegslnkakDEMKASDLDRKVSDLESEARKQEAA--------------IMD 1572
Cdd:PRK02224 521 ---------------LEELIAERRETIEE---------KRERAEELRERAAELEAEAEEKREAaaeaeeeaeeareeVAE 576
|
570 580
....*....|....*....|..
gi 153791270 1573 YNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLL 598
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1094-1569 |
4.14e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1094 DQNLMDRLQRVNSSLHSQISRLQNIRNTIE-----------------------ETGILAERARSRVES--------TEQL 1142
Cdd:NF041483 133 DQELAERRQTVESHVNENVAWAEQLRARTEsqarrlldesraeaeqalaaaraEAERLAEEARQRLGSeaesaraeAEAI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1143 IEIASRELEK--------AKMAAANVSITQPESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKT-ANETSAEAYNLL 1213
Cdd:NF041483 213 LRRARKDAERllnaastqAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAeAEKVVAEAKEAA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1214 LRTLAG-----ENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQltpvdSEALENEANKIK 1288
Cdd:NF041483 293 AKQLASaesanEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKAR-----TVAAEDTAAQLA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1289 KEAADLDRLIDqklKDYEDLREDMRGKEHEVKNLLEKGKAEqqtADQLLAradaakalaeeaakkgrstlqEANDILNNL 1368
Cdd:NF041483 368 KAARTAEEVLT---KASEDAKATTRAAAEEAERIRREAEAE---ADRLRG---------------------EAADQAEQL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1369 KDF---DRRVNDNKTA--AEEALR--------RIPAI---NRTIAEA--------NEKTREAQLALGNAAADATEAKNKA 1424
Cdd:NF041483 421 KGAakdDTKEYRAKTVelQEEARRlrgeaeqlRAEAVaegERIRGEArreavqqiEEAARTAEELLTKAKADADELRSTA 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1425 H-EAERIASAVQKNATSTKADAERTFgEVTDLDNEvngmlRQLEEAENELKKKQDDADQdmmmagMASQAAQEAE--LNA 1501
Cdd:NF041483 501 TaESERVRTEAIERATTLRRQAEETL-ERTRAEAE-----RLRAEAEEQAEEVRAAAER------AARELREETEraIAA 568
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1502 RKAKnsvssllsqlnnLLDQLGQLDTVDLNKLNEIEGSLNKAKDEmkASDLDRKVSDlESEARKQEAA 1569
Cdd:NF041483 569 RQAE------------AAEELTRLHTEAEERLTAAEEALADARAE--AERIRREAAE-ETERLRTEAA 621
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
825-874 |
5.60e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 5.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153791270 825 PCQCNDNIDPNavGNCNRLTGECLkCIYNTAGFYCDRCKEGFFGNPLAPN 874
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1071-1335 |
5.65e-08 |
|
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: 57.77 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1071 DRLKEAEREVTDLLREAQEVKdvdqNLMDRLQRVNSSLHSQISRLQNIRNTIEETgilAERARSRVESTEQLIEIASREL 1150
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIE----NRLDELSQELSDASRKIGEIEKEIEQLEQE---EEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1151 E--KAKMAAANVSITQPESTgepnnmtlLAEEARKLAERHKQEADDIVR-VAKTANETSAEAYNLLLRTLAGENqtalEI 1227
Cdd:TIGR02169 754 EnvKSELKELEARIEELEED--------LHKLEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQ----KL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1228 EELNRKYEQAKNISQDLEKQaaRVHEEAKRAGDKAvEIYASVAQLtpvdsEALENEANKIKKEAADLD-RLIDQKlKDYE 1306
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQ--RIDLKEQIKSIEK-EIENLNGKK-----EELEEELEELEAALRDLEsRLGDLK-KERD 892
|
250 260
....*....|....*....|....*....
gi 153791270 1307 DLREDMRgkehEVKNLLEKGKAEQQTADQ 1335
Cdd:TIGR02169 893 ELEAQLR----ELERKIEELEAQIEKKRK 917
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1042-1477 |
6.30e-08 |
|
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: 57.88 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1042 EHRVKLQE--LESLIANLGTGDDMVTDQAfeDRLKEAERE---VTDLLREAqEVKDVdqnlmdRLQRVNSSLHSQISRLQ 1116
Cdd:pfam01576 404 EHKRKKLEgqLQELQARLSESERQRAELA--EKLSKLQSElesVSSLLNEA-EGKNI------KLSKDVSSLESQLQDTQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1117 NIRNtiEETGI---LAERARS----RVESTEQLIE--IASRELEKaKMAAANVSITQPESTGEPNNMTL-LAEEARKLAE 1186
Cdd:pfam01576 475 ELLQ--EETRQklnLSTRLRQledeRNSLQEQLEEeeEAKRNVER-QLSTLQAQLSDMKKKLEEDAGTLeALEEGKKRLQ 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1187 R----------HKQEADDivRVAKTANETSAEaYNLLLRTLAGENQTALEIEELNRKYEQA----KNISqdlekqaARVH 1252
Cdd:pfam01576 552 RelealtqqleEKAAAYD--KLEKTKNRLQQE-LDDLLVDLDHQRQLVSNLEKKQKKFDQMlaeeKAIS-------ARYA 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1253 EEAKRAGDKAVEIYASVAQLtpvdSEALEnEANKIKKEaadLDRLIDQKLKDYEDL--REDMRGKE-HEvknlLEKGK-- 1327
Cdd:pfam01576 622 EERDRAEAEAREKETRALSL----ARALE-EALEAKEE---LERTNKQLRAEMEDLvsSKDDVGKNvHE----LERSKra 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1328 AEQQTADQllaradaakalaeeaakkgRSTLQEANDILnnlkdfdrrvndnkTAAEEALRRIpainrtiaEANEKTREAQ 1407
Cdd:pfam01576 690 LEQQVEEM-------------------KTQLEELEDEL--------------QATEDAKLRL--------EVNMQALKAQ 728
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791270 1408 LALG-NAAADATEAKNKA-------HEAERIASAVQK-NATSTKADAErtfGEVTDLDNEVNGMLRQLEEAENELKKKQ 1477
Cdd:pfam01576 729 FERDlQARDEQGEEKRRQlvkqvreLEAELEDERKQRaQAVAAKKKLE---LDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1226-1507 |
1.59e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1226 EIEELNRKYEQAKNISQDLEKQAARVHEEAkragdkaveiyasvaqltpvdsEALENEANKIKKEAADLDRLIDQKLKDY 1305
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAEL----------------------EELNEEYNELQAELEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1306 EDLREDMRGKEHEVKNLLekgKAEQQTADQLLARadaakalaeeaakkgrSTLQEANDIlnnlKDFDRRVndnktaaeEA 1385
Cdd:COG3883 75 AEAEAEIEERREELGERA---RALYRSGGSVSYL----------------DVLLGSESF----SDFLDRL--------SA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1386 LRRIPAINRTIAEAnekTREAQLALGNAAADATEAKNKAHEAERIASAVQKNATSTKADAErtfGEVTDLDNEVNGMLRQ 1465
Cdd:COG3883 124 LSKIADADADLLEE---LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE---ALLAQLSAEEAAAEAQ 197
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 153791270 1466 LEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKNS 1507
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1036-1606 |
1.70e-07 |
|
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: 56.18 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1036 VKDKVAEHRVKLQELESLIANLgtgddmvtdqafEDRLKEAEREVTDLLREAQevkdvdQNLmdrlqrvNSSLHSQIsrl 1115
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKEL------------EKQLNQLKSEISDLNNQKE------QDW-------NKELKSEL--- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1116 QNIRNTIEETgilaeraRSRVESTEQLI-----EIASRELEKAKMAAANVSITqpestgepnnmtllaeeaRKLAERHKQ 1190
Cdd:TIGR04523 317 KNQEKKLEEI-------QNQISQNNKIIsqlneQISQLKKELTNSESENSEKQ------------------RELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1191 eaddIVRVAKTANETSAEAYNLllrtlagENQtaleIEELNRKYEQAKNISQDLEKQAarvheeakragdkaveiyasva 1270
Cdd:TIGR04523 372 ----IEKLKKENQSYKQEIKNL-------ESQ----INDLESKIQNQEKLNQQKDEQI---------------------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1271 qltpvdsEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLlEKGKAEQQTadqllaradaakalaeea 1350
Cdd:TIGR04523 415 -------KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLET------------------ 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1351 akkgrstlqeandilnNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKaheaeri 1430
Cdd:TIGR04523 469 ----------------QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK------- 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1431 asavQKNATSTKADAERtfgEVTDLDNEVNGM-------------------LRQLEEAENELKKKQDDADqdmmmagmas 1491
Cdd:TIGR04523 526 ----IEKLESEKKEKES---KISDLEDELNKDdfelkkenlekeideknkeIEELKQTQKSLKKKQEEKQ---------- 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1492 qaaqeaELNARKAKNsvssllsqlnnlldqlgqldTVDLNKlnEIEgslnkaKDEMKASDLDRKVSDLESEARKQEAAIM 1571
Cdd:TIGR04523 589 ------ELIDQKEKE--------------------KKDLIK--EIE------EKEKKISSLEKELEKAKKENEKLSSIIK 634
|
570 580 590
....*....|....*....|....*....|....*
gi 153791270 1572 DYNRDIAEIIKDIHNledIKKTLPTGCFNTPSIEK 1606
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQ---IKETIKEIRNKWPEIIK 666
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1067-1603 |
2.15e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.99 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1067 QAFEDRL-KEAEREVTDLL----REAQEVKDVDQNLMDRLQRvnsslhsQISRLqniRNTIEETgilAERARSrvESTEQ 1141
Cdd:NF041483 752 QAEAQRLvEEADRRATELVsaaeQTAQQVRDSVAGLQEQAEE-------EIAGL---RSAAEHA---AERTRT--EAQEE 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1142 LIEIASRELEKAKMAAANVSITQPESTGEpnnmtllAEEARKLAERHKQEA-DDIVRVAKTANETSAEAYNLLLRTLAGE 1220
Cdd:NF041483 817 ADRVRSDAYAERERASEDANRLRREAQEE-------TEAAKALAERTVSEAiAEAERLRSDASEYAQRVRTEASDTLASA 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1221 NQTALEIEELNRkyEQAKNISQDLEKQAARVHEEAKRAGDKAVEiyASVAQLTPVDSEALENEANKIKKEAADLDRLIDQ 1300
Cdd:NF041483 890 EQDAARTRADAR--EDANRIRSDAAAQADRLIGEATSEAERLTA--EARAEAERLRDEARAEAERVRADAAAQAEQLIAE 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1301 KLKDYEDLR--------------EDMRGKEHEVKNLLEkGKAEQQTADqllaradaakalaeeAAKKGRSTLQEANdiln 1366
Cdd:NF041483 966 ATGEAERLRaeaaetvgsaqqhaERIRTEAERVKAEAA-AEAERLRTE---------------AREEADRTLDEAR---- 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1367 nlKDFDRRVNDnktAAEEALRripAINRTIAEANEKTREAQLALGNAAADATEAKNKA-----HEAERIAS--AVQKNAT 1439
Cdd:NF041483 1026 --KDANKRRSE---AAEQADT---LITEAAAEADQLTAKAQEEALRTTTEAEAQADTMvgaarKEAERIVAeaTVEGNSL 1097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1440 STKA--DA----------------------ERTFGEVTDLDNevngmlRQLEEAENELKKKQDDADQdMMMAGMASQAAQ 1495
Cdd:NF041483 1098 VEKArtDAdellvgarrdataireraeelrDRITGEIEELHE------RARRESAEQMKSAGERCDA-LVKAAEEQLAEA 1170
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1496 EAelnarKAKNSVssllsqlnnlLDQLGQLDTVDLNKLNEIEGSLNKAkdEMKASDLDRKVSDLESEA-RKQEAAIMDYN 1574
Cdd:NF041483 1171 EA-----KAKELV----------SDANSEASKVRIAAVKKAEGLLKEA--EQKKAELVREAEKIKAEAeAEAKRTVEEGK 1233
|
570 580 590
....*....|....*....|....*....|....*.
gi 153791270 1575 RDI-------AEIIKDIHNLEDIKKTLPTgcFNTPS 1603
Cdd:NF041483 1234 RELdvlvrrrEDINAEISRVQDVLEALES--FEAPS 1267
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1225-1588 |
2.24e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1225 LEIEELNRKY--EQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALEN-------EANK-IKKEAADL 1294
Cdd:PRK02224 72 LWFEHAGGEYhiERRVRLSGDRATTAKCVLETPEGTIDGARDVREEVTELLRMDAEAFVNcayvrqgEVNKlINATPSDR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1295 DRLIDQ-----KLKDY-----------EDLREDMRGKEHEVKNLLEkGKAEqqtadqllaradaakalaeeaakkgrstl 1358
Cdd:PRK02224 152 QDMIDDllqlgKLEEYrerasdarlgvERVLSDQRGSLDQLKAQIE-EKEE----------------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1359 qeandilnnlKDFDRRVNDNKTAAEEalrripaINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAVQKnA 1438
Cdd:PRK02224 202 ----------KDLHERLNGLESELAE-------LDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED-L 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1439 TSTKADAERtfgEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMmmAGMASQAAQEAELNARKAKnsvssllsqlnnL 1518
Cdd:PRK02224 264 RETIAETER---EREELAEEVRDLRERLEELEEERDDLLAEAGLDD--ADAEAVEARREELEDRDEE------------L 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1519 LDQLGQLDTVDLNKLNEIEGSLNKAKD-EMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLE 1588
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDlEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1034-1579 |
2.38e-07 |
|
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: 55.95 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKLQELESLIANLGT----GDDMVTDqaFEDRLKEAE--REVTDLLREAQEVKDVD-QNLMDRLQRVNS 1106
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKlknkHEAMISD--LEERLKKEEkgRQELEKAKRKLEGESTDlQEQIAELQAQIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1107 SLHSQISR----LQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSiTQPESTGEpnNMTLLAEE-- 1180
Cdd:pfam01576 233 ELRAQLAKkeeeLQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAE-KQRRDLGE--ELEALKTEle 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1181 ------ARKLAERHKQEADdiVRVAKTANETSAEAYNLLLRTLAGENQTALEieELNRKYEQAKNISQDLEK-------- 1246
Cdd:pfam01576 310 dtldttAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQALE--ELTEQLEQAKRNKANLEKakqalese 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1247 -----------QAARVHEEAKR-----------------------AGDKAVEIYASVAQLTPVDSEAlENEANKIKKEAA 1292
Cdd:pfam01576 386 naelqaelrtlQQAKQDSEHKRkklegqlqelqarlseserqraeLAEKLSKLQSELESVSSLLNEA-EGKNIKLSKDVS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1293 DLD-RLID----------QKL------KDYED----LREDMRGKEHEVKNL---------------------------LE 1324
Cdd:pfam01576 465 SLEsQLQDtqellqeetrQKLnlstrlRQLEDernsLQEQLEEEEEAKRNVerqlstlqaqlsdmkkkleedagtleaLE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1325 KGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEAND-----------ILNNL----KDFDRRVNDNKTA----AEEA 1385
Cdd:pfam01576 545 EGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdldhqrqLVSNLekkqKKFDQMLAEEKAIsaryAEER 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1386 lrripaiNRTIAEANEKTREAqLALGNAAADATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTD----LDNEVNG 1461
Cdd:pfam01576 625 -------DRAEAEAREKETRA-LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERskraLEQQVEE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1462 MLRQLEEAENELKKKQdDADQDMMMAGMASQAAQEAELNARkaknsvssllsqlnnllDQLGQLDTVDLNK-LNEIEGSL 1540
Cdd:pfam01576 697 MKTQLEELEDELQATE-DAKLRLEVNMQALKAQFERDLQAR-----------------DEQGEEKRRQLVKqVRELEAEL 758
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1541 N------------KAKDEMKASDLDRKVSDL---ESEARKQ----EAAIMDYNRDIAE 1579
Cdd:pfam01576 759 EderkqraqavaaKKKLELDLKELEAQIDAAnkgREEAVKQlkklQAQMKDLQRELEE 816
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1061-1283 |
3.63e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 54.62 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1061 DDMVTDQAFEDRLKEAE--REVTDLL-REAQEvkdvdqnlmdrlqrvnsslhsQISRLQNIRNTIEETGILAERARSRVE 1137
Cdd:pfam05262 179 DKKVVEALREDNEKGVNfrRDMTDLKeRESQE---------------------DAKRAQQLKEELDKKQIDADKAQQKAD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1138 STEQLIEIASRELEKAKMAAANVSitQPESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSAEAynlLLRTL 1217
Cdd:pfam05262 238 FAQDNADKQRDEVRQKQQEAKNLP--KPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFD---LKQES 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791270 1218 AGENQTAlEIEELNRKYEQaKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENE 1283
Cdd:pfam05262 313 KASEKEA-EDKELEAQKKR-EPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPVYGLKVVDPITNLSE 376
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1225-1594 |
5.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1225 LEIEELNRKYEQAKNISQDLEKQAARVHEEAKRagdkaveiyasvaqltpvdSEALENEANKIKKEAADLDRLIDQKLKD 1304
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKR-------------------TENIEELIKEKEKELEEVLREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1305 YEDLREDMRGKEHEVKnllekgkaeqqtadqllaradaakalaeeaakkgrsTLQEANDILNNLKDFDRRVNDNKTAAEE 1384
Cdd:PRK03918 216 LPELREELEKLEKEVK------------------------------------ELEELKEEIEELEKELESLEGSKRKLEE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1385 alrRIPAINRTIAEANEKTREaqlaLGNAAADATEAKNKAHEAERIaSAVQKNATSTKADAERtfgEVTDLDNEVNGMLR 1464
Cdd:PRK03918 260 ---KIRELEERIEELKKEIEE----LEEKVKELKELKEKAEEYIKL-SEFYEEYLDELREIEK---RLSRLEEEINGIEE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1465 QLEEAEN------ELKKKQDDADQDMM---------------MAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLG 1523
Cdd:PRK03918 329 RIKELEEkeerleELKKKLKELEKRLEeleerhelyeeakakKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1524 QLdTVDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLEDIKKTL 1594
Cdd:PRK03918 409 KI-TARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1040-1507 |
5.55e-07 |
|
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: 54.59 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1040 VAEHRVKLQELESLIANLGTGDDMVTDQAFED--RLKEAEREVTDL--LREAQEVKDVDQNL----------MDRLQRVN 1105
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsIREISCQQHTLTqhIHTLQQQKTTLTQKlqslckeldiLQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1106 SSLHSQISRLQnIRNTIEETGILAERARS---RVESTEQLIEIASRELEKAKMAAANVSITQPESTGEpnNMTLLAEEAR 1182
Cdd:TIGR00618 413 DTRTSAFRDLQ-GQLAHAKKQQELQQRYAelcAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE--QIHLQETRKK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1183 KLAERHKQEADDIVR-VAKTANETSAEAYNLLL------RTLAGENQTALEIEELNRKYEQAknisQDLEKQAARVHEEA 1255
Cdd:TIGR00618 490 AVVLARLLELQEEPCpLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDVYHQL----TSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1256 KRAgDKAVEIYASVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLkdyEDLREDMRGKEHEVkNLLEKGKAEQQTADQ 1335
Cdd:TIGR00618 566 QEI-QQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA---CEQHALLRKLQPEQ-DLQDVRLHLQQCSQE 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1336 LLARADAAKALAEEAakkgrsTLQEANDILNNLKDFDRRVNDNKTAAEEAL----RRIPAINRTIAEANEKTR------- 1404
Cdd:TIGR00618 641 LALKLTALHALQLTL------TQERVREHALSIRVLPKELLASRQLALQKMqsekEQLTYWKEMLAQCQTLLRelethie 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1405 -------EAQLALGNAAADaTEAKNKAH-----EAERIASAVQKNATSTKADA-------ERTFGEVTDLDNEVNGMLRQ 1465
Cdd:TIGR00618 715 eydrefnEIENASSSLGSD-LAAREDALnqslkELMHQARTVLKARTEAHFNNneevtaaLQTGAELSHLAAEIQFFNRL 793
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 153791270 1466 LEEAENELKKKQD------DADQDMMMAGMASQAAQEAELNARKAKNS 1507
Cdd:TIGR00618 794 REEDTHLLKTLEAeigqeiPSDEDILNLQCETLVQEEEQFLSRLEEKS 841
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1025-1334 |
5.83e-07 |
|
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: 54.67 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1025 GCqeCPACYRLVKDKvAEHRVKLQELESLIanlgtgddmvtdQAFEDRLKEAEREVTDLLREAQEV---KDVDQNLMDRL 1101
Cdd:TIGR00606 678 SC--CPVCQRVFQTE-AELQEFISDLQSKL------------RLAPDKLKSTESELKKKEKRRDEMlglAPGRQSIIDLK 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1102 QRvnsslhsqisRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEA 1181
Cdd:TIGR00606 743 EK----------EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1182 RKLaerhkqEADDIVRVAKTANETSAEAYNlLLRTLAGENqtaleieELNRKyeqaknISQDLEKQAARVHEEAKRAGDK 1261
Cdd:TIGR00606 813 AKL------QGSDLDRTVQQVNQEKQEKQH-ELDTVVSKI-------ELNRK------LIQDQQEQIQHLKSKTNELKSE 872
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1262 AVEIYASVAQltpvdSEALENEANKIKKEAADLDRLIDQK----LKDYEDLREDMRGKEHEV-KNLLEKGKAEQQTAD 1334
Cdd:TIGR00606 873 KLQIGTNLQR-----RQQFEEQLVELSTEVQSLIREIKDAkeqdSPLETFLEKDQQEKEELIsSKETSNKKAQDKVND 945
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1050-1586 |
6.70e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1050 LESLIANLGTGDDMVTDQAfedrlkeAEREvtDLLREAQEVKDVDQNlMDRLQRVNSSLHSQISRLQNIRNTIEETGILA 1129
Cdd:PRK01156 130 LNSIFVGQGEMDSLISGDP-------AQRK--KILDEILEINSLERN-YDKLKDVIDMLRAEISNIDYLEEKLKSSNLEL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1130 ERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSA-- 1207
Cdd:PRK01156 200 ENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEle 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1208 EAYNLLLRTLAGENQTAL-----EIEELNRKYEQAKNISQDLEKqaarvHEEAKRagdKAVEIyasvaqltpvdsEALEN 1282
Cdd:PRK01156 280 ERHMKIINDPVYKNRNYIndyfkYKNDIENKKQILSNIDAEINK-----YHAIIK---KLSVL------------QKDYN 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1283 EANKIKKEAADLDRLIDQkLKDYEDlreDMRGKEHEVKNLleKGKAEQQTADQLLARADAAKALAEEAAKKG-------- 1354
Cdd:PRK01156 340 DYIKKKSRYDDLNNQILE-LEGYEM---DYNSYLKSIESL--KKKIEEYSKNIERMSAFISEILKIQEIDPDaikkelne 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 -RSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRI------PAINRTIAEanEKTREAQLALGNaaaDATEAKNKAHEA 1427
Cdd:PRK01156 414 iNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcPVCGTTLGE--EKSNHIINHYNE---KKSRLEEKIREI 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1428 ERIASAVQKNATSTKADAER-TFGEVTDLDNEVNgmlrQLEEAENELKKKQDDADQdmmmagmasqaAQEAELNARKAKN 1506
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYlESEEINKSINEYN----KIESARADLEDIKIKINE-----------LKDKHDKYEEIKN 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1507 SVSSLlsqlnnlldQLGQLDT--VDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDI 1584
Cdd:PRK01156 554 RYKSL---------KLEDLDSkrTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI 624
|
..
gi 153791270 1585 HN 1586
Cdd:PRK01156 625 EN 626
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1036-1589 |
8.44e-07 |
|
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: 53.97 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1036 VKDKVAEHRVKLQELESlianlgTGDDMVTDQAFEDRLKEAER-EVTDLLREAQEVKDVDQNLMD----RLQRVNSSLHS 1110
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQM------ERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKCLKEDMLEdsntQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1111 QISRLQNIRNTIEEtgiLAERARSRVESTEQLIEIASRELEKA-----KMAAANVSITQPESTGEPNNMTLLAEEARKLA 1185
Cdd:pfam15921 182 HEGVLQEIRSILVD---FEEASGKKIYEHDSMSTMHFRSLGSAiskilRELDTEISYLKGRIFPVEDQLEALKSESQNKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1186 ERHKQEADDivRVAKTANETSAEAYNLL-----LRTLAGENQTALEIEElnrkyEQAKNIS-------QDLEKQAARVH- 1252
Cdd:pfam15921 259 ELLLQQHQD--RIEQLISEHEVEITGLTekassARSQANSIQSQLEIIQ-----EQARNQNsmymrqlSDLESTVSQLRs 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1253 --EEAKRAGDKAVEIYASvaQLTPVDSEALE--NEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKA 1328
Cdd:pfam15921 332 elREAKRMYEDKIEELEK--QLVLANSELTEarTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1329 EQQTADQLLARADAAKALaeeaakkgrstLQEANDILNNLKDFDRRVNDNKTAA----EEALRRIPAINRTIaeanEKTR 1404
Cdd:pfam15921 410 NSITIDHLRRELDDRNME-----------VQRLEALLKAMKSECQGQMERQMAAiqgkNESLEKVSSLTAQL----ESTK 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1405 EAqlaLGNAAADATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENE---LKKKQDD-- 1479
Cdd:pfam15921 475 EM---LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTEce 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1480 ------ADQDMMMAGMASQAAQEAELNARKAKNSVSSLLsqlnnlldQLGQLDT-VDLNKLNEIEGSLNKAKDEMKASDL 1552
Cdd:pfam15921 552 alklqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQV--------EKAQLEKeINDRRLELQEFKILKDKKDAKIREL 623
|
570 580 590
....*....|....*....|....*....|....*..
gi 153791270 1553 DRKVSDLESEARKqeaaIMDYNRDIAEIIKDIHNLED 1589
Cdd:pfam15921 624 EARVSDLELEKVK----LVNAGSERLRAVKDIKQERD 656
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1192-1333 |
8.56e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 52.76 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1192 ADDIVRVAKTANETSAEAYNLLLRtLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKaveiYASVAQ 1271
Cdd:cd22656 75 AGDIYNYAQNAGGTIDSYYAEILE-LIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDK----LTDFEN 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1272 LTPVDSEALENEANKIKK---------EAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTA 1333
Cdd:cd22656 150 QTEKDQTALETLEKALKDlltdeggaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1067-1310 |
1.00e-06 |
|
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: 52.84 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1067 QAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIA 1146
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1147 SRELEKAKMAAANVSITQpESTGEPNNMTLLAeearklaerHKQEADDIVRvaktanetSAEAYNLLLRTLAGE-NQTAL 1225
Cdd:COG4942 96 RAELEAQKEELAELLRAL-YRLGRQPPLALLL---------SPEDFLDAVR--------RLQYLKYLAPARREQaEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1226 EIEELNRKYEQAKNISQDLEKQAARVhEEAKRAGDKAVEIYASVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLKDY 1305
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 153791270 1306 EDLRE 1310
Cdd:COG4942 237 AAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1070-1597 |
1.45e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREV----TDLLREAQEVKDVDQNLMDRLQRVNSS------LHSQISRLQN--------IRNTIEETGILAER 1131
Cdd:TIGR04523 32 DTEEKQLEKKLktikNELKNKEKELKNLDKNLNKDEEKINNSnnkikiLEQQIKDLNDklkknkdkINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1132 ARSRVESTEQL-IEIASRELEK----AKMAAANVSITQPEstgepNNMTLLAEEARKLaERHKQE--------ADDIVRV 1198
Cdd:TIGR04523 112 IKNDKEQKNKLeVELNKLEKQKkenkKNIDKFLTEIKKKE-----KELEKLNNKYNDL-KKQKEElenelnllEKEKLNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1199 AKTANETSAE--AYNLLLRTLAGENQtalEIEELNRKYEQAKNISQDLEKQaarVHEEAKRAGDKAVEIYASVAQLTpvd 1276
Cdd:TIGR04523 186 QKNIDKIKNKllKLELLLSNLKKKIQ---KNKSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEISNTQTQLN--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1277 seALENEANKIKKEaadldrlIDQKLKDYEDLREDMRGKEHEVKNLlekgKAEQQTADQllaradaakalaeeaakkgrs 1356
Cdd:TIGR04523 257 --QLKDEQNKIKKQ-------LSEKQKELEQNNKKIKELEKQLNQL----KSEISDLNN--------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1357 tlQEANDILNNLKDFDRRVNDNKTAAEEALR----RIPAINRTIA----EANEKTREaqlalgNAAADaTEAKNKAHEAE 1428
Cdd:TIGR04523 303 --QKEQDWNKELKSELKNQEKKLEEIQNQISqnnkIISQLNEQISqlkkELTNSESE------NSEKQ-RELEEKQNEIE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1429 RIASAVQ------KNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMmmagmASQAAQEAELNAR 1502
Cdd:TIGR04523 374 KLKKENQsykqeiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI-----IKNNSEIKDLTNQ 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1503 KA--KNSVssllsqlnnllDQLGQLDTVDLNKLNEIEGSLNKAKDEMKA-------------------SDLDRKVSDLES 1561
Cdd:TIGR04523 449 DSvkELII-----------KNLDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekelkklneekKELEEKVKDLTK 517
|
570 580 590
....*....|....*....|....*....|....*.
gi 153791270 1562 EARKQEAAIMDYNRDIAEIIKDIHNLEDIKKTLPTG 1597
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1047-1326 |
1.68e-06 |
|
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: 53.26 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1047 LQELESLIANLGTGDDMVTDQafedrLKEAEREVTDLLREAQEVKdvdqnlMDRLQRVNSSLHSQiSRLQNIRNTI---E 1123
Cdd:pfam01576 779 LKELEAQIDAANKGREEAVKQ-----LKKLQAQMKDLQRELEEAR------ASRDEILAQSKESE-KKLKNLEAELlqlQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1124 ETGILAERARSRV--ESTEQLIEIASRELEKAKMA------AANVSITQPESTGEPNNMTLLAEEARKLAerhkQEADDI 1195
Cdd:pfam01576 847 EDLAASERARRQAqqERDELADEIASGASGKSALQdekrrlEARIAQLEEELEEEQSNTELLNDRLRKST----LQVEQL 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1196 vrvaktANETSAEaynlllRTLAGENQTALEieELNRKYEQAKNISQDLEKQAARVHeeakRAGDKAVEiyASVAQLtpv 1275
Cdd:pfam01576 923 ------TTELAAE------RSTSQKSESARQ--QLERQNKELKAKLQEMEGTVKSKF----KSSIAALE--AKIAQL--- 979
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1276 dSEALENEAnKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKG 1326
Cdd:pfam01576 980 -EEQLEQES-RERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKG 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1038-1607 |
2.07e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1038 DKVAEHRVKLQELESLIANLGtGDDMVtdqAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQN 1117
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLG-EEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1118 IRNTIEETGILAERARSRVESTEQLIEIASRELE---------KAKMAAANVSITQPESTGEPNNMTL--LAEEARKLAE 1186
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkefaetRDELKDYREKLEKLKREINELKRELdrLQEELQRLSE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1187 R---HKQEADDIvRVAKTANETSAEAYNLLLRTLAGENQTALEI-EELNRKYEQAKNISQDLEKQAARVHEEAKRA---- 1258
Cdd:TIGR02169 421 EladLNAAIAGI-EAKINELEEEKEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaqa 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1259 --------GDKAVE---------IYASVAQLTPVDSE---ALENEA---------------------------------- 1284
Cdd:TIGR02169 500 raseervrGGRAVEevlkasiqgVHGTVAQLGSVGERyatAIEVAAgnrlnnvvveddavakeaiellkrrkagratflp 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1285 -NKIKKEAADLDRL--------------IDQK------------------------------------------------ 1301
Cdd:TIGR02169 580 lNKMRDERRDLSILsedgvigfavdlveFDPKyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggs 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1302 ----------LKDYEDLREdMRGKEHEVKNLLEKGKAE----QQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNN 1367
Cdd:TIGR02169 660 raprggilfsRSEPAELQR-LRERLEGLKRELSSLQSElrriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1368 LKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAaadateaknKAHEAERIASAVQKNATSTKADAER 1447
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1448 TFGEVTDLDNEVNGMLRQLEEAENELKKKQDdaDQDMMMAGMASQAAQEAELNARKAKnsvssllsqlnnlldqlgqLDT 1527
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQE--QRIDLKEQIKSIEKEIENLNGKKEE-------------------LEE 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1528 vdlnKLNEIEGSLNKAKDEMKasDLDRKVSDLESEARKQEAAIMDYNrdiAEIIKDIHNLEDIKKTLPTGCFNTPSIEKP 1607
Cdd:TIGR02169 869 ----ELEELEAALRDLESRLG--DLKKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1387-1483 |
2.25e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 49.57 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1387 RRIPAINRTIAEANEKTREAQLALGNAAADATEAKnkaHEAERIASAVQKNATSTKADAE-RTFGEV--------TDLDN 1457
Cdd:PRK07352 50 ERREAILQALKEAEERLRQAAQALAEAQQKLAQAQ---QEAERIRADAKARAEAIRAEIEkQAIEDMarlkqtaaADLSA 126
|
90 100 110
....*....|....*....|....*....|....*
gi 153791270 1458 E---VNGMLRQ------LEEAENELKKKQDDADQD 1483
Cdd:PRK07352 127 EqerVIAQLRReaaelaIAKAESQLPGRLDEDAQQ 161
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1044-1568 |
2.84e-06 |
|
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: 52.28 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1044 RVKLQ---ELESLIANLGTGDDMVTDQAFEDRLKEAeREVTDLLREAQEV---KDVDQNLMDRLQRVNSSLHSQISRLQN 1117
Cdd:TIGR00618 196 AELLTlrsQLLTLCTPCMPDTYHERKQVLEKELKHL-REALQQTQQSHAYltqKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1118 IRNTIEETGILAERARsrvesteqlieiasrelEKAKMAAANVSITQPESTGEPNNMTLLAEEARKLAERHKqeaddivR 1197
Cdd:TIGR00618 275 QEAVLEETQERINRAR-----------------KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK-------R 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1198 VAKTANETSAEAYNLLLRTLAGENqtaleiEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKaveiyasvaqltpvds 1277
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQE------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK---------------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1278 EALENEANKIKKEAADLDRL---IDQKLKDYEDLREDMRGKEHEVKnlLEKGKAEQQtaDQLLARADAAKALAEEAAKKG 1354
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLAHAKKQQE--LQQRYAELC--AAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 RSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAAD-----ATEAKNKAHE--- 1426
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrrmqRGEQTYAQLEtse 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1427 --AERIASAVQKNATSTKADAER---TFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQaAQEAELNA 1501
Cdd:TIGR00618 545 edVYHQLTSERKQRASLKEQMQEiqqSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH-ALLRKLQP 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1502 RKAKNSVSSllsqlnnlldQLGQLDTVDLNKLNEIEG-SLNKAKDEMKASDLDRKVSDLESEARKQEA 1568
Cdd:TIGR00618 624 EQDLQDVRL----------HLQQCSQELALKLTALHAlQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1043-1561 |
2.90e-06 |
|
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: 52.43 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1043 HRVKLQELESLIANL--GTG------DDMVT------DQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQ-RVNSS 1107
Cdd:pfam15921 182 HEGVLQEIRSILVDFeeASGkkiyehDSMSTmhfrslGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQnKIELL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1108 LHSQISRLQNI--RNTIEETGIL--AERARSRVESTEQLIEIAsRELEKAKMAAANVSITQPESTgepnnMTLLAEEARK 1183
Cdd:pfam15921 262 LQQHQDRIEQLisEHEVEITGLTekASSARSQANSIQSQLEII-QEQARNQNSMYMRQLSDLEST-----VSQLRSELRE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1184 LAERHKQEADDIVRVAKTANETSAEAynlllRTlagenqtaleieELNRKYEQAKNISQDLEKQAARVHEEAKRAgdkav 1263
Cdd:pfam15921 336 AKRMYEDKIEELEKQLVLANSELTEA-----RT------------ERDQFSQESGNLDDQLQKLLADLHKREKEL----- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1264 eiyasvaqltpvdseALENEANKikkeaadldRLIDQKLKD---YEDLREDMRGKEHEVKNLLE---------KGKAEQQ 1331
Cdd:pfam15921 394 ---------------SLEKEQNK---------RLWDRDTGNsitIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQ 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1332 TA-----DQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTI----AEANEK 1402
Cdd:pfam15921 450 MAaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEItklrSRVDLK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1403 TREAQLA------LGNAAADATEAKNKAHEAERIASAVQK---NATSTKADAERTFG----EVTDLDNEVNGmlRQLEEA 1469
Cdd:pfam15921 530 LQELQHLknegdhLRNVQTECEALKLQMAEKDKVIEILRQqieNMTQLVGQHGRTAGamqvEKAQLEKEIND--RRLELQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1470 ENELKKKQDDADQDMMMAGMASQAAQEAEL-NA-----RKAK----------NSVSSLLSQLNNLLDQLGQLDTVDLNKL 1533
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKVKLvNAgserlRAVKdikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
570 580 590
....*....|....*....|....*....|
gi 153791270 1534 NEIEGSLNKAKDEMKA--SDLDRKVSDLES 1561
Cdd:pfam15921 688 EEMETTTNKLKMQLKSaqSELEQTRNTLKS 717
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1040-1333 |
2.96e-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: 52.13 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1040 VAEHRVKLQELESLIAN-----LGTGDDMVTDQA----FEDRLKEAEREVTDLLRE----AQEVKDVDQ---NLMDRLQr 1103
Cdd:pfam10174 347 VDALRLRLEEKESFLNKktkqlQDLTEEKSTLAGeirdLKDMLDVKERKINVLQKKienlQEQLRDKDKqlaGLKERVK- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1104 vnsSLHSQISRLQNIRNTIEETgiLAE-----------RARSRVESTEQLiEIASRELEKAKmaaANVSITQPESTGEPN 1172
Cdd:pfam10174 426 ---SLQTDSSNTDTALTTLEEA--LSEkeriierlkeqREREDRERLEEL-ESLKKENKDLK---EKVSALQPELTEKES 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1173 NMTLLAEEARKLAERHKQEaDDIVRVAKTANETSAEAYNlllrTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVH 1252
Cdd:pfam10174 497 SLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECS----KLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYK 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1253 EEAKRAgdkaveiYASVAQLTPVDSEAlENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVK----NLLEKGKA 1328
Cdd:pfam10174 572 EESGKA-------QAEVERLLGILREV-ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkgaQLLEEARR 643
|
....*
gi 153791270 1329 EQQTA 1333
Cdd:pfam10174 644 REDNL 648
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-328 |
4.49e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 4.49e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 153791270 283 RCKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRPWRR 328
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1071-1605 |
6.60e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1071 DRLKEAEREVTDLLREAQEVKDvDQNLMDRLQRVNSSLHSQISRLqnIRNTIEETGILAERARSRVES-TEQLIEIA--S 1147
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIEK-DKTSLEEVKGINLSYGKNLGKL--FLEKIDEEKKKSEHMIKAMEAyIEDLDEIKekS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1148 RELE---------KAKMAAANVSITQPE-----STGEPNNMTLLAEEARKLAERHKQEAD--DIVRVAKTaNETSAEAYN 1211
Cdd:TIGR01612 1260 PEIEnemgiemdiKAEMETFNISHDDDKdhhiiSKKHDENISDIREKSLKIIEDFSEESDinDIKKELQK-NLLDAQKHN 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1212 LLLRTLAGENQTALEIEELNRkyeqAKNISQDLEKQAARVHEEAKRAGDkavEIYASVAQLTPV-DSEALENEANKIKKE 1290
Cdd:TIGR01612 1339 SDINLYLNEIANIYNILKLNK----IKKIIDEVKEYTKEIEENNKNIKD---ELDKSEKLIKKIkDDINLEECKSKIEST 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1291 AADLDrlIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDI-LNNLK 1369
Cdd:TIGR01612 1412 LDDKD--IDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFnINELK 1489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1370 DFDRRVNDNKTAAEEAlrripainrtiAEANEKTREAqlaLGNAAADATEAKNKAHEAEriasaVQKNATSTKADAERTF 1449
Cdd:TIGR01612 1490 EHIDKSKGCKDEADKN-----------AKAIEKNKEL---FEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIII 1550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1450 GEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVD 1529
Cdd:TIGR01612 1551 KEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIE 1630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1530 ------------------LNKLNEIEGSLNKAKDEMK-ASDLDRKVSDLESEARKQEAAI----MDYNRDIAEIIKDI-- 1584
Cdd:TIGR01612 1631 kkissfsidsqdtelkenGDNLNSLQEFLESLKDQKKnIEDKKKELDELDSEIEKIEIDVdqhkKNYEIGIIEKIKEIai 1710
|
570 580 590
....*....|....*....|....*....|
gi 153791270 1585 ---HNLEDIKKTLP------TGCFNTPSIE 1605
Cdd:TIGR01612 1711 ankEEIESIKELIEptienlISSFNTNDLE 1740
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1267-1502 |
7.65e-06 |
|
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: 49.84 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1267 ASVAQLTPVDSEALENEANKIK---KEAADLDRLIDQKL-KDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQllarada 1342
Cdd:TIGR02794 35 AEIIQAVLVDPGAVAQQANRIQqqkKPAAKKEQERQKKLeQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1343 akalaeeaakkgrstlQEANdilnnlkdfdRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADAT---- 1418
Cdd:TIGR02794 108 ----------------EQAA----------KQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKakaa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1419 -EAKNKAHEAERIASAVQKNATSTKADAERtfgEVTDLDNEvngmlRQLEEAENELKKKQdDADQDMMMAGMASQAAQEA 1497
Cdd:TIGR02794 162 aEAKKKAEEAKKKAEAEAKAKAEAEAKAKA---EEAKAKAE-----AAKAKAAAEAAAKA-EAEAAAAAAAEAERKADEA 232
|
....*
gi 153791270 1498 ELNAR 1502
Cdd:TIGR02794 233 ELGDI 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1359-1569 |
2.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1359 QEANDILNNLKDFDRRVNDNKTAAEEAL-------RRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIA 1431
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQaelealqAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1432 SAvqKNATS--TKADAERTfgeVTDLDNEvngMLRQLEEAENELKKKQDDAD--QDMMMAGMASQAAQEAELNARKAKNS 1507
Cdd:COG3883 110 GS--ESFSDflDRLSALSK---IADADAD---LLEELKADKAELEAKKAELEakLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791270 1508 vssllsqlnnllDQLGQLDTvDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAA 1569
Cdd:COG3883 182 ------------ALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1071-1304 |
2.16e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1071 DRLKEAEREVTDL---LREAQEVKDVDQNLMDRLQRVNSSlhsQISRLQNIrntIEETGILAERARSRVES-TEQLIEIA 1146
Cdd:PHA02562 174 DKIRELNQQIQTLdmkIDHIQQQIKTYNKNIEEQRKKNGE---NIARKQNK---YDELVEEAKTIKAEIEElTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1147 ------SRELEKAKMAAANVS---------------------ITQPESTgEPNNMTLLAEEARKLAERHKQEADDIVRVA 1199
Cdd:PHA02562 248 mdiedpSAALNKLNTAAAKIKskieqfqkvikmyekggvcptCTQQISE-GPDRITKIKDKLKELQHSLEKLDTAIDELE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1200 KTANEtsaeaYNLLLRTlagenqtaleIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQltpvdsea 1279
Cdd:PHA02562 327 EIMDE-----FNEQSKK----------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK-------- 383
|
250 260 270
....*....|....*....|....*....|.
gi 153791270 1280 LENEANKIKKEAADLDRLIDQK------LKD 1304
Cdd:PHA02562 384 LQDELDKIVKTKSELVKEKYHRgivtdlLKD 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1355-1595 |
2.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 RSTLQEANDILNNLKDFDRRVNDNKTAAE--EALRRIPAINRTIAEANEKTREAQLALgnAAADATEAKNKAHEAERIAS 1432
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLR--AALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1433 AVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEA----ENELKKKQDDAdqdmmmagmasqaaqEAELNARKAKnsv 1508
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERL---------------ERELEERERR--- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1509 ssllsqlnnLLDQLGQLDTVDLnKLNEIEGSLNKAKDEMKA--SDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHN 1586
Cdd:COG4913 361 ---------RARLEALLAALGL-PLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
....*....
gi 153791270 1587 LEDIKKTLP 1595
Cdd:COG4913 431 LERRKSNIP 439
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1034-1554 |
2.67e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKLQELESLIANLGTGDDMVTD-----QAFED---RLKEAEREVTDLLREAQEVKDVDqNLMDRLQRVN 1105
Cdd:PRK01156 284 KIINDPVYKNRNYINDYFKYKNDIENKKQILSNidaeiNKYHAiikKLSVLQKDYNDYIKKKSRYDDLN-NQILELEGYE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1106 SSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELeKAKMAAANVSITQPESTgepnnmtLLAEEARKLA 1185
Cdd:PRK01156 363 MDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI-KKELNEINVKLQDISSK-------VSSLNQRIRA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1186 ERHKQEaddivRVAKTANETSAEAYNLLLRTLAGENQtaleIEELNRKYEQAKNisqDLEKQAARVHEEAKRAGDKAVEI 1265
Cdd:PRK01156 435 LRENLD-----ELSRNMEMLNGQSVCPVCGTTLGEEK----SNHIINHYNEKKS---RLEEKIREIEIEVKDIDEKIVDL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1266 YASVAQLTPVDSEALENEANKIKKEAADLDRLIDQ--KLKD----YEDLR--------EDMRGKEHEVKNLLEKgkaeqq 1331
Cdd:PRK01156 503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIKinELKDkhdkYEEIKnrykslklEDLDSKRTSWLNALAV------ 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1332 tadqllaradaakalaeeaakkgRSTLqeanDILNNLKDFD---RRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQL 1408
Cdd:PRK01156 577 -----------------------ISLI----DIETNRSRSNeikKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEAN 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1409 ALGNAaadateaKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLdNEVNGMLRQLEEAENELKKKQDDAdqdmmmag 1488
Cdd:PRK01156 630 NLNNK-------YNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDL-KEITSRINDIEDNLKKSRKALDDA-------- 693
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1489 MASQAAQEAELNARKAKNSvssllsqlnnlldQLGQldtvdlnKLNEIEGSLNKAKDEMKA-SDLDR 1554
Cdd:PRK01156 694 KANRARLESTIEILRTRIN-------------ELSD-------RINDINETLESMKKIKKAiGDLKR 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1355-1594 |
3.12e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 RSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAV 1434
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1435 QKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQdmmmagmASQAAQEAELNARKAKNSVSSLLSQ 1514
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-------AEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1515 LNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMK-ASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLEDIKKT 1593
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
.
gi 153791270 1594 L 1594
Cdd:COG1196 461 L 461
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1049-1569 |
3.22e-05 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 48.86 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1049 ELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLhSQISRLQNIRNTIEETGIL 1128
Cdd:COG5271 156 LPSLADNDEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVTTDPGDSV-AADDDLAAEEGASAVVEEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1129 AERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSAE 1208
Cdd:COG5271 235 DASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1209 AYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENEANKIK 1288
Cdd:COG5271 315 LEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADD 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1289 KEAADLDRLIDQKLKDYEDLREdmrgkEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNL 1368
Cdd:COG5271 395 SADDEEASADGGTSPTSDTDEE-----EEEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDT 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1369 KDFDRRVNDNKTAAEEALR--RIPAINRTIAEANEKTREAQLALGNA-AADATEAKNKAHEAERIASAVQKNATSTKADA 1445
Cdd:COG5271 470 ESAEEDADGDEATDEDDASddGDEEEAEEDAEAEADSDELTAEETSAdDGADTDAAADPEDSDEDALEDETEGEENAPGS 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1446 ERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAknsvssllsqlnnlldqlgql 1525
Cdd:COG5271 550 DQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEE--------------------- 608
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 153791270 1526 DTVDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAA 1569
Cdd:COG5271 609 EADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDA 652
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1070-1322 |
3.62e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQ--ISRLQ------NIRntIEETGILAERARSRVESTEQ 1141
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQekIERYQadleelEER--LEEQNEVVEEADEQQEENEA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1142 LIEIASRELEKAKMAAANVS---ITQPESTGEPNNMTLLAEEARKL-----------------AERHKQEADDIV----- 1196
Cdd:PRK04863 384 RAEAAEEEVDELKSQLADYQqalDVQQTRAIQYQQAVQALERAKQLcglpdltadnaedwleeFQAKEQEATEELlsleq 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1197 --RVAKTANETSAEAYNlLLRTLAGE---NQTALEIEELNRKYEQAKNISQDLEKQAARVHE-----EAKRAGDKAVEIY 1266
Cdd:PRK04863 464 klSVAQAAHSQFEQAYQ-LVRKIAGEvsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSEleqrlRQQQRAERLLAEF 542
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791270 1267 ASVAQLTPVDSEALENEAnkIKKEAAdLDRLIDQKlkdyEDLREDMRGKEHEVKNL 1322
Cdd:PRK04863 543 CKRLGKNLDDEDELEQLQ--EELEAR-LESLSESV----SEARERRMALRQQLEQL 591
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1208-1596 |
4.12e-05 |
|
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: 48.43 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1208 EAYNLLLRTLAGENQTALEIEELNRKY----EQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENE 1283
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQElklkEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1284 ANKIKKEAADLDRLIDQKLKDY-EDLREDMRGKEH--EVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTL-- 1358
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENkEEEKEKKLQEEElkLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELkk 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1359 --QEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAVQK 1436
Cdd:pfam02463 333 ekEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1437 NATSTKADAERtfgEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLN 1516
Cdd:pfam02463 413 LARQLEDLLKE---EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1517 NLLDQLGQLDTVDLNKLNEIEGSLNKAKD--EMKASDLDRKVSDLESEARKQEAAIMDY--------NRDIAEIIKDIHN 1586
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLALIKDgvGGRIISAHGRLGDLGVAVENYKVAISTAvivevsatADEVEERQKLVRA 569
|
410
....*....|
gi 153791270 1587 LEDIKKTLPT 1596
Cdd:pfam02463 570 LTELPLGARK 579
|
|
| 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 ... |
1391-1503 |
4.16e-05 |
|
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: 45.00 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1391 AINRTIAEANEKTREAQLALgnaaADATEAKNKAH-EAERIASAVQKNATSTKADAertfgeVTDLDNEVNgmlRQLEEA 1469
Cdd:pfam00430 34 LIADEIAEAEERRKDAAAAL----AEAEQQLKEARaEAQEIIENAKKRAEKLKEEI------VAAAEAEAE---RIIEQA 100
|
90 100 110
....*....|....*....|....*....|....
gi 153791270 1470 ENELKKKQDDAdqdmmMAGMASQAAQEAELNARK 1503
Cdd:pfam00430 101 AAEIEQEKDRA-----LAELRQQVVALAVQIAEK 129
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1044-1333 |
4.37e-05 |
|
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: 48.20 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1044 RVKLQELESLIANLgTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRV-------NSSLHSQISRLQ 1116
Cdd:pfam05557 1 RAELIESKARLSQL-QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLekreaeaEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1117 NIRNTIEETGILAERARSRVESTEQLI-----EIAS--RELEKAKMAaanVSITQPEstgepnNMTLlaEEARKLAERHK 1189
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADAREVIsclknELSElrRQIQRAELE---LQSTNSE------LEEL--QERLDLLKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1190 QEADDIVRVAKTANETSAEAynlllrtlageNQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRagdkaveiyasV 1269
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEA-----------EQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKE-----------L 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791270 1270 AQLTPVDSEALENEANK--IKKEAADLDRlidqKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTA 1333
Cdd:pfam05557 207 ERLREHNKHLNENIENKllLKEEVEDLKR----KLEREEKYREEAATLELEKEKLEQELQSWVKLA 268
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1227-1461 |
4.43e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1227 IEELNRKYEQAKNiSQDLEKQaaRVHEEAKRAGDKAVEIYASVAQLTPVDSEALEneANKIKKEAADLDRLIDQKLKdye 1306
Cdd:PRK09510 61 VEQYNRQQQQQKS-AKRAEEQ--RKKKEQQQAEELQQKQAAEQERLKQLEKERLA--AQEQKKQAEEAAKQAALKQK--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1307 dLREDMRGKEHEVKNLleKGKAEQQTADQLLARADAAKALAEEAAKKGRSTlQEANdilnnlkdfdrrvndnKTAAEEAL 1386
Cdd:PRK09510 133 -QAEEAAAKAAAAAKA--KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA-AEAK----------------KKAEAEAA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791270 1387 RRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAhEAERIASAVQKNATSTKADAERTFGEvTDLDNEVNG 1461
Cdd:PRK09510 193 AKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA-AAEAKAAAEKAAAAKAAEKAAAAKAA-AEVDDLFGG 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1070-1325 |
4.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDL---LREAQEVKDVDQNLMDRLQRVNS----------------SLHSQISRLQNIRNTIEETGILAE 1130
Cdd:COG4913 609 RAKLAALEAELAELeeeLAEAEERLEALEAELDALQERREalqrlaeyswdeidvaSAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1131 RARSRVESTEQLIEIASRELEKAKmaaanvsitqpestgepNNMTLLAEEARKLAERHKQEADDIVRVAKTANETSAEAY 1210
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELK-----------------GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1211 NLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAgdkaveiYASVAQLTPVDSEALEnEANKIkke 1290
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE-------WPAETADLDADLESLP-EYLAL--- 820
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 153791270 1291 aadLDRLIDQKLKDYED-----LREDMrgkEHEVKNLLEK 1325
Cdd:COG4913 821 ---LDRLEEDGLPEYEErfkelLNENS---IEFVADLLSK 854
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1359-1583 |
5.34e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1359 QEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAVQKNA 1438
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1439 TSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQdmmmAGMASQAAQEAELNARKAKNSVSSLLSQLNNL 1518
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA----LEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791270 1519 LDQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKD 1583
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1226-1505 |
5.56e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1226 EIEELNRKYEQAKNISQDLEKQ------------------AARVHE---EAKRAGDKAVEIYASVAQLTPVDSEALEnEA 1284
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKrdelneelkelaekrdelNAQVKElreEAQELREKRDELNEKVKELKEERDELNE-KL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1285 NKIKKEAADLDRLIDQKLK---DYEDLREDMRGkehevknlLEKgkaEQQTADqllaradaakalaeeaakkgrSTLQEA 1361
Cdd:COG1340 88 NELREELDELRKELAELNKaggSIDKLRKEIER--------LEW---RQQTEV---------------------LSPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1362 NDILNNLKDFDRRVNDNKTAAEEalrripaiNRTIAEANEKTREAQLALGNAAADATEAKNKAHEA-ERIASAVQKnATS 1440
Cdd:COG1340 136 KELVEKIKELEKELEKAKKALEK--------NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELhEEMIELYKE-ADE 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1441 TKADAERTFGEVTDLDNEVNgmlrQLEEAENELKKKQDDADQDMMMA---GMASQAAQEAELNARKAK 1505
Cdd:COG1340 207 LRKEADELHKEIVEAQEKAD----ELHEEIIELQKELRELRKELKKLrkkQRALKREKEKEELEEKAE 270
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1128-1558 |
5.97e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1128 LAERARSRVESTEQLIEIASRE-LEKAKMAAANVSITQPEstgepnnmtLLAEEARKLAERHKQEADDIVRVAKTANETS 1206
Cdd:COG3064 31 AEQKAKEEAEEERLAELEAKRQaEEEAREAKAEAEQRAAE---------LAAEAAKKLAEAEKAAAEAEKKAAAEKAKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1207 AEAYNLLlrtlagENQTALEIEElNRKYEQAKnisQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENEANK 1286
Cdd:COG3064 102 KEAEAAA------AAEKAAAAAE-KEKAEEAK---RKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1287 IKKEAADLDRLIDQKLKDYEdlredmRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILN 1366
Cdd:COG3064 172 ARAAAGAAAALVAAAAAAVE------AADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1367 NLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEkTREAQLALGNAAADATEAKNKAHEAERIASAVQKNATSTKADAE 1446
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV-VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1447 RTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLD 1526
Cdd:COG3064 325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
|
410 420 430
....*....|....*....|....*....|..
gi 153791270 1527 TVDLNKLNEIEGSLNKAKDEMKASDLDRKVSD 1558
Cdd:COG3064 405 LDLGAALLEAASAVELRVLLALAGAAGAVVAL 436
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
826-870 |
6.68e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 6.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 153791270 826 CQCNDniDPNAVGNCNRLTGECLkCIYNTAGFYCDRCKEGFFGNP 870
Cdd:smart00180 1 CDCDP--GGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1406-1588 |
6.72e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1406 AQLALGNAAADATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQ--- 1482
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1483 DMMMAG---------MASQAAQEAeLNARKAKNSVssllsqLNNLLDQLGQLDTvDLNKLNEIEGSLNKAKDEMKA--SD 1551
Cdd:COG3883 94 ALYRSGgsvsyldvlLGSESFSDF-LDRLSALSKI------ADADADLLEELKA-DKAELEAKKAELEAKLAELEAlkAE 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 153791270 1552 LDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLE 1588
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1049-1592 |
6.87e-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: 47.91 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1049 ELESLIANLGTGDDMVTDQA---------FEDRLKEAEREVtDLLREAQevKDVDQNLMDRLQRVNSSLHSQISRLQNIR 1119
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAaadqeqlpsWQSELENLEERL-KALTGKH--QDVTAKYNRRRSKIKEQNNRDIAGIKDKL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1120 NTIEETgilAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTL---LAEEARKLAERHKQEADDIV 1196
Cdd:pfam12128 400 AKIREA---RDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLnqaTATPELLLQLENFDERIERA 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1197 RVAKTANETSAEAYNLLLRTLAGENQTALE-IEELNRKYEQAKNISQDLEKQ----AARVHE-EAKRAGDKAVEI--YAS 1268
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEaLRQASRRLEERQSALDELELQlfpqAGTLLHfLRKEAPDWEQSIgkVIS 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1269 VAQL-----TPVDSEALENEANKIKKEAADLDRLidqKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAA 1343
Cdd:pfam12128 557 PELLhrtdlDPEVWDGSVGGELNLYGVKLDLKRI---DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1344 KALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKT--------AAEEALRRIPA---------------INRTIAEAN 1400
Cdd:pfam12128 634 LEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNkalaerkdSANERLNSLEAqlkqldkkhqawleeQKEQKREAR 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1401 ----------EKTREAQLALGNAAADATEAKNKAHeaeriASAVQK-NATSTKA---DAERtfgeVTDLDNEVNGMLRQL 1466
Cdd:pfam12128 714 tekqaywqvvEGALDAQLALLKAAIAARRSGAKAE-----LKALETwYKRDLASlgvDPDV----IAKLKREIRTLERKI 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1467 EEAEnelKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVssllsqlNNLLDQLGQL--DT-VDLNKLNEIEGSLNKA 1543
Cdd:pfam12128 785 ERIA---VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI-------SELQQQLARLiaDTkLRRAKLEMERKASEKQ 854
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1544 KDEM-----KASDLDRKVSDLESEARKQEAAIMDYNR-DIAEIIKDIHN--LEDIKK 1592
Cdd:pfam12128 855 QVRLsenlrGLRCEMSKLATLKEDANSEQAQGSIGERlAQLEDLKLKRDylSESVKK 911
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1583 |
6.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1056 NLGTGDDMVTDQAFEdrlkeaEREVTDLLREAQE-VKDVD--QNLMDRLQRvnsslhsQISRLQNIRNTIEEtgilAERA 1132
Cdd:COG4913 205 PIGDLDDFVREYMLE------EPDTFEAADALVEhFDDLEraHEALEDARE-------QIELLEPIRELAER----YAAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1133 RSRVESTEQLIEIASRELEKAKMAaanvsitqpestgepnnmtLLAEEARKLAERHKQEADDIVRVAKTANETSAEAYNL 1212
Cdd:COG4913 268 RERLAELEYLRAALRLWFAQRRLE-------------------LLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1213 L--LRTLAGENQTAL--EIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQL---TPVDSEALENEAN 1285
Cdd:COG4913 329 EaqIRGNGGDRLEQLerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALleaLEEELEALEEALA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1286 KIKKEAADLDRLIDQKLKDYEDLR----------EDMRG--------KEHEVK---NLLE-KGKAEQ-QTA------DQl 1336
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLErrksniparlLALRDalaealglDEAELPfvgELIEvRPEEERwRGAiervlgGF- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1337 laradaakalaeeaakkgRSTL-------QEANDILNNLK-------------------------------DFD------ 1372
Cdd:COG4913 488 ------------------ALTLlvppehyAAALRWVNRLHlrgrlvyervrtglpdperprldpdslagklDFKphpfra 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1373 -------RRVNDNKTAAEEALRRIP-AI--------NRTIAEANEKTR-----------EAQLALgnAAADATEAKNKAH 1425
Cdd:COG4913 550 wleaelgRRFDYVCVDSPEELRRHPrAItragqvkgNGTRHEKDDRRRirsryvlgfdnRAKLAA--LEAELAELEEELA 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1426 EAERIASAVQK--NATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELkKKQDDADQDMMMAGMASQAAQEAELNARK 1503
Cdd:COG4913 628 EAEERLEALEAelDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1504 AKNSVssllsqlnnlLDQLGQLDtvdlNKLNEIEGSLNKAKDEM-KASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIK 1582
Cdd:COG4913 707 ELDEL----------KGEIGRLE----KELEQAEEELDELQDRLeAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
.
gi 153791270 1583 D 1583
Cdd:COG4913 773 E 773
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1212-1570 |
7.70e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1212 LLLRTLAGENQTAL-EIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDkavEIYASVAQLtpvdsEALENEANKIKKE 1290
Cdd:COG4372 24 ILIAALSEQLRKALfELDKLQEELEQLREELEQAREELEQLEEELEQARS---ELEQLEEEL-----EELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1291 AADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKalaeeaakkgrSTLQEANDILNNLKD 1370
Cdd:COG4372 96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE-----------EELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1371 --FDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAVQKNATSTKADAERT 1448
Cdd:COG4372 165 elAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1449 FGEVTDLDNEVNGMLRQLEEAENeLKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTV 1528
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAI-LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 153791270 1529 DLNKLNEIEG----SLNKAKDEMKASDLDRKVSDLESEARKQEAAI 1570
Cdd:COG4372 324 LAKKLELALAillaELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1100-1370 |
7.90e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 46.25 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1100 RLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEiasRELEKAKMAAANVSITQPESTGEPNNMTLLAE 1179
Cdd:pfam06008 13 APYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETE---ELQKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1180 EARKLaerhkqeaddiVRVAKTANEtSAEAYNlllrtlagENQTALEIEELNRKYEQAKNI-----SQDLEKQaarvHEE 1254
Cdd:pfam06008 90 AIKNL-----------IDNIKEINE-KVATLG--------ENDFALPSSDLSRMLAEAQRMlgeirSRDFGTQ----LQN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1255 AKRAGDKAVEIYASVAQLTpvdsEALENEANKIKKeaADLDRLID--QKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQT 1332
Cdd:pfam06008 146 AEAELKAAQDLLSRIQTWF----QSPQEENKALAN--ALRDSLAEyeAKLSDLRELLREAAAKTRDANRLNLANQANLRE 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 153791270 1333 ADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKD 1370
Cdd:pfam06008 220 FQRKKEEVSEQKNQLEETLKTARDSLDAANLLLQEIDD 257
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1035-1259 |
8.42e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1035 LVKDKVAEH--RVKLQELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVnssLHSQI 1112
Cdd:TIGR00618 655 LTQERVREHalSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA---SSSLG 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1113 SRLQNIRNTIEET-GILAERARSRVESTEQLIEIASRELEKAKMAAANVSitqpESTGEPNNMTLLAEE-----ARKLAE 1186
Cdd:TIGR00618 732 SDLAAREDALNQSlKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS----HLAAEIQFFNRLREEdthllKTLEAE 807
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1187 rHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAG 1259
Cdd:TIGR00618 808 -IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1041-1254 |
9.20e-05 |
|
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: 46.81 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1041 AEHRVKLQELESLIANLGtgDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDR-----------LQRVNSSLH 1109
Cdd:pfam07888 125 AAHEARIRELEEDIKTLT--QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrslskeFQELRNSLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1110 SQISRLQNIRNTIEETGILAERARSRVESTEQLIE--IASRELekakmaaANVSITQPESTGEpNNMTLLAEEARKLAER 1187
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEelRSLQER-------LNASERKVEGLGE-ELSSMAAQRDRTQAEL 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791270 1188 HKqeaddiVRV-AKTANETSAEAyNLLLR----TLAGENQTALEIEELNRkyEQAKNISQDLEKQAARVHEE 1254
Cdd:pfam07888 275 HQ------ARLqAAQLTLQLADA-SLALRegraRWAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEE 337
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1427-1594 |
9.73e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1427 AERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQdmmmagMASQAAQ-EAELNARKak 1505
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ------AREELEQlEEELEQAR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1506 nsvssllsqlnnllDQLGQLDtvdlNKLNEIEGSLNKAKDEMKAsdLDRKVSDLESEARKQEAaimdynrDIAEIIKDIH 1585
Cdd:COG4372 73 --------------SELEQLE----EELEELNEQLQAAQAELAQ--AQEELESLQEEAEELQE-------ELEELQKERQ 125
|
....*....
gi 153791270 1586 NLEDIKKTL 1594
Cdd:COG4372 126 DLEQQRKQL 134
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1044-1432 |
1.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1044 RVKLQELESLIANLGTgddmVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSlhsqISRLQNIRNTI- 1122
Cdd:PRK03918 368 KAKKEELERLKKRLTG----LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA----IEELKKAKGKCp 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1123 ---------EETGILAERARSRVESTEQLIEIASRElEKAKMAAANVSItqpESTGEPNNMTL--LAEEARKLAErhKQE 1191
Cdd:PRK03918 440 vcgrelteeHRKELLEEYTAELKRIEKELKEIEEKE-RKLRKELRELEK---VLKKESELIKLkeLAEQLKELEE--KLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1192 ADDIVRVAKTANEtsAEAYNLLLRTLAGE----NQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVE--- 1264
Cdd:PRK03918 514 KYNLEELEKKAEE--YEKLKEKLIKLKGEikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEele 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1265 --------IYASVAQLTPVDSE---------ALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHE-VKNLLEKG 1326
Cdd:PRK03918 592 erlkelepFYNEYLELKDAEKElereekelkKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEeLREEYLEL 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1327 KAEQQTAdqllaradaakalaeeaakkgRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEAnEKTREA 1406
Cdd:PRK03918 672 SRELAGL---------------------RAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV-EELREK 729
|
410 420
....*....|....*....|....*..
gi 153791270 1407 QLALGNaaadatEAKNKA-HEAERIAS 1432
Cdd:PRK03918 730 VKKYKA------LLKERAlSKVGEIAS 750
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1371-1593 |
1.04e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1371 FDRRVNDNK-TAAEEALRRIpaINRTIAEANEKTREAQLalgnaaadatEAKNKAHEAeriasavqknatstKADAERtf 1449
Cdd:PRK12704 24 VRKKIAEAKiKEAEEEAKRI--LEEAKKEAEAIKKEALL----------EAKEEIHKL--------------RNEFEK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1450 gEVTDLDNEVNGMLRQLEEAENELKKKQDDADQdmmmagmasqaaQEAELNARKAKNSVssllsqlnnlldqlgQLDTVD 1529
Cdd:PRK12704 76 -ELRERRNELQKLEKRLLQKEENLDRKLELLEK------------REEELEKKEKELEQ---------------KQQELE 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1530 lNKLNEIEGSLNKAKDEMKasdldrKVSDL-ESEARKQ--EAAIMDYNRDIAEIIKDIHnlEDIKKT 1593
Cdd:PRK12704 128 -KKEEELEELIEEQLQELE------RISGLtAEEAKEIllEKVEEEARHEAAVLIKEIE--EEAKEE 185
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
340-394 |
1.19e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.18 E-value: 1.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 340 CDCNGR---SQECYFdpelyrstgHGGHCTnCRDNTDGAKCERCRENFFRLGNTEACS 394
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1239-1579 |
1.22e-04 |
|
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: 46.21 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1239 NISQDLEKQAARVHE-EAK----RAGDKAVEiyASVAQLTpVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMR 1313
Cdd:pfam19220 38 AILRELPQAKSRLLElEALlaqeRAAYGKLR--RELAGLT-RRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1314 GKEHEVKNLLEKGKAEQQ-----TADQLLARADAAKALAEEAAKKG-RSTLQEANDILnnlKDFDRRVNDNktaAEEALR 1387
Cdd:pfam19220 115 DKTAQAEALERQLAAETEqnralEEENKALREEAQAAEKALQRAEGeLATARERLALL---EQENRRLQAL---SEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1388 RIPAINRTIAEaNEKTREAQLAlgnaAADATEAKNKAHEAERIASAVQKNATSTKADAERTF-----------GEVTD-L 1455
Cdd:pfam19220 189 ELAELTRRLAE-LETQLDATRA----RLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASlrmklealtarAAATEqL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1456 DNEVNGMLRQLEEAENELKKKQDDADQDMMMAgMASQAAQEAELNARKAknsvssllsqlnnlldQLGQLDTVDlNKLNE 1535
Cdd:pfam19220 264 LAEARNQLRDRDEAIRAAERRLKEASIERDTL-ERRLAGLEADLERRTQ----------------QFQEMQRAR-AELEE 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1536 IEGSLNKA---KD------EMKASDLDRKVSDLESEARKQEAAIMDYNRDIAE 1579
Cdd:pfam19220 326 RAEMLTKAlaaKDaaleraEERIASLSDRIAELTKRFEVERAALEQANRRLKE 378
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1122-1505 |
1.27e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.13 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1122 IEETGILAER--ARSRVESTEqLIEIASRELEKAKMAAANVSIT---QPESTgepnnmtllAEEARKLAERHKQEADDIV 1196
Cdd:NF041483 475 IEEAARTAEEllTKAKADADE-LRSTATAESERVRTEAIERATTlrrQAEET---------LERTRAEAERLRAEAEEQA 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1197 RVAKTANETSA----------------EAYNLL--LRTLAGENQTALEiEELNRKYEQAKNISQDLEKQAARVH------ 1252
Cdd:NF041483 545 EEVRAAAERAArelreeteraiaarqaEAAEELtrLHTEAEERLTAAE-EALADARAEAERIRREAAEETERLRteaaer 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1253 ---------EEAKRAGDKAV-EIYASVAQLTPV----DSEAlENEANKIKKEAAD-LDRLIDQKLKDYEDL--------- 1308
Cdd:NF041483 624 irtlqaqaeQEAERLRTEAAaDASAARAEGENVavrlRSEA-AAEAERLKSEAQEsADRVRAEAAAAAERVgteaaeala 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1309 --REDMRGKEHEVKNLLEKGKAEqqtADQllaRADAAKALAEEAAKKGRSTLQEANDILNNL-KDFDRRVNDNKTAAEE- 1384
Cdd:NF041483 703 aaQEEAARRRREAEETLGSARAE---ADQ---ERERAREQSEELLASARKRVEEAQAEAQRLvEEADRRATELVSAAEQt 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1385 --------------ALRRIPAInRTIAE-ANEKTR-EAQLALGNAAADATEAKNKAHE-AERIASAVQKNATSTKADAER 1447
Cdd:NF041483 777 aqqvrdsvaglqeqAEEEIAGL-RSAAEhAAERTRtEAQEEADRVRSDAYAERERASEdANRLRREAQEETEAAKALAER 855
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1448 TFGEVtdldnevngmlrqLEEAEnelKKKQDDADQDMMMAGMASQAAQEAELNARKAK 1505
Cdd:NF041483 856 TVSEA-------------IAEAE---RLRSDASEYAQRVRTEASDTLASAEQDAARTR 897
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
770-818 |
1.53e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153791270 770 PCPCPGGSSCAIVPKTKEVVCtHCPTGTAGKRCELCDDGYFGDPLGSNG 818
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1034-1594 |
1.77e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKlQELESLIANLGtgddmVTDQAFEDRLKEAEREVTDLLreAQEVKDVDQNLMDRLQRVNSSLHSQIS 1113
Cdd:PTZ00440 985 KLDKEKDEWEHFK-SEIDKLNVNYN-----ILNKKIDDLIKKQHDDIIELI--DKLIKEKGKEIEEKVDQYISLLEKMKT 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1114 RLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPEstgepnNMTLLAEEARKLAERHKQEAD 1193
Cdd:PTZ00440 1057 KLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHE------HVVNADKEKNKQTEHYNKKKK 1130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1194 DIVRVAKTANETSAEaynllLRTLAGENQTALEIEELNRKYEQAKnISQDLEKqaarVHEEAKRAGDKAVEIYASVAQLT 1273
Cdd:PTZ00440 1131 SLEKIYKQMEKTLKE-----LENMNLEDITLNEVNEIEIEYERIL-IDHIVEQ----INNEAKKSKTIMEEIESYKKDID 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1274 PVDsealeneANKIKKEAADLDRLidqklkDYEDLREDMRGKEHEVKNLLEKGKAEQQTADqllaradaakalaeeaakk 1353
Cdd:PTZ00440 1201 QVK-------KNMSKERNDHLTTF------EYNAYYDKATASYENIEELTTEAKGLKGEAN------------------- 1248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1354 gRST-LQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINrTIAEANEKTREAQLALGNAaadateakNKAHEAERias 1432
Cdd:PTZ00440 1249 -RSTnVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMY-EFLISIDSEKILKEILNST--------KKAEEFSN--- 1315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1433 avqknatstkaDAERTFGEVTDLDNEVNGMLRQLEEAEN------------------ELKKKQDDADQDMMMAGM--ASQ 1492
Cdd:PTZ00440 1316 -----------DAKKELEKTDNLIKQVEAKIEQAKEHKNkiygsledkqiddeikkiEQIKEEISNKRKEINKYLsnIKS 1384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1493 AAQEAELNARKAKNSVssllsqlnnlldqlgqlDTVD-LNKLNEIEGSLNKAKDEMKASDLDRK-------VSDLESEAR 1564
Cdd:PTZ00440 1385 NKEKCDLHVRNASRGK-----------------DKIDfLNKHEAIEPSNSKEVNIIKITDNINKckqysneAMETENKAD 1447
|
570 580 590
....*....|....*....|....*....|
gi 153791270 1565 KQEAAIMDYNRDIAEIIKDIHNLEdIKKTL 1594
Cdd:PTZ00440 1448 ENNDSIIKYEKEITNILNNSSILG-KKTKL 1476
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1314 |
1.90e-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: 44.92 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1094 DQNLMDRLQRvnssLHSQISRLQNIRNTIEEtgilaerarsRVESTEQLIEIASRELEKAKMAAANvsitqpestgepnn 1173
Cdd:COG1579 5 DLRALLDLQE----LDSELDRLEHRLKELPA----------ELAELEDELAALEARLEAAKTELED-------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1174 mtlLAEEARKLAERHKQEADDIVRV-AKTANETSAEAYNLLLRTLAG--ENQTALEIEELnRKYEQAKNISQDLEKQAAR 1250
Cdd:COG1579 57 ---LEKEIKRLELEIEEVEARIKKYeEQLGNVRNNKEYEALQKEIESlkRRISDLEDEIL-ELMERIEELEEELAELEAE 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791270 1251 VHEEAKRAGDKAVEIYASVAQltpvdseaLENEANKIKKEAADLDRLIDQKLKD-YEDLREDMRG 1314
Cdd:COG1579 133 LAELEAELEEKKAELDEELAE--------LEAELEELEAEREELAAKIPPELLAlYERIRKRKNG 189
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1035-1310 |
1.96e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1035 LVKDKVAEHRVKLQELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQR------VNSSL 1108
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdlVASDL 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1109 HSQISRLQNIRNTIEETGILAER---ARSRVESTEQLIEIASRELEKAKMAAANVSITQPEstgepnnmtlLAEEARKLA 1185
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARleaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE----------LLAALLEAE 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1186 ERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEi 1265
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP- 757
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 153791270 1266 yasvaqlTPVDSEALENEANKIKKeaaDLDRL-------IDqklkDYEDLRE 1310
Cdd:COG1196 758 -------EPPDLEELERELERLER---EIEALgpvnllaIE----EYEELEE 795
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1070-1256 |
2.22e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQEVkDVDQN---LMDRLQRVNSSLH---SQISRLQNIRNTIEETGILAERARSRVESTEQLI 1143
Cdd:COG3206 188 RKELEEAEAALEEFRQKNGLV-DLSEEaklLLQQLSELESQLAearAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1144 EIASRELE-KAKMAAANVSITqpestgePNN--MTLLAEEARKLAERHKQEADDI-------VRVAKTANETSAEAYNLL 1213
Cdd:COG3206 267 QLRAQLAElEAELAELSARYT-------PNHpdVIALRAQIAALRAQLQQEAQRIlasleaeLEALQAREASLQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153791270 1214 LRTLAGENQTALEIEELNRKYEQAKNISQDLEK--QAARVHEEAK 1256
Cdd:COG3206 340 EARLAELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1355-1569 |
2.35e-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: 45.53 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 RSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALgnaaadateAKNKAHEAERIASAv 1434
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1435 QKNATSTK----------ADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDD--ADQDMMMAGMASQAAQEAELNAR 1502
Cdd:COG4942 114 YRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEleAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791270 1503 KAKNSVSsllsqlnnlldqlgqldtvdLNKLNEIEGSLNKAKDEMKAS--DLDRKVSDLESEARKQEAA 1569
Cdd:COG4942 194 KAERQKL--------------------LARLEKELAELAAELAELQQEaeELEALIARLEAEAAAAAER 242
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1126-1584 |
2.67e-04 |
|
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: 45.72 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1126 GILAERARSRVESTEQLIEIASRELEKAKMAaaNVSITQPESTGEPNNMTLLAEEARKLAERHKQeaddivrVAKTAN-E 1204
Cdd:COG5185 43 TILFFPLGISRDSLRVTLRSVINVLDGLNYQ--NDVKKSESSVKARKFLKEKKLDTKILQEYVNS-------LIKLPNyE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1205 TSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDL-EKQAARVHEEAKRAGDKAVEIY----------------- 1266
Cdd:COG5185 114 WSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYgEVETGIIKDIFGKLTQELNQNLkkleifgltlgllkgis 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1267 ------ASVAQLTPVDSEALENEANKIKKEAAD---LDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKgKAEQQTADqll 1337
Cdd:COG5185 194 elkkaePSGTVNSIKESETGNLGSESTLLEKAKeiiNIEEALKGFQDPESELEDLAQTSDKLEKLVEQ-NTDLRLEK--- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1338 aradaakalaeeaAKKGRSTLQEANDILNNLKDFDRRVND---NKTAAEEALRRIPAINRTIAEANEktrEAQLALGNAA 1414
Cdd:COG5185 270 -------------LGENAESSKRLNENANNLIKQFENTKEkiaEYTKSIDIKKATESLEEQLAAAEA---EQELEESKRE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1415 ADaTEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEvngmlRQLEEAENELKKKQDDADQDMMMAgmaSQAA 1494
Cdd:COG5185 334 TE-TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSS-----EELDSFKDTIESTKESLDEIPQNQ---RGYA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1495 QEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMKasdlDRKVSDLESEARKQEAAIMDYN 1574
Cdd:COG5185 405 QEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD----EESQSRLEEAYDEINRSVRSKK 480
|
490
....*....|
gi 153791270 1575 RDIAEIIKDI 1584
Cdd:COG5185 481 EDLNEELTQI 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1040-1296 |
3.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1040 VAEHRVKLQELESLIANLGTGDDMVtdQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNsslhSQISRLQNIR 1119
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDL--AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE----EELDELQDRL 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1120 NTIEETGILAERARsrveSTEQLIEIASRELEKAKMAAanvsitqpestgepnnmtlLAEEARKLAERHKQEADDIVRVA 1199
Cdd:COG4913 737 EAAEDLARLELRAL----LEERFAAALGDAVERELREN-------------------LEERIDALRARLNRAEEELERAM 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1200 KTANETSAEAYNLLLRTLAGenqtaleIEELNRKYEQAKNisQDLekqaARVHEEAKRAGDKAVEiyASVAQLtpvdSEA 1279
Cdd:COG4913 794 RAFNREWPAETADLDADLES-------LPEYLALLDRLEE--DGL----PEYEERFKELLNENSI--EFVADL----LSK 854
|
250
....*....|....*..
gi 153791270 1280 LENEANKIKKEAADLDR 1296
Cdd:COG4913 855 LRRAIREIKERIDPLND 871
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1032-1524 |
3.27e-04 |
|
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: 45.55 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1032 CYRLVKDkVAEHRVKLQELESLIA-------NLGTgddmvtdqafedRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRV 1104
Cdd:pfam01576 456 NIKLSKD-VSSLESQLQDTQELLQeetrqklNLST------------RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1105 NSSLHSQISRLQNIRNTIEetgiLAERARSRVESTeqlIEIASRELEKAKMAAANVSITQPESTGEPNNMT--------- 1175
Cdd:pfam01576 523 QAQLSDMKKKLEEDAGTLE----ALEEGKKRLQRE---LEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldhqrql 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1176 -------------LLAEE----ARKLAERHKQEADdivrvaktANETSAEAYnlllrTLAGENQTALE-IEELNRKYEQA 1237
Cdd:pfam01576 596 vsnlekkqkkfdqMLAEEkaisARYAEERDRAEAE--------AREKETRAL-----SLARALEEALEaKEELERTNKQL 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1238 KNISQDL--EKQAA--RVH--EEAKRAGDKAVEiyASVAQLTPVDSEALENEANKIKKEA------ADLDRLIDQKLKDY 1305
Cdd:pfam01576 663 RAEMEDLvsSKDDVgkNVHelERSKRALEQQVE--EMKTQLEELEDELQATEDAKLRLEVnmqalkAQFERDLQARDEQG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1306 EDLREDMRGKEHEVKNLLE---KGKAEQQTADQLLARADAAKALAEEAAKKGRstlQEANDILNNL----KDFDRRVNDN 1378
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELEderKQRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKKLqaqmKDLQRELEEA 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1379 KTAAEEALrripainrTIAEANE---KTREAQ-LALGNAAADATEAKNKAhEAER------IASAVQKNAtSTKADAERT 1448
Cdd:pfam01576 818 RASRDEIL--------AQSKESEkklKNLEAElLQLQEDLAASERARRQA-QQERdeladeIASGASGKS-ALQDEKRRL 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1449 FGEVTDLDNE----------VNGMLR----QLEEAENELK------KKQDDADQDMmmagmasqAAQEAELNAR------ 1502
Cdd:pfam01576 888 EARIAQLEEEleeeqsntelLNDRLRkstlQVEQLTTELAaerstsQKSESARQQL--------ERQNKELKAKlqemeg 959
|
570 580
....*....|....*....|....*.
gi 153791270 1503 ----KAKNSVSSLLSQLNNLLDQLGQ 1524
Cdd:pfam01576 960 tvksKFKSSIAALEAKIAQLEEQLEQ 985
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1033-1246 |
3.37e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1033 YRLVKDKVAEHRVKLQELESLIANLGTGDDMVTDQA--FEDRLKEAEREVTDL---LREAQEVKDVDQNLMDRLQRvnsS 1107
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIeeLSEDIESLAAEIEELeelIEELESELEALLNERASLEE---A 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1108 LHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKM--------AAANVSITQPESTGEPNNMTLLAE 1179
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerLSEEYSLTLEEAEALENKIEDDEE 968
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1180 EARKLAERHKQEADDIVRVaktaNETSAEaynlllrtlagenqtalEIEELNRKYEQAKNISQDLEK 1246
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPV----NLAAIE-----------------EYEELKERYDFLTAQKEDLTE 1014
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
339-387 |
4.20e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 39.64 E-value: 4.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 153791270 339 PCDCNGR---SQECYFdpelyrstgHGGHCTnCRDNTDGAKCERCRENFFRL 387
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| V_AnPalA_UmRIM20_like |
cd09236 |
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ... |
1178-1310 |
4.60e-04 |
|
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.
Pssm-ID: 185749 [Multi-domain] Cd Length: 353 Bit Score: 44.27 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1178 AEEAR--KLAERHKQEADDIVRVAKTANETSAEAYNLLLrtlagenQTALEIEELNRKY-------EQAKNISQDLEKQA 1248
Cdd:cd09236 64 AEEIRqeDGLERIRASLDDVARLAASDRAILEEAMDILD-------DEASEDESLRRKFgtdrwtrPDSHEANPKLYTQA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1249 ARVHEEAKRAG--DKAV-----EIYASVAQLT---------------PVDSEALENEANKIKKEAADLDRLIDQKLKDYE 1306
Cdd:cd09236 137 AEYEGYLKQAGasDELVrrkldEWEDLIQILTgderdlenfvpssrrPSIPPELERHVRALRVSLEELDRLESRRRRKVE 216
|
....
gi 153791270 1307 DLRE 1310
Cdd:cd09236 217 RART 220
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1278-1470 |
4.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1278 EALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEK--GKAEQQTADQLLARADAAKALAEEAAKKGR 1355
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1356 STLQEANDILNNLKDFDRRVNDNKTAAE---EALRRIPAINRTIAEANEKTREA--------QLALGNAAADATEAKNKA 1424
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791270 1425 HEAERIASAVQKNATSTKADAERTFGEVTDLDnevngMLRQLEEAE 1470
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAA-----LEERLKEAR 249
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1243-1589 |
4.78e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 45.01 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1243 DLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKE-----H 1317
Cdd:COG5271 585 DETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAeasadE 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1318 EVKNLLEKGKAEQQTADqllaradaakalaeeAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIA 1397
Cdd:COG5271 665 SEEEAEDESETSSEDAE---------------EDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAE 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1398 EANEKTREA--QLALGNAAADATEAKNKAHEAEriASAVQKNATSTKADAERTFGEVTDldnevngmlrqlEEAENELKK 1475
Cdd:COG5271 730 EAAEEAESAdeEAASLPDEADAEEEAEEAEEAE--EDDADGLEEALEEEKADAEEAATD------------EEAEAAAEE 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1476 KQDDADQDmmmagmasQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRK 1555
Cdd:COG5271 796 KEKVADED--------QDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDAD 867
|
330 340 350
....*....|....*....|....*....|....
gi 153791270 1556 VSDLESEARKQEAAIMDYNRDIAEIIKDIHNLED 1589
Cdd:COG5271 868 LAADEHEAEEAQEAETDADADADAGEADSSGESS 901
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1049-1590 |
4.86e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 45.01 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1049 ELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNlmdrlqrvNSSLHSQISRLQNIRNTIEETGIL 1128
Cdd:COG5271 505 DSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQD--------ADETDEPEATAEEDEPDEAEAETE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1129 AERARSRVESTEQLIEIASR----ELEKAKMAAANVSITQPESTGEPNNMTLLAEEArklAERHKQEADDIVRVAKTANE 1204
Cdd:COG5271 577 DATENADADETEESADESEEaeasEDEAAEEEEADDDEADADADGAADEEETEEEAA---EDEAAEPETDASEAADEDAD 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1205 TSAEAYNLllrtlagENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSE----AL 1280
Cdd:COG5271 654 AETEAEAS-------ADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADAEEADTEadgtAE 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1281 ENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEH----EVKNLLEKGK--AEQQTADQllaradaakalaeeaakkg 1354
Cdd:COG5271 727 EAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEddadGLEEALEEEKadAEEAATDE------------------- 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 rsTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAV 1434
Cdd:COG5271 788 --EAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLD 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1435 QKNATSTKaDAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQ 1514
Cdd:COG5271 866 ADLAADEH-EAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAE 944
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1515 LNNLLD----QLGQLDTVDLNKLNEIEGSLNK---AKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNL 1587
Cdd:COG5271 945 DDLDALaldeAGDEESDDAAADDAGDDSLADDdeaLADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEATA 1024
|
...
gi 153791270 1588 EDI 1590
Cdd:COG5271 1025 DLA 1027
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1047-1252 |
5.37e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.20 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1047 LQELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEEtg 1126
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRE-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1127 iLAERARSRVESTEQLieiaSRELEKAKMAAANVSITQPESTGEPNNMTLlaEEARKLAERHKQEADDIVRVAKTANETS 1206
Cdd:cd00176 94 -LAEERRQRLEEALDL----QQFFRDADDLEQWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHEPRLKSLN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153791270 1207 AEAYNLL-LRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVH 1252
Cdd:cd00176 167 ELAEELLeEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1235-1447 |
6.37e-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: 44.07 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1235 EQAKNISQDLEKQAARVHEEAKRAgdkaveiyasvaqltpvdSEALENEANKIKKEAADLDRLIDQKL-----KDYEDLR 1309
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL------------------EQQAEEAEKQRAAEQARQKELEQRAAaekaaKQAEQAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1310 EDMRGKEHEVKNLLEKGKAEQQTADQLLARadaakalaeeaakkgrstlQEANDILNNLKDFDRRVN---DNKTAAEEAL 1386
Cdd:TIGR02794 112 KQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-------------------RKAKEEAAKQAEEEAKAKaaaEAKKKAEEAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1387 RRIPAINRTIAEAnektrEAQLALGNAAADATEAKNKAhEAERIASAVQKNATSTKADAER 1447
Cdd:TIGR02794 173 KKAEAEAKAKAEA-----EAKAKAEEAKAKAEAAKAKA-AAEAAAKAEAEAAAAAAAEAER 227
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1128-1280 |
6.47e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 43.56 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1128 LAERARSRVESTEQLIEI--ASRELEKA-----KMAAANvsitqpestgePNNMTLLAEEARKLAERHK-QEADDIVRVA 1199
Cdd:COG2956 102 LLELDPDDAEALRLLAEIyeQEGDWEKAievleRLLKLG-----------PENAHAYCELAELYLEQGDyDEAIEALEKA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1200 KTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKqAARVHEEAKRAgDKAVEIYASVAQLTPVDSEA 1279
Cdd:COG2956 171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPR-LAELYEKLGDP-EEALELLRKALELDPSDDLL 248
|
.
gi 153791270 1280 L 1280
Cdd:COG2956 249 L 249
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1356-1569 |
6.68e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1356 STLQEANDILNNL-KDFDRRVNDNKTAAEEAlrripaiNRTIAEAN--EKT-REAQLALgNAAADATEAKNKAH-EAEri 1430
Cdd:pfam05701 138 AELKSVKEELESLrKEYASLVSERDIAIKRA-------EEAVSASKeiEKTvEELTIEL-IATKESLESAHAAHlEAE-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1431 asavqknatstkadaERTFGEVTDLDNEVNGMLRQLEEAENELKK--KQDDADQDMMM---AGMASQAAQEAELNARKAK 1505
Cdd:pfam05701 208 ---------------EHRIGAALAREQDKLNWEKELKQAEEELQRlnQQLLSAKDLKSkleTASALLLDLKAELAAYMES 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791270 1506 NSVSSLLSQLNNLLDQLGQLDTVDLNK--LNEIEGSLNKAKDEMKA---------SDLDRKVSDLESEARKQEAA 1569
Cdd:pfam05701 273 KLKEEADGEGNEKKTSTSIQAALASAKkeLEEVKANIEKAKDEVNClrvaaaslrSELEKEKAELASLRQREGMA 347
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1034-1584 |
7.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1034 RLVKDKVAEHRVKLQELESLIANLGTgddmvtdqafeDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQIS 1113
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGG-----------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1114 RLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAK---------MAAANVSITQP---------ESTGEPNN-- 1173
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreleaeiasLERRKSNIPARllalrdalaEALGLDEAel 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1174 ------MTLLAEEAR-KLA---------------ERHKQEADDIVRVAKT----------ANETSAEAYNLLLRTLAGEn 1221
Cdd:COG4913 461 pfvgelIEVRPEEERwRGAiervlggfaltllvpPEHYAAALRWVNRLHLrgrlvyervrTGLPDPERPRLDPDSLAGK- 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1222 qtaLEIEE------LNRKYEQAKNI-----SQDLE------------KQAARVHEeaKRAGDKAVEIYA----SVAQLTP 1274
Cdd:COG4913 540 ---LDFKPhpfrawLEAELGRRFDYvcvdsPEELRrhpraitragqvKGNGTRHE--KDDRRRIRSRYVlgfdNRAKLAA 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1275 VDSE--ALENEANKIKKEAADLDRLID---------QKLKDYEDLREDMRGKEHEVKNLlekgkaEQQtadqllaradaa 1343
Cdd:COG4913 615 LEAElaELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDVASAEREIAEL------EAE------------ 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1344 kalaeeaakkgRSTLQEANDILNNLKdfdRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALgNAAADATEAKNK 1423
Cdd:COG4913 677 -----------LERLDASSDDLAALE---EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAED 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1424 AHEAERIASAVQKNATSTKADAERTFGEvtDLDNEVNGMLRQLEEAENELKKKQDDADQD--MMMAGMASQAAQEAELNA 1501
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRAFNREwpAETADLDADLESLPEYLA 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1502 RkaknsvssllsqlnnlldqLGQLDTVDL-NKLNEIEGSLNKAKdemkasdlDRKVSDLESEARKQEaaimdynRDIAEI 1580
Cdd:COG4913 820 L-------------------LDRLEEDGLpEYEERFKELLNENS--------IEFVADLLSKLRRAI-------REIKER 865
|
....
gi 153791270 1581 IKDI 1584
Cdd:COG4913 866 IDPL 869
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1221-1590 |
7.38e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1221 NQTALEIEELNRKYEQAK-NISQDLEKQAARVHEEAKRAGDKAVEIyasvAQLTpVDSEALENEANK-IKKEAADLDRLI 1298
Cdd:PTZ00440 955 NNLKMQIEKTLEYYDKSKeNINGNDGTHLEKLDKEKDEWEHFKSEI----DKLN-VNYNILNKKIDDlIKKQHDDIIELI 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1299 DqklKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARAdaakalaeeaakkgrstLQEANDILNNLKDFDRRVNdn 1378
Cdd:PTZ00440 1030 D---KLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIK-----------------KYKNPKIKEEIKLLEEKVE-- 1087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1379 ktaaeealrripAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAeriASAVQKNATSTKADAERTFGEVTDLDNE 1458
Cdd:PTZ00440 1088 ------------ALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEH---YNKKKKSLEKIYKQMEKTLKELENMNLE 1152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1459 VNgMLRQLEEAENELKKK--QDDADQDMMMAGMASQAAQEAELNARK---AKNSVSSLLSQLNNLLDQLGQLDTVDLNKl 1533
Cdd:PTZ00440 1153 DI-TLNEVNEIEIEYERIliDHIVEQINNEAKKSKTIMEEIESYKKDidqVKKNMSKERNDHLTTFEYNAYYDKATASY- 1230
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1534 NEIEGSLNKAKDEMKASDLDRKVSDLE---SEARKQEAAIMDYNRDIAEIIKDIHNLEDI 1590
Cdd:PTZ00440 1231 ENIEELTTEAKGLKGEANRSTNVDELKeikLQVFSYLQQVIKENNKMENALHEIKNMYEF 1290
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1184-1415 |
7.52e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 43.18 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1184 LAERHKQEADDIVRVAKTANETsAEAY----NLLLRTlaGENQTALEI-EELNRKYEQAKNISQDLekqaARVHEEAKRA 1258
Cdd:COG2956 20 LNGQPDKAIDLLEEALELDPET-VEAHlalgNLYRRR--GEYDRAIRIhQKLLERDPDRAEALLEL----AQDYLKAGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1259 gDKAVEIYASVAQLTPVDSEALENEANkIKKEAADLDRLIDQklkdYEDLREDMRGKEHevkNLLEKGKAEQQTADqlla 1338
Cdd:COG2956 93 -DRAEELLEKLLELDPDDAEALRLLAE-IYEQEGDWEKAIEV----LERLLKLGPENAH---AYCELAELYLEQGD---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1339 radaakalaeeaAKKGRSTLQEANDI-------LNNLKDFDRRVNDNKtAAEEALRRIPAINRTIAEANEKTREAQLALG 1411
Cdd:COG2956 160 ------------YDEAIEALEKALKLdpdcaraLLLLAELYLEQGDYE-EAIAALERALEQDPDYLPALPRLAELYEKLG 226
|
....
gi 153791270 1412 NAAA 1415
Cdd:COG2956 227 DPEE 230
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1268-1592 |
7.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1268 SVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLR--EDMRgKEHEVKNLLEKGKAEQQTADQLLARADAAKA 1345
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARkaEEAR-KAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1346 LAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEA-----------------LRRIPAINRtIAEANEKTREAQL 1408
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAArkaeeerkaeearkaedAKKAEAVKK-AEEAKKDAEEAKK 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1409 A---LGNAAADATEAKNKAHEAERiaSAVQKNATSTKADAERTFGEVTDLDNevngmLRQLEEAE--NELKKKQDD---A 1480
Cdd:PTZ00121 1245 AeeeRNNEEIRKFEEARMAHFARR--QAAIKAEEARKADELKKAEEKKKADE-----AKKAEEKKkaDEAKKKAEEakkA 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1481 DQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDqlgqldtvdlnklnEIEGSLNKAK-DEMKASDLDRKVSDL 1559
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD--------------EAEAAEEKAEaAEKKKEEAKKKADAA 1383
|
330 340 350
....*....|....*....|....*....|...
gi 153791270 1560 ESEARKQEAAimDYNRDIAEiiKDIHNLEDIKK 1592
Cdd:PTZ00121 1384 KKKAEEKKKA--DEAKKKAE--EDKKKADELKK 1412
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1125-1304 |
8.40e-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: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1125 TGILAERArsrvESTEQLIEIAsrelEKAKMAAANvsitqpestgepnnmtLLAEEARKLAERhKQEADDIVRVAK-TAN 1203
Cdd:COG0711 26 LKALDERQ----EKIADGLAEA----ERAKEEAEA----------------ALAEYEEKLAEA-RAEAAEIIAEARkEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1204 ETSAEAynlllrtlagenQTALEiEELNRKYEQAKnisQDLEKQAARVHEEAK-RAGDKAVEIYASVaqltpvdseaLEN 1282
Cdd:COG0711 81 AIAEEA------------KAEAE-AEAERIIAQAE---AEIEQERAKALAELRaEVADLAVAIAEKI----------LGK 134
|
170 180
....*....|....*....|..
gi 153791270 1283 EANkikkeAADLDRLIDQKLKD 1304
Cdd:COG0711 135 ELD-----AAAQAALVDRFIAE 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1038-1398 |
8.67e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1038 DKVAEHRVKLQELESLIANLGTGDDMVTDQ--AFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRL 1115
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEEleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1116 QNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTG---------------------EPNNM 1174
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligveaayeaaleaalaaaLQNIV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1175 TLLAEEARKLAERHKQEAD---DIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARV 1251
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1252 HEEAKRA-----GDKAVEIYASVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLkdyEDLREDMRGKEHEVKNLLEKG 1326
Cdd:COG1196 633 EAALRRAvtlagRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL---AEEELELEEALLAEEEEEREL 709
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791270 1327 KAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIpaiNRTIAE 1398
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL---EREIEA 778
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1388-1503 |
9.41e-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: 41.31 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1388 RIPAINRTIAEANEKTREAQLALGNAAADATEAKnkaHEAERIASAVQKNATSTKADAertfgeVTDLDNEVNgmlRQLE 1467
Cdd:COG0711 32 RQEKIADGLAEAERAKEEAEAALAEYEEKLAEAR---AEAAEIIAEARKEAEAIAEEA------KAEAEAEAE---RIIA 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 153791270 1468 EAENELKKKQDDAdqdmmMAGMASQAAQEAELNARK 1503
Cdd:COG0711 100 QAEAEIEQERAKA-----LAELRAEVADLAVAIAEK 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1179-1589 |
9.44e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1179 EEARKLAERHKQ---EADDIVRVAKTAN-ETSAEAYNLLLRTLAGENQtalEIEELNRKYEQAKNISQDLEKQAARVHEE 1254
Cdd:COG4913 255 EPIRELAERYAAareRLAELEYLRAALRlWFAQRRLELLEAELEELRA---ELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1255 AKRAGDKAVEiyasvaQLTpVDSEALENEANKIKKEAADLDRLIDQklkdyedLREDMRGKEHEVKNLLEKGKAEQQTAD 1334
Cdd:COG4913 332 IRGNGGDRLE------QLE-REIERLERELEERERRRARLEALLAA-------LGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1335 QLLARADAAKALAEEAAKKGRSTLQEANDILNNLK----DFDRRVNDNKTAAEEALRRIPA--------INrtIAEANEK 1402
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLErrksNIPARLLALRDALAEALGLDEAelpfvgelIE--VRPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1403 TREA-QLALGNAA----------ADATEAKNKAHEAERI----ASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQL- 1466
Cdd:COG4913 476 WRGAiERVLGGFAltllvppehyAAALRWVNRLHLRGRLvyerVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAEl 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1467 ---------EEAEnELKkkqdDADQDMMMAGMASQAAQEAELNARKAKNSVSsllsqlnnlldQLGQlDTVDlnKLNEIE 1537
Cdd:COG4913 556 grrfdyvcvDSPE-ELR----RHPRAITRAGQVKGNGTRHEKDDRRRIRSRY-----------VLGF-DNRA--KLAALE 616
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1538 GSLNKAKDEMkaSDLDRKVSDLESEARKQEAAIMDYNR---------DIAEIIKDIHNLED 1589
Cdd:COG4913 617 AELAELEEEL--AEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEA 675
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1179-1409 |
1.11e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1179 EEARKLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRA 1258
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1259 G-----------DKAVEIYASVAQLTPVdSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEvKNLLEKGK 1327
Cdd:COG4942 117 GrqpplalllspEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERAELEALLAELEEE-RAALEALK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1328 AEQQTadqllaradaakalaeeaakkgrsTLQEANdilNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQ 1407
Cdd:COG4942 195 AERQK------------------------LLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
..
gi 153791270 1408 LA 1409
Cdd:COG4942 248 FA 249
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
284-325 |
1.36e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 153791270 284 CKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRP 325
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1220-1455 |
1.38e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1220 ENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEiyASVAQLTPVDSEALENEANKIKKEAadldrlid 1299
Cdd:PRK09510 82 KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ--AALKQKQAEEAAAKAAAAAKAKAEA-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1300 qklkdyedlrEDMRGKEHEVKNLLEKGKAEQQTADQLLAradaakalaeeaakkgrstlQEAndilnnlkdfdrrvndNK 1379
Cdd:PRK09510 152 ----------EAKRAAAAAKKAAAEAKKKAEAEAAKKAA--------------------AEA----------------KK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791270 1380 TAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAH-EAERIASAVQKNATSTKADAERTFGEVTDL 1455
Cdd:PRK09510 186 KAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAaEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1070-1259 |
1.40e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETgilaeraRSRVESTEQLIEIASRE 1149
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-------EAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1150 LEKAK------MAAANVSITQPE-----STGEPNN-------MTLLAEEARKLAERHKQEADDIVRVAKTANETSAEAYN 1211
Cdd:COG4942 99 LEAQKeelaelLRALYRLGRQPPlalllSPEDFLDavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791270 1212 LL---------LRTLAGENQTAL------------EIEELNRKYEQAKNISQDLEKQAARVHEEAKRAG 1259
Cdd:COG4942 179 LLaeleeeraaLEALKAERQKLLarlekelaelaaELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1235-1489 |
1.68e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 43.21 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1235 EQAKNI----SQDLEKQAARVHEEAKRAGDKAVEIyasvaqltpvdsEALENEANKIKKEAAD-LDRLIDQKLKDYEDLR 1309
Cdd:COG1193 503 ERARELlgeeSIDVEKLIEELERERRELEEEREEA------------ERLREELEKLREELEEkLEELEEEKEEILEKAR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1310 ED----MRGKEHEVKNLLEKGKAEQQTADQllaradaakalaeeaakkgrstLQEANDILNNLKD-FDRRVNDNKTAAEE 1384
Cdd:COG1193 571 EEaeeiLREARKEAEELIRELREAQAEEEE----------------------LKEARKKLEELKQeLEEKLEKPKKKAKP 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1385 ALR----------RIPAINR--TIAEANEKtREAQLALG----NAAADATEAKNKAHEAERIASAVQKNATSTKADAERT 1448
Cdd:COG1193 629 AKPpeelkvgdrvRVLSLGQkgEVLEIPKG-GEAEVQVGilkmTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSP 707
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 153791270 1449 fgevtDLDneVNGMLrqLEEAENELKKKQDDAdqdmMMAGM 1489
Cdd:COG1193 708 -----ELD--LRGMR--VEEALPELDKYLDDA----LLAGL 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1189-1446 |
1.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1189 KQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKnisQDLEKQAARVHEEAKRAGDKAVEIYAS 1268
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1269 VAQLTPVD--------SEALENeankikkeAADLDRLIDQKLKDYEDLREDmrgkehevKNLLEKGKAEQQTAdqllara 1340
Cdd:COG3883 99 GGSVSYLDvllgsesfSDFLDR--------LSALSKIADADADLLEELKAD--------KAELEAKKAELEAK------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1341 daakalaeeaakkgRSTLQEANDILNNLKDfdrRVNDNKTAAEEALRRIpainrtiaEANEKTREAQLALGNAAADATEA 1420
Cdd:COG3883 156 --------------LAELEALKAELEAAKA---ELEAQQAEQEALLAQL--------SAEEAAAEAQLAELEAELAAAEA 210
|
250 260
....*....|....*....|....*.
gi 153791270 1421 KNKAHEAERIASAVQKNATSTKADAE 1446
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1257-1596 |
1.75e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1257 RAGDKAVEIYASVAQLTPVDSEALENEANKIKKEAADLDRLidqkLKDYEDLREDMRGKEHEVKNL---LEKGKAEQQTA 1333
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKL----QEELEQLREELEQAREELEQLeeeLEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1334 DQLlaradaakalaeeaakkgrstLQEANDILnnlkdfdrrvndnktaaEEALRRIPAINRTIAEANEKTREAQLALgna 1413
Cdd:COG4372 79 EEE---------------------LEELNEQL-----------------QAAQAELAQAQEELESLQEEAEELQEEL--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1414 AADATEAKNKAHEAERIASAVQKNATSTKADAErtfgEVTDLDNEVNGMLRQLEEAENELKK-KQDDADQDmmMAGMASQ 1492
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREE----ELKELEEQLESLQEELAALEQELQAlSEAEAEQA--LDELLKE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1493 AAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMD 1572
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
330 340
....*....|....*....|....
gi 153791270 1573 YNRDIAEIIKDIHNLEDIKKTLPT 1596
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALEL 295
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1036-1344 |
1.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1036 VKDKVAEHRVKLQELESLIANLGT----------GDDmVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVN 1105
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEAlleagkcpecGQP-VEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1106 S--SLHSQISRLQNIRNTIEEtgiLAERARSRVESTEQLIEiASRElEKAKMAAAnvsitqpestgepnnmtllAEEARK 1183
Cdd:PRK02224 503 DlvEAEDRIERLEERREDLEE---LIAERRETIEEKRERAE-ELRE-RAAELEAE-------------------AEEKRE 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1184 LAERHKQEADDIVRVAKT------ANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAknisQDLEKQAaRVHEEAKR 1257
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAElnsklaELKERIESLERIRTLLAAIADAEDEIERLREKREAL----AELNDER-RERLAEKR 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1258 agDKAVEIYASVaqltpvDSEALEnEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLL 1337
Cdd:PRK02224 634 --ERKRELEAEF------DEARIE-EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALE 704
|
....*..
gi 153791270 1338 ARADAAK 1344
Cdd:PRK02224 705 NRVEALE 711
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1432-1596 |
1.90e-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: 42.68 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1432 SAVQKNATSTKADAERTFGE----------VTDL-DNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAA----QE 1496
Cdd:pfam05262 170 SDVDTDSISDKKVVEALREDnekgvnfrrdMTDLkERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNAdkqrDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1497 AELNARKAKNSVSSLLSQLNNLLDQLGQldtvdlNKLNEIEGS----------LNKAKDEmKASDLDRKVSDLESEARKQ 1566
Cdd:pfam05262 250 VRQKQQEAKNLPKPADTSSPKEDKQVAE------NQKREIEKAqieikkndeeALKAKDH-KAFDLKQESKASEKEAEDK 322
|
170 180 190
....*....|....*....|....*....|
gi 153791270 1567 EAaimDYNRDIAEIIKDIHNLEDIKKTLPT 1596
Cdd:pfam05262 323 EL---EAQKKREPVAEDLQKTKPQVEAQPT 349
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1385-1583 |
1.96e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1385 ALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNK----AHEAERIASAVQKN---ATSTKADAERTFGEVTDLDN 1457
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKElsslAQETEELQKKATQTlakAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1458 EVNGMLRQLEE---------------AENELKKKQDDADQdmMMAGMAS----QAAQEAELNARKAKNSVSSLLSQLNNL 1518
Cdd:pfam06008 90 AIKNLIDNIKEinekvatlgendfalPSSDLSRMLAEAQR--MLGEIRSrdfgTQLQNAEAELKAAQDLLSRIQTWFQSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1519 LDQLGQLDTVDLNKLNEIEGSL-------NKAKDEMK-ASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKD 1583
Cdd:pfam06008 168 QEENKALANALRDSLAEYEAKLsdlrellREAAAKTRdANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1095-1296 |
2.33e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.04 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1095 QNLMDRLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTE----QLIeiASRElekakmaaanvsitqpestge 1170
Cdd:pfam15619 10 LHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTEselpQLI--ARHN--------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1171 pnnmtllaEEARKLAERHKQEADDIVRVAKTANETSAEAYNLL-----LRTLAgENQTALEIEELNRK-------YEQAK 1238
Cdd:pfam15619 67 --------EEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRdqlkrLEKLS-EDKNLAEREELQKKleqleakLEDKD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791270 1239 NISQDLEKQ-----AARVHEEAkRAGDKAVEIYASVAQltpvdseaLENEANKIKKEAADLDR 1296
Cdd:pfam15619 138 EKIQDLERKlelenKSFRRQLA-AEKKKHKEAQEEVKI--------LQEEIERLQQKLKEKER 191
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1392-1495 |
2.92e-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: 39.34 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1392 INRTIAEANEKTREAQLALGNAAADATEAKNkahEAERIASAVQKNATSTKADAertfgeVTDLDNEVNGMLRQ-LEEAE 1470
Cdd:cd06503 35 IAESLEEAEKAKEEAEELLAEYEEKLAEARA---EAQEIIEEARKEAEKIKEEI------LAEAKEEAERILEQaKAEIE 105
|
90 100
....*....|....*....|....*
gi 153791270 1471 NELKKKQDDADQDmmMAGMASQAAQ 1495
Cdd:cd06503 106 QEKEKALAELRKE--VADLAVEAAE 128
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1035-1488 |
2.95e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1035 LVKDKVAEHRV--KLQELESlianlgtgDDMVTDQAFEDRLKEAERE-VTDLLREAQEVKDVDQNLMDRLQRVnSSLHSQ 1111
Cdd:COG3064 4 ALEEKAAEAAAqeRLEQAEA--------EKRAAAEAEQKAKEEAEEErLAELEAKRQAEEEAREAKAEAEQRA-AELAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1112 ISRLQNirnTIEETGILAERaRSRVESTEQLIEI-ASRELEKAKMAAANVSITQPESTGEpnnmtllaEEARKLAERHKQ 1190
Cdd:COG3064 75 AAKKLA---EAEKAAAEAEK-KAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEEAKRKAE--------EEAKRKAEEERK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1191 EADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVA 1270
Cdd:COG3064 143 AAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1271 QLTPVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMR---GKEHEVKNLLEKGKAEQQTADQLLARADAAKALA 1347
Cdd:COG3064 223 ARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAaaaAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1348 EEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADA---TEAKNKA 1424
Cdd:COG3064 303 LAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAgalLLGKLAD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791270 1425 HEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQDMMMAG 1488
Cdd:COG3064 383 VEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAG 446
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1379-1582 |
3.16e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1379 KTAAEEAlrripainRTIAEANEKTREAQLALGNAAADATEAKNKA-HEAERIASAVQKNATSTKADAERTFGEVTDLDN 1457
Cdd:COG3064 92 KAAAEKA--------KAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1458 EVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDtvDLNKLNEIE 1537
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREA--ALAAVEATE 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153791270 1538 GSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIK 1582
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALA 286
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1114-1333 |
4.55e-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: 40.40 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1114 RLQNIRNTIEETGILAERARSRVESTEQLI-----EIAS---------RELEKAKmaaanvsitqpestgepnnmTLLAE 1179
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAekaeaEVAAlnrriqlleEELERTE--------------------ERLAE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1180 EARKLAERHKQeADDIVRVAKTanetsaeaynLLLRTLAGENQtaleIEELNRKYEQAKNISQDLEKQ---AAR----VH 1252
Cdd:pfam00261 62 ALEKLEEAEKA-ADESERGRKV----------LENRALKDEEK----MEILEAQLKEAKEIAEEADRKyeeVARklvvVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1253 EEAKRAGDKAVEIYASVAQLtpvdSEALENEANKIKK-EAAdldrliDQKLKDYEDLredmrgKEHEVKNLLEKGKAEQQ 1331
Cdd:pfam00261 127 GDLERAEERAELAESKIVEL----EEELKVVGNNLKSlEAS------EEKASEREDK------YEEQIRFLTEKLKEAET 190
|
..
gi 153791270 1332 TA 1333
Cdd:pfam00261 191 RA 192
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
685-981 |
4.77e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 41.11 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 685 VESCTCPVGYGGQFCETCLPG-YRRETPSLGPYS---PCVLCTCNGHSETCDPETGVCDCRDNTAGPHCEKCSDGYY--G 758
Cdd:pfam03302 25 TENCKACSNDKREVCEECNSNnYLTPTSQCIDDCakiGNYYYTTNANNKKICKECTVANCKTCEDQGQCQACNDGFYksG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 759 DSTLGTSSDCQPCPCPGGSSCAIVPK----------TKEVVCTHCPTGTAGKRCELCDDGYFGdplgsngpVRLCRPCQC 828
Cdd:pfam03302 105 DACSPCHESCKTCSGGTASDCTECLTgkalrygndgTKGTCGEGCTTGTGAGACKTCGLTIDG--------TSYCSECAT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 829 NDNIDPNAV--GNCNRLTGECLKCiyNTAGFYCDRCKEGFF-------------GNPL--APNPADKCKACACNPYGTVQ 891
Cdd:pfam03302 177 ETEYPQNGVctSTAARATATCKAS--SVANGMCSSCANGYFrmnggcyettkfpGKSVceEANSGGTCQKEAPGYKLNNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 892 QQSSCNPVTGQCQclphvSGRDCGTCDPGYynLQSGQGCERCDchalgSTNGQCDIRTGQCEC------QPGITGQHCER 965
Cdd:pfam03302 255 DLVTCSPGCKTCT-----SNTVCTTCMDGY--VKTSDSCTKCD-----SSCETCTGATTTCKTcatgyyKSGTGCVSCTS 322
|
330
....*....|....*.
gi 153791270 966 CETNHFGFGPEGCKPC 981
Cdd:pfam03302 323 SESDNGITGVKGCLNC 338
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1285-1506 |
4.78e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.86 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1285 NKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEK----GKAEQQTADQllaradaakalaeeaakkGRSTLQE 1360
Cdd:pfam06008 15 YKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQEteelQKKATQTLAK------------------AQQVNAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1361 ANDILNNlkdfdrrvndnktaAEEALRRIPAINRTIAEANEKTreAQLALGNAAADATEAKNKAHEAERIA--------S 1432
Cdd:pfam06008 77 SERTLGH--------------AKELAEAIKNLIDNIKEINEKV--ATLGENDFALPSSDLSRMLAEAQRMLgeirsrdfG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791270 1433 AVQKNATSTKADAERTFGEVTDL----DNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQAAQeaELNARKAKN 1506
Cdd:pfam06008 141 TQLQNAEAELKAAQDLLSRIQTWfqspQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDAN--RLNLANQAN 216
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1067-1295 |
5.45e-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: 40.40 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1067 QAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEEtgilAERARSRVESTEQLIEIA 1146
Cdd:pfam00261 18 KEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADE----SERGRKVLENRALKDEEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1147 SRELEkakmAAANVSITQPESTGEPnnmtlLAEEARKLAERhKQEADDIVRVAKTANETSAEAYNLL------LRTLAGE 1220
Cdd:pfam00261 94 MEILE----AQLKEAKEIAEEADRK-----YEEVARKLVVV-EGDLERAEERAELAESKIVELEEELkvvgnnLKSLEAS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791270 1221 NQTALEIEELNRkyEQAKNISQDLeKQAARVHEEAKRagdKAVEIYASVAQLtpvdSEALENEANKIKKEAADLD 1295
Cdd:pfam00261 164 EEKASEREDKYE--EQIRFLTEKL-KEAETRAEFAER---SVQKLEKEVDRL----EDELEAEKEKYKAISEELD 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1035-1254 |
5.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1035 LVKDKVAEHRVKLQELESLIANLGTGDDMvtdqafEDRLKEAEREVTDL--LREAQEVKDVDQNLMDRLQRVNSSLHSQI 1112
Cdd:COG4913 212 FVREYMLEEPDTFEAADALVEHFDDLERA------HEALEDAREQIELLepIRELAERYAAARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1113 S--RLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSitqpestGEpnNMTLL------AEEARKL 1184
Cdd:COG4913 286 AqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------GD--RLEQLereierLERELEE 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791270 1185 AERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGE-NQTALEIEELNRKYEQAKNISQDLEKQAARVHEE 1254
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALlEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1096-1330 |
5.70e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1096 NLMDRLQR-VNSSLHSqisrlqnirntieetgiLAERARSRVESTEQLIEIASRELEKAKMAAANVsitqpestgepnnM 1174
Cdd:COG1842 1 GIFKRLSDiIRANINA-----------------LLDKAEDPEKMLDQAIRDMEEDLVEARQALAQV-------------I 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1175 TLLAEEARKLAERHKQEA--------------DDIVRVA---KTANETSAEAYNLLLRTLAgENQTALE--IEELNRKYE 1235
Cdd:COG1842 51 ANQKRLERQLEELEAEAEkweekarlalekgrEDLAREAlerKAELEAQAEALEAQLAQLE-EQVEKLKeaLRQLESKLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1236 QAKNisqdlEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDS-EALENEANKIKKEAADLDRL-----IDQKLKDYEdlr 1309
Cdd:COG1842 130 ELKA-----KKDTLKARAKAAKAQEKVNEALSGIDSDDATSAlERMEEKIEEMEARAEAAAELaagdsLDDELAELE--- 201
|
250 260
....*....|....*....|.
gi 153791270 1310 edmrgKEHEVKNLLEKGKAEQ 1330
Cdd:COG1842 202 -----ADSEVEDELAALKAKM 217
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1033-1307 |
5.82e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.46 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1033 YRLVKDKVAEHRVKLQ---ELESLIANLgtgddmvtdQAFEDRLKEAEREVtdLLREAQEVKD-----VDQNLMDRLQRv 1104
Cdd:PLN03188 949 HKLLKEKYENHPEVLRtkiELKRVQDEL---------EHYRNFYDMGEREV--LLEEIQDLRSqlqyyIDSSLPSARKR- 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1105 NSSLH-------SQISRLQNIRNTIEETG-------------------ILAERARSRVESTEQLIEIASRELEKAKMAAa 1158
Cdd:PLN03188 1017 NSLLKltyscepSQAPPLNTIPESTDESPekkleqerlrwteaeskwiSLAEELRTELDASRALAEKQKHELDTEKRCA- 1095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1159 nvsitqpESTGEPNNMTL------------LAEEARKLAERHK--QEA-DDIVRVAKTANETSAEAYnlLLRTLAGEnQT 1223
Cdd:PLN03188 1096 -------EELKEAMQMAMegharmleqyadLEEKHIQLLARHRriQEGiDDVKKAAARAGVRGAESK--FINALAAE-IS 1165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1224 ALEIE-ELNRKYEQAKNISqdLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENEankikKEAADLDRLIDQKL 1302
Cdd:PLN03188 1166 ALKVErEKERRYLRDENKS--LQAQLRDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAE-----QEAAEAYKQIDKLK 1238
|
....*
gi 153791270 1303 KDYED 1307
Cdd:PLN03188 1239 RKHEN 1243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1177-1467 |
5.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1177 LAEEARKLAERHKQEADDI--VRVAKTANETSAEAYNLLLRTLAGEN---QTALEIEELNRKYEQAKNISQDLEKQAARV 1251
Cdd:COG4913 615 LEAELAELEEELAEAEERLeaLEAELDALQERREALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1252 hEEAKRAGDKAVEiyasvaqltpvDSEALENEANKIKKEAADLDRLIDQKLKDYEDLreDMRGKEHEVKNLLEKGKAEQQ 1331
Cdd:COG4913 695 -EELEAELEELEE-----------ELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1332 TADQLLAradaakalaeeaakkgRSTLQEANDILNNLKDfdrrvndnktAAEEALRRIpainrtIAEANEKTREAQLALG 1411
Cdd:COG4913 761 DAVEREL----------------RENLEERIDALRARLN----------RAEEELERA------MRAFNREWPAETADLD 808
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791270 1412 NAAADATE--------AKNKAHEAE-RIASAVQKNATSTKAD----AERTFGEVTDLDNEVNGMLRQLE 1467
Cdd:COG4913 809 ADLESLPEylalldrlEEDGLPEYEeRFKELLNENSIEFVADllskLRRAIREIKERIDPLNDSLKRIP 877
|
|
| t_SNARE |
smart00397 |
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
1070-1153 |
7.56e-03 |
|
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".
Pssm-ID: 197699 [Multi-domain] Cd Length: 66 Bit Score: 36.41 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1070 EDRLKEAEREVTDLLREAQEVKDVDQNLMDRLqrvnsslHSQISRLQNIRNtieetgilaerarsRVESTEQLIEIASRE 1149
Cdd:smart00397 4 LAREEERDEELEQLEKSIQELKQIFLDMGTEL-------EEQGEQLDRIED--------------NVDDADVNLKKANKR 62
|
....
gi 153791270 1150 LEKA 1153
Cdd:smart00397 63 LKKA 66
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1278-1567 |
7.99e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1278 EALENEANKIKKEAADLDRLIDQ---KLKDYEDLREDMRGKeheVKNLLEKGKAEQQTADQLLARADAAkalaeeaakkg 1354
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKEL----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1355 RSTLQEANDILNNLKD-FD--RRVNDNKTAA---EEALRRipAINR--------------------TIAEANEKTREAQL 1408
Cdd:COG1340 77 KEERDELNEKLNELREeLDelRKELAELNKAggsIDKLRK--EIERlewrqqtevlspeeekelveKIKELEKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1409 ALgNAAADATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKKKQDDADQdmmmag 1488
Cdd:COG1340 155 AL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE------ 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791270 1489 masqaaQEAELNARKAKnsvssllsqlnnlldqLGQLDTvdlnKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQE 1567
Cdd:COG1340 228 ------LHEEIIELQKE----------------LRELRK----ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGE 280
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1278-1484 |
8.23e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.98 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1278 EALENeANKIKKEAADLDRLiDQKLKDYEDLREDMR--------GKEHEVKNLLEK---GKAEQQTADQllaradaakal 1346
Cdd:pfam12795 24 QALSL-LDKIDASKQRAAAY-QKALDDAPAELRELRqelaalqaKAEAAPKEILASlslEELEQRLLQT----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1347 aeeaakkgRSTLQEANdilNNLKDFDRRVNDNKTAAE-------EALRRIPAINRTI---AEANEKTREAQLALGNAAAD 1416
Cdd:pfam12795 91 --------SAQLQELQ---NQLAQLNSQLIELQTRPEraqqqlsEARQRLQQIRNRLngpAPPGEPLSEAQRWALQAELA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791270 1417 ATEAKNKAHEAE------RIASAvQKNATSTKADAERTFGEVTDLDNEVNGmlRQLEEAENELKKKQDDADQDM 1484
Cdd:pfam12795 160 ALKAQIDMLEQEllsnnnRQDLL-KARRDLLTLRIQRLEQQLQALQELLNE--KRLQEAEQAVAQTEQLAEEAA 230
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
284-326 |
8.39e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 35.75 E-value: 8.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 153791270 284 CKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRPW 326
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1303-1507 |
9.88e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 40.35 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1303 KDYEDLREDM--RGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAakkgrsTLQEANdilnnlkdfdrrvndnKT 1380
Cdd:PRK07735 5 KDLEDLKKEAarRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDM------TIEEAK----------------RR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791270 1381 AAEEALRRIPAINRTIAEANEKTREAQLALGNAAAdATEAKNKAHEAERI-------ASAVQKNATSTKADAERTfgevt 1453
Cdd:PRK07735 63 AAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKA-AAAAKAKAAALAKQkregteeVTEEEKAAAKAKAAAAAK----- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791270 1454 dldNEVNGMLRQLEEAENELKKKQDDADQDMMMAGMASQA-AQEAELNARKAKNS 1507
Cdd:PRK07735 137 ---AKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAkAKAAALAKQKAAEA 188
|
|
| |
