|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
8.44e-106 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 337.25 E-value: 8.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 6981142 283 RG 284
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-284 |
4.95e-84 |
|
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: 275.39 E-value: 4.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136 151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 6981142 277 LYELVIRG 284
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1730-1801 |
4.26e-37 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 134.11 E-value: 4.26e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1448-1793 |
1.10e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196 320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1767
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528
|
330 340
....*....|....*....|....*.
gi 6981142 1768 ELEVKAAQLDGLEARMRSVLQAINLQ 1793
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVE 554
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1465-1790 |
4.72e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1465 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1536
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1537 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:PRK02224 290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1609 TVQAALEEAQRAQGAAQGAI----------RGAVVDTKNT-----------EQTLQQVQERMAGTEQSLNSASERARQLH 1667
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIeeleeeieelRERFGDAPVDlgnaedfleelREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1714
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1715 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEaRMRSVLQAI 1790
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1796 |
4.23e-15 |
|
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: 81.64 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1199 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1276
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1277 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1354
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1355 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1414
Cdd:TIGR02168 518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1415 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1484
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1564
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1565 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK----NTEQ 1640
Cdd:TIGR02168 752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRE 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1641 TLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKQLreqvgdqyqtVRALA 1720
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--------------ELEELIEELESEL----------EALLN 880
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1721 ERKAegvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:TIGR02168 881 ERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
786-831 |
2.74e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.49 E-value: 2.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 831
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
785-832 |
4.68e-14 |
|
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: 67.76 E-value: 4.68e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 785 PCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGF--GPAGCQ 832
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
786-834 |
5.04e-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: 67.76 E-value: 5.04e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 834
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1448-1756 |
5.83e-14 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 77.94 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1514
Cdd:NF041483 478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1515 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDA- 1593
Cdd:NF041483 558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADAr 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 ---QRARSRA--EGERQKAE------TVQA-ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQvqERMAGTEQSLNSASE 1661
Cdd:NF041483 600 aeaERIRREAaeETERLRTEaaerirTLQAqAEQEAERLRTEAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQE 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1662 RARQLHALLEALKLK---RAGNSLAAST---------AEETAGSAQS-------RAREAEKQL----REQVGD-QYQTVR 1717
Cdd:NF041483 678 SADRVRAEAAAAAERvgtEAAEALAAAQeeaarrrreAEETLGSARAeadqereRAREQSEELlasaRKRVEEaQAEAQR 757
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 6981142 1718 ALAE---RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ 1756
Cdd:NF041483 758 LVEEadrRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1790 |
1.14e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 73.71 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1446 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1524
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1525 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1591
Cdd:NF041483 984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1592 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1654
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1655 SLNsasERARQLHAllEALKlkRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AA 1730
Cdd:NF041483 1136 ELH---ERARRESA--EQMK--SAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAE 1204
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1731 QARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1790
Cdd:NF041483 1205 QKKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1458-1776 |
1.15e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.24 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1458 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1529
Cdd:NF041483 158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1530 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1607
Cdd:NF041483 234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1608 ETVQAALEEAQRAQGAAQGAIRGAvvdtknTEQTLQQVQERMAGTEqSLNSASERARQlHALLEALKL-KRAGNSLAAST 1686
Cdd:NF041483 287 EAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTVA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1687 AEETAGSAQSRAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDE----ARGLLQAAQD--KLQRLQELE 1759
Cdd:NF041483 359 AEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE-EAERIRReAEAEADRLRGEaadqAEQLKGAAKDdtKEYRAKTVE 437
|
330
....*....|....*..
gi 6981142 1760 gtYEENERELEVKAAQL 1776
Cdd:NF041483 438 --LQEEARRLRGEAEQL 452
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1146-1193 |
1.73e-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: 60.44 E-value: 1.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 6981142 1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1193
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-565 |
2.18e-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: 2.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6981142 524 PCDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-564 |
2.53e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6981142 525 CDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFR 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1463-1784 |
3.92e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 68.24 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1463 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1521
Cdd:pfam07111 354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1522 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1592
Cdd:pfam07111 434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1593 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1672
Cdd:pfam07111 508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1673 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1736
Cdd:pfam07111 562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 6981142 1737 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1784
Cdd:pfam07111 634 rLQDEARK--EEGQRLARRVQEL-----ERDKNLMLATLQQEGLLSRYK 675
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
413-470 |
8.45e-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: 58.52 E-value: 8.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 470
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1098-1146 |
1.11e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.11e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1770 |
1.38e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.77 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1446 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1521
Cdd:NF041483 720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1522 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1600
Cdd:NF041483 787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1601 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1670
Cdd:NF041483 843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1671 --EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1748
Cdd:NF041483 923 tsEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002
|
330 340
....*....|....*....|..
gi 6981142 1749 QDKLQRLQelEGTYEENERELE 1770
Cdd:NF041483 1003 AAEAERLR--TEAREEADRTLD 1022
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1145-1194 |
2.15e-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: 57.36 E-value: 2.15e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 1145 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1194
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1041-1095 |
2.90e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 2.90e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 1095
Cdd:pfam00053 1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
834-882 |
3.04e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 3.04e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 882
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1146-1190 |
7.37e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 7.37e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1190
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-523 |
8.45e-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: 55.82 E-value: 8.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6981142 472 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1040-1096 |
8.87e-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: 55.82 E-value: 8.87e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1040 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 1096
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
473-527 |
1.20e-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: 55.44 E-value: 1.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1556-1778 |
1.81e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.92 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1618
Cdd:NF041483 130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1619 RAQGAAQGAIRGAVVDTknteqtlqqvqERMagteqsLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSR 1697
Cdd:NF041483 204 SARAEAEAILRRARKDA-----------ERL------LNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1698 AREAEKQLREqvgdqyqtvralaerkaegvlaAQARAEQLRDEARgllQAAQdklQRLQELEGTYEENERELEVKAAQLD 1777
Cdd:NF041483 267 MQEAEEALRE----------------------ARAEAEKVVAEAK---EAAA---KQLASAESANEQRTRTAKEEIARLV 318
|
.
gi 6981142 1778 G 1778
Cdd:NF041483 319 G 319
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
412-471 |
2.25e-09 |
|
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: 54.67 E-value: 2.25e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 471
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
525-564 |
2.40e-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: 54.67 E-value: 2.40e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6981142 525 CDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFR 564
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1098-1143 |
3.67e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 3.67e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1143
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1097-1144 |
4.21e-09 |
|
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: 53.90 E-value: 4.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 1097 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1144
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1041-1095 |
8.26e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 8.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 1095
Cdd:smart00180 1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
989-1031 |
1.22e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 1.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
833-875 |
3.35e-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: 51.20 E-value: 3.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 833 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1554-1770 |
4.81e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1627
Cdd:NF041483 44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1628 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRArEAEK---Q 1704
Cdd:NF041483 121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARA-EAERlaeE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1705 LREQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQEL 1758
Cdd:NF041483 194 ARQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEA 270
|
250
....*....|..
gi 6981142 1759 EGTYEENERELE 1770
Cdd:NF041483 271 EEALREARAEAE 282
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1789 |
5.06e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1459 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1533
Cdd:NF041483 252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1598
Cdd:NF041483 326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1599 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1650
Cdd:NF041483 401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1651 GTEQSLNSA--------------SERARQlHALLEALKLKRagnslaasTAEETAgsaqSRAREAEKQLREQVGDQYQTV 1716
Cdd:NF041483 481 TAEELLTKAkadadelrstataeSERVRT-EAIERATTLRR--------QAEETL----ERTRAEAERLRAEAEEQAEEV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1717 RALAERKA-----EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSv 1786
Cdd:NF041483 548 RAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT- 626
|
...
gi 6981142 1787 LQA 1789
Cdd:NF041483 627 LQA 629
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
834-875 |
5.42e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 5.42e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6981142 834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
413-470 |
8.67e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 8.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 470
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
989-1035 |
9.11e-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: 50.05 E-value: 9.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6981142 989 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 1035
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-516 |
9.95e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.95e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 6981142 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 516
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
880-927 |
3.91e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 3.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6981142 880 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 927
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
879-924 |
5.64e-07 |
|
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: 47.73 E-value: 5.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 879 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 924
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
929-987 |
2.93e-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: 45.81 E-value: 2.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 929 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 987
Cdd:cd00055 1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
989-1031 |
2.99e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 989 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
350-402 |
1.54e-05 |
|
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: 43.88 E-value: 1.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1476-1747 |
1.67e-05 |
|
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: 48.44 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1476 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1553
Cdd:smart00283 2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRArsraeGERQK-----AETVQaAL 1614
Cdd:smart00283 75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARA-----GEAGRgfavvADEVR-KL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1615 eeAQRAQGAAqgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTaEETAGSA 1694
Cdd:smart00283 139 --AERSAESA-----------KEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE--ETGDALEEIVDSV-EEIADLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1695 QSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1747
Cdd:smart00283 203 QEIAAATDEQAAgsEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
350-401 |
1.71e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 1.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 350 CECNGH---SHSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 401
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
956-986 |
1.92e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 1.92e-05
10 20 30
....*....|....*....|....*....|.
gi 6981142 956 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 986
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-338 |
1.99e-05 |
|
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: 43.50 E-value: 1.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
930-979 |
3.44e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.68 E-value: 3.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 930 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 979
Cdd:smart00180 1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1684-1795 |
3.52e-05 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 46.09 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1684 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:PRK14475 36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 6981142 1760 GTYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1795
Cdd:PRK14475 115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1696-1791 |
7.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1696 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKL----QRLQELEGTYEENERELE 1770
Cdd:COG4913 238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312
|
90 100
....*....|....*....|.
gi 6981142 1771 VKAAQLDGLEARMRSVLQAIN 1791
Cdd:COG4913 313 RLEARLDALREELDELEAQIR 333
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1585-1620 |
2.86e-04 |
|
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.
Pssm-ID: 468572 [Multi-domain] Cd Length: 90 Bit Score: 41.52 E-value: 2.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6981142 1585 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1620
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
880-919 |
4.02e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 4.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 880 CVCNGR---ADECDAHTGACLgCRDYTGGEHCERCIAGFHGDP 919
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1469-1756 |
4.76e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1469 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1548
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1549 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1625
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1626 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALL---EALKLKRAGNSLA----------ASTAEET 1690
Cdd:NF012221 1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1691 AGSAQSRAR-----EAEKQLREQV------GDQYqTVRALAER----KAEGVLAAQAR-AEQLRDEARGLLQAAQDKLQR 1754
Cdd:NF012221 1762 ANQAQADAKgakqdESDKPNRQGAagsglsGKAY-SVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNR 1840
|
..
gi 6981142 1755 LQ 1756
Cdd:NF012221 1841 LQ 1842
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1571-1770 |
4.79e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 43.50 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1571 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1650
Cdd:cd07596 1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1651 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKQlREQVGDQYQTV-------RALAE 1721
Cdd:cd07596 71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDD-RADALLTLQSLkkdlaskKAQLE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981142 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1770
Cdd:cd07596 135 KLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
350-403 |
1.21e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.45 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 350 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 403
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| 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 ... |
1720-1796 |
2.23e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.99 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1720 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1791
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121
|
....*
gi 6981142 1792 LQVQI 1796
Cdd:pfam00430 122 LAVQI 126
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
309-341 |
3.67e-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: 36.95 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|...
gi 6981142 309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
8.44e-106 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 337.25 E-value: 8.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 6981142 283 RG 284
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-284 |
4.95e-84 |
|
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: 275.39 E-value: 4.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136 151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 6981142 277 LYELVIRG 284
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1730-1801 |
4.26e-37 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 134.11 E-value: 4.26e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1731-1800 |
2.48e-24 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 97.73 E-value: 2.48e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1731 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1448-1793 |
1.10e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196 320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1767
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528
|
330 340
....*....|....*....|....*.
gi 6981142 1768 ELEVKAAQLDGLEARMRSVLQAINLQ 1793
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVE 554
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1730-1800 |
7.27e-22 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 91.00 E-value: 7.27e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22300 2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1452-1782 |
2.34e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1452 ADLALGRARHTQAELQRAlvegggilsrvSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLSQEga 1531
Cdd:COG1196 227 AELLLLKLRELEAELEEL-----------EAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEE-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1532 dpdsiemvatRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1611
Cdd:COG1196 291 ----------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1612 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETA 1691
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1692 GSAQSRAREAEKQLREQvgdQYQTVRALAERKAEgvlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERelEV 1771
Cdd:COG1196 441 EEALEEAAEEEAELEEE---EEALLELLAELLEE-----AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE--GV 510
|
330
....*....|.
gi 6981142 1772 KAAQLDGLEAR 1782
Cdd:COG1196 511 KAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1554-1790 |
7.88e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLA--SEIAERVRSLADVDTILAHTM---------GDVRRAEQLLQDAQRARSRAEGERQKAET----VQAALEEAQ 1618
Cdd:COG1196 201 QLEPLErqAEKAERYRELKEELKELEAELlllklreleAELEELEAELEELEAELEELEAELAELEAeleeLRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1619 RAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA 1698
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1699 REAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDG 1778
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250
....*....|..
gi 6981142 1779 LEARMRSVLQAI 1790
Cdd:COG1196 440 EEEALEEAAEEE 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1492-1794 |
1.39e-18 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 92.39 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1492 QRAQAALDKANASRGQVEQANQELRELIQNVKdflsqegadpdsIEMVA-TRVLDISIPA-SPEQIQRLASEIAErvrsl 1569
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLT------------VEPVKgSNVIEISYTSpDPELAAAVANALAE----- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1570 ADVDTILAHTMGDVRRAEQLLQDaqrarsRAEGERQKAETVQAALEEAQRAQGAAqgairgavvdtkNTEQTLQQVQERM 1649
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLLQQL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1650 AGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE-----KQLREQVGDQYQTVRALAERKA 1724
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEleaelAELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1725 E-----------GVLAAQARAEQLR---DEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3206 302 AlraqlqqeaqrILASLEAELEALQareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
....
gi 6981142 1791 NLQV 1794
Cdd:COG3206 382 ALTV 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1448-1755 |
3.98e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 QEGADPDSIEMVATRVLDISipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1608 EtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 427 E---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRL 1755
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1465-1790 |
4.72e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1465 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1536
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1537 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:PRK02224 290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1609 TVQAALEEAQRAQGAAQGAI----------RGAVVDTKNT-----------EQTLQQVQERMAGTEQSLNSASERARQLH 1667
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIeeleeeieelRERFGDAPVDlgnaedfleelREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1714
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1715 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEaRMRSVLQAI 1790
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1245-1789 |
1.18e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1245 QAIVAARNTSAASTAKLVEAtEGLRHEIGKTTERLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDIL 1324
Cdd:COG1196 208 QAEKAERYRELKEELKELEA-ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1325 KHSNFLGAYDSIRHAHSQSTEAERRANAstfaipspvsnsADTRRRAEvlmgAQRENFNRQHLANQQALGRLSThthtls 1404
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRREL------------EERLEELE----EELAELEEELEELEEELEELEE------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1405 ltgvnelvcgapgdapcatspcggagcrdedgqprcgglgcsgAAATADLALGRARHTQAELQRALVEgggILSRVSETR 1484
Cdd:COG1196 345 -------------------------------------------ELEEAEEELEEAEAELAEAEEALLE---AEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASpEQIQRLASEIAE 1564
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1565 RVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQG-AAQGAIRGAVVDTKNTEQTLQ 1643
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1644 QVQE-RMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER 1722
Cdd:COG1196 538 AALEaALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1723 KAEGV------------LAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1789
Cdd:COG1196 616 YVLGDtllgrtlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1564-1782 |
1.40e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.12 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1564 ERVRSLADVDTILAHtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGA-IRGAVVDTKNTEQTL 1642
Cdd:COG4913 219 EEPDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1643 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQT-VRAL-- 1719
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----REIERLERELEERERRRARLEAlLAALgl 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981142 1720 -AERKAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENERELEVKAAQLDGLEAR 1782
Cdd:COG4913 374 pLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1199-1791 |
3.93e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1199 DWDRVVQDLAARTRRLEQWAQELQQT-GVLGAFESSFLNLQgklgmvQAIVAARNTSAASTAKLVEATEGLRHEigktTE 1277
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELeAELEELRLELEELE------LELEEAQAEEYELLAELARLEQDIARL----EE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1278 RLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDILKH--SNFLGAYDSIRHAHSQSTEAERRANASTF 1355
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1356 AIpspVSNSADTRRRAEVLMGAQRENFNRQHLANQQALGRLSTHTHTLSLtgvnelvcgapgdapcatspcggagcRDED 1435
Cdd:COG1196 390 EA---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------------------------EEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1436 GQprcgglgcsgAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQEL 1515
Cdd:COG1196 441 EE----------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1516 RELIQNVKDF-LSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVD-----TILAHTMGDVRRAEQL 1589
Cdd:COG1196 511 KAALLLAGLRgLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1590 LQDA---QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMA----------GTEQSL 1656
Cdd:COG1196 591 ALARgaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltgGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1657 NSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAA 1730
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleellEEEELLEE 750
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1731 QARAEQLRDEARGLLQAAQDKLQR------------LQELEgtyEENER--ELEvkaAQLDGLEARMRSVLQAIN 1791
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEReiealgpvnllaIEEYE---ELEERydFLS---EQREDLEEARETLEEAIE 819
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1796 |
4.23e-15 |
|
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: 81.64 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1199 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1276
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1277 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1354
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1355 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1414
Cdd:TIGR02168 518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1415 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1484
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1564
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1565 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK----NTEQ 1640
Cdd:TIGR02168 752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRE 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1641 TLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKQLreqvgdqyqtVRALA 1720
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--------------ELEELIEELESEL----------EALLN 880
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1721 ERKAegvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:TIGR02168 881 ERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1731-1800 |
8.19e-15 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 70.72 E-value: 8.19e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1731 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
786-831 |
2.74e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.49 E-value: 2.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 831
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
785-832 |
4.68e-14 |
|
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: 67.76 E-value: 4.68e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 785 PCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGF--GPAGCQ 832
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1204-1791 |
4.78e-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: 78.17 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1204 VQDLAARTRRLEQWAQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEATEGLRHEIGKTTERLTQLE 1283
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1284 AELTDVQD-------------ENFNANHALSGL-----------ERDGLALNLTLRQLDQHL------------DILKHS 1327
Cdd:TIGR02168 489 ARLDSLERlqenlegfsegvkALLKNQSGLSGIlgvlselisvdEGYEAAIEAALGGRLQAVvvenlnaakkaiAFLKQN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1328 N-----FLgAYDSIRHAHSQSTEAERRANASTFAipSPVSNSADTRRRAEVLMGAQrenFNR----QHLANQQALGRLST 1398
Cdd:TIGR02168 569 ElgrvtFL-PLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKFDPKLRKALSYL---LGGvlvvDDLDNALELAKKLR 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1399 HTHTL-SLTGvnELV--CG--APGDAPCATspcgGAGCRD---EDGQPRCGGLGcsGAAATADLALGRARHTQAELQ--- 1467
Cdd:TIGR02168 643 PGYRIvTLDG--DLVrpGGviTGGSAKTNS----SILERRreiEELEEKIEELE--EKIAELEKALAELRKELEELEeel 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1468 -----------RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASR----GQVEQANQELRELIQNVKDFlsQEGAD 1532
Cdd:TIGR02168 715 eqlrkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEEL--EAQIE 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1533 PDSIEMVATRvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvqA 1612
Cdd:TIGR02168 793 QLKEELKALR----------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---A 859
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1613 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAG 1692
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-------QLELRLE 932
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1693 SAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRdeargllqaaqDKLQRL--------QELEgtyEE 1764
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----------NKIKELgpvnlaaiEEYE---EL 998
|
650 660
....*....|....*....|....*..
gi 6981142 1765 NEReLEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:TIGR02168 999 KER-YDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
786-834 |
5.04e-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: 67.76 E-value: 5.04e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 834
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1448-1756 |
5.83e-14 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 77.94 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1514
Cdd:NF041483 478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1515 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDA- 1593
Cdd:NF041483 558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADAr 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 ---QRARSRA--EGERQKAE------TVQA-ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQvqERMAGTEQSLNSASE 1661
Cdd:NF041483 600 aeaERIRREAaeETERLRTEaaerirTLQAqAEQEAERLRTEAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQE 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1662 RARQLHALLEALKLK---RAGNSLAAST---------AEETAGSAQS-------RAREAEKQL----REQVGD-QYQTVR 1717
Cdd:NF041483 678 SADRVRAEAAAAAERvgtEAAEALAAAQeeaarrrreAEETLGSARAeadqereRAREQSEELlasaRKRVEEaQAEAQR 757
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 6981142 1718 ALAE---RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ 1756
Cdd:NF041483 758 LVEEadrRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1477-1792 |
1.52e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.96 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQ 1556
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLL-----QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgA 1631
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-Q 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1632 VVDTKNTEQTLQQVQERM------------AGTEQSLNSASERARQLHALLEAL------KLKRAGNSLAASTAEETAGS 1693
Cdd:COG4717 232 LENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1694 AQSRAREAE-KQLREQVG--------------DQYQTVRALAERKAEgvLAAQARAEQLRDEARGLLQAAQ----DKLQR 1754
Cdd:COG4717 312 ALEELEEEElEELLAALGlppdlspeellellDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAGvedeEELRA 389
|
330 340 350
....*....|....*....|....*....|....*...
gi 6981142 1755 LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINL 1792
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1449-1796 |
1.59e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1449 AATADLALGRARHtQAELQRALVEGGGILSRVSETRRQAEEAQQRA---QAALDKANASRGQVEQANQELRELIQNVKDF 1525
Cdd:PRK04863 265 ESTNYVAADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1526 LSQEGAdpdsIEMVATRVLDISIPA-SPEQIQRLASEIAERVRSLA-----DVDTiLAHTMGDVRRAEQLLQdaqrarSR 1599
Cdd:PRK04863 344 LRQQEK----IERYQADLEELEERLeEQNEVVEEADEQQEENEARAeaaeeEVDE-LKSQLADYQQALDVQQ------TR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1600 AeGERQKAetvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlHAllEALKLKRag 1679
Cdd:PRK04863 413 A-IQYQQA---VQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ-FE--QAYQLVR-- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1680 nSLAASTAEETAgsaQSRAREAEKQLREQ--VGDQYQTVRA-LAErkAEGVLAAQARAEQLRDEArglLQAAQDKLQRLQ 1756
Cdd:PRK04863 484 -KIAGEVSRSEA---WDVARELLRRLREQrhLAEQLQQLRMrLSE--LEQRLRQQQRAERLLAEF---CKRLGKNLDDED 554
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 6981142 1757 ELEGTYEENERELEVKAAQLDGLEARmRSVLQAINLQVQI 1796
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQA 593
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1440-1736 |
1.68e-13 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 74.48 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1440 CGGLGCSGAAATADLALGRARHTQAELQRALVEgggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELI 1519
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1520 QNVKD----------FLSQEGADPDSIEMVATrvldisipaspeqiqrlASEIAERVRSLADVDTILAHTMGDVRRAEQL 1589
Cdd:COG3883 79 AEIEErreelgerarALYRSGGSVSYLDVLLG-----------------SESFSDFLDRLSALSKIADADADLLEELKAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1590 LQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlhal 1669
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA---- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1670 lEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQ 1736
Cdd:COG3883 218 -AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1456-1789 |
1.74e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.26 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1456 LGRARHTQAELQRALVEGGGILSRVSETRRQAE-------EAQQRAQ----AALDKANASRGQVEQANQELRELIQNVKD 1524
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYEGyellKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1525 FLSQEGADPDSIEmvatRVLDisipASPEQIQRLASEIAERVRS-LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGE 1603
Cdd:TIGR02169 259 EISELEKRLEEIE----QLLE----ELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1604 RQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL----QQVQERMAGTEQSLNSASERarqlhalLEALKLKRag 1679
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETRDELKDYREK-------LEKLKREI-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1680 NSLAAStaeetagsaQSRAREAEKQLREQVGDqyqtVRALAERKAEGVLAAQARAEQLRDE---ARGLLQAAQDKL---- 1752
Cdd:TIGR02169 402 NELKRE---------LDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEikkQEWKLEQLAADLskye 468
|
330 340 350
....*....|....*....|....*....|....*..
gi 6981142 1753 QRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1789
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1452-1784 |
5.19e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 74.60 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1452 ADLALGRARhtQAELQRALVEGGGILSRVSETRRQAEEAQQ-----RAQAAL-------DKANASRGQVEQANQELRELI 1519
Cdd:COG3096 836 AELAALRQR--RSELERELAQHRAQEQQLRQQLDQLKEQLQllnklLPQANLladetlaDRLEELREELDAAQEAQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1520 QN------VKDFLSQEGADPDSIEMVATRVLDISipASPEQIQRLA---SEIAERVRSLA--DVDTILAHTMGDVRRAEQ 1588
Cdd:COG3096 914 QHgkalaqLEPLVAVLQSDPEQFEQLQADYLQAK--EQQRRLKQQIfalSEVVQRRPHFSyeDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1589 LLQDAQRARSRAegeRQKAETVQAALEEAQRAQGAAQGAIrgavvDTKNteQTLQQVQERMAGTEQSLNS-ASERAR--- 1664
Cdd:COG3096 992 RLEQAEEARREA---REQLRQAQAQYSQYNQVLASLKSSR-----DAKQ--QTLQELEQELEELGVQADAeAEERARirr 1061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1665 -QLHALLEALKLKRagNSLAASTA--EETAGSAQSRAREAEK---QLREQV---GDQYQTVRALA-ERKAEGVLA----A 1730
Cdd:COG3096 1062 dELHEELSQNRSRR--SQLEKQLTrcEAEMDSLQKRLRKAERdykQEREQVvqaKAGWCAVLRLArDNDVERRLHrrelA 1139
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1731 QARAEQLR---DEARGLLQAAQDKLQRLQELEGTYEEN---ERELEVKAAQLDGLEARMR 1784
Cdd:COG3096 1140 YLSADELRsmsDKALGALRLAVADNEHLRDALRLSEDPrrpERKVQFYIAVYQHLRERIR 1199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1458-1791 |
9.20e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1458 RARHTQAELQRALVEGG-GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVkdflsQEGADPDSI 1536
Cdd:COG4717 171 ELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1537 EMVATRVLDISIPASpeqIQRLASEIAERVRSLADVDTI---LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvQAA 1613
Cdd:COG4717 246 KEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLvlgLLALLFLLLAREKASLGKEAEELQALPALEELE--EEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1614 LEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsaseRARQLHALLEALkLKRAGnslaaSTAEETAGS 1693
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAAL-LAEAG-----VEDEEELRA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1694 AQSRAREAEK------QLREQVGDQYQTVRALAERKAEGVLAAQ-ARAEQLRDEARGLLQAAQDKL----QRLQELE--G 1760
Cdd:COG4717 390 ALEQAEEYQElkeeleELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELaeleAELEQLEedG 469
|
330 340 350
....*....|....*....|....*....|....
gi 6981142 1761 TYEENERELEVKAAQLDGLE---ARMRSVLQAIN 1791
Cdd:COG4717 470 ELAELLQELEELKAELRELAeewAALKLALELLE 503
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1455-1789 |
1.00e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.83 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1455 ALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA--------------QAALDKANASRGQVEQANQELREliq 1520
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAeeevdslksqladyQQALDVQQTRAIQYQQAVQALEK--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1521 nvkdflSQE--GADPDSIEMVATRVldisipaspEQIQRLASEIAERVRSLadvdtilahtmgdvrraEQLLQDAQRARS 1598
Cdd:COG3096 425 ------ARAlcGLPDLTPENAEDYL---------AAFRAKEQQATEEVLEL-----------------EQKLSVADAARR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1599 R------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:COG3096 473 QfekayelvckiaGEVERSQAwQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1664 RQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGDQYQTVRAlaerKAEGVLAAQARAEQLRDEARG 1743
Cdd:COG3096 553 EELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQL-EQLRARIKELAA----RAPAWLAAQDALERLREQSGE 620
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 6981142 1744 LLQAAQDKLQRLQELegtyEENERELEVK----AAQLDGLEARMRSVLQA 1789
Cdd:COG3096 621 ALADSQEVTAAMQQL----LEREREATVErdelAARKQALESQIERLSQP 666
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1790 |
1.14e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 73.71 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1446 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1524
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1525 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1591
Cdd:NF041483 984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1592 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1654
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1655 SLNsasERARQLHAllEALKlkRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AA 1730
Cdd:NF041483 1136 ELH---ERARRESA--EQMK--SAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAE 1204
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1731 QARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1790
Cdd:NF041483 1205 QKKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1576-1790 |
1.49e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1576 LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtKNTEQTLQQVQERMAGTEQS 1655
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKL------RELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1656 LNSASERARQLHALLEALKLKRagnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAE 1735
Cdd:COG1196 255 LEELEAELAELEAELEELRLEL-----------EELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1736 QLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1449-1778 |
2.03e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.68 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1449 AATADLALGR-ARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFls 1527
Cdd:PRK04863 332 AASDHLNLVQtALRQQEKIERYQAD-------LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADY-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 QEGadpdsIEMVATRVLdisipaspeQIQRlASEIAERVRSLADVDTILAHTMGD---------------VRRAEQLLQD 1592
Cdd:PRK04863 403 QQA-----LDVQQTRAI---------QYQQ-AVQALERAKQLCGLPDLTADNAEDwleefqakeqeateeLLSLEQKLSV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1593 AQRARSR------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLN 1657
Cdd:PRK04863 468 AQAAHSQfeqayqlvrkiaGEVSRSEAwDVARELLRRLreQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1658 SASERARQLHALLEALKLKRAGNSLAASTAEETagsaqsraREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQL 1737
Cdd:PRK04863 548 KNLDDEDELEQLQEELEARLESLSESVSEARER--------RMALRQQLEQLQARIQRLAARAPA----WLAAQDALARL 615
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6981142 1738 RD-------EARGLLQAAQDKLQRLQELEgtyeENERELEVKAAQLDG 1778
Cdd:PRK04863 616 REqsgeefeDSQDVTEYMQQLLERERELT----VERDELAARKQALDE 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1553-1758 |
3.45e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIAERVRSLADVDTILAhtMGDVRRAEQLLQDAQRARSRAEGERQKAEtvqAALEEAQRAQGAAQGAIRGAV 1632
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLE---AELERLEARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1633 VD-TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGN--SLAA--STAEETAGSAQSRAREAEKQLRE 1707
Cdd:COG4913 330 AQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeEFAAlrAEAAALLEALEEELEALEEALAE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1708 QVGDQYQTVRALAERKAE-GVLAAQ-----ARAEQLRDEARGLLQAAQDKLQRLQEL 1758
Cdd:COG4913 410 AEAALRDLRRELRELEAEiASLERRksnipARLLALRDALAEALGLDEAELPFVGEL 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1450-1779 |
3.88e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1450 ATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALdkaNASRGQVEQANQELRELIQNVKDflsqe 1529
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLAN----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1530 gadpdsiemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLqdaqrarSRAEGERQKAET 1609
Cdd:TIGR02168 314 --------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1610 VQAALEEAQRAQgaaqgaiRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAGNSLAAstaee 1689
Cdd:TIGR02168 373 RLEELEEQLETL-------RSKVAQLELQIASLNNEIERL---EARLERLEDRRERLQQEIEELLKKLEEAELKE----- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1690 tagsAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARglLQAAQDKLQRLQELEGTYEENEREL 1769
Cdd:TIGR02168 438 ----LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ--LQARLDSLERLQENLEGFSEGVKAL 511
|
330
....*....|
gi 6981142 1770 EVKAAQLDGL 1779
Cdd:TIGR02168 512 LKNQSGLSGI 521
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1463-1758 |
7.08e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1463 QAELQRALVEGGGilSRVSETRRQAEEAQQRA----------QAALDKANASRGQVEQANQELRE----------LIQNV 1522
Cdd:PRK04863 363 RLEEQNEVVEEAD--EQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1523 KDFLSQEGADPDSiemVATRVLDIsipaspEQIQRLASEIAER-------VRSLAD-VDTILAHtmgdvRRAEQLLQDA- 1593
Cdd:PRK04863 441 EDWLEEFQAKEQE---ATEELLSL------EQKLSVAQAAHSQfeqayqlVRKIAGeVSRSEAW-----DVARELLRRLr 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 -QRARS-RAEGERQKAETVQAALEEAQRAQGAAQGAIR--GAVVDTKNTEQTLQQVQE-RMAGTEQSLNSASERARQLHA 1668
Cdd:PRK04863 507 eQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlGKNLDDEDELEQLQEELEaRLESLSESVSEARERRMALRQ 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1669 LLEALKLKRAGNslaasTAEETAGSAqsrAREAEKQLREQVGDQY---QTVRALAERKAEGVLAAQ-------ARAEQLR 1738
Cdd:PRK04863 587 QLEQLQARIQRL-----AARAPAWLA---AQDALARLREQSGEEFedsQDVTEYMQQLLERERELTverdelaARKQALD 658
|
330 340
....*....|....*....|
gi 6981142 1739 DEARGLLQAAQDKLQRLQEL 1758
Cdd:PRK04863 659 EEIERLSQPGGSEDPRLNAL 678
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1458-1776 |
1.15e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.24 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1458 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1529
Cdd:NF041483 158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1530 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1607
Cdd:NF041483 234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1608 ETVQAALEEAQRAQGAAQGAIRGAvvdtknTEQTLQQVQERMAGTEqSLNSASERARQlHALLEALKL-KRAGNSLAAST 1686
Cdd:NF041483 287 EAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTVA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1687 AEETAGSAQSRAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDE----ARGLLQAAQD--KLQRLQELE 1759
Cdd:NF041483 359 AEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE-EAERIRReAEAEADRLRGEaadqAEQLKGAAKDdtKEYRAKTVE 437
|
330
....*....|....*..
gi 6981142 1760 gtYEENERELEVKAAQL 1776
Cdd:NF041483 438 --LQEEARRLRGEAEQL 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1584-1798 |
1.32e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1584 RRAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG-------- 1651
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerqleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1652 ------TEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAE 1725
Cdd:TIGR02168 322 eaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1726 GVLA------AQARAEQLRDEARGLLQAAQDklQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1798
Cdd:TIGR02168 402 IERLearlerLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1146-1193 |
1.73e-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: 60.44 E-value: 1.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 6981142 1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1193
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1456-1798 |
1.93e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 68.00 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1456 LGRARhtqAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELreliQNVKDFLSQegadpds 1535
Cdd:COG4372 8 VGKAR---LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL----EQLEEELEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1536 iemvatrvldisipaSPEQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKaetVQAALE 1615
Cdd:COG4372 71 ---------------ARSELEQLEEELEELNEQLQAAQAELA-------QAQEELESLQEEAEELQEELEE---LQKERQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1616 EAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsasERARQLHALLEALKLKRAGNSLaASTAEETAGSAQ 1695
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL----AALEQELQALSEAEAEQALDEL-LKEANRNAEKEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1696 SRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1775
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
330 340
....*....|....*....|...
gi 6981142 1776 LDGLEARMRSVLQAINLQVQIYN 1798
Cdd:COG4372 281 AALELEALEEAALELKLLALLLN 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1549-1782 |
2.17e-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: 69.33 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1549 PASPEQIQRLASEIAERVRSLADVdtilahtMGDVRRAEQLLQDAQRARSRAEgerQKAETVQAALEEAQRAQGAAQGAI 1628
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSL-------QSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1629 RGAVVDTKNTEQTLQQVQERMAGTEQSLnsaSERARQLHALLEALklkragNSLAASTAEETAGSAQSRAREAEKQLREQ 1708
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARI---EELEEDLHKLEEAL------NDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1709 VGdqyqTVRALaERKAEGVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELEGTYEENERELEVKAAQLDGLEAR 1782
Cdd:TIGR02169 811 EA----RLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-565 |
2.18e-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: 2.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6981142 524 PCDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-564 |
2.53e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6981142 525 CDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFR 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1463-1784 |
3.92e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 68.24 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1463 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1521
Cdd:pfam07111 354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1522 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1592
Cdd:pfam07111 434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1593 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1672
Cdd:pfam07111 508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1673 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1736
Cdd:pfam07111 562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 6981142 1737 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1784
Cdd:pfam07111 634 rLQDEARK--EEGQRLARRVQEL-----ERDKNLMLATLQQEGLLSRYK 675
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1464-1788 |
5.93e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.89 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1464 AELQRALVEgggILSRVSETRRQ---AEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGAD-------- 1532
Cdd:pfam01576 218 TDLQEQIAE---LQAQIAELRAQlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqr 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1533 ---PDSIEMVATRVLDI--SIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRR---------AEQLLQdAQRARS 1598
Cdd:pfam01576 295 rdlGEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelTEQLEQ-AKRNKA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1599 RAEGERQKAETVQAAL-EEAQRAQGAAQGAIRGavvdTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL---- 1673
Cdd:pfam01576 374 NLEKAKQALESENAELqAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssll 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1674 -----KLKRAGNSLAASTA----------EET----AGSAQSRAREAEKQ-LREQVGDQYQTVRALaERKAEGVLAAQAR 1733
Cdd:pfam01576 450 neaegKNIKLSKDVSSLESqlqdtqellqEETrqklNLSTRLRQLEDERNsLQEQLEEEEEAKRNV-ERQLSTLQAQLSD 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1734 AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyeenERELEVKAAQLDGLEaRMRSVLQ 1788
Cdd:pfam01576 529 MKKKLEEDAGTLEALEEGKKRLQrELEAL----TQQLEEKAAAYDKLE-KTKNRLQ 579
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1448-1797 |
6.92e-11 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 66.21 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQR----ALVEGGGIlsrvsetRRQAEEAQQRAQAAldkanasrgqVEQANQELRELIQNV- 1522
Cdd:COG1538 17 RAARARVEAARAQLRQARAGLlpsqELDLGGKR-------RARIEAAKAQAEAA----------EADLRAARLDLAAEVa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1523 KDFLSQEGADpdsiemvatRVLDISipaspEQIQRLASEIAERVRSLADVDTIlahTMGDVRRAEQLLQDAQRARSRAEG 1602
Cdd:COG1538 80 QAYFDLLAAQ---------EQLALA-----EENLALAEELLELARARYEAGLA---SRLDVLQAEAQLAQARAQLAQAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1603 ERQKAEtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAserARQLHALLEALKLKRAGN-- 1680
Cdd:COG1538 143 QLAQAR---NALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAA---EAQLEAAEAEIGVARAAFlp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1681 --SLAASTAEE------------------------TAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARA 1734
Cdd:COG1538 217 slSLSASYGYSssddlfsggsdtwsvglslslplfDGGRNRARVRAAKAQLEQAE-AQYEQTVLQALQEVEDALAALRAA 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1735 EQLRDEARGLLQAAQDKLQRLQELegtYEENERE-LEVKAAQLDGLEARMRSV---LQAINLQVQIY 1797
Cdd:COG1538 296 REQLEALEEALEAAEEALELARAR---YRAGLASlLDVLDAQRELLQAQLNLIqarYDYLLALVQLY 359
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
413-470 |
8.45e-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: 58.52 E-value: 8.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 470
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1458-1775 |
1.07e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1458 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE 1537
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1538 mVATRVLDisipASPEQIQRLASEI--AERVRSLADVDTI-LAHTMGDVRRAEQlLQDAQRARsRAEgERQKAETVQAAL 1614
Cdd:PTZ00121 1168 -EARKAED----AKKAEAARKAEEVrkAEELRKAEDARKAeAARKAEEERKAEE-ARKAEDAK-KAE-AVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1615 EEAQRAQgaaqgAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSA 1694
Cdd:PTZ00121 1240 EEAKKAE-----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1695 QsRAREAEKQlREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQ-DKLQRLQELEGTYEENERELEVKA 1773
Cdd:PTZ00121 1315 K-KADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKKAEEKKK 1392
|
..
gi 6981142 1774 AQ 1775
Cdd:PTZ00121 1393 AD 1394
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1098-1146 |
1.11e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.11e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1776 |
1.16e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisiPASPEQIQ 1556
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEE-----------AKKADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLLQDAQRARsRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVD 1634
Cdd:PTZ00121 1451 KKAEEAkkAEEAKKKAE----------EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA---REAEKQLREQVGD 1711
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeeaKKAEEARIEEVMK 1599
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1712 QYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYE--ENERELEVKAAQL 1776
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEE 1666
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1770 |
1.38e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.77 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1446 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1521
Cdd:NF041483 720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1522 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1600
Cdd:NF041483 787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1601 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1670
Cdd:NF041483 843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1671 --EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1748
Cdd:NF041483 923 tsEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002
|
330 340
....*....|....*....|..
gi 6981142 1749 QDKLQRLQelEGTYEENERELE 1770
Cdd:NF041483 1003 AAEAERLR--TEAREEADRTLD 1022
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1145-1194 |
2.15e-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: 57.36 E-value: 2.15e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 1145 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1194
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1448-1789 |
2.25e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQRALVEgggiLSRVSETRRQAEEAQQRAQAALDKANASR-----GQVEQANQELRELIQNV 1522
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRleqleREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1523 KDFlsqegadpdsieMVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEG 1602
Cdd:COG4913 362 ARL------------EALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1603 ER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRGA------------------- 1631
Cdd:COG4913 427 EIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGFaltllvppehyaaalrwvn 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1632 --------------------------------VVDTKN---------------------TEQTLQQV------------- 1645
Cdd:COG4913 507 rlhlrgrlvyervrtglpdperprldpdslagKLDFKPhpfrawleaelgrrfdyvcvdSPEELRRHpraitragqvkgn 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1646 -----------------------------QERMAGTEQSLNSASERARQLHALLEAL-KLKRAGNSLAASTAEET-AGSA 1694
Cdd:COG4913 587 gtrhekddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEALEAELDALqERREALQRLAEYSWDEIdVASA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1695 QSRAREAEKQLR---------EQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTY 1762
Cdd:COG4913 667 EREIAELEAELErldassddlAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
490 500
....*....|....*....|....*..
gi 6981142 1763 EENERELEVKAAQLDGLEARMRSVLQA 1789
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEE 773
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1478-1784 |
2.27e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.13 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1478 SRVSETRRQAEE-AQQRAQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-I 1555
Cdd:COG3096 785 KRLEELRAERDElAEQYAKASFDV------------QKLQRLHQAFSQFVGGH--------------LAVAFAPDPEAeL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 QRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRAQG--AAQGAi 1628
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQEAQAfiQQHGK- 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1629 RGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK--LKR--------AGNSLAASTAE--------ET 1690
Cdd:COG3096 918 ALAQLEPL--VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevVQRrphfsyedAVGLLGENSDLneklrarlEQ 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1691 AGSAQSRAREAEKQLREQVgDQY---------------QTVRALAERKAE-GVLA---AQARAEQLRDEARGLLQAAQdk 1751
Cdd:COG3096 996 AEEARREAREQLRQAQAQY-SQYnqvlaslkssrdakqQTLQELEQELEElGVQAdaeAEERARIRRDELHEELSQNR-- 1072
|
330 340 350
....*....|....*....|....*....|...
gi 6981142 1752 lQRLQELEGTYEENERElevkaaqLDGLEARMR 1784
Cdd:COG3096 1073 -SRRSQLEKQLTRCEAE-------MDSLQKRLR 1097
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1434-1782 |
2.36e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1434 EDGQPRCGGLGCSGAAATADLALGRARHTQAELQRALVEgggilSRVSETRRQAEEAQQRAQAALDKANASRG---QVEQ 1510
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE-----DRDEELRDRLEECRVAAQAHNEEAESLREdadDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1511 ANQELREL-------IQN----VKDFLSQEGADPDSIEMVATRVLDIsiPASPEQIQRLASEIAE---RVRS-LADVDTI 1575
Cdd:PRK02224 357 RAEELREEaaeleseLEEareaVEDRREEIEELEEEIEELRERFGDA--PVDLGNAEDFLEELREerdELRErEAELEAT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1576 LAHTMGDVRRAEQLLQ---------------------DAQRARSRAEGERQKAETVQAALEEA-QRAQGAAQGAIRgavV 1633
Cdd:PRK02224 435 LRTARERVEEAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERlERAEDLVEAEDR---I 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1634 DTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQL-------- 1705
Cdd:PRK02224 512 ERL--EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkerie 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1706 -----------REQVGDQYQTVR----ALAE--------------RKAE--------GVLAAQA---RAEQLRDEARGLL 1745
Cdd:PRK02224 590 slerirtllaaIADAEDEIERLRekreALAElnderrerlaekreRKREleaefdeaRIEEAREdkeRAEEYLEQVEEKL 669
|
410 420 430
....*....|....*....|....*....|....*..
gi 6981142 1746 QAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEAR 1782
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEELEELRERREALENR 706
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1041-1095 |
2.90e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 2.90e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 1095
Cdd:pfam00053 1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1448-1749 |
2.98e-10 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 65.04 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLAlGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDfls 1527
Cdd:COG0840 273 AASAEELA-AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 qegadpdsiemVATRVLDISipASPEQIqrlaSEIaervrsladVDTIlahtmGDVrrAEQ--LLqdaqrarsraegerq 1605
Cdd:COG0840 349 -----------TAETIEELG--ESSQEI----GEI---------VDVI-----DDI--AEQtnLL--------------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1606 kaetvqaALE---EAQRA--QGaaqgaiRG-AVV-D------------TKNTEQTLQQVQERMAGTEQSLNSASERARQL 1666
Cdd:COG0840 381 -------ALNaaiEAARAgeAG------RGfAVVaDevrklaersaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1667 HALLEalklkRAGNSLA--ASTAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEAR 1742
Cdd:COG0840 448 VELVE-----EAGEALEeiVEAVEEVSDLIQEIAAASEEQSAgtEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAE 522
|
....*..
gi 6981142 1743 GLLQAAQ 1749
Cdd:COG0840 523 ELQELVS 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1443-1699 |
3.00e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1443 LGCSGAAATADlalgRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV 1522
Cdd:COG4942 10 LLALAAAAQAD----AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1523 KDFLSQEGADPDSIE----MVATRVLDISIPASPEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRA 1596
Cdd:COG4942 86 AELEKEIAELRAELEaqkeELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1597 RSRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLK 1676
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|...
gi 6981142 1677 ragnslAASTAEETAGSAQSRAR 1699
Cdd:COG4942 236 ------AAAAAERTPAAGFAALK 252
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
834-882 |
3.04e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 3.04e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 882
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1590-1785 |
3.39e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1590 LQDAQRARSRAEGerQKAETVQAALEEAQRAQGAAQGAIRgavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHAL 1669
Cdd:COG4717 51 LEKEADELFKPQG--RKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1670 LEALKLKRAGNSLAASTAEEtagsaQSRAREAEKQLRE--QVGDQYQTVRA-LAERKAEGVLAAQARAEQLRDEARGLLQ 1746
Cdd:COG4717 125 LQLLPLYQELEALEAELAEL-----PERLEELEERLEElrELEEELEELEAeLAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 6981142 1747 AAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1449-1795 |
3.58e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1449 AATADLALGRARHTQAELQRALVEgggilsrvsETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdfLSQ 1528
Cdd:COG4913 271 LAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAELERL---EARLDALREELDELEAQI---RGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1529 EGADPDSIE--------------------MVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQ 1588
Cdd:COG4913 336 GGDRLEQLEreierlereleererrrarlEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1589 LLQDAQRARSRAEGER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRG------ 1630
Cdd:COG4913 413 ALRDLRRELRELEAEIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltll 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1631 ----------AVVDTKNTEQTLQ--------QVQERMAGTEQSL--------NSASERARQL------HALLEALK-LKR 1677
Cdd:COG4913 493 vppehyaaalRWVNRLHLRGRLVyervrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAElgrrfdYVCVDSPEeLRR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1678 AGNSLAAS---------------------------------TAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAER 1722
Cdd:COG4913 573 HPRAITRAgqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEalEAELDALQERREALQR 652
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1723 KAE------GVLAAQARAEQLRDEaRGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG4913 653 LAEyswdeiDVASAEREIAELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1462-1781 |
3.91e-10 |
|
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: 63.93 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1462 TQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGADPDSIEMVAT 1541
Cdd:pfam19220 39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE--AEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1542 RvldisipASPEQIQRLASEIAERVRSLADvdtilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQ 1621
Cdd:pfam19220 117 T-------AQAEALERQLAAETEQNRALEE----------ENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1622 gaaqgairgavvdTKNTEQTLQQVQE---RMAGTEQSLNSASERARQLHAllealklkragnSLAASTAEetagsaqsRA 1698
Cdd:pfam19220 180 -------------QALSEEQAAELAEltrRLAELETQLDATRARLRALEG------------QLAAEQAE--------RE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1699 ReAEKQLREQVGdQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLqaaQDKLQRLQELEGTYEENERELEVKAAQLDG 1778
Cdd:pfam19220 227 R-AEAQLEEAVE-AHRAERASLRMKLEALTARAAATEQLLAEARNQL---RDRDEAIRAAERRLKEASIERDTLERRLAG 301
|
...
gi 6981142 1779 LEA 1781
Cdd:pfam19220 302 LEA 304
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1199-1795 |
4.62e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.99 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1199 DWDRVVQDLAARTRRLeqwAQELQQTGVLGAFESSFLNLQGKLGMVQAiVAARNTSAASTAKLVEATEGLRHEIgktTER 1278
Cdd:TIGR00618 308 QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTL---TQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1279 LTQLEAELTDVQDENFNANHALSGLERD-GLALNLTLRQLDQHLDILkhsnflgaydsirHAHSQSTEAERRANASTFAI 1357
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLA-------------HAKKQQELQQRYAELCAAAI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1358 pSPVSNSADTRRRAEVLMgAQRENFNRQHLANQQALGRLSTHTHTLSLTGVNELvcgapgdapcATSPCggagcrdedgq 1437
Cdd:TIGR00618 448 -TCTAQCEKLEKIHLQES-AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL----------QEEPC----------- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1438 PRCGGLGCSGAAATADLALG-------RARHTQAELQRALV----EGGGILSRVSETRRQAEEAQQRAQAALDKANASRG 1506
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGpltrrmqRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1507 QVEQanqeLRELIQNVKDFLSQEGADPDSIEMVATRVLdisIPASPEQ-IQRLASEIAERVRSLADVDTILAhtmgdvRR 1585
Cdd:TIGR00618 585 DIPN----LQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQdLQDVRLHLQQCSQELALKLTALH------AL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1586 AEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQGAAQGairgavvdtknTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:TIGR00618 652 QLTLTQERVREHALSirVLPKELLASRQLALQKMQSEKEQLTY-----------WKEMLAQCQTLLRELETHIEEYDREF 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1664 RQLHALLEALKLKRAGNSlaaSTAEETAGSAQsraREAEKQLREQVGDQyqtvralaERKAEGVLAAQARaeqlrdearg 1743
Cdd:TIGR00618 721 NEIENASSSLGSDLAARE---DALNQSLKELM---HQARTVLKARTEAH--------FNNNEEVTAALQT---------- 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1744 llqaaqdkLQRLQELEGTYEENERELEVKAAQLDGLEARMR----SVLQAINLQVQ 1795
Cdd:TIGR00618 777 --------GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1458-1792 |
4.65e-10 |
|
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: 65.09 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1458 RARHTQAELQRALvegGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFLSQegadpd 1534
Cdd:TIGR02169 678 RLRERLEGLKREL---SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSS------ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1535 siemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAhtmgDVRR--AEQLLQDAQRARSRAEGERQKAEtvqA 1612
Cdd:TIGR02169 749 ---------LEQEIENVKSELKELEARIEELEEDLHKLEEALN----DLEArlSHSRIPEIQAELSKLEEEVSRIE---A 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1613 ALEEAQRAQGAAQgairgavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG 1692
Cdd:TIGR02169 813 RLREIEQKLNRLT-------LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1693 SAQSRAREAEKQLREQvGDQYQTVRALAERKAEGVLAAQARAEQLRDEarglLQAAQDKLQRLQElegtYEENERELEVK 1772
Cdd:TIGR02169 886 DLKKERDELEAQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEE----IPEEELSLEDV 956
|
330 340
....*....|....*....|
gi 6981142 1773 AAQLDGLEARMRSvLQAINL 1792
Cdd:TIGR02169 957 QAELQRVEEEIRA-LEPVNM 975
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1582-1779 |
4.79e-10 |
|
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: 61.93 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1582 DVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT-------------KNTEQTLQQVQER 1648
Cdd:pfam12795 21 DLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleqrlLQTSAQLQELQNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1649 MAGTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETA-GSAQSRAREAEKQLREQVGDQYQ------TVR-A 1718
Cdd:pfam12795 101 LAQLNSQLIELQTRPERAQQQLSEARqrLQQIRNRLNGPAPPGEPlSEAQRWALQAELAALKAQIDMLEqellsnNNRqD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1719 LAERKAEgvlAAQARAEQLRDEARgLLQAAQDKlQRLQELEGTYEENERELEVKAAQLDGL 1779
Cdd:pfam12795 181 LLKARRD---LLTLRIQRLEQQLQ-ALQELLNE-KRLQEAEQAVAQTEQLAEEAAGDHPLV 236
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1584-1795 |
4.81e-10 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 64.29 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1584 RRAEQLLQdaQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAvvdtkntEQtlQQVQERMAGTEQSLNSASERA 1663
Cdd:COG3064 8 KAAEAAAQ--ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQA-------EE--EAREAKAEAEQRAAELAAEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1664 RQLhalleaLKLKRAGNSLAASTAEETAgsaqSRAREAEKQLREQVGDQYQTVRALAE--RKAEGvlAAQARAEQLRDEA 1741
Cdd:COG3064 77 KKL------AEAEKAAAEAEKKAAAEKA----KAAKEAEAAAAAEKAAAAAEKEKAEEakRKAEE--EAKRKAEEERKAA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981142 1742 RGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG3064 145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1146-1190 |
7.37e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 7.37e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1190
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-523 |
8.45e-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: 55.82 E-value: 8.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6981142 472 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1788 |
8.47e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFL--SQEGADPDSIEMVATRvldisipAS 1551
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEAeaAEEKAEAAEKKKEEAK-------KK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1552 PEQIQRLASEI--AERVRSLADVDTILAHtmgDVRRAEQLLQDAQRARSRAEgERQKAETVQAALEEAQRAQGAAQGAir 1629
Cdd:PTZ00121 1380 ADAAKKKAEEKkkADEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKA-- 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1630 gavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSL-----AASTAEETAGSAQSR----ARE 1700
Cdd:PTZ00121 1454 ----EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaaeAKKKADEAKKAEEAKkadeAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1701 AEKQLREQVGDQYQTVRALAE-RKAEGVLAAQA--------RAEQLRDEA-RGLLQAAQDKLQRLQELEGTYEEN----- 1765
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADElKKAEELKKAEEkkkaeeakKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEEkkmka 1609
|
330 340
....*....|....*....|....*...
gi 6981142 1766 -----ERELEVKAAQLDGLEARMRSVLQ 1788
Cdd:PTZ00121 1610 eeakkAEEAKIKAEELKKAEEEKKKVEQ 1637
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1040-1096 |
8.87e-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: 55.82 E-value: 8.87e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1040 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 1096
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1454-1775 |
1.16e-09 |
|
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: 62.99 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1454 LALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEQANQELRELIQNVKDFLSQEGADP 1533
Cdd:pfam07888 24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD-------REQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARsRAEGERQKAET---- 1609
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK-KAGAQRKEEEAerkq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRagNSLAAS--TA 1687
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ--ERLNASerKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1688 E------ETAGSAQSRAREAEKQLREQVGDqyqtvraLAERKAEGVLAAQARAEQLRDEARGLLQAAQ---DKLQRL--- 1755
Cdd:pfam07888 254 EglgeelSSMAAQRDRTQAELHQARLQAAQ-------LTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLsae 326
|
330 340
....*....|....*....|....
gi 6981142 1756 -QELEGTYEEN--ERE-LEVKAAQ 1775
Cdd:pfam07888 327 lQRLEERLQEErmEREkLEVELGR 350
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
473-527 |
1.20e-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: 55.44 E-value: 1.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1479-1772 |
1.22e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisipaspeqiQRL 1558
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE------------------ARK 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1559 ASEI--AERVRSLADvdtilAHTMGDVRRAEQLLQDAQRARS------RAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1630
Cdd:PTZ00121 1280 ADELkkAEEKKKADE-----AKKAEEKKKADEAKKKAEEAKKadeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1631 AVVDTKNTEQTLQQVQERmagTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE-ETAGSAQSRAREAEKQLREQV 1709
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1710 GDQYQTVRALAERKAEgvlAAQARAEQLRdEARGLLQAAQDKlQRLQELEGTYEENERELEVK 1772
Cdd:PTZ00121 1432 KADEAKKKAEEAKKAD---EAKKKAEEAK-KAEEAKKKAEEA-KKADEAKKKAEEAKKADEAK 1489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1553-1791 |
1.29e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIAERVRS------------LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEaqra 1620
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKdlherlngleseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1621 qgaaqgairgavvdtknteqtlqqVQERMAGTEQSLNSASERARQLHALLEALKLKRAGnSLAASTAEETAGSAQSRARE 1700
Cdd:PRK02224 263 ------------------------LRETIAETEREREELAEEVRDLRERLEELEEERDD-LLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1701 AEKQLREQVGDQYQTVRALAERKAEgvlaaqaRAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLE 1780
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNE-------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
250
....*....|.
gi 6981142 1781 ARMRSVLQAIN 1791
Cdd:PRK02224 391 EEIEELRERFG 401
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1447-1796 |
1.38e-09 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 63.00 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1447 GAAATADLALGRARHTQAELQRALVegggILSRVSETRRQAEEAQ--QRA------QAALDKANASRGQVEQANQELREL 1518
Cdd:COG5278 23 VLGVLSYLSLNRLREASEWVEHTYE----VLRALEELLSALLDAEtgQRGylltgdESFLEPYEEARAEIDELLAELRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1519 IQNvkdflsqegadpdsiemvatrvldisipaSPEQIQRLAS--EIAERVRSLADvDTILAHTMGDVRRAEQLLQ----- 1591
Cdd:COG5278 99 TAD-----------------------------NPEQQARLDEleALIDQWLAELE-QVIALRRAGGLEAALALVRsgegk 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1592 ---DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1668
Cdd:COG5278 149 almDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1669 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1748
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6981142 1749 QDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1455-1789 |
1.70e-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: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1455 ALGRARHTQA-ELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQV--------------EQANQELRELI 1519
Cdd:pfam01576 629 AEAREKETRAlSLARALEE-------ALEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskralEQQVEEMKTQL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1520 QNVKDFLsQEGADpdsiemvATRVLDISIPASPEQIQRLAS---EIAE-RVRSLADvdtilahtmgDVRRAEQLLQDAQR 1595
Cdd:pfam01576 702 EELEDEL-QATED-------AKLRLEVNMQALKAQFERDLQardEQGEeKRRQLVK----------QVRELEAELEDERK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1596 ARSRAEGERQKAET-------------------------VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQ------- 1643
Cdd:pfam01576 764 QRAQAVAAKKKLELdlkeleaqidaankgreeavkqlkkLQAQMKDLQRELEEARASRDEILAQSKESEKKLKnleaell 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1644 QVQERMAgteqslnsASERARQlHALLEALKLKragNSLAASTAEETAGSAQSRAREAE-KQLREQVGDQYQTVRALAER 1722
Cdd:pfam01576 844 QLQEDLA--------ASERARR-QAQQERDELA---DEIASGASGKSALQDEKRRLEARiAQLEEELEEEQSNTELLNDR 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1723 KAEGV---------LAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGT----YEENERELEVKAAQL-DGLEARMRSVL 1787
Cdd:pfam01576 912 LRKSTlqveqltteLAAERSTSQKSESARQQLERQNKELKaKLQEMEGTvkskFKSSIAALEAKIAQLeEQLEQESRERQ 991
|
..
gi 6981142 1788 QA 1789
Cdd:pfam01576 992 AA 993
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1556-1778 |
1.81e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.92 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1618
Cdd:NF041483 130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1619 RAQGAAQGAIRGAVVDTknteqtlqqvqERMagteqsLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSR 1697
Cdd:NF041483 204 SARAEAEAILRRARKDA-----------ERL------LNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1698 AREAEKQLREqvgdqyqtvralaerkaegvlaAQARAEQLRDEARgllQAAQdklQRLQELEGTYEENERELEVKAAQLD 1777
Cdd:NF041483 267 MQEAEEALRE----------------------ARAEAEKVVAEAK---EAAA---KQLASAESANEQRTRTAKEEIARLV 318
|
.
gi 6981142 1778 G 1778
Cdd:NF041483 319 G 319
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1584-1792 |
2.01e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1584 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1664 RQLHALLEAL--KLKRAGNS------LAASTAEETAGSAQ-----SRAREAE-KQLREQVGDQYQTVRALAERKAE---- 1725
Cdd:COG4942 100 EAQKEELAELlrALYRLGRQpplallLSPEDFLDAVRRLQylkylAPARREQaEELRADLAELAALRAELEAERAEleal 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1726 --GVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELegtyEENERELEVKAAQLDGLEARMRSVLQAINL 1792
Cdd:COG4942 180 laELEEERAALEALKAERQKLLARLEKELaelaAELAEL----QQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
412-471 |
2.25e-09 |
|
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: 54.67 E-value: 2.25e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 471
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1200-1755 |
2.39e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1200 WDRVVQDLAARTRRLEQWAQELQQTgvlgafESSFLNLQGKLGMVQAIVAARntsaastaKLVEATEGLRHEIGKTTERL 1279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEEL------EAELEELREELEKLEKLLQLL--------PLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1280 TQLEAELTDVQDenfnanhalsgLERDGLALNLTLRQLDQHLDILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAIps 1359
Cdd:COG4717 149 EELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1360 pvsnsADTRRRAEVLMgAQRENFNRQHLAnQQALGRLSTHTHTLSLTGVnelvcgapgdapcatspcggagcrdedgqpR 1439
Cdd:COG4717 216 -----EEAQEELEELE-EELEQLENELEA-AALEERLKEARLLLLIAAA------------------------------L 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1440 CGGLGCSGAAATADLALGRArhtqaelqrALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasrgqveqANQELREli 1519
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGV---------LFLVLGLLALLFLLLAREKASLGKEAEELQALP---------ALEELEE-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1520 QNVKDFLSQEGADPD-SIEMVATRVLDIsipaspEQIQRLASEIAERVRSL------ADVDTILAHtmGDVRRAEQLLQD 1592
Cdd:COG4717 319 EELEELLAALGLPPDlSPEELLELLDRI------EELQELLREAEELEEELqleeleQEIAALLAE--AGVEDEEELRAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1593 AQRARSRAEgERQKAETVQAALEEAQRAQGAAQgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEA 1672
Cdd:COG4717 391 LEQAEEYQE-LKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1673 LklkragnslaastaeETAGSAqSRAREAEKQLREQvgdqyqtVRALAERKAEGVLAAQArAEQLRDEAR-----GLLQA 1747
Cdd:COG4717 465 L---------------EEDGEL-AELLQELEELKAE-------LRELAEEWAALKLALEL-LEEAREEYReerlpPVLER 520
|
....*...
gi 6981142 1748 AQDKLQRL 1755
Cdd:COG4717 521 ASEYFSRL 528
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
525-564 |
2.40e-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: 54.67 E-value: 2.40e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6981142 525 CDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFR 564
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1732-1801 |
2.80e-09 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 55.14 E-value: 2.80e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1732 ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1098-1143 |
3.67e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 3.67e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1143
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1553-1791 |
3.70e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.11 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIA---ERVRSLADVDTILAHTMGDV----RRAEQLLQDAQRARSRAEGE---------------------- 1603
Cdd:pfam01576 159 ERISEFTSNLAeeeEKAKSLSKLKNKHEAMISDLeerlKKEEKGRQELEKAKRKLEGEstdlqeqiaelqaqiaelraql 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1604 RQKAETVQAAL---EEAQRAQGAAQGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK--LKRA 1678
Cdd:pfam01576 239 AKKEEELQAALarlEEETAQKNNALKKIREL-------EAQISELQEDLESERAARNKAEKQRRDLGEELEALKteLEDT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1679 GNSLAAS----TAEETAGSAQSRAREAEKQLRE-QVGD----QYQTVRALAE-----RKAEGVL--AAQA----RAEqLR 1738
Cdd:pfam01576 312 LDTTAAQqelrSKREQEVTELKKALEEETRSHEaQLQEmrqkHTQALEELTEqleqaKRNKANLekAKQAleseNAE-LQ 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1739 DEARGLLQAAQDKLQR-------LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:pfam01576 391 AELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1097-1144 |
4.21e-09 |
|
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: 53.90 E-value: 4.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 1097 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1144
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1553-1769 |
5.26e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIAERVRSLADVDTILA------HTMGDVRRAEQLLQD----------AQRARSRAEGERQKAE-------T 1609
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEaleaelDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDassddlaA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ-LHALLEALKlkragnslaastae 1688
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERF-------------- 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1689 etagsAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARA-EQLRDEARGL---LQAAQDKLQRLQELEGT--- 1761
Cdd:COG4913 756 -----AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLdadLESLPEYLALLDRLEEDglp 830
|
....*....
gi 6981142 1762 -YEENEREL 1769
Cdd:COG4913 831 eYEERFKEL 839
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1592-1757 |
7.98e-09 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 56.80 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1592 DAQRARSRAEGERQKAETVQAALEeaqrAQGAAQGAIRG--AVVD-----TKNTEQTLQQVQERMAGTEQSLNSASERAR 1664
Cdd:pfam05335 22 DAQAAAAEAAARQVKNQLADKALQ----AAKAAEAALAGkqQIVEqleqeLREAEAVVQEESASLQQSQANANAAQRAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1665 QLHALLEALKlkragNSLAAstAEETAGSAQSRAREAEKQLREQvgdqyqtvRALAErkaegvlAAQARAEQLRDEargl 1744
Cdd:pfam05335 98 QAQQQLEALT-----AALKA--AQANLENAEQVAAGAQQELAEK--------TQLLE-------AAKKRVERLQRQ---- 151
|
170
....*....|...
gi 6981142 1745 LQAAQDKLQRLQE 1757
Cdd:pfam05335 152 LAEARADLEKTKK 164
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1041-1095 |
8.26e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 8.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 1095
Cdd:smart00180 1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
989-1031 |
1.22e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 1.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1550-1777 |
1.55e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.24 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1550 ASPEQIQRLaseiaervRSLADVDTILAHTMgdvRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgair 1629
Cdd:COG1579 1 AMPEDLRAL--------LDLQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1630 gavvdtKNTEQTLQQVQERMAGTEQSLNSASErARQLHAL---LEALKLKRAgnslaastaeetagsaqsrarEAEKQLR 1706
Cdd:COG1579 62 ------KRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRIS---------------------DLEDEIL 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1707 EqvgdqyqtvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLD 1777
Cdd:COG1579 114 E------------LMERIEELEEELAELEAELAELEAELEEKKAELDeELAELEAELEELEAEREELAAKIP 173
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1477-1797 |
2.59e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 58.51 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELRELIQNVKdflsqegadpdsiemvatrvldisipasPEQIQ 1556
Cdd:COG3064 18 LEQAEAEKRAAAEAEQKAKE---EAEEERLAELEAKRQAEEEAREAK----------------------------AEAEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEIAERVRSLADvdtilahtmgdvrrAEQLLQDAQRarsRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdTK 1636
Cdd:COG3064 67 RAAELAAEAAKKLAE--------------AEKAAAEAEK---KAAAEKAKAAKEAEAAAAAEKAAAAAE---------KE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1637 NTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG--SAQSRAREAEKQLREQVGDQYQ 1714
Cdd:COG3064 121 KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAgaAAALVAAAAAAVEAADTAAAAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1715 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQV 1794
Cdd:COG3064 201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
...
gi 6981142 1795 QIY 1797
Cdd:COG3064 281 VAA 283
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1555-1777 |
2.84e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1555 IQRLASEIAERVRSLADVDTILahtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG--AV 1632
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1633 VDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaasTAEETAGSAQSRAREAEKQLREQvgdQ 1712
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-----------ELEAELAELQEELEELLEQLSLA---T 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1713 YQTVRALAERKAEgvlaAQARAEQLRDEarglLQAAQDKLQRLQElEGTYEENERELEVKAAQLD 1777
Cdd:COG4717 191 EEELQDLAEELEE----LQQRLAELEEE----LEEAQEELEELEE-ELEQLENELEAAALEERLK 246
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1485-1743 |
3.10e-08 |
|
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: 56.54 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNvkdfLSQEGADPDSiemvatrvldisipASPEQIQRLaseiae 1564
Cdd:pfam12795 23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAEA--------------APKEILASL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1565 rvrSLADVDTILAHTMGDVRRAEQLLQDAQrarSRAEGERQKAETVQAALEEAQRaqgaAQGAIRGAVVDTKNTEQTLQQ 1644
Cdd:pfam12795 79 ---SLEELEQRLLQTSAQLQELQNQLAQLN---SQLIELQTRPERAQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1645 VQERMAGTEQSLnsaserarqLHALLEALKLKRAGNS----LAASTAEETAgsAQSRAREAEKQ-LREQVGDQYQtvrAL 1719
Cdd:pfam12795 149 AQRWALQAELAA---------LKAQIDMLEQELLSNNnrqdLLKARRDLLT--LRIQRLEQQLQaLQELLNEKRL---QE 214
|
250 260
....*....|....*....|....
gi 6981142 1720 AERkaegvlaAQARAEQLRDEARG 1743
Cdd:pfam12795 215 AEQ-------AVAQTEQLAEEAAG 231
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
833-875 |
3.35e-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: 51.20 E-value: 3.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 833 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1791 |
3.63e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1591 QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALL 1670
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1671 EALKLKRAgnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQD 1750
Cdd:COG4942 100 EAQKEELA----------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6981142 1751 KLQRLQELEGTYEENERELevkaAQLDGLEARMRSVLQAIN 1791
Cdd:COG4942 169 LEAERAELEALLAELEEER----AALEALKAERQKLLARLE 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1592-1790 |
3.77e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1592 DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLhalle 1671
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1672 ALKLKRAGNS-------LAASTAEETAGSAQSRAREAEKQlREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEargl 1744
Cdd:COG3883 92 ARALYRSGGSvsyldvlLGSESFSDFLDRLSALSKIADAD-ADLLEELKADKAELEAKKAE-LEAKLAELEALKAE---- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981142 1745 LQAAQDKLQRLQElegtyeenereleVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3883 166 LEAAKAELEAQQA-------------EQEALLAQLSAEEAAAEAQL 198
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1627-1786 |
3.77e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1627 AIRGAVVDTKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnslaastaEETAGSAQSRAREAEKQLR 1706
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1707 EqvgdqyqtvraLAERKAEgvlaAQARAEQLRDEARGLLQA-AQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:COG4913 306 R-----------LEAELER----LEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
.
gi 6981142 1786 V 1786
Cdd:COG4913 371 L 371
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1555-1756 |
3.81e-08 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 57.05 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1555 IQRLASEIAERVR---SLADVDTILAHTMGDVRRAEqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGA 1631
Cdd:pfam00529 31 VTRVLVKEGDRVKagdVLFQLDPTDYQAALDSAEAQ--LAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1632 VVDTKNTEQTLQQVQERMAGTEqslNSASERARQLHALLEalklkrAGNSLAastaeetagSAQSRAREAEKQLREQVGD 1711
Cdd:pfam00529 109 QAAVKAAQAQLAQAQIDLARRR---VLAPIGGISRESLVT------AGALVA---------QAQANLLATVAQLDQIYVQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981142 1712 QYQTVRALAERKAEGVLAAQARAEQLRDEarglLQAAQDKLQRLQ 1756
Cdd:pfam00529 171 ITQSAAENQAEVRSELSGAQLQIAEAEAE----LKLAKLDLERTE 211
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1486-1758 |
3.84e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 58.53 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1486 QAE--EAQQRAQAALDKANASRGQVEQANQ---ELRELIQNVKDFLSQEGADPDSIEmvatrvLDISIPASPEQIQRLAS 1560
Cdd:PRK10929 43 QAEivEALQSALNWLEERKGSLERAKQYQQvidNFPKLSAELRQQLNNERDEPRSVP------PNMSTDALEQEILQVSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1561 EIAE----------RVRSLADVDTILAhtmgdvrraeQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1630
Cdd:PRK10929 117 QLLEksrqaqqeqdRAREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1631 AVVDtkntEQTLQQV-----QE--RMagteqSLNSASERARQLHALLEALKlkragNSLAASTAEETagsaqSRAREAEK 1703
Cdd:PRK10929 187 ALVD----ELELAQLsannrQElaRL-----RSELAKKRSQQLDAYLQALR-----NQLNSQRQREA-----ERALESTE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1704 QLREQVGD-------QYQTVRALAErkaegVLAAQA-RAEQLRDEARgllQAAQDKLQRLQEL 1758
Cdd:PRK10929 248 LLAEQSGDlpksivaQFKINRELSQ-----ALNQQAqRMDLIASQQR---QAASQTLQVRQAL 302
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1554-1770 |
4.81e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1627
Cdd:NF041483 44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1628 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRArEAEK---Q 1704
Cdd:NF041483 121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARA-EAERlaeE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1705 LREQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQEL 1758
Cdd:NF041483 194 ARQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEA 270
|
250
....*....|..
gi 6981142 1759 EGTYEENERELE 1770
Cdd:NF041483 271 EEALREARAEAE 282
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1789 |
5.06e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1459 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1533
Cdd:NF041483 252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1598
Cdd:NF041483 326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1599 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1650
Cdd:NF041483 401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1651 GTEQSLNSA--------------SERARQlHALLEALKLKRagnslaasTAEETAgsaqSRAREAEKQLREQVGDQYQTV 1716
Cdd:NF041483 481 TAEELLTKAkadadelrstataeSERVRT-EAIERATTLRR--------QAEETL----ERTRAEAERLRAEAEEQAEEV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1717 RALAERKA-----EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSv 1786
Cdd:NF041483 548 RAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT- 626
|
...
gi 6981142 1787 LQA 1789
Cdd:NF041483 627 LQA 629
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1455-1684 |
5.16e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.22 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1455 ALGRARHTQAEL--QRALVEgggilSRVSETRRQAEEAQQRAQAALDKANasrgqveqanqelreliqnvkdflsqegad 1532
Cdd:COG1842 38 DLVEARQALAQViaNQKRLE-----RQLEELEAEAEKWEEKARLALEKGR------------------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1533 pdsiEMVATRVLdisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKAETVqA 1612
Cdd:COG1842 83 ----EDLAREAL--------ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEL----------KAKKDTL-K 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1613 ALEEAQRAQGAAQGAIRGavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRAGNS-LAA 1684
Cdd:COG1842 140 ARAKAAKAQEKVNEALSG--IDSDDATSALERMEEKIEEMEARAEAAAELAAGdsLDDELAELEADSEVEDeLAA 212
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1582-1788 |
5.34e-08 |
|
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: 56.78 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1582 DVRRAEQLLQDAQRARSRAEGERQKAETV-QAALEEAQRAQGAAQGAirgavvdtknTEQTLQQVQERMAGTEQSLNSAS 1660
Cdd:TIGR02794 61 PAAKKEQERQKKLEQQAEEAEKQRAAEQArQKELEQRAAAEKAAKQA----------EQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1661 ERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQyqtvrALAERKAEGVlAAQARAEQLRDE 1740
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK-----AEAEAKAKAE-EAKAKAEAAKAK 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981142 1741 ARgllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ 1788
Cdd:TIGR02794 205 AA---AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
834-875 |
5.42e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 5.42e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6981142 834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1543-1775 |
6.76e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1543 VLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQG 1622
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1623 AAQGAIRGAVVDTKNTEQTLQQVQERMAGTE--------QSLNSASERARQLHALLEALKlkRAGNSLAASTAEETAgsA 1694
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARR--EQAEELRADLAELAA--L 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1695 QSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAA 1774
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAE----RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
.
gi 6981142 1775 Q 1775
Cdd:COG4942 242 R 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1488-1790 |
7.84e-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: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1488 EEAQQRAQAALDKANASRGQVEQANQELRELIQNVkDFLSQEGADPDSIEMVATRVLDI-------SIPASPEQIQRLAS 1560
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYegyellkEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1561 EIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQrARSRAEGERQKAEtVQAALEEAQRAQGAAQGAIRGAvvdtkntEQ 1640
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEK-------ER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1641 TLQQVQERMAGTEQSLNSASERARQLhallealklkragnslaastaeetagsaqSRAREAEKQLREQVGDQY---QTVR 1717
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEEL-----------------------------EREIEEERKRRDKLTEEYaelKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1718 ALAERKAEGVLAAQARA-----------EQLRDEaRGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETrdelkdyreklEKLKRE-INELKRELDRLQeELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
....*
gi 6981142 1786 VLQAI 1790
Cdd:TIGR02169 446 KALEI 450
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
413-470 |
8.67e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 8.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 470
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1446-1786 |
8.91e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1446 SGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASrgqveqanqelrELIQNVKDF 1525
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP------------ECGQPVEGS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1526 LSQEGADPD--SIEMVATRVLDISipaspEQIQRLASEIaERVRSLADVDTILAHTMGDVRRAEQLLQD----AQRARSR 1599
Cdd:PRK02224 465 PHVETIEEDreRVEELEAELEDLE-----EEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAErretIEEKRER 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1600 AEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERArQLHALLEALKLKRAG 1679
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1680 -------------------NSLAASTAEETAGSAQSRAREAEKQLrEQVGDQyqtVRALAERKAE------GVLAAQARA 1734
Cdd:PRK02224 618 laelnderrerlaekrerkRELEAEFDEARIEEAREDKERAEEYL-EQVEEK---LDELREERDDlqaeigAVENELEEL 693
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1735 EQLRDEarglLQAAQDKLQRLQELegtYEENErELEVKAAQLDGlEARMRSV 1786
Cdd:PRK02224 694 EELRER----REALENRVEALEAL---YDEAE-ELESMYGDLRA-ELRQRNV 736
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
989-1035 |
9.11e-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: 50.05 E-value: 9.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6981142 989 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 1035
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-516 |
9.95e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.95e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 6981142 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 516
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1585-1785 |
1.51e-07 |
|
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: 54.26 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1585 RAEQLLQDAQRARSRAEGERQKAETVQAAL--------EEAQRAQG--------------AAQGAIRGavvdTKNTEQTL 1642
Cdd:pfam00261 12 EAEERLKEAMKKLEEAEKRAEKAEAEVAALnrriqlleEELERTEErlaealekleeaekAADESERG----RKVLENRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1643 QQVQERMAGTEQSLNSASERARQLHALLE--ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLReQVGDQYQTVRALA 1720
Cdd:pfam00261 88 LKDEEKMEILEAQLKEAKEIAEEADRKYEevARKLVVVEGDL--ERAEERAELAESKIVELEEELK-VVGNNLKSLEASE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1721 ErkaegvlAAQARAEQLRDEARgLLQAaqdklqRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:pfam00261 165 E-------KASEREDKYEEQIR-FLTE------KLKEAETRAEFAERSVQKLEKEVDRLEDELEA 215
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1452-1781 |
2.83e-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: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1452 ADLALGRARHTQAELQRALVEG--GGILSRVSETRRQAEEAQQR---AQAALDKANASRGQVEQAN-------------- 1512
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEGqlQELQARLSESERQRAELAEKlskLQSELESVSSLLNEAEGKNiklskdvsslesql 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1513 QELRELIQ-------NVKDFLSQEGADPDSI------EMVATRVLDisipaspEQIQRLASEIAERVRSLADVDTILaht 1579
Cdd:pfam01576 471 QDTQELLQeetrqklNLSTRLRQLEDERNSLqeqleeEEEAKRNVE-------RQLSTLQAQLSDMKKKLEEDAGTL--- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1580 mgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQ---TLQQVQ---ERMAGTE 1653
Cdd:pfam01576 541 -------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsNLEKKQkkfDQMLAEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1654 QSLNS--ASERARQlhallEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQY-------QTVRAL--AER 1722
Cdd:pfam01576 614 KAISAryAEERDRA-----EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHELerSKR 688
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981142 1723 KAEGVLAA-QARAEQLRDEarglLQAAQDKLQRLQ------------ELEGTYEENE--RELEVKaaQLDGLEA 1781
Cdd:pfam01576 689 ALEQQVEEmKTQLEELEDE----LQATEDAKLRLEvnmqalkaqferDLQARDEQGEekRRQLVK--QVRELEA 756
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1514-1796 |
3.46e-07 |
|
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: 55.61 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1514 ELRELIQNVKDFLSQEGADpdsIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGD---------VR 1584
Cdd:pfam12128 143 EYRSIIQNDRTLLGRERVE---LRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDdgvvppksrLN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1585 RAE--------QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSL 1656
Cdd:pfam12128 220 RQQvehwirdiQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1657 NSASERARQ-LHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARAE 1735
Cdd:pfam12128 300 KEKRDELNGeLSAADAAVAKDRS----ELEALEDQHGAFLDADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVT 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1736 QLRDEARGLL-QAAQDKLQRL-QELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:pfam12128 375 AKYNRRRSKIkEQNNRDIAGIkDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNE 437
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1464-1776 |
3.52e-07 |
|
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: 55.61 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1464 AELQRALVEGGGILSRVSETRRQaeEAQQRAQAALDKANAS-RGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATR 1542
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1543 VLDISIP---ASPEQIQRLASEIAERVRSLAdvdtILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETvqaaleEAQR 1619
Cdd:pfam12128 334 FLDADIEtaaADQEQLPSWQSELENLEERLK----ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL------AKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1620 aqgaaQGAIRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKragnsLAASTAEETAGSAQSRAR 1699
Cdd:pfam12128 404 -----EARDRQLAVAEDDLQALESELREQL---EAGKLEFNEEEYRLKSRLGELKLR-----LNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1700 EAEKQLREQVGDQYQTVRALAErkaegvlaAQARAEQLRDEArglLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1776
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQS--------ELRQARKRRDQA---SEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1534-1791 |
3.74e-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: 55.36 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEMVATRVLDIS------IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDA-------------- 1593
Cdd:TIGR00618 176 DQYTQLALMEFAKKkslhgkAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShayltqkreaqeeq 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 ---QRARSRAEGERQKAETVQAALEEAQRA-----QGAAQGAIRGAVVDT-KNTEQTLQQVQERMA-------------- 1650
Cdd:TIGR00618 256 lkkQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIeQQAQRIHTELQSKMRsrakllmkraahvk 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1651 ---------GTEQSLNSASERAR--------------QLHALLEALK--------LKRAGNSLAASTAEETAGSAQSRAR 1699
Cdd:TIGR00618 336 qqssieeqrRLLQTLHSQEIHIRdahevatsireiscQQHTLTQHIHtlqqqkttLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1700 --------------EAEKQLREQVGDQYQ-----TVRALAERKAEGVLAAQA---RAEQLRDEARGLLQAAQDK------ 1751
Cdd:TIGR00618 416 tsafrdlqgqlahaKKQQELQQRYAELCAaaitcTAQCEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKavvlar 495
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 6981142 1752 LQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:TIGR00618 496 LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
880-927 |
3.91e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 3.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6981142 880 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 927
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1484-1735 |
3.99e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.60 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1484 RRQAEEAQQRAQAALdkanASRGQVEQANQELreliQNVKDFLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIA 1563
Cdd:PRK07735 12 KEAARRAKEEARKRL----VAKHGAEISKLEE----ENREKEKALPKNDDMTIE---------------EAKRRAAAAAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1564 ERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-EGERQKAETVQAALEE--AQRAQGAAQGAIRGAVVDTKNTEQ 1640
Cdd:PRK07735 69 AKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAaALAKQKREGTEEVTEEekAAAKAKAAAAAKAKAAALAKQKRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1641 TLQQVQERMAGTEQSL--NSASERARQLHALLEALKLKRAGNSLAASTAEE-------TAGSAQSRAREAEKQLREQV-- 1709
Cdd:PRK07735 149 GTEEVTEEEEETDKEKakAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEkakakakAAAAAKAKAAALAKQKASQGng 228
|
250 260
....*....|....*....|....*...
gi 6981142 1710 --GDQYQTVRALAERKAEGVLAAQARAE 1735
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1590-1750 |
4.09e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1590 LQDAQRARSRAEGERQKAETVQAalEEAQRAQGAAQgairgavvdtknteQTLQQV-QERMAGTEQslNSASERARQLHA 1668
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQA--EELQQKQAAEQ--------------ERLKQLeKERLAAQEQ--KKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1669 L----LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARAE-QLRDEARG 1743
Cdd:PRK09510 129 LkqkqAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA-EAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEA 207
|
....*..
gi 6981142 1744 LLQAAQD 1750
Cdd:PRK09510 208 KKKAAAE 214
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1534-1721 |
4.40e-07 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 51.88 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEMVATRVLDISipaspEQIQRLASEIAERV-RSLADVDTILAHTMGDVR-RAEQLLQDAQrarsraegerqkaETVQ 1611
Cdd:pfam01442 4 DSLDELSTYAEELQ-----EQLGPVAQELVDRLeKETEALRERLQKDLEEVRaKLEPYLEELQ-------------AKLG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1612 AALEEAQRAQGAAQGAIRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASERAR-QLHALLEALKLK-----RAGNSLAAS 1685
Cdd:pfam01442 66 QNVEELRQRLEPYTEELRKRL--NADAEELQEKLAPYGEELRERLEQNVDALRaRLAPYAEELRQKlaerlEELKESLAP 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 6981142 1686 TAEEtagsAQSRAREAEKQLREQVGDQYQTVRALAE 1721
Cdd:pfam01442 144 YAEE----VQAQLSQRLQELREKLEPQAEDLREKLD 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1636-1796 |
4.44e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAA-----STAEETAGSAQSRAREAEKQLREQ 1708
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerRIAALARRIRAleqelAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1709 VGDQYQTVRALAER----------KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDG 1778
Cdd:COG4942 103 KEELAELLRALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170
....*....|....*...
gi 6981142 1779 LEARMRSVLQAINLQVQI 1796
Cdd:COG4942 183 LEEERAALEALKAERQKL 200
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1479-1775 |
5.11e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1479 RVSETRRQAEEA---QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVAtrvldisipaspEQI 1555
Cdd:PTZ00121 1558 KKAEEKKKAEEAkkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------------EEL 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 QRlaseiAERVRSlaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGaaqgairgavvDT 1635
Cdd:PTZ00121 1626 KK-----AEEEKK--KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-----------DE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSA-QSRAREAEKQLREQVGDQYQ 1714
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1715 TVRALAERKAEGVLAAQARAE--QLRDEARGLLQAAQDKLQRLQE--LEGT-YEENERELEVKAAQ 1775
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIEggKEGNlVINDSKEMEDSAIK 1833
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
879-924 |
5.64e-07 |
|
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: 47.73 E-value: 5.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6981142 879 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 924
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1733-1800 |
7.45e-07 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 48.12 E-value: 7.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1733 RAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1477-1790 |
9.80e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQ-ANQELRELiqnvkDFLSQEGADPDSiemvatrvldisipaspEQI 1555
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERmAMEREREL-----ERIRQEERKREL-----------------ERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 --QRLASEIaERVRSLADVDtilahtMGDVRRAEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQgaaQGAIRGa 1631
Cdd:pfam17380 366 rqEEIAMEI-SRMRELERLQ------MERQQKNERVRQELEAARKVKilEEERQRKIQQQKVEMEQIRAE---QEEARQ- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1632 vVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETagsaQSRAREAEKQLREQVGD 1711
Cdd:pfam17380 435 -REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQAMI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1712 QYQTVRALAERKAEGVLAAQARAEQLR--DEARGLLQAAQDKLQRLQELEGTYEENERelevkaaqLDGLEaRMRSVLQA 1789
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRReaEEERRKQQEMEERRRIQEQMRKATEERSR--------LEAME-REREMMRQ 580
|
.
gi 6981142 1790 I 1790
Cdd:pfam17380 581 I 581
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1453-1665 |
1.15e-06 |
|
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: 51.85 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1453 DLALGRARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegad 1532
Cdd:COG1579 16 DSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1533 pdsiemvatrvldISipaSPEQIQRLASEIAervrSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEGERQKAETVQA 1612
Cdd:COG1579 85 -------------VR---NNKEYEALQKEIE----SLK-------------RRISDLEDEILELMERIEELEEELAELEA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981142 1613 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGT-EQSLNSASERARQ 1665
Cdd:COG1579 132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYERIRK 185
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1586-1790 |
1.52e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1586 AEQLLQDAQRARsrAEgERQKAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERARQ 1665
Cdd:COG3096 290 LRRELFGARRQL--AE-EQYRLVEMARELEELSARESDLEQDYQAAS-DHLNLVQTALRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1666 LHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQL--REQVGDQYQTvRALAERKAegvLAAQARAEQLRDEARG 1743
Cdd:COG3096 366 QEEVVEEAAEQLA-------EAEARLEAAEEEVDSLKSQLadYQQALDVQQT-RAIQYQQA---VQALEKARALCGLPDL 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981142 1744 LLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1545-1775 |
1.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1545 DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE--AQRA-- 1620
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelGERAra 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1621 ---QGAAQGAIrGAVVDTKNTEQTLQQVQermagteqSLNSASERARQLhalLEALKLKRAGNSLAASTAEETAGSAQSR 1697
Cdd:COG3883 95 lyrSGGSVSYL-DVLLGSESFSDFLDRLS--------ALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1698 AREAEKQLRE---QVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAA 1774
Cdd:COG3883 163 KAELEAAKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
.
gi 6981142 1775 Q 1775
Cdd:COG3883 243 A 243
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1452-1683 |
1.67e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 50.83 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1452 ADLALGRARHTQAEL---QRALVEgggilsRVSETRRQAEEAQQRAQAALDKanasrgqveqANQEL-RELIQnvkdfls 1527
Cdd:pfam04012 34 MQSELVKARQALAQTiarQKQLER------RLEQQTEQAKKLEEKAQAALTK----------GNEELaREALA------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 qegadpdsiemvatrvldisipaspeQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKA 1607
Cdd:pfam04012 91 --------------------------EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL----------KAKK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1608 ETVQAAlEEAQRAQGAAQGAIRGAvvDTKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALLEALKLKRAGNSLA 1683
Cdd:pfam04012 135 NLLKAR-LKAAKAQEAVQTSLGSL--STSSATDSFERIEEKIEEREARADAAAELAsaVDLDAKLEQAGIQMEVSEDV 209
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1566-1781 |
2.00e-06 |
|
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: 51.26 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1566 VRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAAL----EEAQRAQGAAQGAIRGAvvdtknteqt 1641
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELsslaQETEELQKKATQTLAKA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1642 lQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLaasTAEETAGSAQSRA-REAEKQLREQVGDQYQTVRALA 1720
Cdd:pfam06008 71 -QQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMlAEAQRMLGEIRSRDFGTQLQNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1721 E---RKAEGVLAA------------QARAEQLRD----------EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1775
Cdd:pfam06008 147 EaelKAAQDLLSRiqtwfqspqeenKALANALRDslaeyeaklsDLRELLREAAAKTRDANRLNLANQANLREFQRKKEE 226
|
....*.
gi 6981142 1776 LDGLEA 1781
Cdd:pfam06008 227 VSEQKN 232
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1449-1796 |
2.06e-06 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 52.89 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1449 AATADLALGRARHTQAELQRALvegggilsrvsETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1528
Cdd:COG2203 337 ADQAAIAIERARLYEALEAALA-----------ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1529 EGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:COG2203 406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1609 TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE 1688
Cdd:COG2203 486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1689 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERE 1768
Cdd:COG2203 566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645
|
330 340
....*....|....*....|....*...
gi 6981142 1769 LEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG2203 646 LALALASLVLLRALLATELDLILDSSLL 673
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1485-1795 |
2.13e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.38 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1485 RQAEEAQQRAQ--AALDKANASRGQVEQANQELRELiqnvKDFLSQEG--ADPDSIEMvatRVLDISIPASPEQIQRLAS 1560
Cdd:pfam05622 160 RNAEYMQRTLQleEELKKANALRGQLETYKRQVQEL----HGKLSEESkkADKLEFEY---KKLEEKLEALQKEKERLII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1561 E---------------IAERVRSLADVDTILAHTMGDVRRAE-----------QLLQDAQRARSRAEG-ERQKAETVQAA 1613
Cdd:pfam05622 233 ErdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEimpaeirekliRLQHENKMLRLGQEGsYRERLTELQQL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1614 LEEAQRAQGAAQGAIRgavvdtKNTEQ--TLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAASTA-- 1687
Cdd:pfam05622 313 LEDANRRKNELETQNR------LANQRilELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHleKLHEAQSELQKKKEqi 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAA-QARAEQLR-DEARGLLQAAQDKLQRLQELE 1759
Cdd:pfam05622 387 EELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERykkyveKAKSVIKTlDPKQNPASpPEIQALKNQLLEKDKKIEHLE 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 6981142 1760 GTYEEN--ERELEVK-----------AAQLDGLEARmrsvLQAINLQVQ 1795
Cdd:pfam05622 467 RDFEKSklQREQEEKlivtawynmgmALHRKAIEER----LAGLSSPGQ 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1514-1791 |
2.19e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1514 ELRELIQNVKDFLSQEgadpdsiemvatrvldisipaspEQIQRLASEIAERvrsladvdtiLAHTMGDVRRAEQLLQDA 1593
Cdd:PRK03918 173 EIKRRIERLEKFIKRT-----------------------ENIEELIKEKEKE----------LEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ------SLNSASERARQLH 1667
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEK---QLREQVGDQYQTVRALAE-----RKAEGVLAAQARAEQLRD 1739
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEEleerhELYEEAKAKKEELERLKK 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1740 EARGLlqaAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:PRK03918 380 RLTGL---TPEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1448-1796 |
2.52e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 52.33 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 QEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ-------SLNSASER---ARQLHALLEALK--- 1674
Cdd:COG0840 176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgdltvriDVDSKDEIgqlADAFNRMIENLRelv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1675 --LKRAGNSLAAStAEETAGSAQSRAREAEKQlREQVgdqyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKL 1752
Cdd:COG0840 256 gqVRESAEQVASA-SEELAASAEELAAGAEEQ-AASL----EETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 6981142 1753 QRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG0840 330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDI 373
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1479-1796 |
2.53e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 52.35 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKdfLSQEGADPDSIEMVATRVLDISipASPEQIQRL 1558
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK--AEAEQRAAELAAEAAKKLAEAE--KAAAEAEKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1559 ASEIAERVRSLADVDTIL--AHTMGDVRRAEQLLQDAQR-ARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:COG3064 93 AAAEKAKAAKEAEAAAAAekAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHAllEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQT 1715
Cdd:COG3064 173 RAAAGAAAALVAAAAAAVEAADTAAAAAAALAA--AAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1716 VRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG3064 251 AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVR 330
|
.
gi 6981142 1796 I 1796
Cdd:COG3064 331 G 331
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
929-987 |
2.93e-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: 45.81 E-value: 2.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 929 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 987
Cdd:cd00055 1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
989-1031 |
2.99e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 989 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1464-1767 |
3.19e-06 |
|
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: 51.95 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1464 AELQrALVEGggILSRVSETRRQAEEAQQRAQAALDKANAS----RGQVEQANQE---LRELIQNVKDFLSQEGADPDSI 1536
Cdd:pfam05701 264 AELA-AYMES--KLKEEADGEGNEKKTSTSIQAALASAKKEleevKANIEKAKDEvncLRVAAASLRSELEKEKAELASL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1537 ---EMVATrvldISIPASPEQIQRLASEIA---ERVRSLADVDTILAHTMGDVRR-AEQLLQDAQRAR-----SRAEGER 1604
Cdd:pfam05701 341 rqrEGMAS----IAVSSLEAELNRTKSEIAlvqAKEKEAREKMVELPKQLQQAAQeAEEAKSLAQAAReelrkAKEEAEQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1605 QKAE--TVQAALEEAQRAQGAAQGAIRGAVVdtknteqTLQQVQERMAGTEQSLNSASERARQLhALLEALKL-KRagns 1681
Cdd:pfam05701 417 AKAAasTVESRLEAVLKEIEAAKASEKLALA-------AIKALQESESSAESTNQEDSPRGVTL-SLEEYYELsKR---- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1682 laASTAEETAG----SAQSR---AREAEKQLREQVGDQYqtvRALAERKaEGVLAAQARAEQLRDEargllqaaqdKLQR 1754
Cdd:pfam05701 485 --AHEAEELANkrvaEAVSQieeAKESELRSLEKLEEVN---REMEERK-EALKIALEKAEKAKEG----------KLAA 548
|
330
....*....|...
gi 6981142 1755 LQELEGTYEENER 1767
Cdd:pfam05701 549 EQELRKWRAEHEQ 561
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1612-1785 |
3.43e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1612 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAS--------ERARQLHALLEALK-----LKRA 1678
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetlaDRVEEIREQLDEAEeakrfVQQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1679 GNSL------AASTAEETAGSAQSRAR--EAEKQLReqvgDQYQTVRALAE----------RKAEGVLAA---------- 1730
Cdd:PRK04863 917 GNALaqlepiVSVLQSDPEQFEQLKQDyqQAQQTQR----DAKQQAFALTEvvqrrahfsyEDAAEMLAKnsdlneklrq 992
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1731 -QARAEQLRDEARGLLQAAQDKL----QRLQELEGTYE-------ENERELEVKAAQLD-GLEARMRS 1785
Cdd:PRK04863 993 rLEQAEQERTRAREQLRQAQAQLaqynQVLASLKSSYDakrqmlqELKQELQDLGVPADsGAEERARA 1060
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1455-1755 |
3.77e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1455 ALGRARHTQAELQRALVEGGGILSRVSETR----RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEG 1530
Cdd:pfam07888 88 ELRQSREKHEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1531 ADPDSiemvaTRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQR--------------A 1596
Cdd:pfam07888 168 EEEAE-----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleelrsL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1597 RSRAEGERQKAETVQAALEE--AQRAQGAA---QGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERAR-QLHALL 1670
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSmaAQRDRTQAelhQARLQAA-------QLTLQLADASLALREGRARWAQERETlQQSAEA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1671 EALKLKRAgnSLAASTAEETAGSAQSRAREAEKQL-REQVGDQYQ---TVRALAERKAeGVLAAQARAEQLRDEARGLLQ 1746
Cdd:pfam07888 316 DKDRIEKL--SAELQRLEERLQEERMEREKLEVELgREKDCNRVQlseSRRELQELKA-SLRVAQKEKEQLQAEKQELLE 392
|
....*....
gi 6981142 1747 AAQDKLQRL 1755
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1585-1797 |
3.95e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1585 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgAIRGAVV-----DTKNTEQTLQQVQERMAGTEQSlNSA 1659
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQERE-QMDEIVEriqeeDQAEAEEKLEKQRQLREEIDEF-NEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1660 SERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQ-----LREQvgdQYQTVRALAERkaEGVLAAQARA 1734
Cdd:pfam13868 139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEreiarLRAQ---QEKAQDEKAER--DELRAKLYQE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1735 EQLRDEARGLLQAAQDKLQRLQELEGTYEE---NERELEVKAAQLDglEARMRSVLQAINLQVQIY 1797
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEqieLKERRLAEEAERE--EEEFERMLRKQAEDEEIE 277
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1504-1706 |
3.98e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 51.00 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1504 SRGQVEQANQELreliqNVKDFLSQEGADP-------DSIE--------MVATR------VLDISIPA-SPEQIQRLA-- 1559
Cdd:COG3524 84 SRDAVERLDAEL-----DLRAHYSRPGIDPlsrldpdASIEdlykyyrrRVKVEydstsgIITLEVRAfDPEDAQAIAea 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1560 ----SE-----IAERVRSladvDTIlAHTMGDVRRAEQLLQDAQRA----RSR---------AEG--------ERQKAET 1609
Cdd:COG3524 159 llaeSEelvnqLSERARE----DAV-RFAEEEVERAEERLRDAREAllafRNRngildpeatAEAllqliatlEGQLAEL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1610 vQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG--TEQSLNSASERarqlhalLEALKLKRAgnslaasTA 1687
Cdd:COG3524 234 -EAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGasGGDSLASLLAE-------YERLELERE-------FA 298
|
250 260
....*....|....*....|...
gi 6981142 1688 EETAGSAQS---RAR-EAEKQLR 1706
Cdd:COG3524 299 EKAYTSALAaleQARiEAARQQR 321
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1479-1789 |
4.34e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1479 RVSETRRQAEEAQQR-AQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-IQ 1556
Cdd:PRK04863 787 RIEQLRAEREELAERyATLSFDV------------QKLQRLHQAFSRFIGSH--------------LAVAFEADPEAeLR 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRA------QGAAQ 1625
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladETLADRVEEIREQLDEAEEAkrfvqqHGNAL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1626 GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLE---ALKLKRAGNSLAASTA--------EETAGSA 1694
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrraHFSYEDAAEMLAKNSDlneklrqrLEQAEQE 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1695 QSRAREAEKQLREQVgDQYQTVRA------------LAERKAE----GVLA---AQARAEQLRDEARGLLQAAQdklQRL 1755
Cdd:PRK04863 1001 RTRAREQLRQAQAQL-AQYNQVLAslkssydakrqmLQELKQElqdlGVPAdsgAEERARARRDELHARLSANR---SRR 1076
|
330 340 350
....*....|....*....|....*....|....*....
gi 6981142 1756 QELEGTYEENERELE-----VKAAQLDGLEARmRSVLQA 1789
Cdd:PRK04863 1077 NQLEKQLTFCEAEMDnltkkLRKLERDYHEMR-EQVVNA 1114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1772 |
4.44e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQAEEAQQRAQAAlDKANASRGQVEQAnQELRELIQNVKDFLSQEGADPDSIEmvATRVLDISIPAspEQIQ 1556
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKKKA--EEAK 1496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLlQDAQRARsRAEgERQKAETVQAAlEEAQRAQGAAQGAIRGAVVD 1634
Cdd:PTZ00121 1497 KKADEAkkAAEAKKKAD----------EAKKAEEA-KKADEAK-KAE-EAKKADEAKKA-EEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1635 TKNTEQTLQQVQER-MAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQY 1713
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKnMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1714 QTVRALAE--RKAE---GVLAAQ--ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVK 1772
Cdd:PTZ00121 1643 AEEKKKAEelKKAEeenKIKAAEeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1491-1785 |
6.75e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1491 QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE----M--VATR---VLDISIPASPEQIQ---RL 1558
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRdlkdMldVKERkinVLQKKIENLQEQLRdkdKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1559 ASEIAERVRSL----ADVDTILAhTMgdvrraEQLLQDAQRARSRAEGERQKAEtvQAALEEAQRAQGaaqgairgavvD 1634
Cdd:pfam10174 417 LAGLKERVKSLqtdsSNTDTALT-TL------EEALSEKERIIERLKEQRERED--RERLEELESLKK-----------E 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQL--HALLEALKLKRAGNSLAASTAEETAGSAQS-RAREAEKQLR--EQV 1709
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLkKAHNAEEAVRtnPEI 556
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1710 GDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1432-1758 |
8.80e-06 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 50.76 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1432 RDEDGQprcgglgcSGAAATADLALGRARHTQaELQRALVEgggilsrvsetrrqaeeaqQRAQAALDKANASRgqveqA 1511
Cdd:pfam13779 379 TDGAGQ--------EGRSEPLEIRLPERRFSD-PLARALIE-------------------QRRRLALDRENRPR-----V 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1512 NQELRELIqnvkdfLSQEGADPDSIEMVATRVL--DISIPASPEQIQRLAS---EIAERVRSladvdtilahtmGDVRRA 1586
Cdd:pfam13779 426 ARALDALT------LAPEEFGPDAGVYLGLRSAlaRLELARSDEALDEVADllwELALRIED------------GDLSDA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1587 EQLLQDAQRARSRA------EGERQK-AETVQAALEE-----AQRAQGAAQGAIRGAVVDTK-NTEQTLQQVQERMAgtE 1653
Cdd:pfam13779 488 ERRLRAAQERLSEAlergasDEEIAKlMQELREALDDymqalAEQAQQNPQDLQQPDDPNAQeMTQQDLQRMLDRIE--E 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1654 QSLNSASERARQlhaLLEAlkLKRAGNSLAASTAEETAGSAQSRAREAEKQLRE-------------------------Q 1708
Cdd:pfam13779 566 LARSGRRAEAQQ---MLSQ--LQQMLENLQAGQPQQQQQQGQSEMQQAMDELGDllreqqqlldetfrqlqqqggqqqgQ 640
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 6981142 1709 VGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQEL 1758
Cdd:pfam13779 641 PGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEEL 690
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1584-1784 |
9.11e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1584 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgAIRGAvvdtknteQTL-QQVQERmagteqslnsasER 1662
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE-----RKRYR--------QELeEQIEER------------EQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1663 ARQL---HALLEALKLKRAgnsLAASTAEETAgsAQSRAREAEKQLREQVgDQYQtvRALAERKaegvlaaQARAEQLRD 1739
Cdd:pfam13868 88 KRQEeyeEKLQEREQMDEI---VERIQEEDQA--EAEEKLEKQRQLREEI-DEFN--EEQAEWK-------ELEKEEERE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981142 1740 EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:pfam13868 153 EDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1482-1796 |
9.38e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1482 ETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvKDFLSQEGADPDSIEMVATRvldisipaspEQIQRLASE 1561
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQ--AQEAANRQREKEKERYKRDR----------EQWERQRRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1562 IAERVrslADVDTILAHTMGDVRRAEQLLQDAQRARsraegerqkaetvqAALEEAQRAQGAAQGAirgAVVDTKNTEQT 1641
Cdd:pfam07888 78 LESRV---AELKEELRQSREKHEELEEKYKELSASS--------------EELSEEKDALLAQRAA---HEARIRELEED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1642 LQQVQERMAGTEQSLNSASERARQLHALL-------EALKLKragnsLAASTAEETAGSAQ---SRAREAEK-----QLR 1706
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRkeeeaerKQLQAK-----LQQTEEELRSLSKEfqeLRNSLAQRdtqvlQLQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1707 EQVGDQYQTVRALAERKAEgvlaaqarAEQLRDEARGLlqaaQDklqRLQELEGTYEENERELEVKAAQLDGLEARM-RS 1785
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAE--------NEALLEELRSL----QE---RLNASERKVEGLGEELSSMAAQRDRTQAELhQA 277
|
330
....*....|.
gi 6981142 1786 VLQAINLQVQI 1796
Cdd:pfam07888 278 RLQAAQLTLQL 288
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1484-1784 |
9.60e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1484 RRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNVKDFLSQegadpdsiemvatrvldisipaspeQIQRLASEI 1562
Cdd:pfam13868 118 AEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDERILEYLKE-------------------------KAEREEERE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1563 AERVRSLADVDtilahtmgdvRRAEQLLQDAQRARS-RAEGERQKAETVQAALEEAQRAqgaaqgairgavvdtknteqt 1641
Cdd:pfam13868 173 AEREEIEEEKE----------REIARLRAQQEKAQDeKAERDELRAKLYQEEQERKERQ--------------------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1642 lqqvQERMAgteqslnsASERARQLHALLEALKLKRAGNSLaastaeetagsAQSRAREAEKQLREQVgdqyqtVRALAE 1721
Cdd:pfam13868 222 ----KEREE--------AEKKARQRQELQQAREEQIELKER-----------RLAEEAEREEEEFERM------LRKQAE 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDK-LQRLQELEGTYEENERELEVKAAQLDGL-EARMR 1784
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRRELEKQIEEReEQRAAEREEELEEGERLREEEAERRERIeEERQK 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1550-1794 |
9.98e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1550 ASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtVQAALEEAQRaqgaAQGAIR 1629
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE-LPERLEELEE----RLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1630 GAVVDTKNTEQTLQQVQERMA--------GTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETAGSAQSRAR 1699
Cdd:COG4717 160 ELEEELEELEAELAELQEELEelleqlslATEEELQDLAEELEELQQRLAELEeeLEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1700 EAEKQLREQ----------------VGDQYQTVRALAE----------------RKAEGVLAAQARAEQLRDEARGLLQA 1747
Cdd:COG4717 240 ALEERLKEArlllliaaallallglGGSLLSLILTIAGvlflvlgllallflllAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6981142 1748 AQDKLQRLQELEGTYEENE-RELEVKAAQLDGLEARMRSVLQAINLQV 1794
Cdd:COG4717 320 ELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEE 367
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1480-1684 |
1.05e-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: 48.95 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1480 VSETRRQAEEAQQ-RAQAALDKANASR--GQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDisipASPEQIQ 1556
Cdd:pfam06008 53 AQETEELQKKATQtLAKAQQVNAESERtlGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLS----RMLAEAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEIAERvrslaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQK-AETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:pfam06008 129 RMLGEIRSR-----DFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAlANALRDSLAEYEAKLSDLRELLREAAAKT 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981142 1636 KNTEQTLQQVQERMagteQSLNSASERARQLHALLEALkLKRAGNSLAA 1684
Cdd:pfam06008 204 RDANRLNLANQANL----REFQRKKEEVSEQKNQLEET-LKTARDSLDA 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1639-1791 |
1.06e-05 |
|
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: 48.77 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1639 EQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGD--QYQtv 1716
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEEQL-GNVRNnkEYE-- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1717 rALaERKAEgvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:COG1579 93 -AL-QKEIE---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
350-402 |
1.54e-05 |
|
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: 43.88 E-value: 1.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1476-1747 |
1.67e-05 |
|
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: 48.44 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1476 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1553
Cdd:smart00283 2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRArsraeGERQK-----AETVQaAL 1614
Cdd:smart00283 75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARA-----GEAGRgfavvADEVR-KL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1615 eeAQRAQGAAqgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTaEETAGSA 1694
Cdd:smart00283 139 --AERSAESA-----------KEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE--ETGDALEEIVDSV-EEIADLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1695 QSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1747
Cdd:smart00283 203 QEIAAATDEQAAgsEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
350-401 |
1.71e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 1.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 350 CECNGH---SHSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 401
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1452-1673 |
1.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1452 ADLALGRARHTQAELQ---RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1528
Cdd:COG4913 659 DEIDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1529 --EGADPDSIEMVATRVLDISIPASPEQIQRlasEIAERVRSLAdvdtilahtmGDVRRAEQLLQDAQRA-RSRAEGERQ 1605
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE---NLEERIDALR----------ARLNRAEEELERAMRAfNREWPAETA 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1606 KAETVQAALEEAQR------AQG--AAQGAIRGAVvdTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEAL 1673
Cdd:COG4913 806 DLDADLESLPEYLAlldrleEDGlpEYEERFKELL--NENSIEFVADLLSKL---RRAIREIKERIDPLNDSLKRI 876
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1589-1782 |
1.82e-05 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 49.58 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1589 LLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEqSLNSASerarQLHA 1668
Cdd:PRK15374 13 YTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDAARE-KLSSEG----QLTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1669 LLEALKLKRAGNSLAASTAEETAGSAQsraREAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRDEARGLL 1745
Cdd:PRK15374 88 LLGKLMTLLGDVSLSQLESRLAVWQAM---IESQKEMGIQVSKEFQTALGEAQeatDLYEASIKKTDTAKSVYDAAEKKL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 6981142 1746 QAAQDKLQRLQELEGTYEENERELEVKAAqlDGLEAR 1782
Cdd:PRK15374 165 TQAQNKLQSLDPADPGYAQAEAAVEQAGK--EATEAK 199
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
956-986 |
1.92e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 1.92e-05
10 20 30
....*....|....*....|....*....|.
gi 6981142 956 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 986
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-338 |
1.99e-05 |
|
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: 43.50 E-value: 1.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1477-1795 |
2.05e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETRRQA-------EEAQQRAQAA-LDKANASRGQVEQANQELRELIQNVKDFLSQEgadpdsiemvatrvldisi 1548
Cdd:COG3096 245 LEAIRVTQSDRdlfkhliTEATNYVAADyMRHANERRELSERALELRRELFGARRQLAEEQ------------------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1549 paspEQIQRLASEIAERVRSLADVDTilahtmgDVRRAE---QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQ 1625
Cdd:COG3096 306 ----YRLVEMARELEELSARESDLEQ-------DYQAASdhlNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1626 GAIRGAVVDTKNTEQT----------LQQ---VQERMAGTEQSLNSASERARQLHAlLEALKLKRAGNSLAASTAEE--- 1689
Cdd:COG3096 375 EQLAEAEARLEAAEEEvdslksqladYQQaldVQQTRAIQYQQAVQALEKARALCG-LPDLTPENAEDYLAAFRAKEqqa 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1690 -----------------------------------TAGSAQSRAREAEKQLREQ--VGDQYQTVRA-LAErkAEGVLAAQ 1731
Cdd:COG3096 454 teevleleqklsvadaarrqfekayelvckiagevERSQAWQTARELLRRYRSQqaLAQRLQQLRAqLAE--LEQRLRQQ 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 1732 ARAEQLRDEargLLQAAQDKLQRLQELEGTYEENERELEVKAAQL-DGLEARM--RSVLQAINLQVQ 1795
Cdd:COG3096 532 QNAERLLEE---FCQRIGQQLDAAEELEELLAELEAQLEELEEQAaEAVEQRSelRQQLEQLRARIK 595
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1479-1795 |
2.13e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1479 RVSETRRQAEE-AQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQR 1557
Cdd:COG3064 121 KAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1558 LASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKN 1637
Cdd:COG3064 201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1638 TEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAG-------NSLAASTAEETAGSAQSRAREAEK------Q 1704
Cdd:COG3064 281 VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAaagalvvRGGGAASLEAALSLLAAGAAAAAAgagalaT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1705 LREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:COG3064 361 GALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKL 440
|
330
....*....|.
gi 6981142 1785 SVLQAINLQVQ 1795
Cdd:COG3064 441 VADLAGGLVGI 451
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1477-1647 |
2.32e-05 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 46.24 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1477 LSRVSETR-RQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvatrvldisipaSPEQI 1555
Cdd:pfam07321 4 LLRVKHLReDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAW--------------------------------RPQEE 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 QRLASEIAERVRSLADVDTILaHTMGDVRRAEQLL-QDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAIRGAVVD 1634
Cdd:pfam07321 52 QRLYAEIQGKLVLLKELEKVK-QQVALLRENEADLeKQVAEARQQLEAEREALRQARQALAEARRAV--EKFAELVRLVQ 128
|
170
....*....|...
gi 6981142 1635 TKntEQTLQQVQE 1647
Cdd:pfam07321 129 AE--ELRQQERQE 139
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1475-1765 |
2.35e-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: 47.79 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1475 GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegadpdsiemvATRVLdisipASPEQ 1554
Cdd:pfam06008 9 GALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK-----------ATQTL-----AKAQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1555 IQRLASEIAERVRSLADvdtilahtmgdvrRAEQLLQDAQRARSRAEGERQKAE-----TVQAALEEAQRAQGAaqgaIR 1629
Cdd:pfam06008 73 VNAESERTLGHAKELAE-------------AIKNLIDNIKEINEKVATLGENDFalpssDLSRMLAEAQRMLGE----IR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1630 GavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEETAgsAQSRAREAEKQLREqv 1709
Cdd:pfam06008 136 S-----RDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA-NALRDSLAEYEAKLSD--LRELLREAAAKTRD-- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1710 gdqyqtvralaerkAEGVLAAQARAeqlrdearglLQAAQDKLQRLQELEGTYEEN 1765
Cdd:pfam06008 206 --------------ANRLNLANQAN----------LREFQRKKEEVSEQKNQLEET 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1607-1791 |
2.66e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1607 AETVQAALEEAQRAQGAAQGAIRGavvdtKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnSLAAST 1686
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQG-----RKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEE--ELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1687 AEETAgsAQSRAREAEKQLreQVGDQYQTVRALAERKAEGvlaaQARAEQLRDEarglLQAAQDKLQRLQELEGTYEENE 1766
Cdd:COG4717 109 AELEE--LREELEKLEKLL--QLLPLYQELEALEAELAEL----PERLEELEER----LEELRELEEELEELEAELAELQ 176
|
170 180
....*....|....*....|....*.
gi 6981142 1767 RELEVKAAQLD-GLEARMRSVLQAIN 1791
Cdd:COG4717 177 EELEELLEQLSlATEEELQDLAEELE 202
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1554-1796 |
2.77e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLAS-EIAERVRSLADVDTILAHTMGDVRRAEQLLQDA----QRARSR-----AEGE-RQKA-ETVQAALEEAQRAQ 1621
Cdd:COG3206 86 QIEILKSrPVLERVVDKLNLDEDPLGEEASREAAIERLRKNltvePVKGSNvieisYTSPdPELAaAVANALAEAYLEQN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1622 GAAQgairgavvdTKNTEQTLQQVQERMAGTEQSLNSAsERArqlhalLEALKLKRAGNSLaastaEETAGSAQSRAREA 1701
Cdd:COG3206 166 LELR---------REEARKALEFLEEQLPELRKELEEA-EAA------LEEFRQKNGLVDL-----SEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1702 EKQLREqvgdqyqtvrALAERKAegvlaAQARAEQLRDEARGLLQAA---------QDKLQRLQELEGTYEENEREL--- 1769
Cdd:COG3206 225 ESQLAE----------ARAELAE-----AEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYtpn 289
|
250 260 270
....*....|....*....|....*....|.
gi 6981142 1770 --EVKA--AQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG3206 290 hpDVIAlrAQIAALRAQLQQEAQRILASLEA 320
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1587-1776 |
2.78e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 47.37 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1587 EQLLQDAQRARSRAEGERQKAETVQAALEeaQRAqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSASER-ARq 1665
Cdd:pfam04012 28 EQAIRDMQSELVKARQALAQTIARQKQLE--RRL------------------EQQTEQAKKLEEKAQAALTKGNEElAR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1666 lhallEAL-KLKRAGNSLAASTAEetagsaQSRAREAEKQLREQVGDQYQTVRALaERKAEGVLA--AQARAEQLRDEAR 1742
Cdd:pfam04012 87 -----EALaEKKSLEKQAEALETQ------LAQQRSAVEQLRKQLAALETKIQQL-KAKKNLLKArlKAAKAQEAVQTSL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981142 1743 GLLQA--AQDKLQRLQ----ELEGTYE-----ENERELEVKAAQL 1776
Cdd:pfam04012 155 GSLSTssATDSFERIEekieEREARADaaaelASAVDLDAKLEQA 199
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
1564-1785 |
3.10e-05 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 47.39 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1564 ERVRSLADVDTILaHTMGDVRRAEqlLQDAQrarsrAEGERQKAETVQAALEE--AQRAQGAAQ----------GAIRGA 1631
Cdd:pfam16591 3 ERSDRMTDISQLN-DTLTDLRIAR--LQYML-----SNGDATAAQAVQKKLDElkQQLQQLKTTftspenvrllQEQLQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1632 VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRAREAEKQLREQV-G 1710
Cdd:pfam16591 75 IQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEA----EVLQTPEADSRRAAQYQAISELKRQVQMARYQVrG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1711 DQYQTVRALAERKAEGVLAAQARAEQLRDeargllQAAQDKLQRLQELE---GTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:pfam16591 151 YTFTPNEDSEQAAYQQLDAALASLDQLRQ------ALAGDPGAALQQLTsalQGYRDALDTFKAAVAAIEQARQEMTS 222
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1554-1718 |
3.23e-05 |
|
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: 47.23 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGErqkAETVQAALEEAQRAQG---------AA 1624
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGnvrnnkeyeAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1625 QGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgNSLAASTAEETAgsAQSRAREAEKQ 1704
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEE--LEAEREELAAK 171
|
170
....*....|....
gi 6981142 1705 LREQVGDQYQTVRA 1718
Cdd:COG1579 172 IPPELLALYERIRK 185
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
930-979 |
3.44e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.68 E-value: 3.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6981142 930 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 979
Cdd:smart00180 1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1684-1795 |
3.52e-05 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 46.09 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1684 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:PRK14475 36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 6981142 1760 GTYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1795
Cdd:PRK14475 115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1484-1790 |
3.56e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1484 RRQAEEAQQRA-QAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEI 1562
Cdd:COG3064 119 KEKAEEAKRKAeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1563 AERVRSLADVDTILAHTMGDVRRAEqllQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL 1642
Cdd:COG3064 199 AAAALAAAAAAAAADAALLALAVAA---RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1643 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER 1722
Cdd:COG3064 276 SGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGA 355
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1723 KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3064 356 GALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1613-1751 |
4.13e-05 |
|
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: 47.92 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1613 ALEEAQRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMAGT----EQSLNSASERARQLHA--LLEALKLK----RAGNS 1681
Cdd:TIGR02794 22 SLYHSVKPEPGGGAEIIQAVlVDPGAVAQQANRIQQQKKPAakkeQERQKKLEQQAEEAEKqrAAEQARQKeleqRAAAE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1682 LAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEArgllQAAQDK 1751
Cdd:TIGR02794 102 KAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA----AEAKKK 167
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1489-1774 |
4.93e-05 |
|
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: 48.03 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1489 EAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRS 1568
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1569 LADVDTILahtmgdVRRAEQLLQDAQRARSRAEGERQKA--ETVQAALEEAQRAQGAAQGAIRGAVVDT-KNTEQTLQQV 1645
Cdd:COG5185 352 LTENLEAI------KEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEEL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1646 QERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALaerkae 1725
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL------ 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6981142 1726 gvlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTyEENERELEVKAA 1774
Cdd:COG5185 498 -----KATLEKLRAKLERQLEGVRSKLDQVAESLKD-FMRARGYAHILA 540
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1647-1776 |
5.36e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1647 ERMAGTEQSLNsasERARQLHALLEALKLKRAGN-SLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAERKAE 1725
Cdd:PRK09039 46 REISGKDSALD---RLNSQIAELADLLSLERQGNqDLQDSVANLRASLSAA---EAERSRLQALLAELAGAGAAAEGRAG 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1726 GVLAAQARAEQLRDEARG---LLQ----AAQDKLQRLQELEGTYEENERELEVKAAQL 1776
Cdd:PRK09039 120 ELAQELDSEKQVSARALAqveLLNqqiaALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1637-1784 |
5.63e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1637 NTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLREQVGdqyqtv 1716
Cdd:COG1842 23 DPEKMLDQAIRDM---EEDLVEARQALAQVIANQKRLERQLE-------ELEAEAEKWEEKARLALEKGREDLA------ 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1717 RALAERKAEgvlaAQARAEQLRdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:COG1842 87 REALERKAE----LEAQAEALE-AQLAQLEEQVEKLKEaLRQLESKLEELKAKKDTLKARAKAAKAQEK 150
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1478-1757 |
6.25e-05 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 46.58 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1478 SRVSETRRQAEEAQQRAqAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvATRVLDISIPASPEQIQR 1557
Cdd:COG4223 7 AAVAELPAQLTALEQRL-AALEAAPAAAAATAALEARLAAL---------------------RAALAAAREAVAAAAAAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1558 LASEIAErvrsladvdtilahtmgdvrraeqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQG------AIRGA 1631
Cdd:COG4223 65 LEARLAA-------------------------LEAKAAAPEAEAAAAARAAALALAAAALRAAVERGQPfaaelaALEAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1632 VVDtknteqtlQQVQERMAGTEQS-LNSASERARQLHALLEALklkragnsLAASTAEETAGSAQSRAREAekqLREQVg 1710
Cdd:COG4223 120 APD--------APALAALAAFAATgVPTLAALRAEFPAAARAA--------LAAARAPEADASWLDRLLAF---ARSLV- 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6981142 1711 dqyqTVRALAERKAEGVLAAQARAEQ-LRdeaRGLLQAAQDKLQRLQE 1757
Cdd:COG4223 180 ----TVRRVGPVEGDDPDAILARAEAaLA---AGDLAGALAELEALPE 220
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1577-1760 |
6.32e-05 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 47.21 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1577 AHTMGDVRRAEQLLqdaQRARSRAEGERQKAETVQAaleEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSL 1656
Cdd:COG3071 60 AQALGDYERRDEYL---AQALELAPEAELAVLLTRA---ELLLDQGQAEQAL-----------ATLEALRAGAPRHPQVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1657 NSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQTVRAL------AERKAEGVLAA 1730
Cdd:COG3071 123 RLLLQAYRQLGDWEELLELLPALRKHKALSAEE----AQALERRAYLGLLRQAARDAEALKALwkalprAERRDPELAAA 198
|
170 180 190
....*....|....*....|....*....|....*....
gi 6981142 1731 QARA-EQLRD--EARGLLQAAQDK------LQRLQELEG 1760
Cdd:COG3071 199 YARAlIALGDhdEAERLLREALKRqwdprlVRLYGRLQG 237
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1532-1751 |
6.45e-05 |
|
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: 47.15 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1532 DPDSIEMVATRV-LDISIPASPEQ-----IQRLASE-----IAERVRSLADVDTILAHTmgDVRRAEQLLQDAQRARSRA 1600
Cdd:TIGR02794 44 DPGAVAQQANRIqQQKKPAAKKEQerqkkLEQQAEEaekqrAAEQARQKELEQRAAAEK--AAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1601 EGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL--QQVQERMAGTEQSLNSASERARQlhALLEALKLKra 1678
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEAEAK--AKAEEAKAK-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1679 gnslaASTAEETAGS-AQSRArEAEKQLREqvgdqyqtvRALAERKAE-------GVLAAQARAEQLRDEARGLLQAAQD 1750
Cdd:TIGR02794 198 -----AEAAKAKAAAeAAAKA-EAEAAAAA---------AAEAERKADeaelgdiFGLASGSNAEKQGGARGAAAGSEVD 262
|
.
gi 6981142 1751 K 1751
Cdd:TIGR02794 263 K 263
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1553-1791 |
6.58e-05 |
|
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: 46.51 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIAERVRSLADVDTILAHTMgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAqgAAQGAIRgav 1632
Cdd:smart00283 7 EEIAAGAEEQAEELEELAERMEELSASI------EEVAANADEIAATAQSAAEAAEEGREAVEDAITA--MDQIREV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1633 vdTKNTEQTLQQVQERMAGTEQSLNSASERARQ-----LHALLEAlklKRAGNS------LAA---STAEETAGSA---Q 1695
Cdd:smart00283 76 --VEEAVSAVEELEESSDEIGEIVSVIDDIADQtnllaLNAAIEA---ARAGEAgrgfavVADevrKLAERSAESAkeiE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1696 SRAREAEKQLREQVGDQYQTVR------ALAERK-------AEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTY 1762
Cdd:smart00283 151 SLIKEIQEETNEAVAAMEESSSeveegvELVEETgdaleeiVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVT 230
|
250 260
....*....|....*....|....*....
gi 6981142 1763 EENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:smart00283 231 QETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1584-1625 |
7.45e-05 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 42.37 E-value: 7.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6981142 1584 RRAEQLLQDAQRARSRAEGERQKA----ETVQAALEEAQRAQGAAQ 1625
Cdd:pfam11839 8 SKADQAEQDAAAAQSAADSAKAKAdeaaARANAAEAAAEEAQQAAE 53
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
1605-1740 |
7.57e-05 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 44.19 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1605 QKAETvqaALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRagNSL 1682
Cdd:pfam02050 1 DEAAR---ELAEAQRELQQAEEKLE-------ELQQYRAEYQQQLSGAGQGISAAELRNYQafISQLDEAIAQQQ--QEL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1683 AASTAEetagsaQSRAREA--EKQLReqvgdqYQTVRALAERKAEGVLAAQARAEQLR-DE 1740
Cdd:pfam02050 69 AQAEAQ------VEKAREEwqEARQE------RKSLEKLREREKKEERKEQNRREQKQlDE 117
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1696-1791 |
7.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1696 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKL----QRLQELEGTYEENERELE 1770
Cdd:COG4913 238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312
|
90 100
....*....|....*....|.
gi 6981142 1771 VKAAQLDGLEARMRSVLQAIN 1791
Cdd:COG4913 313 RLEARLDALREELDELEAQIR 333
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1479-1706 |
7.86e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQ------NVKDFLSQEGADPDSIE--------MVATRVL 1544
Cdd:COG1340 51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREeldelrKELAELNKAGGSIDKLRkeierlewRQQTEVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1545 disipaSPEQIQRLASEIAErvrsladvdtiLAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE-AQRAQga 1623
Cdd:COG1340 131 ------SPEEEKELVEKIKE-----------LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQ-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1624 aqgAIRGAVVDTKnteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK---------LKRAGNSLAASTAEETAGSA 1694
Cdd:COG1340 192 ---ELHEEMIELY---KEADELRKEADELHKEIVEAQEKADELHEEIIELQkelrelrkeLKKLRKKQRALKREKEKEEL 265
|
250
....*....|..
gi 6981142 1695 QSRAREAEKQLR 1706
Cdd:COG1340 266 EEKAEEIFEKLK 277
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1587-1773 |
8.73e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.95 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1587 EQLLQDAQRARSRAEGERQKA-ETVQAALEEAqraqgaaqgaiRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASER--- 1662
Cdd:pfam01442 18 EQLGPVAQELVDRLEKETEALrERLQKDLEEV-----------RAKL--EPYLEELQAKLGQNVEELRQRLEPYTEElrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1663 --ARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVgdqyqtvralaerkaegvlaaQARAEQLRDE 1740
Cdd:pfam01442 85 rlNADAEELQEKLAPYGEE---LRERLEQNVDALRARLAPYAEELRQKL---------------------AERLEELKES 140
|
170 180 190
....*....|....*....|....*....|....
gi 6981142 1741 ARGLLQAAQDKL-QRLQELEGTYEENERELEVKA 1773
Cdd:pfam01442 141 LAPYAEEVQAQLsQRLQELREKLEPQAEDLREKL 174
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1484-1784 |
9.21e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1484 RRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflsQEgadpdsiemvatRVLDisipaspEQIQRLASEIA 1563
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EE------------REED-------ERILEYLKEKA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1564 ERVRSladvdtilahtmgdvRRAEQLLQDAQRARsraegERQKaetVQAALEEAQRAQgAAQGAIRgavvdtkntEQTLQ 1643
Cdd:pfam13868 166 EREEE---------------REAEREEIEEEKER-----EIAR---LRAQQEKAQDEK-AERDELR---------AKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1644 QVQERMagteqslnsasERARQLHALLEALKLKRAgnslaastaeetagsaQSRAREAEKQLREQvgdQYQTVRALAERK 1723
Cdd:pfam13868 213 EEQERK-----------ERQKEREEAEKKARQRQE----------------LQQAREEQIELKER---RLAEEAEREEEE 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1724 AEGVLAAQA---RAEQLRDEARgllqaAQDKLQRLQELEGTYEENE--RELEVKAAQLDGLEARMR 1784
Cdd:pfam13868 263 FERMLRKQAedeEIEQEEAEKR-----RMKRLEHRRELEKQIEEREeqRAAEREEELEEGERLREE 323
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1606-1750 |
9.56e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 47.17 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1606 KAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERArqlhallEAlKLKRAGNSLAAS 1685
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAAD-EAKTAAAAAAREAAPLKASLRKLERAKARA-------DA-ELKRADKALAAA 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1686 TAEETAGSAQSRAREAEKQLREqVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQD 1750
Cdd:PRK12472 252 KTDEAKARAEERQQKAAQQAAE-AATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATD 315
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
1663-1781 |
9.98e-05 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 44.57 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1663 ARQLHALLEALKLKRAGNSLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRD 1739
Cdd:pfam16535 1 AGQLTLLLGNLMSLLGEVSLSQLESRIAAWKAMQ---EAQQQKGLELSDEFQTALSEAEeatDAYEKAINKLKNAKSKAK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6981142 1740 EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA 1781
Cdd:pfam16535 78 AAEKKIDQAQTRLQSLAPDSPGKAKLEAAEQQAGIKKDALQA 119
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1580-1775 |
1.06e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.90 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1580 MGDVRRAEQLLQDA-QRARSRAEGE---RQKAEtvQAALEEAQRAQGAAQgairgavvdTKNTEQTLQQVQERMAgtEQS 1655
Cdd:PRK07735 1 MDPEKDLEDLKKEAaRRAKEEARKRlvaKHGAE--ISKLEEENREKEKAL---------PKNDDMTIEEAKRRAA--AAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1656 LNSASERARQLHALLEALklkrAGNSLAASTAEeTAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGvlAAQARAE 1735
Cdd:PRK07735 68 KAKAAALAKQKREGTEEV----TEEEKAKAKAK-AAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAA--AAKAKAA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6981142 1736 QLRDEARGllqaaqdklqrlQELEGTYEENERELEVKAAQ 1775
Cdd:PRK07735 141 ALAKQKRE------------GTEEVTEEEEETDKEKAKAK 168
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1445-1795 |
1.44e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1445 CSGAAATADLALGRARHTQAELQRALVEGGGIL-------------------SRVSETRRQAEEAQQRAQAAL----DKA 1501
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLrlapDKL 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1502 NASRGQVEQANQELRELI------QNVKDFLSQEgadpdsiemvatrvldisIPASPEQIQRLASEIAERVRSLADVDTI 1575
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLglapgrQSIIDLKEKE------------------IPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1576 LAHTMGDVRRAEQLLQDAqrarsraegerQKAETVQAALEEAQR--AQGAAQgairgavVDTKNTEQTLQQVQERMAGTE 1653
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDV-----------TIMERFQMELKDVERkiAQQAAK-------LQGSDLDRTVQQVNQEKQEKQ 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1654 QSLNSASERARQLHALLE-----ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVL 1728
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQdqqeqIQHLKSKTNEL--KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1729 AAQARaEQLRDEARGLL-------QAAQDKLQRLQE-----------LEGTYEE--------NERELEVKAAQLDGLEAR 1782
Cdd:TIGR00606 914 LETFL-EKDQQEKEELIssketsnKKAQDKVNDIKEkvknihgymkdIENKIQDgkddylkqKETELNTVNAQLEECEKH 992
|
410 420
....*....|....*....|
gi 6981142 1783 -------MRSVLQAINLQVQ 1795
Cdd:TIGR00606 993 qekinedMRLMRQDIDTQKI 1012
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1452-1791 |
1.47e-04 |
|
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: 46.76 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1452 ADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA-----QAAL----DKANASRGQVEQANQELRELIQNV 1522
Cdd:pfam12128 651 ARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQldkkhQAWLeeqkEQKREARTEKQAYWQVVEGALDAQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1523 KDFLSQE--------GADPDSIEMVATRVLDiSIPASPEQIQRLASEIAERVRSLADVdtilAHTMGDVRRAEQLLQDA- 1593
Cdd:pfam12128 731 LALLKAAiaarrsgaKAELKALETWYKRDLA-SLGVDPDVIAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETw 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 ----QRARSRAEGERQKAETVQ---AALEEAQRAQGAA----QGAIRGAVVDTKNTEQTLQQVQERMA------GTEQSL 1656
Cdd:pfam12128 806 lqrrPRLATQLSNIERAISELQqqlARLIADTKLRRAKlemeRKASEKQQVRLSENLRGLRCEMSKLAtlkedaNSEQAQ 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1657 NSASERARQlhalLEALKLKRAGNSLAASTAEE---TAGSAQSRAREAEKQLREQVGDQYQT---VRALAERKAEGVLA- 1729
Cdd:pfam12128 886 GSIGERLAQ----LEDLKLKRDYLSESVKKYVEhfkNVIADHSGSGLAETWESLREEDHYQNdkgIRLLDYRKLVPYLEq 961
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981142 1730 -AQARAEQ----LRDEARGLLQAAQDKLQRLQELEGTYEENEREL--EVKA-AQLDGL---EARMRSVLQAIN 1791
Cdd:pfam12128 962 wFDVRVPQsimvLREQVSILGVDLTEFYDVLADFDRRIASFSRELqrEVGEeAFFEGVsesAVRIRSKVSELE 1034
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1553-1798 |
1.96e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQ----RLASEIaERVRSLADVDTILAhtmgdvRRAEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQGAI 1628
Cdd:pfam00038 4 EQLQelndRLASYI-DKVRFLEQQNKLLE------TKISELRQKKGAEPSRLY------SLYEKEIEDLRRQLDTLTVER 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1629 RGAVVDTKNTEQTLQQVQERMAgTEQSLNSASERA-----RQLHAL-LEALKLKRAGNSLAastaEETAgsAQSRAREAE 1702
Cdd:pfam00038 71 ARLQLELDNLRLAAEDFRQKYE-DELNLRTSAENDlvglrKDLDEAtLARVDLEAKIESLK----EELA--FLKKNHEEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1703 -KQLREQVGDQYQTV-----------RALAERKAE-GVLAA----------QARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:pfam00038 144 vRELQAQVSDTQVNVemdaarkldltSALAEIRAQyEEIAAknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELR 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 6981142 1760 GTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1798
Cdd:pfam00038 224 RTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQ 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1448-1668 |
2.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1448 AAATADLALGRARHTQAELQRALVEGggILSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIqnvkdfls 1527
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEA--ELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLD-------- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1528 qegadpdsiemvatrvldisipASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA 1607
Cdd:COG4913 682 ----------------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---QDRL 736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1608 ETVQAALEEAQRAQGAAQgaiRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1668
Cdd:COG4913 737 EAAEDLARLELRALLEER---FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1699-1795 |
2.17e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1699 REAEKQL---REQVGDQyQTVRALAERKAEgvlAAQARAEQLRDEARGLLQAAQDKL-----QRLQELEGTYEENERELE 1770
Cdd:COG1842 33 RDMEEDLveaRQALAQV-IANQKRLERQLE---ELEAEAEKWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA 108
|
90 100
....*....|....*....|....*
gi 6981142 1771 vkaaQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG1842 109 ----QLEEQVEKLKEALRQLESKLE 129
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1647-1754 |
2.23e-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: 43.24 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1647 ERMAGTEQSLNSASERARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEg 1726
Cdd:COG0711 31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAE---ARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE- 106
|
90 100 110
....*....|....*....|....*....|
gi 6981142 1727 vlAAQARA-EQLRDEARGL-LQAAQDKLQR 1754
Cdd:COG0711 107 --QERAKAlAELRAEVADLaVAIAEKILGK 134
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1553-1737 |
2.31e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIAERVRSLADVDTIlahtmgDVRRAEQLLQDAQRARSrAEGERQKAETVQAALEE--AQRAQGAAQGAIRG 1630
Cdd:PRK07735 32 AEISKLEEENREKEKALPKNDDM------TIEEAKRRAAAAAKAKA-AALAKQKREGTEEVTEEekAKAKAKAAAAAKAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1631 AVVDTKNTEQTLQQVQE------RMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGS-AQSRAREAEK 1703
Cdd:PRK07735 105 AAALAKQKREGTEEVTEeekaaaKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAkAKAAALAKQK 184
|
170 180 190
....*....|....*....|....*....|....
gi 6981142 1704 QLREQVGDQYQTVRALAERKAEGVLAAQARAEQL 1737
Cdd:PRK07735 185 AAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAL 218
|
|
| DUF4398 |
pfam14346 |
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. ... |
1446-1511 |
2.52e-04 |
|
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 127 and 269 amino acids in length.
Pssm-ID: 464144 [Multi-domain] Cd Length: 78 Bit Score: 41.09 E-value: 2.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1446 SGAAATADLALGRARHTQAELQRALVEGggilsRVSETRRQAEEAQQRAQAALDKANA--SRGQVEQA 1511
Cdd:pfam14346 16 DGAAQYAPLELKRARDALAKAEAAMAEK-----DYEKARHLAYLAEADAELAEAKARAakAEAAAAQA 78
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1588-1791 |
2.59e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1588 QLLQDAQRARSRAEGERQKAETVQAALEEAQRaQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASErarqlh 1667
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA-ELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQN------ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1668 ALLEAlklkragNSLAAS--TAEETAGSAQSRAREAEKQLREQvgdqyqtvraLAERKAEGvlaaqaraEQLRDEARGLL 1745
Cdd:PRK11281 143 DLAEY-------NSQLVSlqTQPERAQAALYANSQRLQQIRNL----------LKGGKVGG--------KALRPSQRVLL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1746 QA------AQDKLQRlQELEG-----TYEENERELevKAAQLDGLEaRMRSVLQ-AIN 1791
Cdd:PRK11281 198 QAeqallnAQNDLQR-KSLEGntqlqDLLQKQRDY--LTARIQRLE-HQLQLLQeAIN 251
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1694-1796 |
2.82e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1694 AQSRAREAEKQLrEQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQDKL---QRLQELEGTYEENERELE 1770
Cdd:COG1566 88 AEAQLAAAEAQL-ARLEAELGAEAEIAAAEAQ-LAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDAAQAQLE 165
|
90 100
....*....|....*....|....*.
gi 6981142 1771 VKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG1566 166 AAQAQLAQAQAGLREEEELAAAQAQV 191
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1585-1620 |
2.86e-04 |
|
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.
Pssm-ID: 468572 [Multi-domain] Cd Length: 90 Bit Score: 41.52 E-value: 2.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6981142 1585 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1620
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1455-1650 |
2.88e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1455 ALGRARHTQ----AELQRALVEGGGILsRVSETRRQAEEAQQRAQAALDKAnasrgQVEQANQELRELIQNVKdfLSQEG 1530
Cdd:COG2268 188 ALGRRKIAEiirdARIAEAEAERETEI-AIAQANREAEEAELEQEREIETA-----RIAEAEAELAKKKAEER--REAET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1531 AdpdsiEMVATRVLDISIPASPEQIQRLAsEIAERVRSLAdvdtiLAHtmgdvRRAEQLLQDAQRA-RSRAEGERQKAET 1609
Cdd:COG2268 260 A-----RAEAEAAYEIAEANAEREVQRQL-EIAEREREIE-----LQE-----KEAEREEAELEADvRKPAEAEKQAAEA 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTE----------QTLQQVQERMA 1650
Cdd:COG2268 324 EAEAEAEAIRAKGLAEAEGKRALAEAWNKLgdaaillmliEKLPEIAEAAA 374
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1548-1703 |
2.88e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 45.63 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1548 IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEgerqkaetvqAALEEAQRAQGAAQga 1627
Cdd:PRK12472 185 LAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARAD----------AELKRADKALAAAK-- 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981142 1628 irgavvdtknTEQTLQQVQERMAGTEQslnSASERARQLHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEK 1703
Cdd:PRK12472 253 ----------TDEAKARAEERQQKAAQ---QAAEAATQLDTAKADAEAKRA----AAAATKEAAKAAAAKKAETAK 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1638-1790 |
2.94e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1638 TEQTLQQVQERMA-----GTE-----QSLNSASERARQLHALLEALKLKRAgnSLAASTAEEtagsAQSRAREAEKQLRE 1707
Cdd:COG1196 177 AERKLEATEENLErlediLGElerqlEPLERQAEKAERYRELKEELKELEA--ELLLLKLRE----LEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1708 qvgdqyqtvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ----ELEGTYEENERELEVKAAQLDGLEARM 1783
Cdd:COG1196 251 ------------LEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERL 318
|
....*..
gi 6981142 1784 RSVLQAI 1790
Cdd:COG1196 319 EELEEEL 325
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1454-1709 |
3.38e-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: 44.72 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1454 LALGRARHTQAELQRALvegggilsRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvkdflsqegADP 1533
Cdd:COG2956 46 LALGNLYRRRGEYDRAI--------RIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE----------LDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEmVATRVLDISipaspEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1611
Cdd:COG2956 108 DDAE-ALRLLAEIY-----EQEGDWekAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1612 AALEEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEET 1690
Cdd:COG2956 182 LLLAELYLEQGDYEEAI-----------AALERALEQDPDYLPALPRLAELYEKLGDPEEALElLRKALELDPSDDLLLA 250
|
250 260
....*....|....*....|..
gi 6981142 1691 AGS---AQSRAREAEKQLREQV 1709
Cdd:COG2956 251 LADlleRKEGLEAALALLERQL 272
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1447-1748 |
3.66e-04 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 44.90 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1447 GAAATAD--LALGRARHTQAE--LQRAlvegggilsrvsetrrqAEEAQQRAQAALDKANAS--RGQVEQANQELRELIQ 1520
Cdd:COG3071 16 LLAALLEglLALAEGRYARAEklLSKA-----------------AEHSEAPLLAYLLAARAAqaLGDYERRDEYLAQALE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1521 NvkdflsqegaDPDSIEMVAtrvldisipaspeqiqrlaseiaervrsladvdtilahtmgdVRRAEQLLQ--DAQRARS 1598
Cdd:COG3071 79 L----------APEAELAVL------------------------------------------LTRAELLLDqgQAEQALA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1599 RAEGERQKA---ETVQAALEEAQRAQGAAQGAI--------RGAVvdtknTEQTLQQVQERMAgtEQSLNSASERARQLH 1667
Cdd:COG3071 107 TLEALRAGAprhPQVLRLLLQAYRQLGDWEELLellpalrkHKAL-----SAEEAQALERRAY--LGLLRQAARDAEALK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1668 ALLEAL-KLKRAGNSLAASTAEetAGSAQSRAREAEKQLREQVGDQYQT--VRALAERKAEGVLAAQARAE--------- 1735
Cdd:COG3071 180 ALWKALpRAERRDPELAAAYAR--ALIALGDHDEAERLLREALKRQWDPrlVRLYGRLQGGDPAKQLKRAEkwlkkhpnd 257
|
330 340
....*....|....*....|....*..
gi 6981142 1736 --------------QLRDEARGLLQAA 1748
Cdd:COG3071 258 pdlllalgrlclrnQLWGKAREYLEAA 284
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1636-1783 |
3.90e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.90 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaastaeETAGSAQSRAREAEKQLREQVgdqyqt 1715
Cdd:pfam04012 25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQT--------------EQAKKLEEKAQAALTKGNEEL------ 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1716 VRALAERKAEgvLAAQARAEQlrdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARM 1783
Cdd:pfam04012 85 AREALAEKKS--LEKQAEALE---TQLAQQRSAVEQLRKqLAALETKIQQLKAKKNLLKARLKAAKAQE 148
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1612-1789 |
3.94e-04 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 44.27 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1612 AALEEAQRAQGA-AQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEET 1690
Cdd:COG4223 24 AALEAAPAAAAAtAALEARLAALRAALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAA-RAAALALAAAALRAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1691 AGSAQSRAREAEkQLREQVGDQyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAqdklqrlqelegtyeeneRELE 1770
Cdd:COG4223 103 VERGQPFAAELA-ALEALAPDA-PALAALAAFAATGVPTLAALRAEFPAAARAALAAA------------------RAPE 162
|
170
....*....|....*....
gi 6981142 1771 VKAAQLDGLEARMRSVLQA 1789
Cdd:COG4223 163 ADASWLDRLLAFARSLVTV 181
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
880-919 |
4.02e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 4.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6981142 880 CVCNGR---ADECDAHTGACLgCRDYTGGEHCERCIAGFHGDP 919
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| 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 ... |
1641-1737 |
4.28e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 42.30 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1641 TLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQtvRALA 1720
Cdd:pfam00430 38 EIAEAEERRKDAAAALAEAEQQLKE--ARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKD--RALA 113
|
90
....*....|....*..
gi 6981142 1721 ERKAEGVLAAQARAEQL 1737
Cdd:pfam00430 114 ELRQQVVALAVQIAEKL 130
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1605-1763 |
4.43e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 45.05 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1605 QKAETVQAAleEAQRAQGAAQGAIRGAVVDTKnTEQTLQQVQERMAGTEQSLNsaseRARQLHALLEALKLKRAgnslAA 1684
Cdd:pfam15070 1 QLMESLKQL--QTERDQYAENLKEEGAVWQQK-MQQLSEQVRTLREEKERSVS----QVQELETSLAELKNQAA----VP 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1685 STAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAerkaegvlaAQARAeQLRDEArGLLQAAQDKLQRLQELEGTYE 1763
Cdd:pfam15070 70 PAEEEQPPAGPS---EEEQRLQEEAEQLQKELEALA---------GQLQA-QVQDNE-QLSRLNQEQEQRLLELERAAE 134
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1469-1756 |
4.76e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1469 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1548
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1549 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1625
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1626 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALL---EALKLKRAGNSLA----------ASTAEET 1690
Cdd:NF012221 1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1691 AGSAQSRAR-----EAEKQLREQV------GDQYqTVRALAER----KAEGVLAAQAR-AEQLRDEARGLLQAAQDKLQR 1754
Cdd:NF012221 1762 ANQAQADAKgakqdESDKPNRQGAagsglsGKAY-SVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNR 1840
|
..
gi 6981142 1755 LQ 1756
Cdd:NF012221 1841 LQ 1842
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1571-1770 |
4.79e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 43.50 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1571 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1650
Cdd:cd07596 1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1651 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKQlREQVGDQYQTV-------RALAE 1721
Cdd:cd07596 71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDD-RADALLTLQSLkkdlaskKAQLE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981142 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1770
Cdd:cd07596 135 KLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1562-1759 |
5.39e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1562 IAErVRSLADVDTILAHTMGDVRRAEQ--------LLQDAQRAR---SRAEGERQKAEtvQAALEEAQRAQGAAQgairg 1630
Cdd:COG2268 194 IAE-IIRDARIAEAEAERETEIAIAQAnreaeeaeLEQEREIETariAEAEAELAKKK--AEERREAETARAEAE----- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1631 avvdtknteqtlQQVQERMAGTEQSLNSASERARQLHALleALKLKRagnslaastaeetagsAQSRAREAEKQLREQVG 1710
Cdd:COG2268 266 ------------AAYEIAEANAEREVQRQLEIAEREREI--ELQEKE----------------AEREEAELEADVRKPAE 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1711 DQYQTVRALAERKAEGVLA---AQARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:COG2268 316 AEKQAAEAEAEAEAEAIRAkglAEAEGKRALAEAWNKLGDAAILLMLIEKLP 367
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1585-1775 |
5.56e-04 |
|
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: 44.73 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1585 RAEQLLQDAQRA-----RSRAEGERqKAETVQAALEEAqraqgaaqgairgavVDTKNTEQT-LQQVQERMAGTEQSLNS 1658
Cdd:pfam05557 10 RLSQLQNEKKQMelehkRARIELEK-KASALKRQLDRE---------------SDRNQELQKrIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1659 ASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRARE-------AEKQLREQVGDQYQTVRALAERKAEgvlaaQ 1731
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSElrrqiqrAELELQSTNSELEELQERLDLLKAK-----A 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1732 ARAEQLRDEarglLQAAQDKL----QRLQELEgtYE---ENERELEVKAAQ 1775
Cdd:pfam05557 149 SEAEQLRQN----LEKQQSSLaeaeQRIKELE--FEiqsQEQDSEIVKNSK 193
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1556-1645 |
6.18e-04 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.88 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1556 QRLASEIAERVRSLAD-VDTILAHTMGDVRRAEQ----LLQDAQ----------RARSRAEGERQKAETVQAALEEAQRA 1620
Cdd:pfam16999 4 SRLLSELAEREAALDQqIEAARKEAEREVEAAEAeaarILREAEakakalqaeyRQELAAETARIREEARARAEAEAQAV 83
|
90 100
....*....|....*....|....*
gi 6981142 1621 QGAAQGAIRGAVvdtkntEQTLQQV 1645
Cdd:pfam16999 84 RTRAEGRLQQAV------ELILRAV 102
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1485-1660 |
6.63e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 43.67 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1485 RQAEEA-QQRAQAAL---------DKA-NASRGQVeqaNQELRELIQnvkdflsqEGADPDSIEMVATRVLDISIPaspE 1553
Cdd:COG0330 102 ENAEEAlRQLAESALrevigkmtlDEVlSTGRDEI---NAEIREELQ--------EALDPYGIEVVDVEIKDIDPP---E 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1554 QIQRlaseiaervrsladvdtilahTMGDVRRAEQllqDAQRARSRAEGERQKAETVqaALEEAQR----AQGAAQGAIR 1629
Cdd:COG0330 168 EVQD---------------------AMEDRMKAER---EREAAILEAEGYREAAIIR--AEGEAQRaiieAEAYREAQIL 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 6981142 1630 GAVVDTKNTEQTLQQ-------VQERMAGT-EQSLNSAS 1660
Cdd:COG0330 222 RAEGEAEAFRIVAEAysaapfvLFYRSLEAlEEVLSPNS 260
|
|
| DUF6781 |
pfam20572 |
Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. ... |
1620-1754 |
6.97e-04 |
|
Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 223 and 298 amino acids in length.
Pssm-ID: 466721 Cd Length: 213 Bit Score: 43.02 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1620 AQGAAQGAIRGAVVDTkntEQTLQQVqerMAGTEQSLNSASErARQLhALLEALK---------LKRAGNSLAA------ 1684
Cdd:pfam20572 56 TEGASQGANAARGGEV---EALLKQA---VAGLDDALLKAAE-ASRL-ALEEAVDqgaafseqdLKKALDDLEKledtff 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1685 ----STAEETAGSAQS------------------RAREAEKQLREQVGDqyqtvrALAERKAEGVLAAQARAEQLRDEAR 1742
Cdd:pfam20572 128 dtlrKAAKSAGGPLKGpwgdlldhlkrsgtdtgaQARAAVEQLAAQLQA------ALREGRAAGSRAARALADSYAALAS 201
|
170
....*....|..
gi 6981142 1743 GLLQAAQDKLQR 1754
Cdd:pfam20572 202 GVLIGLSEALQP 213
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1564-1784 |
7.28e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1564 ERVRSLADVDTILAHTMGDVRRaeQLLQDAQRARSRAEGERQKA-ETVQAALEEA-----QRAQGAAQG----------- 1626
Cdd:PHA03247 1552 ERVDQSPVKDTAYAEYVAFVAR--RDLAEAKDALVRAKQQRAEAtDRVTAALREAlaaheRRAQSEAESlanlktllrva 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1627 AIRGAVVDT----KNTEQTLQQVQERMAGTEQS--LNSAS----ERARQL---HALLEALK-----LKRAGNSLAASTAE 1688
Cdd:PHA03247 1630 AIPATAAKTldqaRSVAEIVDQIELLLEQTEKAaeLDVAAvdwlEHARRVfeaHPLTAARGggpdpLARLHARLDALGET 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1689 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLL----QAAQDKL-QRLQELEGTyE 1763
Cdd:PHA03247 1710 RRRTEALRRSLEAAEAEWDEVWGRFGRVRGGAWKSPEALRAAREQLRALQTATNTVLglraDAHYERLpAKYQGALGA-K 1788
|
250 260
....*....|....*....|....*.
gi 6981142 1764 ENER-----ELEVKAAQLDGLEARMR 1784
Cdd:PHA03247 1789 SAERagaveELGAAVARHDGLLARLR 1814
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1618-1790 |
7.53e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1618 QRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMagtEQSLNSASERAR---QLHALLEALKLKRAgnsLAASTAEETAGS 1693
Cdd:PTZ00491 643 ERTRDSLQKSVQLAIeITTKSQEAAARHQAELL---EQEARGRLERQKmhdKAKAEEQRTKLLEL---QAESAAVESSGQ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1694 AQSRAR-EAEKqlreqvgdqyqtvrALAERKAEgVLAAQARAEQLRDEARGLLqaaqDKLQRLQELEGTYEENERELEV- 1771
Cdd:PTZ00491 717 SRAEALaEAEA--------------RLIEAEAE-VEQAELRAKALRIEAEAEL----EKLRKRQELELEYEQAQNELEIa 777
|
170 180
....*....|....*....|
gi 6981142 1772 KAAQLDGLEA-RMRSVLQAI 1790
Cdd:PTZ00491 778 KAKELADIEAtKFERIVEAL 797
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1640-1778 |
7.72e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 44.28 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1640 QTLQQVQERmagteqsLNSASERARQLHALLEALKLKRAGNSLAASTAEETA---------------------GSAQSRA 1698
Cdd:pfam15070 288 QELQETQER-------LEALTQQNQQLQAQLSLLANPGEGDGLESEEEEEEAprpslsipedfesreamvaffNSALAQA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1699 REAEKQLREQVGDQYQTVRALAERKAEG-------VLAAQARAEQLRDEARGLLQAAQDKLQ-RLQEL-EGTYEENER-- 1767
Cdd:pfam15070 361 EEERAELRRQLKEQKRRCRRLAQQAAPAqeepeheAHAPGTGGDSVPVEVHQALQVAMEKLQsRFTELmQEKADLKERve 440
|
170
....*....|.
gi 6981142 1768 ELEVKAAQLDG 1778
Cdd:pfam15070 441 ELEHRCIQLSG 451
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1470-1617 |
8.05e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 43.87 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1470 LVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdflsqegadpdsiemvatRVLDISIP 1549
Cdd:COG1538 250 LFDGGRNRARVRAAKAQLEQAEAQYEQTVLQA---LQEVEDALAALRAAREQL-------------------EALEEALE 307
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981142 1550 ASpEQIQRLAseiaeRVRSLADVDTILahtmgDVRRAEQLLQDAQRARSRAEGERQKAetvQAALEEA 1617
Cdd:COG1538 308 AA-EEALELA-----RARYRAGLASLL-----DVLDAQRELLQAQLNLIQARYDYLLA---LVQLYRA 361
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1583-1757 |
8.92e-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: 42.82 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1583 VRRAEQLLQDAQRARS--RAEGERQKAETVQAALEEAQRA----QGAAQGAIRGAVVDTKNTEQTLQQVQER-------M 1649
Cdd:cd00176 16 LSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERvealNELGEQLIEEGHPDAEEIQERLEELNQRweelrelA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1650 AGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEETAGSAQSRAREaEKQLREQVgDQYQTVRALAERKAEGVL 1728
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADDLEQwLEEKEAALASEDLGKDLESVEELLKK-HKELEEEL-EAHEPRLKSLNELAEELL 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 6981142 1729 AA---------QARAEQLRDEARGLLQAAQDKLQRLQE 1757
Cdd:cd00176 174 EEghpdadeeiEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1469-1653 |
9.21e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1469 ALVEGGGILSRVSETRRQAEEAQqrAQAALDKAnasRGQVEQANQELRELiQNVKDFLSQEGADPDSIEmVATRVLDISI 1548
Cdd:pfam00529 40 DRVKAGDVLFQLDPTDYQAALDS--AEAQLAKA---QAQVARLQAELDRL-QALESELAISRQDYDGAT-AQLRAAQAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1549 PASPEQIQrLASEIAERVRSLADVDTILAHTMGDVRRaeqLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAI 1628
Cdd:pfam00529 113 KAAQAQLA-QAQIDLARRRVLAPIGGISRESLVTAGA---LVAQAQANLLATVAQLDQIYVQITQSAAENQAE--VRSEL 186
|
170 180
....*....|....*....|....*
gi 6981142 1629 RGAVVDTKNTEQTLQQVQERMAGTE 1653
Cdd:pfam00529 187 SGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
350-403 |
1.21e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.45 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981142 350 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 403
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1646-1796 |
1.22e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1646 QERMAGTEQSLNSASERARQLHALLEalKLKRAgnslaASTAEEtAGSAQSRAREAEKQLReqvGDQYQTVRALAERKAE 1725
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLE--PLERQ-----AEKAER-YRELKEELKELEAELL---LLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1726 GVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ-AINLQVQI 1796
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErRRELEERL 318
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1634-1760 |
1.22e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.48 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1634 DTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlKLKRAGNSLAASTAEETAGSAQSRARE--AEKQlreqvgd 1711
Cdd:PRK07352 58 ALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKA-RAEAIRAEIEKQAIEDMARLKQTAAADlsAEQE------- 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1712 qyqtvRALAERKAEGVLAAQARAE-QLRDearGLLQAAQDKL--QRLQELEG 1760
Cdd:PRK07352 130 -----RVIAQLRREAAELAIAKAEsQLPG---RLDEDAQQRLidRSIANLGG 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1691-1790 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1691 AGSAQSRAREAEKQLREQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENER 1767
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKElaaLKKEEKALLKQLAALERRIAALARRIRALE---QELAALEAELAELEK 90
|
90 100
....*....|....*....|...
gi 6981142 1768 ELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAL 113
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1585-1776 |
1.59e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1585 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgaIRGAVV----DTKNTEQTLQQVQERMAGTEQSL---- 1656
Cdd:PRK10246 251 RLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQ--LRPHWEriqeQSAALAHTRQQIEEVNTRLQSTMalra 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1657 ---NSASERARQLHALLEALKLKRAGNSLAASTAEETAG-----SAQSRAREAEKQLREQVGDQYQTVRALAE------- 1721
Cdd:PRK10246 329 rirHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLRQWQQQLTHAEQKLNALPAitltlta 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981142 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1776
Cdd:PRK10246 409 DEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1636-1793 |
1.79e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.94 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLaastaEETAGSAQSRAREAEKQLRE--QVGDQY 1713
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEK--AEAEVAALNRRIQLL-----EEELERTEERLAEALEKLEEaeKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1714 QTVR-ALAERKAEG-----VLAAQAR-AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyEENERELEVKAAQldgLEARMRS 1785
Cdd:pfam00261 77 ERGRkVLENRALKDeekmeILEAQLKeAKEIAEEADRKYEEVARKLVVVEgDLERA-EERAELAESKIVE---LEEELKV 152
|
....*...
gi 6981142 1786 VLQaiNLQ 1793
Cdd:pfam00261 153 VGN--NLK 158
|
|
| 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 ... |
1720-1796 |
2.23e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.99 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1720 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1791
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121
|
....*
gi 6981142 1792 LQVQI 1796
Cdd:pfam00430 122 LAVQI 126
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1553-1650 |
2.25e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.54 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQ------RARSRAEGERQKAETVQAALEEAQRAQGAAQG 1626
Cdd:COG0711 31 ERQEKIADGLAEAERAKEEAEAALA-------EYEEKLAEARaeaaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEA 103
|
90 100
....*....|....*....|....
gi 6981142 1627 AIRGAVvdtkntEQTLQQVQERMA 1650
Cdd:COG0711 104 EIEQER------AKALAELRAEVA 121
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1594-1775 |
2.38e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.82 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1594 QRARSRAEGERQKAETVQAALEEAQRAQgaaqgairgavvdtkntEQTLQQVQERMagteqslnsasERARQLHALLEAL 1673
Cdd:COG1193 503 ERARELLGEESIDVEKLIEELERERREL-----------------EEEREEAERLR-----------EELEKLREELEEK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1674 KLKragnslaastaeetagsaqsrAREAEKQLREQvgdqyqtvralAERKAEGVLA-AQARAEQLRDEAR---GLLQAAQ 1749
Cdd:COG1193 555 LEE---------------------LEEEKEEILEK-----------AREEAEEILReARKEAEELIRELReaqAEEEELK 602
|
170 180
....*....|....*....|....*.
gi 6981142 1750 DKLQRLQELEGTYEENERELEVKAAQ 1775
Cdd:COG1193 603 EARKKLEELKQELEEKLEKPKKKAKP 628
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1692-1796 |
2.66e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1692 GSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLR---DEARGLLQAAQDKLQR----LQELEGTYEE 1764
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQarseLEQLEEELEE 84
|
90 100 110
....*....|....*....|....*....|...
gi 6981142 1765 NERELEVKAAQLDGLEARMRSV-LQAINLQVQI 1796
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLqEEAEELQEEL 117
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1535-1750 |
2.89e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1535 SIEMVATRVLDISIPASPEQIQRLASEIAERVRSLA-------DVDTILAHTMGDVRRAEQL---LQ--DAQRARSRAEG 1602
Cdd:PRK09039 35 TVFVVAQFFLSREISGKDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQalLAELAGAGAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1603 ERQKAETVQA-ALEEAQRAQGAAQgairgavVDTKNteQTLQQVQERMAGTEQSLNSASERARQLHALLEALklkraGNS 1681
Cdd:PRK09039 115 EGRAGELAQElDSEKQVSARALAQ-------VELLN--QQIAALRRQLAALEAALDASEKRDRESQAKIADL-----GRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1682 LAASTAEETAGSAQSRArEAEKQLREQVGDQyQTVRALAER---KAEgVLAAQARAE-------QLRDEARGLLQAAQD 1750
Cdd:PRK09039 181 LNVALAQRVQELNRYRS-EFFGRLREILGDR-EGIRIVGDRfvfQSE-VLFPTGSAElnpegqaEIAKLAAALIELAKE 256
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1553-1674 |
2.91e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 39.49 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1553 EQIQRL---ASEIAERVRSLADVDTilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgaiR 1629
Cdd:pfam18595 9 EELAELerkARELQAKIDALQVVEK-------DLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEIEL-------R 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6981142 1630 GAVVDTKNTEQTLQQVQERMAGTEQslnSASERARQLHALLEALK 1674
Cdd:pfam18595 75 ELERREERLQRQLENAQEKLERLRE---QAEEKREAAQARLEELR 116
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1456-1544 |
2.95e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 40.29 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1456 LGRA-RHTQAELQRALVEGGGILSRVSEtRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSqegadpD 1534
Cdd:PRK14473 58 LANAkRDYEAELAKARQEAAKIVAQAQE-RARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIA------D 130
|
90
....*....|
gi 6981142 1535 SIEMVATRVL 1544
Cdd:PRK14473 131 LVTLTASRVL 140
|
|
| HrpE_YscL_not |
TIGR02499 |
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ... |
1563-1677 |
3.08e-03 |
|
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274165 [Multi-domain] Cd Length: 166 Bit Score: 40.36 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1563 AERVRSLADVDTILAHTmgdVRRAEQLLQDAQRarsraEGERQKAETVQAALEEAQRAQgAAQGAirGAVVDtknTEQTL 1642
Cdd:TIGR02499 6 AEDLAALAQAQAILAAA---RQRAEAILADAEE-----EAEASRQLGYEQGLEQFWQEA-AAQLA--EWQQE---AEQLE 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6981142 1643 QQVQERMAG-----TEQSLNSASERARQLHALLEALKLKR 1677
Cdd:TIGR02499 72 ASLEERLAElvlqaLEQILGEYDEPERLVRLLRQLLRAVA 111
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1478-1758 |
3.10e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1478 SRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ-EGADPDSIEMVATRVLDISIPASPEQIQ 1556
Cdd:PRK10246 304 AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEhDRFRQWNNELAGWRAQFSQQTSDREQLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1557 RLASEIAERVRSLADV-DTILAHTMGDVRRAEqllqdAQRARSRAegERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:PRK10246 384 QWQQQLTHAEQKLNALpAITLTLTADEVAAAL-----AQHAEQRP--LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1636 KNTEQTLQQVQERMAGTEQSLNSAS---ERARQLHALLEALKLKRAGNS--LAASTAEETAGSAQSRAREAEKQLREQVg 1710
Cdd:PRK10246 457 TQRNAALNEMRQRYKEKTQQLADVKticEQEARIKDLEAQRAQLQAGQPcpLCGSTSHPAVEAYQALEPGVNQSRLDAL- 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6981142 1711 dqYQTVRALAERKAEGVLAAQARAEQLR---DEARGLLQAAQDKLQRLQEL 1758
Cdd:PRK10246 536 --EKEVKKLGEEGAALRGQLDALTKQLQrdeSEAQSLRQEEQALTQQWQAV 584
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1720-1788 |
3.36e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 3.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1720 AERKAEgvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKaaqldgLEARMRSVLQ 1788
Cdd:cd16269 196 KEKEIE---AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK------MEEERENLLK 255
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
309-341 |
3.67e-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: 36.95 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|...
gi 6981142 309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1464-1616 |
4.13e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1464 AELQRALVEG-GGILSRVSETRRQAEEAQQ---RAQAALDKANASRGQVEQANQELRELIQNVkDFlsqegaDPDSIEMV 1539
Cdd:COG0497 229 QEALEALSGGeGGALDLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSL-EF------DPERLEEV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1540 ATRVLDISIPA-----SPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA-----ET 1609
Cdd:COG0497 302 EERLALLRRLArkygvTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA---RKKAakkleKA 378
|
....*..
gi 6981142 1610 VQAALEE 1616
Cdd:COG0497 379 VTAELAD 385
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
1660-1792 |
4.31e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 39.27 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1660 SERARQLHALLEALKLKRA------GNSLAASTAEETAGSAQsrAREAEKQLReqvgdqyQTVRALAERKAEGVLAAQAR 1733
Cdd:pfam05130 8 EEELELLEELLELLEEEQEalkagdIEALEELTEEKQELLQK--LAQLEKERR-------ELLAELGLSPEEATLSELLA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981142 1734 AEQLRDEARGLLQAAQDKLQRLQELEgtyEENeRELevkaaqldgLEARMRSVLQAINL 1792
Cdd:pfam05130 79 KEEEDPELRELWQELLELLERLKELN---ELN-GEL---------IEQSLEFNNRSLNI 124
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1577-1784 |
4.85e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.77 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1577 AHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSL 1656
Cdd:COG3899 755 LYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1657 NSASERARQLHaLLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQ 1736
Cdd:COG3899 835 NLGFILHWLGP-LREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAAL 913
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981142 1737 LRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:COG3899 914 AAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
1531-1774 |
5.75e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 41.50 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1531 ADPDSIEMVA-TRVLDISI-------------PASPEQiqRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAQRA 1596
Cdd:pfam04632 118 ADPEAIFDIAvARVSEISLgilcaalvsalvfPRSVGP--ALRARLRARLRDAL-------------RLAAAALAGAPGA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1597 RSRAEGERQKAETVqAALEeAQRAQGAAQGA-IRGAVvdtknteQTLQQVQERMAgteqslnSASERARQLHALLEALkl 1675
Cdd:pfam04632 183 EAFEAARLRLAADI-LALE-ALRSHAAFESPrGRARA-------RALRRLLARML-------ALLPRLRSLARLLARL-- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1676 kragnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQLRDEARGLLQAAQDKLQRL 1755
Cdd:pfam04632 245 -------RTEGAGTVPELAALLDELAAWEAALAAEALQAALAALRAR----LRALRPALPLDFDTAAELLARLADLLAEL 313
|
250
....*....|....*....
gi 6981142 1756 QELEGTYEENERELEVKAA 1774
Cdd:pfam04632 314 AEALASCRALRHPIAQGAR 332
|
|
| DUF1631 |
pfam07793 |
Protein of unknown function (DUF1631); The members of this family are sequences derived from a ... |
1476-1667 |
5.80e-03 |
|
Protein of unknown function (DUF1631); The members of this family are sequences derived from a group of hypothetical proteins expressed by certain bacterial species. The region concerned is approximately 440 amino acid residues in length.
Pssm-ID: 429661 Cd Length: 742 Bit Score: 41.54 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1476 ILSRVSETRRQAEEAQQRAQAAL---DKANASRGQVEqanQELRELIQN------VKDFLSQ------------EGAD-P 1533
Cdd:pfam07793 459 FEEFLERERRRAELAEQRTVDAAegrERLELARQQAA---DELEQRLAGrplpevVREFLRQawsdvlaltylrHGEDsE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1534 DSIEMVAT------RVLDISIPASPEQIQRLASEIAERVRS-LADVdtilAHTMGDVRRAEQLLQDAQRARSRAEGERQK 1606
Cdd:pfam07793 536 EWQEALATaddlvwSVSPKPTAEERARLLALLPELLKRLRQgLASI----GYDPDESEAFFKELEALHAAAFRAKAAALA 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981142 1607 AETVQAALEEAQRAQGAaqgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSAS-ERARQLH 1667
Cdd:pfam07793 612 AALKAAAAKPAPAAAPA-------SPVEAEEEEALLGADAPPLAVVASPEDDAYlAQARALP 666
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
908-987 |
6.08e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 38.92 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 908 CERCIAGFHGDPRLPYGgqCRPC-PCPEGPGSQRHFATSCHRDgysqqIVCHCRAGYT-------GLRCEACAPGHFGDP 979
Cdd:cd13406 36 CSPCEPGFYNEAVNYEP--CKPCtQCNQRSGSEEKQKCTKTSD-----TVCRCRPGTQpldsykpGVDCVPCPPGHFSRG 108
|
....*...
gi 6981142 980 SkpGGRCQ 987
Cdd:cd13406 109 D--NQACK 114
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1694-1774 |
7.26e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1694 AQSRAREAEKQLREqvgdqYQTVRALAERKAEGVLA-AQARAEQLRDEARgllQAAQDKLQRLQELegtyEENERELEVK 1772
Cdd:COG0711 43 AERAKEEAEAALAE-----YEEKLAEARAEAAEIIAeARKEAEAIAEEAK---AEAEAEAERIIAQ----AEAEIEQERA 110
|
..
gi 6981142 1773 AA 1774
Cdd:COG0711 111 KA 112
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1634-1789 |
9.23e-03 |
|
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: 39.74 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1634 DTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALleALKLKRAGNSLAASTAEEtagsaqsrareaekqlREQVGDQY 1713
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNEL--GEQLIEEGHPDAEEIQER----------------LEELNQRW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1714 QTVRALAERKAEGVLAAQARAEQLRD------------------EARGLLQAAQDKLQRLQELegtyeenERELEVKAAQ 1775
Cdd:cd00176 89 EELRELAEERRQRLEEALDLQQFFRDaddleqwleekeaalaseDLGKDLESVEELLKKHKEL-------EEELEAHEPR 161
|
170
....*....|....
gi 6981142 1776 LDGLEARMRSVLQA 1789
Cdd:cd00176 162 LKSLNELAEELLEE 175
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1620-1784 |
9.40e-03 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 39.09 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1620 AQGAAQGAIrgAVVDTKNT--EQTLQQVQERMAgteqslnsasERARQlhallealklkragnslAASTAEET-AGSAQ- 1695
Cdd:pfam05335 10 AQKAAQEAK--AANDAQAAaaEAAARQVKNQLA----------DKALQ-----------------AAKAAEAAlAGKQQi 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981142 1696 -----SRAREAEKQLrEQVGDQYQTvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDklqRLQELEGTYEENERELE 1770
Cdd:pfam05335 61 veqleQELREAEAVV-QEESASLQQ----SQANANAAQRAAQQAQQQLEALTAALKAAQA---NLENAEQVAAGAQQELA 132
|
170
....*....|....
gi 6981142 1771 VKAAQLDglEARMR 1784
Cdd:pfam05335 133 EKTQLLE--AAKKR 144
|
|
|