|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
8.59e-106 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 337.25 E-value: 8.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 1958794729 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 |
4.90e-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: 4.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136 151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 1958794729 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 ... |
1729-1800 |
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 1958794729 1729 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1800
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1448-1792 |
3.46e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196 320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 etvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 378 ---EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1688 EETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneRE 1767
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----VL 529
|
330 340
....*....|....*....|....*
gi 1958794729 1768 LEVKAAQLDGLEARMRSVLQAINLQ 1792
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVE 554
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1465-1790 |
2.00e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.94 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1465 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1536
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1537 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:PRK02224 290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1609 TVQAALEEAQRAQGAAQGAIR--------------GAVVDTKNTE-------QTLQQVQERMAGTEQSLNSASERARQLH 1667
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEeleeeieelrerfgDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERkAEGVLAAQARAE----------QLR 1737
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIErleerredleELI 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1738 DEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1790 |
4.62e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1199 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1276
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1277 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1354
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1355 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1414
Cdd:TIGR02168 518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1415 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1484
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1564
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1565 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVvdtKNTEQTLQQ 1644
Cdd:TIGR02168 752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL---TLLNEEAAN 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1645 VQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVgdqyQTVRALAERKAE 1724
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELE 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1725 GVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELEG---------------TYEENERELEVKAAQLDGLEARMRSV 1785
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLaqleLRLEGLEVridnlqerlseeyslTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*
gi 1958794729 1786 LQAIN 1790
Cdd:TIGR02168 978 ENKIK 982
|
|
| 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 1958794729 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 |
4.63e-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: 4.63e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 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 |
5.03e-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: 5.03e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958794729 786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 834
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1789 |
1.17e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 73.71 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1446 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1524
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1525 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1591
Cdd:NF041483 984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1592 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1654
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1655 SLNsasERARQLHAllEAlkLKRAGNSLAA--STAEETAGSAQSRAREaekLREQVGDQYQTVRALAERKAEGVL--AAQ 1730
Cdd:NF041483 1136 ELH---ERARRESA--EQ--MKSAGERCDAlvKAAEEQLAEAEAKAKE---LVSDANSEASKVRIAAVKKAEGLLkeAEQ 1205
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794729 1731 ARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1789
Cdd:NF041483 1206 KKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1448-1768 |
2.22e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 72.55 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1514
Cdd:NF041483 478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1515 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDAq 1594
Cdd:NF041483 558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADA- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1595 rarsRAEGERQKAEtvqaALEEAQRAQGAAQGAIRgavvdtknteqTLQQVQERMAgteqslnsasERARQLHAllealk 1674
Cdd:NF041483 599 ----RAEAERIRRE----AAEETERLRTEAAERIR-----------TLQAQAEQEA----------ERLRTEAA------ 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1675 lkrAGNSLAASTAEETAGSAQSRA-REAEKLREQVGDQYQTVRA----LAER----KAEGVLAAQARAEQLRDEARGLLQ 1745
Cdd:NF041483 644 ---ADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAeaaaAAERvgteAAEALAAAQEEAARRRREAEETLG 720
|
330 340
....*....|....*....|...
gi 1958794729 1746 AAQDKLQrlQELEGTYEENEREL 1768
Cdd:NF041483 721 SARAEAD--QERERAREQSEELL 741
|
|
| 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 1958794729 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 |
2.03e-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: 2.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958794729 524 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-564 |
2.84e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958794729 525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1458-1763 |
3.39e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.70 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1458 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1529
Cdd:NF041483 158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1530 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1607
Cdd:NF041483 234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 ETVQAALEEAQRAQGAAQGAIRGAVVD--------TKNTEQTL----QQVQERMAGTEQSLNSASERARQLHALLEALKL 1675
Cdd:NF041483 287 EAKEAAAKQLASAESANEQRTRTAKEEiarlvgeaTKEAEALKaeaeQALADARAEAEKLVAEAAEKARTVAAEDTAAQL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1676 KRagnslAASTAEETAGSAQSRAR-------------------EAEKLREQVGDQYQTVRALA-----ERKAEGV-LAAQ 1730
Cdd:NF041483 367 AK-----AARTAEEVLTKASEDAKattraaaeeaerirreaeaEADRLRGEAADQAEQLKGAAkddtkEYRAKTVeLQEE 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958794729 1731 AR-----AEQLRDEA-------RGllQAAQDKLQRLQELEGTYEE 1763
Cdd:NF041483 442 ARrlrgeAEQLRAEAvaegeriRG--EARREAVQQIEEAARTAEE 484
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1464-1787 |
5.26e-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: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1464 AELQRALVEgggILSRVSETRRQ---AEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGAD-------- 1532
Cdd:pfam01576 218 TDLQEQIAE---LQAQIAELRAQlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqr 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1533 ---PDSIEMVATRVLDI--SIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRR---------AEQLLQdAQRARS 1598
Cdd:pfam01576 295 rdlGEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelTEQLEQ-AKRNKA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1599 RAEGERQKAETVQAAL-EEAQRAQGAAQGAIRGavvdTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL---- 1673
Cdd:pfam01576 374 NLEKAKQALESENAELqAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssll 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1674 -----KLKRAGNSLAASTA----------EET----AGSAQSRAREAEK--LREQVGDQYQTVRALaERKAEGVLAAQAR 1732
Cdd:pfam01576 450 neaegKNIKLSKDVSSLESqlqdtqellqEETrqklNLSTRLRQLEDERnsLQEQLEEEEEAKRNV-ERQLSTLQAQLSD 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1733 AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyeenERELEVKAAQLDGLEaRMRSVLQ 1787
Cdd:pfam01576 529 MKKKLEEDAGTLEALEEGKKRLQrELEAL----TQQLEEKAAAYDKLE-KTKNRLQ 579
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1482-1755 |
7.62e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.54 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1482 ETRRQAEEAQQRAQAALDKANASRGQV-EQANQELRELIQNVKDFLSQEGADPDSIEMVATrvldisipaspEQIQRLAS 1560
Cdd:NF041483 441 EARRLRGEAEQLRAEAVAEGERIRGEArREAVQQIEEAARTAEELLTKAKADADELRSTAT-----------AESERVRT 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 EIAERVRSLAdvdtilahtmgdvRRAEQLLQdaqraRSRAEGERQKAEtvqaALEEAQRAQGAAQGAIRgavvdtKNTEQ 1640
Cdd:NF041483 510 EAIERATTLR-------------RQAEETLE-----RTRAEAERLRAE----AEEQAEEVRAAAERAAR------ELREE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1641 TLQQVQERMAgteqslNSASERARqLHALLEAlKLKRAGNSLAASTAEeTAGSAQSRAREAEKLREQVGDQYQTVRALAE 1720
Cdd:NF041483 562 TERAIAARQA------EAAEELTR-LHTEAEE-RLTAAEEALADARAE-AERIRREAAEETERLRTEAAERIRTLQAQAE 632
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1721 RKAEGVL------AAQARAE------QLRDEARG----LLQAAQDKLQRLQ 1755
Cdd:NF041483 633 QEAERLRteaaadASAARAEgenvavRLRSEAAAeaerLKSEAQESADRVR 683
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
413-470 |
8.44e-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: 8.44e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 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 1958794729 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1769 |
1.31e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.77 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1446 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1521
Cdd:NF041483 720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1522 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1600
Cdd:NF041483 787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1601 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1670
Cdd:NF041483 843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1671 --EALKLKRAGNSLAASTAEETAGSAQSR----AREAEKLREQVGDQYQTVRALAerkAEGVLAAQARAEQLRDEARGLL 1744
Cdd:NF041483 923 tsEAERLTAEARAEAERLRDEARAEAERVradaAAQAEQLIAEATGEAERLRAEA---AETVGSAQQHAERIRTEAERVK 999
|
330 340
....*....|....*....|....*
gi 1958794729 1745 QAAQDKLQRLQelEGTYEENERELE 1769
Cdd:NF041483 1000 AEAAAEAERLR--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 1958794729 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 |
2.89e-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: 2.89e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 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 1958794729 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 1958794729 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 |
8.36e-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: 8.36e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958794729 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 1958794729 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 1958794729 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1556-1763 |
2.05e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.92 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1618
Cdd:NF041483 130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1619 RAQGAAQGAIRGAVVDTK---NTEQTlqQVQERMAGTEQ---SLNSASERARQLHALL------------EALKLKRAGN 1680
Cdd:NF041483 204 SARAEAEAILRRARKDAErllNAAST--QAQEATDHAEQlrsSTAAESDQARRQAAELsraaeqrmqeaeEALREARAEA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1681 SLAASTAEETAG----SAQS----RAREA-EKLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDEA--RGLLQAAQ 1748
Cdd:NF041483 282 EKVVAEAKEAAAkqlaSAESaneqRTRTAkEEIARLVGEATKEAEALKA-EAEQALAdARAEAEKLVAEAaeKARTVAAE 360
|
250
....*....|....*
gi 1958794729 1749 DKLQRLQELEGTYEE 1763
Cdd:NF041483 361 DTAAQLAKAARTAEE 375
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
412-471 |
2.23e-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: 2.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 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 |
3.09e-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: 54.28 E-value: 3.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958794729 525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 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 1958794729 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1143
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1788 |
3.83e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.15 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1459 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1533
Cdd:NF041483 252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1534 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1598
Cdd:NF041483 326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1599 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1650
Cdd:NF041483 401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1651 GTEQSLNSA--------------SERARQlHALLEALKLKRagnslaasTAEETAgsaqSRAR-EAEKLREQVGDQYQTV 1715
Cdd:NF041483 481 TAEELLTKAkadadelrstataeSERVRT-EAIERATTLRR--------QAEETL----ERTRaEAERLRAEAEEQAEEV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1716 RALAERKA-----EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSv 1785
Cdd:NF041483 548 RAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT- 626
|
...
gi 1958794729 1786 LQA 1788
Cdd:NF041483 627 LQA 629
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1097-1144 |
4.20e-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: 4.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 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 1958794729 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 1958794729 989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1206-1573 |
2.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1206 DLAARTRRLEQWAQELQQTgvLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEAtegLRHEIGKTTERLTQLEAE 1285
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA--LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR---LEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1286 LTDVQDENFNANHALSGLERDGLALNLTLRQLDQhlDILKHSNFLGAYDS-IRHAHSQSTEAERRANASTFAIPSPVSNS 1364
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEA--QIEQLKEELKALREaLDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1365 ADTRRRAEVLMgAQRENFNRQHLANQQALGRLSThthtlsltgvnelvcgapgdapcatspcggagcrdedgqprcgglg 1444
Cdd:TIGR02168 834 AATERRLEDLE-EQIEELSEDIESLAAEIEELEE---------------------------------------------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1445 cSGAAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKD 1524
Cdd:TIGR02168 867 -LIEELESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1525 FLSQEGAdpDSIEMVATRVLDisIPASPEQIQRLASEIAERVRSLADVD 1573
Cdd:TIGR02168 944 RLSEEYS--LTLEEAEALENK--IEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1554-1769 |
2.35e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.45 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1627
Cdd:NF041483 44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1628 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRA---REAEKL 1704
Cdd:NF041483 121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARAeaeRLAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1705 REQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQELE 1758
Cdd:NF041483 195 RQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEAE 271
|
250
....*....|.
gi 1958794729 1759 GTYEENERELE 1769
Cdd:NF041483 272 EALREARAEAE 282
|
|
| 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 1958794729 833 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| 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 1958794729 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 1958794729 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 |
9.10e-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: 9.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958794729 989 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 1035
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-516 |
9.94e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.94e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958794729 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 |
3.90e-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: 3.90e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 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 1958794729 879 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 924
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1553-1790 |
1.50e-06 |
|
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: 51.52 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEgerQKAETVQAALEEAQRAQGAAQGAIRGA- 1631
Cdd:smart00283 7 EEIAAGAEEQAEELEELA-------------ERMEELSASIEEVAANAD---EIAATAQSAAEAAEEGREAVEDAITAMd 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1632 --VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ-----LHALLEAlklKRAGNS------LAA---STAEETAGSAQ 1695
Cdd:smart00283 71 qiREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQtnllaLNAAIEA---ARAGEAgrgfavVADevrKLAERSAESAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 SRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRD------EARGLLQ-----------AAQDKLQRLQELE 1758
Cdd:smart00283 148 EIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEivdsveEIADLVQeiaaatdeqaaGSEEVNAAIDEIA 227
|
250 260 270
....*....|....*....|....*....|..
gi 1958794729 1759 GTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:smart00283 228 QVTQETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1684-1794 |
2.34e-06 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 49.55 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1684 ASTAEETAGSAQSRAREAEKLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELEG 1759
Cdd:PRK14475 36 AGALDAYAAKIQAELDEAQRLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERKI 115
|
90 100 110
....*....|....*....|....*....|....*
gi 1958794729 1760 TYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1794
Cdd:PRK14475 116 AQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| 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 1958794729 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 1958794729 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 1958794729 350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| 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 1958794729 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 1958794729 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 |
1.97e-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: 1.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 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 1958794729 930 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 979
Cdd:smart00180 1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1583-1756 |
7.74e-05 |
|
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: 45.90 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1583 VRRAEQLLQDAQRARS--RAEGERQKAETVQAALEEAQRA----QGAAQGAIRGAVVDTKNTEQTLQQVQER-------M 1649
Cdd:cd00176 16 LSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERvealNELGEQLIEEGHPDAEEIQERLEELNQRweelrelA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1650 AGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEETAGSAQSRAREAEKLREQVgDQYQTVRALAERKAEGVLA 1728
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADDLEQwLEEKEAALASEDLGKDLESVEELLKKHKELEEEL-EAHEPRLKSLNELAEELLE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958794729 1729 A---------QARAEQLRDEARGLLQAAQDKLQRLQE 1756
Cdd:cd00176 175 EghpdadeeiEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1696-1797 |
9.82e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 SRAREA-EKLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKLQRLQELEgtyEENERELEVKAA 1773
Cdd:COG4913 238 ERAHEAlEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLELLEAEL---EELRAELARLEA 309
|
90 100
....*....|....*....|....*
gi 1958794729 1774 QLDGLEARMRSVLQAI-NLQVQIYN 1797
Cdd:COG4913 310 ELERLEARLDALREELdELEAQIRG 334
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1585-1620 |
2.97e-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: 2.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958794729 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 1958794729 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 ... |
1469-1753 |
4.27e-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: 45.60 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1469 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1548
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1549 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1625
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1626 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALleaLKLKRAgnSLAASTAEETAGSAQSRareaek 1703
Cdd:NF012221 1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDAL---AKQNEA--QQAESDANAAANDAQSR------ 1750
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1704 lreqvGDQYQTvralaerkaegvlAAQARAEQLRDEARGLLQAAQDKLQR 1753
Cdd:NF012221 1751 -----GEQDAS-------------AAENKANQAQADAKGAKQDESDKPNR 1782
|
|
| 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 1958794729 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 ... |
1719-1795 |
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 1958794729 1719 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1790
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121
|
....*
gi 1958794729 1791 LQVQI 1795
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 1958794729 309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
8.59e-106 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 337.25 E-value: 8.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 1958794729 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 |
4.90e-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: 4.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136 151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 1958794729 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 ... |
1729-1800 |
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 1958794729 1729 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1800
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 ... |
1730-1799 |
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 1958794729 1730 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1799
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1448-1792 |
3.46e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196 320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 etvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 378 ---EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1688 EETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneRE 1767
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----VL 529
|
330 340
....*....|....*....|....*
gi 1958794729 1768 LEVKAAQLDGLEARMRSVLQAINLQ 1792
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVE 554
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1729-1799 |
7.34e-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: 7.34e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1729 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1799
Cdd:cd22300 2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1554-1789 |
1.42e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRLA--SEIAERVRSLADVDTILAHTM---------GDVRRAEQLLQDAQRARSRAEGERQKAET----VQAALEEAQ 1618
Cdd:COG1196 201 QLEPLErqAEKAERYRELKEELKELEAELlllklreleAELEELEAELEELEAELEELEAELAELEAeleeLRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1619 RAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA 1698
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1699 REAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGL 1778
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250
....*....|.
gi 1958794729 1779 EARMRSVLQAI 1789
Cdd:COG1196 441 EEALEEAAEEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1484-1794 |
1.17e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1484 RRQAEEAQQRAQAALDKANAsrgQVEQANQELREL---IQNVKDFLSQEGadpdsiemvatrvldisipaspEQIQRLAS 1560
Cdd:COG1196 234 LRELEAELEELEAELEELEA---ELEELEAELAELeaeLEELRLELEELE----------------------LELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 EIAERVRSLADVDTILAHTMGDVRRA----EQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK 1636
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELeerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1637 NTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQvgdqyqtVR 1716
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE-------EE 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1717 ALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1794
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1492-1793 |
2.54e-18 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 91.23 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1492 QRAQAALDKANASRGQVEQANQELRELIQNVKdflsqegadpdsIEMVA-TRVLDISIPA-SPEQIQRLASEIAErvrsl 1569
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLT------------VEPVKgSNVIEISYTSpDPELAAAVANALAE----- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1570 ADVDTILAHTMGDVRRAEQLLQDaqrarsRAEGERQKAETVQAALEEAQRAQGAAqgairgavvdtkNTEQTLQQVQERM 1649
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLLQQL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1650 AGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE------KLREQVGDQYQTVRALAERKA 1723
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEleaelaELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1724 E-----------GVLAAQARAEQLR---DEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1789
Cdd:COG3206 302 AlraqlqqeaqrILASLEAELEALQareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
....
gi 1958794729 1790 NLQV 1793
Cdd:COG3206 382 ALTV 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1455-1789 |
4.22e-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: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1455 ALGRARHTQAELQRA---LVEgggILSRVSETRRQAEEAQQ----RAQAALDKANASRGQVEQANQELRELIqnvkdfls 1527
Cdd:COG1196 177 AERKLEATEENLERLediLGE---LERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELE-------- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 qegadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTilahtmgdvrraeqllqDAQRARSRAEGERQKA 1607
Cdd:COG1196 246 -------------------------AELEELEAELEELEAELAELEA-----------------ELEELRLELEELELEL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1688 EETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERE 1767
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
330 340
....*....|....*....|..
gi 1958794729 1768 LEVKAAQLDGLEARMRSVLQAI 1789
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELL 465
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1465-1790 |
2.00e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.94 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1465 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1536
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1537 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:PRK02224 290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1609 TVQAALEEAQRAQGAAQGAIR--------------GAVVDTKNTE-------QTLQQVQERMAGTEQSLNSASERARQLH 1667
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEeleeeieelrerfgDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERkAEGVLAAQARAE----------QLR 1737
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIErleerredleELI 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1738 DEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1790 |
4.62e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1199 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1276
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1277 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1354
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1355 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1414
Cdd:TIGR02168 518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1415 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1484
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1564
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1565 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVvdtKNTEQTLQQ 1644
Cdd:TIGR02168 752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL---TLLNEEAAN 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1645 VQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVgdqyQTVRALAERKAE 1724
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELE 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1725 GVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELEG---------------TYEENERELEVKAAQLDGLEARMRSV 1785
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLaqleLRLEGLEVridnlqerlseeyslTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*
gi 1958794729 1786 LQAIN 1790
Cdd:TIGR02168 978 ENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1448-1754 |
1.37e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 QEGADPDSIEMVATRVLDISipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 EtvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196 427 E--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1688 EETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRL 1754
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1448-1783 |
1.54e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.86 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAAT---ADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEqanqELRELIQNVKD 1524
Cdd:PRK02224 232 ARETrdeADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDL-------RERLE----ELEEERDDLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1525 FLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGER 1604
Cdd:PRK02224 301 EAGLDDADAEAVE---------------ARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1605 QKAETVQAALEEAQRAQGAAQGAI----------RGAVVDTKNT-----------EQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIeeleeeieelRERFGDAPVDlgnaedfleelREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1664 RQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERkAEGVLAAQARAEQLRDEargl 1743
Cdd:PRK02224 443 EEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEER---- 517
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958794729 1744 lqaAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1783
Cdd:PRK02224 518 ---REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1564-1781 |
2.92e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.35 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1564 ERVRSLADVDTILAHtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGA-IRGAVVDTKNTEQTL 1642
Cdd:COG4913 219 EEPDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1643 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSRAREAEKLREQVGDQYQTVRALAER 1721
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1722 KAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENERELEVKAAQLDGLEAR 1781
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1199-1791 |
6.68e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1199 DWDRVVQDLAARTRRLEQWAQELQQT-GVLGAFESSFLNLQgklgmvQAIVAARNTSAASTAKLVEATEGLRHEigktTE 1277
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELeAELEELRLELEELE------LELEEAQAEEYELLAELARLEQDIARL----EE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1278 RLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDILKH--SNFLGAYDSIRHAHSQSTEAERRANASTF 1355
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1356 AIpspVSNSADTRRRAEVLMGAQRENFNRQHLANQQALGRLSTHTHTLSLtgvnelvcgapgdapcatspcggagcRDED 1435
Cdd:COG1196 390 EA---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------------------------EEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1436 GQprcgglgcsgAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQEL 1515
Cdd:COG1196 441 EE----------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1516 RELIQNVKDF-LSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVD-----TILAHTMGDVRRAEQL 1589
Cdd:COG1196 511 KAALLLAGLRgLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1590 LQDA---QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQL 1666
Cdd:COG1196 591 ALARgaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1667 HALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1746
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1958794729 1747 AqdkLQRLQELEGTYEENERELEvkaaqldGLEARMRSvLQAINL 1791
Cdd:COG1196 751 E---ALEELPEPPDLEELERELE-------RLEREIEA-LGPVNL 784
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1204-1784 |
2.09e-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: 82.41 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1204 VQDLAARTRRLEQWAQELQQtgvlgafesSFLNLQGKLGMVQAIVA----ARNTSAASTAKLVEATEGLRHEIGKTTERL 1279
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRE---------RLANLERQLEELEAQLEelesKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1280 TQLEAEL-------TDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDILKHSnfLGAYDSIRHAHSQS-TEAERRAN 1351
Cdd:TIGR02168 361 EELEAELeelesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR--RERLQQEIEELLKKlEEAELKEL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1352 ASTFAIPSPVSNSADTR-RRAEVLMGAQRENFNRQHLANQQALGRLSTHTHTLSLTgvnelvcgapgdapcatspcggag 1430
Cdd:TIGR02168 439 QAELEELEEELEELQEElERLEEALEELREELEEAEQALDAAERELAQLQARLDSL------------------------ 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1431 crdEDGQPRCGGLGCSGAAATA---DLALGRAR-----HTQAELQRAL--VEGGGILSRVSETrrqaEEAQQRAQAALDK 1500
Cdd:TIGR02168 495 ---ERLQENLEGFSEGVKALLKnqsGLSGILGVlseliSVDEGYEAAIeaALGGRLQAVVVEN----LNAAKKAIAFLKQ 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1501 ANASR----------GQVEQANQelRELIQNVKDFLSQeGADPDSIEMVATRVLD-----ISIPASPEQIQRLASEIAER 1565
Cdd:TIGR02168 568 NELGRvtflpldsikGTEIQGND--REILKNIEGFLGV-AKDLVKFDPKLRKALSyllggVLVVDDLDNALELAKKLRPG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1566 VR--SLaDVDTILAH---TMGDVRRAEQLLQdaqRARSRAEGERQKAET------VQAALEEAQRAQGAAQGAIRGAVVD 1634
Cdd:TIGR02168 645 YRivTL-DGDLVRPGgviTGGSAKTNSSILE---RRREIEELEEKIEELeekiaeLEKALAELRKELEELEEELEQLRKE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGnslaastAEETAGSAQSRAREAEKLREQVGDQYQT 1714
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE-------LEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1715 VRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1784
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1730-1799 |
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 1958794729 1730 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1799
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 1958794729 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 |
4.63e-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: 4.63e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 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 |
5.03e-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: 5.03e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958794729 786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 834
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1440-1733 |
2.18e-13 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 74.10 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1440 CGGLGCSGAAATADLALGRARHTQAELQRALVEgggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELI 1519
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1520 QNVKD----------FLSQEGADPDSIEMVATrvldisipaspeqiqrlASEIAERVRSLADVDTIlahtmgdVRRAEQL 1589
Cdd:COG3883 79 AEIEErreelgerarALYRSGGSVSYLDVLLG-----------------SESFSDFLDRLSALSKI-------ADADADL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1590 LQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHAL 1669
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1670 LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARA 1733
Cdd:COG3883 215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1477-1791 |
2.80e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQ 1556
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1557 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLL-----QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgA 1631
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-Q 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1632 VVDTKNTEQTLQQVQERM------------AGTEQSLNSASERARQLHALLEAL------KLKRAGNSLAASTAEETAGS 1693
Cdd:COG4717 232 LENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1694 AQSRAREAEKLR-------------EQVGDQYQTVRALAERKAEGV-LAAQARAEQLRDEARGLLQAAQ----DKLQRLQ 1755
Cdd:COG4717 312 ALEELEEEELEEllaalglppdlspEELLELLDRIEELQELLREAEeLEEELQLEELEQEIAALLAEAGvedeEELRAAL 391
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958794729 1756 ELEGTYEENERELEVKAAQLDGLEARMRSVLQAINL 1791
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1449-1795 |
3.26e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 75.38 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1449 AATADLALGRARHtQAELQRALVEGGGILSRVSETRRQAEEAQQRA---QAALDKANASRGQVEQANQELRELIQNVKDF 1525
Cdd:PRK04863 265 ESTNYVAADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1526 LSQEGAdpdsIEMVATRVLDISIPA-SPEQIQRLASEIAERVRSLA-----DVDTiLAHTMGDVRRAEQLLQdaqrarSR 1599
Cdd:PRK04863 344 LRQQEK----IERYQADLEELEERLeEQNEVVEEADEQQEENEARAeaaeeEVDE-LKSQLADYQQALDVQQ------TR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1600 AeGERQKAetvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlHAllEALKL-KRA 1678
Cdd:PRK04863 413 A-IQYQQA---VQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ-FE--QAYQLvRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1679 GNSLAASTAEETAGSAQSRAREAEKLREQVGdqyQTVRALAErkAEGVLAAQARAEQLRDEArglLQAAQDKLQRLQELE 1758
Cdd:PRK04863 486 AGEVSRSEAWDVARELLRRLREQRHLAEQLQ---QLRMRLSE--LEQRLRQQQRAERLLAEF---CKRLGKNLDDEDELE 557
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958794729 1759 GTYEENERELEVKAAQLDGLEARmRSVLQAINLQVQI 1795
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARER-RMALRQQLEQLQA 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1456-1788 |
6.27e-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: 74.33 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1456 LGRARHTQAELQRALVEGGGILSRVSETRRQAE-------EAQQRAQ----AALDKANASRGQVEQANQELRELIQNVKD 1524
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYEGyellKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1525 FLSQEGADPDSIEmvatRVLDisipASPEQIQRLASEIAERVRS-LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGE 1603
Cdd:TIGR02169 259 EISELEKRLEEIE----QLLE----ELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1604 RQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL----QQVQERMAGTEQSLNSASERarqlhalLEALKLKRag 1679
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETRDELKDYREK-------LEKLKREI-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1680 nslaastaEETAGSAQSRAREAEKLREQVGDqyqtVRALAERKAEGVLAAQARAEQLRDE---ARGLLQAAQDKL----Q 1752
Cdd:TIGR02169 402 --------NELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEikkQEWKLEQLAADLskyeQ 469
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958794729 1753 RLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1788
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1455-1788 |
6.79e-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: 74.22 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1455 ALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA--------------QAALDKANASRGQVEQANQELREliq 1520
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAeeevdslksqladyQQALDVQQTRAIQYQQAVQALEK--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1521 nvkdflSQE--GADPDSIEMVATRVldisipaspEQIQRLASEIAERVRSLadvdtilahtmgdvrraEQLLQDAQRARS 1598
Cdd:COG3096 425 ------ARAlcGLPDLTPENAEDYL---------AAFRAKEQQATEEVLEL-----------------EQKLSVADAARR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1599 R------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:COG3096 473 QfekayelvckiaGEVERSQAwQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1664 RQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKLREQVGDQYQTVRAlaerKAEGVLAAQARAEQLRDEARGL 1743
Cdd:COG3096 553 EELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQLEQLRARIKELAA----RAPAWLAAQDALERLREQSGEA 621
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1744 LQAAQDKLQRLQELegtyEENERELEVK----AAQLDGLEARMRSVLQA 1788
Cdd:COG3096 622 LADSQEVTAAMQQL----LEREREATVErdelAARKQALESQIERLSQP 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1458-1790 |
1.07e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1458 RARHTQAELQRALVEGG-GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVkdflsQEGADPDSI 1536
Cdd:COG4717 171 ELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1537 EMVATRVLDISIPASpeqIQRLASEIAERVRSLADVDTI---LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvQAA 1613
Cdd:COG4717 246 KEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLvlgLLALLFLLLAREKASLGKEAEELQALPALEELE--EEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1614 LEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsaseRARQLHALLEALkLKRAGnslaaSTAEETAGS 1693
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAAL-LAEAG-----VEDEEELRA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1694 AQSRAREAEKLRE-------QVGDQYQTVRALAERKAEGVLAAQ-ARAEQLRDEARGLLQAAQDKL----QRLQELE--G 1759
Cdd:COG4717 390 ALEQAEEYQELKEeleeleeQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELaeleAELEQLEedG 469
|
330 340 350
....*....|....*....|....*....|....
gi 1958794729 1760 TYEENERELEVKAAQLDGLE---ARMRSVLQAIN 1790
Cdd:COG4717 470 ELAELLQELEELKAELRELAeewAALKLALELLE 503
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1789 |
1.17e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 73.71 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1446 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1524
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1525 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1591
Cdd:NF041483 984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1592 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1654
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1655 SLNsasERARQLHAllEAlkLKRAGNSLAA--STAEETAGSAQSRAREaekLREQVGDQYQTVRALAERKAEGVL--AAQ 1730
Cdd:NF041483 1136 ELH---ERARRESA--EQ--MKSAGERCDAlvKAAEEQLAEAEAKAKE---LVSDANSEASKVRIAAVKKAEGLLkeAEQ 1205
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794729 1731 ARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1789
Cdd:NF041483 1206 KKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1450-1778 |
1.22e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1450 ATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALdkaNASRGQVEQANQELRELIQNVKDflsqe 1529
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLAN----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1530 gadpdsiemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLqdaqrarSRAEGERQKAET 1609
Cdd:TIGR02168 314 --------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1610 VQAALEEAQRAQgaaqgaiRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALklkraGNSLAASTAEE 1689
Cdd:TIGR02168 373 RLEELEEQLETL-------RSKVAQLELQIASLNNEIERL---EARLERLEDRRERLQQEIEEL-----LKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1690 TAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEgvlaaqarAEQLRDEARGLLQAAQ---DKLQRLQELEGTYEENER 1766
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEE--------AEQALDAAERELAQLQarlDSLERLQENLEGFSEGVK 509
|
330
....*....|..
gi 1958794729 1767 ELEVKAAQLDGL 1778
Cdd:TIGR02168 510 ALLKNQSGLSGI 521
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1452-1783 |
2.00e-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: 72.68 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1452 ADLALGRARhtQAELQRALVEGGGILSRVSETRRQAEEAQQ-----RAQAAL-------DKANASRGQVEQANQELRELI 1519
Cdd:COG3096 836 AELAALRQR--RSELERELAQHRAQEQQLRQQLDQLKEQLQllnklLPQANLladetlaDRLEELREELDAAQEAQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1520 QN------VKDFLSQEGADPDSIEMVATRVLDISipASPEQIQRLA---SEIAERVRSLA--DVDTILAHTMGDVRRAEQ 1588
Cdd:COG3096 914 QHgkalaqLEPLVAVLQSDPEQFEQLQADYLQAK--EQQRRLKQQIfalSEVVQRRPHFSyeDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1589 LLQDAQRARSRAegeRQKAETVQAALEEAQRAQGAAQGAIrgavvDTKNteQTLQQVQERMAGTEQSLNS-ASERAR--- 1664
Cdd:COG3096 992 RLEQAEEARREA---REQLRQAQAQYSQYNQVLASLKSSR-----DAKQ--QTLQELEQELEELGVQADAeAEERARirr 1061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1665 -QLHALLEALKLKRagNSLAASTA--EETAGSAQSRAREAEK----LREQV---GDQYQTVRALA-----ERK-AEGVLA 1728
Cdd:COG3096 1062 dELHEELSQNRSRR--SQLEKQLTrcEAEMDSLQKRLRKAERdykqEREQVvqaKAGWCAVLRLArdndvERRlHRRELA 1139
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1729 AQArAEQLR---DEARGLLQAAQDKLQRLQELEGTYEEN---ERELEVKAAQLDGLEARMR 1783
Cdd:COG3096 1140 YLS-ADELRsmsDKALGALRLAVADNEHLRDALRLSEDPrrpERKVQFYIAVYQHLRERIR 1199
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1448-1768 |
2.22e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 72.55 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1514
Cdd:NF041483 478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1515 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDAq 1594
Cdd:NF041483 558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADA- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1595 rarsRAEGERQKAEtvqaALEEAQRAQGAAQGAIRgavvdtknteqTLQQVQERMAgteqslnsasERARQLHAllealk 1674
Cdd:NF041483 599 ----RAEAERIRRE----AAEETERLRTEAAERIR-----------TLQAQAEQEA----------ERLRTEAA------ 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1675 lkrAGNSLAASTAEETAGSAQSRA-REAEKLREQVGDQYQTVRA----LAER----KAEGVLAAQARAEQLRDEARGLLQ 1745
Cdd:NF041483 644 ---ADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAeaaaAAERvgteAAEALAAAQEEAARRRREAEETLG 720
|
330 340
....*....|....*....|...
gi 1958794729 1746 AAQDKLQrlQELEGTYEENEREL 1768
Cdd:NF041483 721 SARAEAD--QERERAREQSEELL 741
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1463-1757 |
5.88e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1463 QAELQRALVEGGGilSRVSETRRQAEEAQQRA----------QAALDKANASRGQVEQANQELRE----------LIQNV 1522
Cdd:PRK04863 363 RLEEQNEVVEEAD--EQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1523 KDFLSQEGADPDSiemVATRVLDIsipaspEQIQRLASEIAER-------VRSLAD-VDTILAHtmgdvRRAEQLLQDA- 1593
Cdd:PRK04863 441 EDWLEEFQAKEQE---ATEELLSL------EQKLSVAQAAHSQfeqayqlVRKIAGeVSRSEAW-----DVARELLRRLr 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1594 -QRARS-RAEGERQKAETVQAALEEAQRAQGAAQGAIR--GAVVDTKNTEQTLQQVQE-RMAGTEQSLNSASERARQLHA 1668
Cdd:PRK04863 507 eQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlGKNLDDEDELEQLQEELEaRLESLSESVSEARERRMALRQ 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1669 LLEALKLKRAgnSLAASTAEETAgsAQSRareAEKLREQVGDQY---QTVRALAERKAEGVLAAQ-------ARAEQLRD 1738
Cdd:PRK04863 587 QLEQLQARIQ--RLAARAPAWLA--AQDA---LARLREQSGEEFedsQDVTEYMQQLLERERELTverdelaARKQALDE 659
|
330
....*....|....*....
gi 1958794729 1739 EARGLLQAAQDKLQRLQEL 1757
Cdd:PRK04863 660 EIERLSQPGGSEDPRLNAL 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1549-1781 |
7.98e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1549 PASPEQIQRLASEIAERVRSLADVdtilahtMGDVRRAEQLLQDAQRARSRAEgerQKAETVQAALEEAQRAQGAAQGAI 1628
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSL-------QSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1629 RGAVVDTKNTEQTLQQVQERMAGTEQSLnsaSERARQLHALLEALklkragNSLAASTAEEtagSAQSRAREAEKLREQV 1708
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARI---EELEEDLHKLEEAL------NDLEARLSHS---RIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1709 GDQYQTVRALaERKAEGVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELEGTYEENERELEVKAAQLDGLEAR 1781
Cdd:TIGR02169 808 SRIEARLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| 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 1958794729 1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1193
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1448-1796 |
1.80e-11 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 67.76 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQR----ALVEGGGIlsrvsetRRQAEEAQQRAQAAldkanasrgqVEQANQELRELIQNV- 1522
Cdd:COG1538 17 RAARARVEAARAQLRQARAGLlpsqELDLGGKR-------RARIEAAKAQAEAA----------EADLRAARLDLAAEVa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1523 KDFLSQEGADpdsiemvatRVLDISipaspEQIQRLASEIAERVRSLADVDTIlahTMGDVRRAEQLLQDAQRARSRAEG 1602
Cdd:COG1538 80 QAYFDLLAAQ---------EQLALA-----EENLALAEELLELARARYEAGLA---SRLDVLQAEAQLAQARAQLAQAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1603 ERQKAEtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAserARQLHALLEALKLKRAGN-- 1680
Cdd:COG1538 143 QLAQAR---NALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAA---EAQLEAAEAEIGVARAAFlp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1681 --SLAASTAEE------------------------TAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAE 1734
Cdd:COG1538 217 slSLSASYGYSssddlfsggsdtwsvglslslplfDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAR 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1735 QLRDEARGLLQAAQDKLQRLQELegtYEENERE-LEVKAAQLDGLEARMRSV---LQAINLQVQIY 1796
Cdd:COG1538 297 EQLEALEEALEAAEEALELARAR---YRAGLASlLDVLDAQRELLQAQLNLIqarYDYLLALVQLY 359
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-565 |
2.03e-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: 2.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958794729 524 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-564 |
2.84e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 2.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958794729 525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1458-1763 |
3.39e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.70 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1458 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1529
Cdd:NF041483 158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1530 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1607
Cdd:NF041483 234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 ETVQAALEEAQRAQGAAQGAIRGAVVD--------TKNTEQTL----QQVQERMAGTEQSLNSASERARQLHALLEALKL 1675
Cdd:NF041483 287 EAKEAAAKQLASAESANEQRTRTAKEEiarlvgeaTKEAEALKaeaeQALADARAEAEKLVAEAAEKARTVAAEDTAAQL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1676 KRagnslAASTAEETAGSAQSRAR-------------------EAEKLREQVGDQYQTVRALA-----ERKAEGV-LAAQ 1730
Cdd:NF041483 367 AK-----AARTAEEVLTKASEDAKattraaaeeaerirreaeaEADRLRGEAADQAEQLKGAAkddtkEYRAKTVeLQEE 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958794729 1731 AR-----AEQLRDEA-------RGllQAAQDKLQRLQELEGTYEE 1763
Cdd:NF041483 442 ARrlrgeAEQLRAEAvaegeriRG--EARREAVQQIEEAARTAEE 484
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1456-1797 |
3.54e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.23 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1456 LGRARhtqAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELreliQNVKDFLSQegadpds 1535
Cdd:COG4372 8 VGKAR---LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL----EQLEEELEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1536 iemvatrvldisipaSPEQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKaetVQAALE 1615
Cdd:COG4372 71 ---------------ARSELEQLEEELEELNEQLQAAQAELA-------QAQEELESLQEEAEELQEELEE---LQKERQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1616 EAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsasERARQLHALLEALKLKRAGNSLaASTAEETAGSAQ 1695
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL----AALEQELQALSEAEAEQALDEL-LKEANRNAEKEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 SRAREAEKLREQVGDQYQTVRALA-ERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1774
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKdSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
330 340
....*....|....*....|...
gi 1958794729 1775 LDGLEARMRSVLQAINLQVQIYN 1797
Cdd:COG4372 281 AALELEALEEAALELKLLALLLN 303
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1449-1775 |
4.48e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1449 AATADLALGR-ARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFls 1527
Cdd:PRK04863 332 AASDHLNLVQtALRQQEKIERYQAD-------LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADY-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 QEGadpdsIEMVATRVLdisipaspeQIQRlASEIAERVRSLADVDTILAHTMGD---------------VRRAEQLLQD 1592
Cdd:PRK04863 403 QQA-----LDVQQTRAI---------QYQQ-AVQALERAKQLCGLPDLTADNAEDwleefqakeqeateeLLSLEQKLSV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1593 AQRARSR------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLN 1657
Cdd:PRK04863 468 AQAAHSQfeqayqlvrkiaGEVSRSEAwDVARELLRRLreQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1658 SASERARQLHALLEALKLKRAGNSLAASTAEEtagsaqsRAREAEKLREQVGDQYQTVRALAERkaegVLAAQARAEQLR 1737
Cdd:PRK04863 548 KNLDDEDELEQLQEELEARLESLSESVSEARE-------RRMALRQQLEQLQARIQRLAARAPA----WLAAQDALARLR 616
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958794729 1738 D-------EARGLLQAAQDKLQRLQEL---EGTYEENERELEVKAAQL 1775
Cdd:PRK04863 617 EqsgeefeDSQDVTEYMQQLLERERELtveRDELAARKQALDEEIERL 664
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1464-1787 |
5.26e-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: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1464 AELQRALVEgggILSRVSETRRQ---AEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGAD-------- 1532
Cdd:pfam01576 218 TDLQEQIAE---LQAQIAELRAQlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqr 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1533 ---PDSIEMVATRVLDI--SIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRR---------AEQLLQdAQRARS 1598
Cdd:pfam01576 295 rdlGEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelTEQLEQ-AKRNKA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1599 RAEGERQKAETVQAAL-EEAQRAQGAAQGAIRGavvdTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL---- 1673
Cdd:pfam01576 374 NLEKAKQALESENAELqAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssll 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1674 -----KLKRAGNSLAASTA----------EET----AGSAQSRAREAEK--LREQVGDQYQTVRALaERKAEGVLAAQAR 1732
Cdd:pfam01576 450 neaegKNIKLSKDVSSLESqlqdtqellqEETrqklNLSTRLRQLEDERnsLQEQLEEEEEAKRNV-ERQLSTLQAQLSD 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1733 AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyeenERELEVKAAQLDGLEaRMRSVLQ 1787
Cdd:pfam01576 529 MKKKLEEDAGTLEALEEGKKRLQrELEAL----TQQLEEKAAAYDKLE-KTKNRLQ 579
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1482-1755 |
7.62e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.54 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1482 ETRRQAEEAQQRAQAALDKANASRGQV-EQANQELRELIQNVKDFLSQEGADPDSIEMVATrvldisipaspEQIQRLAS 1560
Cdd:NF041483 441 EARRLRGEAEQLRAEAVAEGERIRGEArREAVQQIEEAARTAEELLTKAKADADELRSTAT-----------AESERVRT 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 EIAERVRSLAdvdtilahtmgdvRRAEQLLQdaqraRSRAEGERQKAEtvqaALEEAQRAQGAAQGAIRgavvdtKNTEQ 1640
Cdd:NF041483 510 EAIERATTLR-------------RQAEETLE-----RTRAEAERLRAE----AEEQAEEVRAAAERAAR------ELREE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1641 TLQQVQERMAgteqslNSASERARqLHALLEAlKLKRAGNSLAASTAEeTAGSAQSRAREAEKLREQVGDQYQTVRALAE 1720
Cdd:NF041483 562 TERAIAARQA------EAAEELTR-LHTEAEE-RLTAAEEALADARAE-AERIRREAAEETERLRTEAAERIRTLQAQAE 632
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1721 RKAEGVL------AAQARAE------QLRDEARG----LLQAAQDKLQRLQ 1755
Cdd:NF041483 633 QEAERLRteaaadASAARAEgenvavRLRSEAAAeaerLKSEAQESADRVR 683
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
413-470 |
8.44e-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: 8.44e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 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 1958794729 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1769 |
1.31e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.77 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1446 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1521
Cdd:NF041483 720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1522 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1600
Cdd:NF041483 787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1601 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1670
Cdd:NF041483 843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1671 --EALKLKRAGNSLAASTAEETAGSAQSR----AREAEKLREQVGDQYQTVRALAerkAEGVLAAQARAEQLRDEARGLL 1744
Cdd:NF041483 923 tsEAERLTAEARAEAERLRDEARAEAERVradaAAQAEQLIAEATGEAERLRAEA---AETVGSAQQHAERIRTEAERVK 999
|
330 340
....*....|....*....|....*
gi 1958794729 1745 QAAQDKLQRLQelEGTYEENERELE 1769
Cdd:NF041483 1000 AEAAAEAERLR--TEAREEADRTLD 1022
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1787 |
1.77e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFL--SQEGADPDSIEMVATRvldisipAS 1551
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEAeaAEEKAEAAEKKKEEAK-------KK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1552 PEQIQRLASEI--AERVRSLADVDTILAHtmgDVRRAEQLLQDAQRARSRAEgERQKAETVQAALEEAQRAQGAAQGA-- 1627
Cdd:PTZ00121 1380 ADAAKKKAEEKkkADEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAee 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1628 IRGAVVDTKNTEQT-----LQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSlaASTAEETAGSAQSR----A 1698
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE--AKKAEEAKKADEAKkaeeA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1699 REAEKLR--EQVGDQYQTVRALAERKAEGVLAAQA--RAEQLRDEA-RGLLQAAQDKLQRLQELEGTYEEN--------- 1764
Cdd:PTZ00121 1534 KKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEakKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEEkkmkaeeak 1613
|
330 340
....*....|....*....|....
gi 1958794729 1765 -ERELEVKAAQLDGLEARMRSVLQ 1787
Cdd:PTZ00121 1614 kAEEAKIKAEELKKAEEEKKKVEQ 1637
|
|
| 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 1958794729 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 |
2.89e-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: 2.89e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 1095
Cdd:pfam00053 1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| 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 1958794729 1443 LGCSGAAATADlalgRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV 1522
Cdd:COG4942 10 LLALAAAAQAD----AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1523 KDFLSQEGADPDSIE----MVATRVLDISIPASPEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRA 1596
Cdd:COG4942 86 AELEKEIAELRAELEaqkeELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1597 RSRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLK 1676
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|...
gi 1958794729 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 1958794729 834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 882
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1775 |
3.16e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1477 LSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisiPASPEQIQ 1556
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEE-----------AKKADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1557 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLLQDAQRARsRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVD 1634
Cdd:PTZ00121 1451 KKAEEAkkAEEAKKKAE----------EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA---REAEKLR-EQVGD 1710
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeeaKKAEEARiEEVMK 1599
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1711 QYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYE--ENERELEVKAAQL 1775
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEE 1666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1449-1794 |
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 1958794729 1449 AATADLALGRARHTQAELQRALVEgggilsrvsETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdfLSQ 1528
Cdd:COG4913 271 LAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAELERL---EARLDALREELDELEAQI---RGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1529 EGADPDSIE--------------------MVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQ 1588
Cdd:COG4913 336 GGDRLEQLEreierlereleererrrarlEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1589 LLQDAQRARSRAEGER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRG------ 1630
Cdd:COG4913 413 ALRDLRRELRELEAEIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltll 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1631 ----------AVVDTKNTEQTLQ--------QVQERMAGTEQSL----------------------------NSASE--- 1661
Cdd:COG4913 493 vppehyaaalRWVNRLHLRGRLVyervrtglPDPERPRLDPDSLagkldfkphpfrawleaelgrrfdyvcvDSPEElrr 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1662 ------RARQLH-------------------------ALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKLREQVGD 1710
Cdd:COG4913 573 hpraitRAGQVKgngtrhekddrrrirsryvlgfdnrAKLAALEAELA-------ELEEELAEAEERLEALEAELDALQE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1711 QYQTVRALAERKAE--GVLAAQARAEQLRDEaRGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1788
Cdd:COG4913 646 RREALQRLAEYSWDeiDVASAEREIAELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
....*.
gi 1958794729 1789 INLQVQ 1794
Cdd:COG4913 725 AEEELD 730
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1584-1791 |
4.23e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1584 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1664 RQLHALLEAL--KLKRAGNS------LAASTAEETAGSA-------QSRAREAEKLREQVGDQYQTVRALAERKAE---- 1724
Cdd:COG4942 100 EAQKEELAELlrALYRLGRQpplallLSPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAERAEleal 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1725 --GVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELegtyEENERELEVKAAQLDGLEARMRSVLQAINL 1791
Cdd:COG4942 180 laELEEERAALEALKAERQKLLARLEKELaelaAELAEL----QQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1199-1794 |
4.54e-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: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1199 DWDRVVQDLAARTRRLeqwAQELQQTGVLGAFESSFLNLQGKLGMVQAiVAARNTSAASTAKLVEATEGLRHEIgktTER 1278
Cdd:TIGR00618 308 QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTL---TQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1279 LTQLEAELTDVQDENFNANHALSGLERD-GLALNLTLRQLDQHLDILkhsnflgaydsirHAHSQSTEAERRANASTFAI 1357
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLA-------------HAKKQQELQQRYAELCAAAI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1358 pSPVSNSADTRRRAEVLMgAQRENFNRQHLANQQALGRLSTHTHTLSLTGVNELvcgapgdapcATSPCggagcrdedgq 1437
Cdd:TIGR00618 448 -TCTAQCEKLEKIHLQES-AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL----------QEEPC----------- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1438 PRCGGLGCSGAAATADLALG-------RARHTQAELQRALV----EGGGILSRVSETRRQAEEAQQRAQAALDKANASRG 1506
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGpltrrmqRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1507 QVEQanqeLRELIQNVKDFLSQEGADPDSIEMVATRVLdisIPASPEQ-IQRLASEIAERVRSLADVDTILAhtmgdvRR 1585
Cdd:TIGR00618 585 DIPN----LQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQdLQDVRLHLQQCSQELALKLTALH------AL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1586 AEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQGAAQGairgavvdtknTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:TIGR00618 652 QLTLTQERVREHALSirVLPKELLASRQLALQKMQSEKEQLTY-----------WKEMLAQCQTLLRELETHIEEYDREF 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1664 RQLHALLEALKLKRAGNSlaaSTAEETAGSAQSRAREaeKLREQVGDQyqtvralaERKAEGVLAAQARaeqlrdeargl 1743
Cdd:TIGR00618 721 NEIENASSSLGSDLAARE---DALNQSLKELMHQART--VLKARTEAH--------FNNNEEVTAALQT----------- 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1744 lqaaqdkLQRLQELEGTYEENERELEVKAAQLDGLEARMR----SVLQAINLQVQ 1794
Cdd:TIGR00618 777 -------GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCE 824
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1463-1783 |
5.48e-10 |
|
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: 64.39 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1463 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1521
Cdd:pfam07111 354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1522 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1592
Cdd:pfam07111 434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1593 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1672
Cdd:pfam07111 508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1673 LKLKRagnslAASTAEETAGSA-QSRAREAE-KLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1735
Cdd:pfam07111 562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVEtRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1736 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1783
Cdd:pfam07111 634 rLQDEARK--EEGQRLARRVQEL-----ERDKNLMLATLQQEGLLSRYK 675
|
|
| 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 1958794729 1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1190
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1584-1797 |
7.81e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1584 RRAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG-------- 1651
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerqleel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1652 ------TEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQV-GDQYQTVRALAERKAE 1724
Cdd:TIGR02168 322 eaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1725 GVLA------AQARAEQLRDEARGLLQAAQDklQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1797
Cdd:TIGR02168 402 IERLearlerLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-523 |
8.36e-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: 8.36e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958794729 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 1958794729 1040 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 1096
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1553-1790 |
9.17e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIAERVRS------------LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEaqra 1620
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKdlherlngleseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1621 qgaaqgairgavvdtknteqtlqqVQERMAGTEQSLNSASERARQLHALLEALKLKRAGnSLAASTAEETAGSAQSRARE 1700
Cdd:PRK02224 263 ------------------------LRETIAETEREREELAEEVRDLRERLEELEEERDD-LLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1701 A-EKLREQVGDQYQTVRALAERKAEgvlaaqaRAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLE 1779
Cdd:PRK02224 318 ElEDRDEELRDRLEECRVAAQAHNE-------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
250
....*....|.
gi 1958794729 1780 ARMRSVLQAIN 1790
Cdd:PRK02224 391 EEIEELRERFG 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1200-1754 |
1.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1200 WDRVVQDLAARTRRLEQWAQELQQTgvlgafESSFLNLQGKLGMVQAIVAARntsaastaKLVEATEGLRHEIGKTTERL 1279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEEL------EAELEELREELEKLEKLLQLL--------PLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1280 TQLEAELTDVQDenfnanhalsgLERDGLALNLTLRQLDQHLDILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAIps 1359
Cdd:COG4717 149 EELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1360 pvsnsADTRRRAEVLMgAQRENFNRQHLAnQQALGRLSTHTHTLSLTGVnelvcgapgdapcatspcggagcrdedgqpR 1439
Cdd:COG4717 216 -----EEAQEELEELE-EELEQLENELEA-AALEERLKEARLLLLIAAA------------------------------L 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1440 CGGLGCSGAAATADLALGRArhtqaelqrALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasrgqveqANQELREli 1519
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGV---------LFLVLGLLALLFLLLAREKASLGKEAEELQALP---------ALEELEE-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1520 QNVKDFLSQEGADPD-SIEMVATRVLDIsipaspEQIQRLASEIAERVRSL------ADVDTILAHtmGDVRRAEQLLQD 1592
Cdd:COG4717 319 EELEELLAALGLPPDlSPEELLELLDRI------EELQELLREAEELEEELqleeleQEIAALLAE--AGVEDEEELRAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1593 AQRARSRAEgERQKAETVQAALEEAQRAQGAAQgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEA 1672
Cdd:COG4717 391 LEQAEEYQE-LKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1673 LklkragnslaastaeETAGSAQSRAREAEKLREQvgdqyqtVRALAERKAEGVLAAQArAEQLRDEAR-----GLLQAA 1747
Cdd:COG4717 465 L---------------EEDGELAELLQELEELKAE-------LRELAEEWAALKLALEL-LEEAREEYReerlpPVLERA 521
|
....*..
gi 1958794729 1748 QDKLQRL 1754
Cdd:COG4717 522 SEYFSRL 528
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1458-1775 |
1.04e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1458 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE 1537
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1538 mVATRVLDisipASPEQIQRLASEI--AERVRSLADVDTI-LAHTMGDVRRAEQLlQDAQRARsRAEgERQKAETVQAAL 1614
Cdd:PTZ00121 1168 -EARKAED----AKKAEAARKAEEVrkAEELRKAEDARKAeAARKAEEERKAEEA-RKAEDAK-KAE-AVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1615 EEAQRAQgaaqgairgavvDTKNTEQTLQQVQERMAGTEQSLNSA-SERARQLHALLEALKLKRAgNSLAASTAEETAGS 1693
Cdd:PTZ00121 1240 EEAKKAE------------EERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKKAEEKKKA-DEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1694 AQSRAREAEKlreqvGDQYQTVRALAERKAEgvlAAQARAEQLR--DEA-RGLLQAAQDKLQRLQELEGTYEENERELEV 1770
Cdd:PTZ00121 1307 AKKKAEEAKK-----ADEAKKKAEEAKKKAD---AAKKKAEEAKkaAEAaKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
....*
gi 1958794729 1771 KAAQL 1775
Cdd:PTZ00121 1379 KADAA 1383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1448-1794 |
1.13e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQRALVEgggiLSRVSETRRQAEEAQQRAQAALDKANASR-----GQVEQANQELRELIQNV 1522
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRleqleREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1523 KDFlsqegadpdsieMVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEG 1602
Cdd:COG4913 362 ARL------------EALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1603 ER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRG----------------AVVD 1634
Cdd:COG4913 427 EIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltllvppehyaaalRWVN 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1635 TKNTEQTLQ--------QVQERMAGTEQSL----------------------------NSASE---------RARQLH-- 1667
Cdd:COG4913 507 RLHLRGRLVyervrtglPDPERPRLDPDSLagkldfkphpfrawleaelgrrfdyvcvDSPEElrrhpraitRAGQVKgn 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1668 -----------------------ALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAE 1724
Cdd:COG4913 587 gtrhekddrrrirsryvlgfdnrAKLAALEAELA-------ELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1725 --GVLAAQARAEQLRDEARGL------LQAAQDKLQRLQ-----------ELEGTYEENERELEVKAAQLDGLEARMRSV 1785
Cdd:COG4913 660 eiDVASAEREIAELEAELERLdassddLAALEEQLEELEaeleeleeeldELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
....*....
gi 1958794729 1786 LQAINLQVQ 1794
Cdd:COG4913 740 EDLARLELR 748
|
|
| 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 1958794729 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1458-1790 |
1.53e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1458 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELREL---IQNVKDFLSQegadpd 1534
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAAN------ 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1535 siemVATRVldisipaspEQIQRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEGERQKAETVQAAL 1614
Cdd:TIGR02168 822 ----LRERL---------ESLERRIAATERRLEDLE-------------EQIEELSEDIESLAAEIEELEELIEELESEL 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1615 EEAQRAQGAAqgairgavvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEetagsa 1694
Cdd:TIGR02168 876 EALLNERASL--------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE------ 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1695 QSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRdeargllqaaqDKLQRL--------QELEgtyEENER 1766
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----------NKIKELgpvnlaaiEEYE---ELKER 1001
|
330 340
....*....|....*....|....
gi 1958794729 1767 eLEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:TIGR02168 1002 -YDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1447-1795 |
1.65e-09 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 62.62 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1447 GAAATADLALGRARHTQAELQRALVegggILSRVSETRRQAEEAQ--QRA------QAALDKANASRGQVEQANQELREL 1518
Cdd:COG5278 23 VLGVLSYLSLNRLREASEWVEHTYE----VLRALEELLSALLDAEtgQRGylltgdESFLEPYEEARAEIDELLAELRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1519 I-------QNVKDF----------------LSQEGADPDSIEMVAT----------RVLDISIPASPEQIQRLASEIAER 1565
Cdd:COG5278 99 TadnpeqqARLDELealidqwlaeleqviaLRRAGGLEAALALVRSgegkalmdeiRARLLLLALALAALLLAAAALLLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1566 VRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQV 1645
Cdd:COG5278 179 LLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1646 QERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEG 1725
Cdd:COG5278 259 LAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALA 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1726 VLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1795
Cdd:COG5278 339 AAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAA 408
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1462-1780 |
1.71e-09 |
|
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: 62.01 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1462 TQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGADPDSIEMVAT 1541
Cdd:pfam19220 39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE--AEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1542 RvldisipASPEQIQRLASEIAERVRSLADvdtilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQ 1621
Cdd:pfam19220 117 T-------AQAEALERQLAAETEQNRALEE----------ENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1622 gaaqgairgavvdTKNTEQTLQQVQE---RMAGTEQSLNSASERARQLHAllealklkragnSLAASTAEetagsaqsRA 1698
Cdd:pfam19220 180 -------------QALSEEQAAELAEltrRLAELETQLDATRARLRALEG------------QLAAEQAE--------RE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1699 REAEKLREQVGdQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLqaaQDKLQRLQELEGTYEENERELEVKAAQLDGL 1778
Cdd:pfam19220 227 RAEAQLEEAVE-AHRAERASLRMKLEALTARAAATEQLLAEARNQL---RDRDEAIRAAERRLKEASIERDTLERRLAGL 302
|
..
gi 1958794729 1779 EA 1780
Cdd:pfam19220 303 EA 304
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1590-1795 |
1.83e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1590 LQDAQRARSRAEGerQKAETVQAALEEAQRAQGAAQGAIRgavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHAL 1669
Cdd:COG4717 51 LEKEADELFKPQG--RKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1670 LEALKLKRAGNSLAASTAEETagsaqsraREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQD 1749
Cdd:COG4717 125 LQLLPLYQELEALEAELAELP--------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1750 KLQRLQELEGTYEENERELEVKAAQLDGLEARMRSV---LQAINLQVQI 1795
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLeneLEAAALEERL 245
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1556-1763 |
2.05e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.92 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1618
Cdd:NF041483 130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1619 RAQGAAQGAIRGAVVDTK---NTEQTlqQVQERMAGTEQ---SLNSASERARQLHALL------------EALKLKRAGN 1680
Cdd:NF041483 204 SARAEAEAILRRARKDAErllNAAST--QAQEATDHAEQlrsSTAAESDQARRQAAELsraaeqrmqeaeEALREARAEA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1681 SLAASTAEETAG----SAQS----RAREA-EKLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDEA--RGLLQAAQ 1748
Cdd:NF041483 282 EKVVAEAKEAAAkqlaSAESaneqRTRTAkEEIARLVGEATKEAEALKA-EAEQALAdARAEAEKLVAEAaeKARTVAAE 360
|
250
....*....|....*
gi 1958794729 1749 DKLQRLQELEGTYEE 1763
Cdd:NF041483 361 DTAAQLAKAARTAEE 375
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
412-471 |
2.23e-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: 2.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 471
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1731-1800 |
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 1958794729 1731 ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1800
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1479-1771 |
2.89e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisipaspeqiQRL 1558
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE------------------ARK 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1559 ASEI--AERVRSLADvdtilAHTMGDVRRAEQLLQDAQRARS------RAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1630
Cdd:PTZ00121 1280 ADELkkAEEKKKADE-----AKKAEEKKKADEAKKKAEEAKKadeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1631 AVVDTKNTEQTLQQVQERmagTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE-ETAGSAQSRAREAEKLREQV- 1708
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKk 1431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1709 -GDQYQTvRALAERKAEgvlAAQARAEQLRdEARGLLQAAQDKlQRLQELEGTYEENERELEVK 1771
Cdd:PTZ00121 1432 kADEAKK-KAEEAKKAD---EAKKKAEEAK-KAEEAKKKAEEA-KKADEAKKKAEEAKKADEAK 1489
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1478-1784 |
2.91e-09 |
|
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: 62.28 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1478 SRVSETRRQAEE-AQQRAQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-I 1555
Cdd:COG3096 785 KRLEELRAERDElAEQYAKASFDV------------QKLQRLHQAFSQFVGGH--------------LAVAFAPDPEAeL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRAQG--AAQGAi 1628
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQEAQAfiQQHGK- 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1629 RGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEETAGSAQSRAREaEKLREQV 1708
Cdd:COG3096 918 ALAQLEPL--VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS-EVVQRRPHFSYEDAVGLLGENSDLN-EKLRARL 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1709 gdqyqtvralaerkaegvlaaqARAEQLRDEARGLLQAAQDKL----QRLQELEGTYE-------ENERELEVKAAQLD- 1776
Cdd:COG3096 994 ----------------------EQAEEARREAREQLRQAQAQYsqynQVLASLKSSRDakqqtlqELEQELEELGVQADa 1051
|
....*...
gi 1958794729 1777 GLEARMRS 1784
Cdd:COG3096 1052 EAEERARI 1059
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
525-564 |
3.09e-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: 54.28 E-value: 3.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958794729 525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1454-1774 |
3.11e-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: 61.45 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1454 LALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEQANQELRELIQNVKDFLSQEGADP 1533
Cdd:pfam07888 24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD-------REQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1534 DSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARsRAEGERQKAET---- 1609
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK-KAGAQRKEEEAerkq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaaSTAEE 1689
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR----------SLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1690 TAGSAQSRAREAEKLREQVGDQYQTVRAL-------AE---RKAEGVLAAQARAEQLRDEARGLLQAAQ---DKLQRL-- 1754
Cdd:pfam07888 246 LNASERKVEGLGEELSSMAAQRDRTQAELhqarlqaAQltlQLADASLALREGRARWAQERETLQQSAEadkDRIEKLsa 325
|
330 340
....*....|....*....|....*
gi 1958794729 1755 --QELEGTYEEN--ERE-LEVKAAQ 1774
Cdd:pfam07888 326 elQRLEERLQEErmEREkLEVELGR 350
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1448-1748 |
3.33e-09 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 61.57 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLAlGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDfls 1527
Cdd:COG0840 273 AASAEELA-AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 qegadpdsiemVATRVLDISipASPEQIqrlaSEIaervrsladVDTIlahtmGDVrrAEQ--LLQ-----DAQRArsra 1600
Cdd:COG0840 349 -----------TAETIEELG--ESSQEI----GEI---------VDVI-----DDI--AEQtnLLAlnaaiEAARA---- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1601 eGE------------RQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1668
Cdd:COG0840 392 -GEagrgfavvadevRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1669 LLEalklkragnSLAASTAEETAGSaqsrareaeklrEQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQ 1748
Cdd:COG0840 471 LIQ---------EIAAASEEQSAGT------------EEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1550-1781 |
3.38e-09 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 61.59 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1550 ASPEQIQRLASEIAERVRSLADVDTILAhtMGDVRRAEQllqdaQRARSRAEGERQKAETVqaalEEAQRAQGAAqgair 1629
Cdd:COG3064 19 EQAEAEKRAAAEAEQKAKEEAEEERLAE--LEAKRQAEE-----EAREAKAEAEQRAAELA----AEAAKKLAEA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1630 gavvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNslAASTAEETA-GSAQSRAREAEKLREQV 1708
Cdd:COG3064 83 ---------EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AKRKAEEEAkRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1709 GDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEAR 1781
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAAR 224
|
|
| 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 1958794729 1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1143
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1205-1763 |
3.73e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1205 QDLAARTRRLEQWAQELQQtgVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEATEGLRHEIGKTTERLTQLEA 1284
Cdd:COG1196 344 EELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1285 ELTDVQDEnfnanhaLSGLERDGLALNLTLRQLDQHLdilkhsnfLGAYDSIRHAHSQSTEAERRANAstfaipspvSNS 1364
Cdd:COG1196 422 ELEELEEA-------LAELEEEEEEEEEALEEAAEEE--------AELEEEEEALLELLAELLEEAAL---------LEA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1365 ADTRRRAEVLMGAQRENFNRQHLANQQALGRlsththtlsltgvnelvcgapgdapcatspcGGAGCRDEDGQPRCGGLG 1444
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLE-------------------------------GVKAALLLAGLRGLAGAV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1445 csgaaatADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAA------LDKANASRGQVEQANQELREL 1518
Cdd:COG1196 527 -------AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1519 IQNVKDFLSQEGADPDSIEmVATRVLDISIPASPEQIQRLASEIAERVRS-LADVDTILAHTMGDVRRAEQLLQDAQRAR 1597
Cdd:COG1196 600 AVDLVASDLREADARYYVL-GDTLLGRTLVAARLEAALRRAVTLAGRLREvTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1598 SRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKR 1677
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEA-------EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1678 AgnsLAASTAEETAGSAQSRAREAEKLREQVG-------DQYQtvrALAERKAEgvlaaqaRAEQLRD--EARGLLQAAQ 1748
Cdd:COG1196 752 A---LEELPEPPDLEELERELERLEREIEALGpvnllaiEEYE---ELEERYDF-------LSEQREDleEARETLEEAI 818
|
570 580
....*....|....*....|
gi 1958794729 1749 DKL-----QRLQElegTYEE 1763
Cdd:COG1196 819 EEIdretrERFLE---TFDA 835
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1788 |
3.83e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.15 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1459 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1533
Cdd:NF041483 252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1534 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1598
Cdd:NF041483 326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1599 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1650
Cdd:NF041483 401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1651 GTEQSLNSA--------------SERARQlHALLEALKLKRagnslaasTAEETAgsaqSRAR-EAEKLREQVGDQYQTV 1715
Cdd:NF041483 481 TAEELLTKAkadadelrstataeSERVRT-EAIERATTLRR--------QAEETL----ERTRaEAERLRAEAEEQAEEV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1716 RALAERKA-----EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSv 1785
Cdd:NF041483 548 RAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT- 626
|
...
gi 1958794729 1786 LQA 1788
Cdd:NF041483 627 LQA 629
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1553-1790 |
3.93e-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: 61.73 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIA---ERVRSLADVDTILAHTMGDV----RRAEQLLQDAQRARSRAEGE---------------------- 1603
Cdd:pfam01576 159 ERISEFTSNLAeeeEKAKSLSKLKNKHEAMISDLeerlKKEEKGRQELEKAKRKLEGEstdlqeqiaelqaqiaelraql 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1604 RQKAETVQAAL---EEAQRAQGAAQGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK------ 1674
Cdd:pfam01576 239 AKKEEELQAALarlEEETAQKNNALKKIREL-------EAQISELQEDLESERAARNKAEKQRRDLGEELEALKteledt 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1675 --------------------LKRAGNSLAASTAEETAGSAQSRAREAEKLREQVgDQYQTVRALAErKAEGVLAAQaRAE 1734
Cdd:pfam01576 312 ldttaaqqelrskreqevteLKKALEEETRSHEAQLQEMRQKHTQALEELTEQL-EQAKRNKANLE-KAKQALESE-NAE 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1735 qLRDEARGLLQAAQDKLQR-------LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:pfam01576 389 -LQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1097-1144 |
4.20e-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: 4.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1097 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1144
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1485-1783 |
4.86e-09 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 60.82 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQN--VKDFLSQEGADPDSIEMVAtrvldisipaspEQIQRLASEI 1562
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEerLAELEAKRQAEEEAREAKA------------EAEQRAAELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1563 AERVRSLADVDTILAHTMGDV--------RRAEQLLQdAQRARSRAEGE-----RQKAETvQAALEEAQRAQGAAQGAIR 1629
Cdd:COG3064 73 AEAAKKLAEAEKAAAEAEKKAaaekakaaKEAEAAAA-AEKAAAAAEKEkaeeaKRKAEE-EAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1630 GAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEKLREQVG 1709
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAA----AAALAAAAAAAAADAALLALAVAARAA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1710 DQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1783
Cdd:COG3064 227 AASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDS 300
|
|
| 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 1958794729 1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 1095
Cdd:smart00180 1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1455-1788 |
1.04e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1455 ALGRARHTQA-ELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQV--------------EQANQELRELI 1519
Cdd:pfam01576 629 AEAREKETRAlSLARALEE-------ALEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskralEQQVEEMKTQL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1520 QNVKDFLsQEGADpdsiemvATRVLDISIPASPEQIQRLAS---EIAE-RVRSLADvdtilahtmgDVRRAEQLLQDAQR 1595
Cdd:pfam01576 702 EELEDEL-QATED-------AKLRLEVNMQALKAQFERDLQardEQGEeKRRQLVK----------QVRELEAELEDERK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1596 ARSRAEGERQKAET-------------------------VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQ------- 1643
Cdd:pfam01576 764 QRAQAVAAKKKLELdlkeleaqidaankgreeavkqlkkLQAQMKDLQRELEEARASRDEILAQSKESEKKLKnleaell 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1644 QVQERMAgteqslnsASERARQlHALLEALKLKragNSLAASTAEETAGSAQSRAREAE--KLREQVGDQYQTVRALAER 1721
Cdd:pfam01576 844 QLQEDLA--------ASERARR-QAQQERDELA---DEIASGASGKSALQDEKRRLEARiaQLEEELEEEQSNTELLNDR 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1722 KAEGV---------LAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGT----YEENERELEVKAAQL-DGLEARMRSVL 1786
Cdd:pfam01576 912 LRKSTlqveqltteLAAERSTSQKSESARQQLERQNKELKaKLQEMEGTvkskFKSSIAALEAKIAQLeEQLEQESRERQ 991
|
..
gi 1958794729 1787 QA 1788
Cdd:pfam01576 992 AA 993
|
|
| 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 1958794729 989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1553-1768 |
1.38e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIAERVRSLADVDTILA------HTMGDVRRAEQLLQD----------AQRARSRAEGERQKAE-------T 1609
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEaleaelDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDassddlaA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1610 VQAALEEAQRAQGAAqgairgavvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlkLKRAGNSLAASTAEE 1689
Cdd:COG4913 690 LEEQLEELEAELEEL--------------EEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1690 TAGSAQSRAREAEkLREQVGDQYQTVRALAERKAEGVLAAQARA-EQLRDEARGL---LQAAQDKLQRLQELEGT----Y 1761
Cdd:COG4913 754 RFAAALGDAVERE-LRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLdadLESLPEYLALLDRLEEDglpeY 832
|
....*..
gi 1958794729 1762 EENEREL 1768
Cdd:COG4913 833 EERFKEL 839
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1592-1789 |
1.52e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1592 DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLhalle 1671
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1672 ALKLKRAGNS-------LAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEarglL 1744
Cdd:COG3883 92 ARALYRSGGSvsyldvlLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE-LEAKLAELEALKAE----L 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958794729 1745 QAAQDKLQRLQElegtyeenereleVKAAQLDGLEARMRSVLQAI 1789
Cdd:COG3883 167 EAAKAELEAQQA-------------EQEALLAQLSAEEAAAEAQL 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1206-1573 |
2.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1206 DLAARTRRLEQWAQELQQTgvLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEAtegLRHEIGKTTERLTQLEAE 1285
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA--LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR---LEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1286 LTDVQDENFNANHALSGLERDGLALNLTLRQLDQhlDILKHSNFLGAYDS-IRHAHSQSTEAERRANASTFAIPSPVSNS 1364
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEA--QIEQLKEELKALREaLDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1365 ADTRRRAEVLMgAQRENFNRQHLANQQALGRLSThthtlsltgvnelvcgapgdapcatspcggagcrdedgqprcgglg 1444
Cdd:TIGR02168 834 AATERRLEDLE-EQIEELSEDIESLAAEIEELEE---------------------------------------------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1445 cSGAAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKD 1524
Cdd:TIGR02168 867 -LIEELESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1525 FLSQEGAdpDSIEMVATRVLDisIPASPEQIQRLASEIAERVRSLADVD 1573
Cdd:TIGR02168 944 RLSEEYS--LTLEEAEALENK--IEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1446-1785 |
2.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1446 SGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASrgqveqanqelrELIQNVKDF 1525
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP------------ECGQPVEGS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1526 LSQEGADPD--SIEMVATRVLDISipaspEQIQRLASEIaERVRSLADVDTILAHTMGDVRRAEQLLQD----AQRARSR 1599
Cdd:PRK02224 465 PHVETIEEDreRVEELEAELEDLE-----EEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAErretIEEKRER 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1600 AEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERArQLHALLEALKLKRAG 1679
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1680 -------------------NSLAASTAEETAGSAQSRAREAEKLREQVGDQyqtVRALAERKAE------GVLAAQARAE 1734
Cdd:PRK02224 618 laelnderrerlaekrerkRELEAEFDEARIEEAREDKERAEEYLEQVEEK---LDELREERDDlqaeigAVENELEELE 694
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1735 QLRDEarglLQAAQDKLQRLQELegtYEENErELEVKAAQLDGlEARMRSV 1785
Cdd:PRK02224 695 ELRER----REALENRVEALEAL---YDEAE-ELESMYGDLRA-ELRQRNV 736
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1554-1769 |
2.35e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.45 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1627
Cdd:NF041483 44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1628 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRA---REAEKL 1704
Cdd:NF041483 121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARAeaeRLAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1705 REQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQELE 1758
Cdd:NF041483 195 RQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEAE 271
|
250
....*....|.
gi 1958794729 1759 GTYEENERELE 1769
Cdd:NF041483 272 EALREARAEAE 282
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1592-1756 |
2.47e-08 |
|
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: 55.65 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1592 DAQRARSRAEGERQKAETVQAALEeaqrAQGAAQGAIRG--AVVD-----TKNTEQTLQQVQERMAGTEQSLNSASERAR 1664
Cdd:pfam05335 22 DAQAAAAEAAARQVKNQLADKALQ----AAKAAEAALAGkqQIVEqleqeLREAEAVVQEESASLQQSQANANAAQRAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1665 QLHALLEALK--LKRAGNSLAasTAEETAGSAQSrareaeklreqvgdqyqtvrALAErKAEGVLAAQARAEQLRDEarg 1742
Cdd:pfam05335 98 QAQQQLEALTaaLKAAQANLE--NAEQVAAGAQQ--------------------ELAE-KTQLLEAAKKRVERLQRQ--- 151
|
170
....*....|....
gi 1958794729 1743 lLQAAQDKLQRLQE 1756
Cdd:pfam05335 152 -LAEARADLEKTKK 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1627-1785 |
3.26e-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: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1627 AIRGAVVDTKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagsaqsrAREAEKLRE 1706
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFA-------------------QRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1707 QVGDQYQTVRALAERKAEgvlaAQARAEQLRDEARGLLQA-AQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSV 1785
Cdd:COG4913 296 ELEELRAELARLEAELER----LEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
|
| 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 1958794729 833 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1582-1778 |
4.28e-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: 56.16 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1582 DVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT-------------KNTEQTLQQVQER 1648
Cdd:pfam12795 21 DLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleqrlLQTSAQLQELQNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1649 MAGTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETA-GSAQSRAREAEK--LREQVGDQYQ-----TVR-A 1717
Cdd:pfam12795 101 LAQLNSQLIELQTRPERAQQQLSEARqrLQQIRNRLNGPAPPGEPlSEAQRWALQAELaaLKAQIDMLEQellsnNNRqD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1718 LAERKAEgvlAAQARAEQLRDEARgLLQAAQDKlQRLQELEGTYEENERELEVKAAQLDGL 1778
Cdd:pfam12795 181 LLKARRD---LLTLRIQRLEQQLQ-ALQELLNE-KRLQEAEQAVAQTEQLAEEAAGDHPLV 236
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1639-1782 |
4.74e-08 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 53.00 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1639 EQTLQQVQERMAGTEQSLNSASERARQLhalleALKLKRAgnslaastaEETAGSAQSRAREAE----KLREQvgdqyqt 1714
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEEL-----EEERRQA---------EEEAERLEQKRQEAEeekeRLEES------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1715 vralAERKAEgvlaaqaRAEQLRDEARgllqAAQDKLQRLQElegtyEENERELEVKAAQLDGLEARM 1782
Cdd:pfam20492 71 ----AEMEAE-------EKEQLEAELA----EAQEEIARLEE-----EVERKEEEARRLQEELEEARE 118
|
|
| 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 1958794729 1455 ALGRARHTQAEL--QRALVEgggilSRVSETRRQAEEAQQRAQAALDKANasrgqveqanqelreliqnvkdflsqegad 1532
Cdd:COG1842 38 DLVEARQALAQViaNQKRLE-----RQLEELEAEAEKWEEKARLALEKGR------------------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1533 pdsiEMVATRVLdisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKAETVqA 1612
Cdd:COG1842 83 ----EDLAREAL--------ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEL----------KAKKDTL-K 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1613 ALEEAQRAQGAAQGAIRGavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRAGNS-LAA 1684
Cdd:COG1842 140 ARAKAAKAQEKVNEALSG--IDSDDATSALERMEEKIEEMEARAEAAAELAAGdsLDDELAELEADSEVEDeLAA 212
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1486-1757 |
5.20e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 58.14 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1486 QAE--EAQQRAQAALDKANASRGQVEQANQ---ELRELIQNVKDFLSQEGADPDSIEmvatrvLDISIPASPEQIQRLAS 1560
Cdd:PRK10929 43 QAEivEALQSALNWLEERKGSLERAKQYQQvidNFPKLSAELRQQLNNERDEPRSVP------PNMSTDALEQEILQVSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 EIAE----------RVRSLADVDTILAhtmgdvrraeQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1630
Cdd:PRK10929 117 QLLEksrqaqqeqdRAREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1631 AVVDtkntEQTLQQV-----QE--RMagteqSLNSASERARQLHALLEALKLKRagNSLAASTAEETAGSAQSRAREAEK 1703
Cdd:PRK10929 187 ALVD----ELELAQLsannrQElaRL-----RSELAKKRSQQLDAYLQALRNQL--NSQRQREAERALESTELLAEQSGD 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1704 LREQVGDQYQTVRALAErkaegVLAAQA-RAEQLRDEARgllQAAQDKLQRLQEL 1757
Cdd:PRK10929 256 LPKSIVAQFKINRELSQ-----ALNQQAqRMDLIASQQR---QAASQTLQVRQAL 302
|
|
| 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 1958794729 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 1958794729 413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 470
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1485-1742 |
9.06e-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: 55.00 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNvkdfLSQEGADPDSiemvatrvldisipASPEQIQRLaseiae 1564
Cdd:pfam12795 23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAEA--------------APKEILASL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1565 rvrSLADVDTILAHTMGDVRRAEQLLQDAQrarSRAEGERQKAETVQAALEEAQRaqgaAQGAIRGAVVDTKNTEQTLQQ 1644
Cdd:pfam12795 79 ---SLEELEQRLLQTSAQLQELQNQLAQLN---SQLIELQTRPERAQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1645 VQERMAGTEQSLnsaserarqLHALLEALKLKRAGNS----LAASTAEETAGSAQSRAREAEKLREQVGDQYQtvrALAE 1720
Cdd:pfam12795 149 AQRWALQAELAA---------LKAQIDMLEQELLSNNnrqdLLKARRDLLTLRIQRLEQQLQALQELLNEKRL---QEAE 216
|
250 260
....*....|....*....|..
gi 1958794729 1721 RkaegvlaAQARAEQLRDEARG 1742
Cdd:pfam12795 217 Q-------AVAQTEQLAEEAAG 231
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
989-1035 |
9.10e-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: 9.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958794729 989 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 1035
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1487-1792 |
9.57e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 56.97 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1487 AEEAQQRAQAAlDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATrvldisipaspEQIQRLASEIAERV 1566
Cdd:COG3064 1 AQEALEEKAAE-AAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAE-----------EEAREAKAEAEQRA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1567 RSLAdvdtilahtmgdvrrAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgAAQGAIRGAvvDTKNTEQTLQQVQ 1646
Cdd:COG3064 69 AELA---------------AEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAA-AAEKAAAAA--EKEKAEEAKRKAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1647 ERMAGTEQSLNSASERARQLHALLEAlkLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGV 1726
Cdd:COG3064 131 EEAKRKAEEERKAAEAEAAAKAEAEA--ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1727 LAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQ 1792
Cdd:COG3064 209 AAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAAL 274
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1464-1775 |
9.58e-08 |
|
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: 57.54 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1464 AELQRALVEGGGILSRVSETRRQaeEAQQRAQAALDKANAS-RGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATR 1542
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1543 VLDISIP---ASPEQIQRLASEIAERVRSLAdvdtILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETvqaaleEAQR 1619
Cdd:pfam12128 334 FLDADIEtaaADQEQLPSWQSELENLEERLK----ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL------AKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1620 aqgaaQGAIRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAR 1699
Cdd:pfam12128 404 -----EARDRQLAVAEDDLQALESELREQL---EAGKLEFNEEEYRLKSRLGELKLRLNQ---ATATPELLLQLENFDER 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1700 eAEKLREQVGDQYQTVRALAErkaegvlaAQARAEQLRDEArglLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1775
Cdd:pfam12128 473 -IERAREEQEAANAEVERLQS--------ELRQARKRRDQA---SEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1555-1755 |
9.72e-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: 55.89 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1555 IQRLASEIAERVR---SLADVDTILAHTMGDVRRAEqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGA 1631
Cdd:pfam00529 31 VTRVLVKEGDRVKagdVLFQLDPTDYQAALDSAEAQ--LAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1632 VVDTKNTEQTLQQVQERMAGTEqslNSASERARQLHALLEalklkrAGNSLAASTAEETAGSAQSrareaEKLREQVGDQ 1711
Cdd:pfam00529 109 QAAVKAAQAQLAQAQIDLARRR---VLAPIGGISRESLVT------AGALVAQAQANLLATVAQL-----DQIYVQITQS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958794729 1712 YQTVRALAERKAEGvlaAQARAEQLRDEarglLQAAQDKLQRLQ 1755
Cdd:pfam00529 175 AAENQAEVRSELSG---AQLQIAEAEAE----LKLAKLDLERTE 211
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-516 |
9.94e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.94e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958794729 473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 516
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1550-1746 |
1.15e-07 |
|
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: 54.55 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1550 ASPEQIQRLaseiaervRSLADVDTILAHTMgdvRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgair 1629
Cdd:COG1579 1 AMPEDLRAL--------LDLQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1630 gavvdtKNTEQTLQQVQERMAGTEQSLNSASErARQLHAL---LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLRE 1706
Cdd:COG1579 62 ------KRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958794729 1707 QVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1746
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1789 |
1.18e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1591 QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALL 1670
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1671 EALKLKRAGNSLAASTAEET--------AGSAQSRAREAEKLREQVGDQYQTVRALAERKAEgvlaaqaraeqLRDEARG 1742
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-----------LAALRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958794729 1743 LLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1789
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1587-1780 |
1.35e-07 |
|
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: 54.73 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1587 EQLLQDAQRARSRAEGERQKAETVQAALEEA-QRAQGAAQGAirgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQ 1665
Cdd:pfam06008 50 SSLAQETEELQKKATQTLAKAQQVNAESERTlGHAKELAEAI--------KNLIDNIKEINEKVATLGENDFALPSSDLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1666 -LHA----LLEALKLKRAGNSLAASTAEetagsaqsrAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEA 1740
Cdd:pfam06008 122 rMLAeaqrMLGEIRSRDFGTQLQNAEAE---------LKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958794729 1741 RGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA 1780
Cdd:pfam06008 193 RELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKN 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1479-1770 |
1.61e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1479 RVSETRRQAEEA---QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVAtrvldisipaspEQI 1555
Cdd:PTZ00121 1558 KKAEEKKKAEEAkkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------------EEL 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRlaseiAERVRSlaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGaaqgairgavvDT 1635
Cdd:PTZ00121 1626 KK-----AEEEKK--KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-----------DE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQlhalleALKLKRAgNSLAASTAEETAGSAQSRAREAEKLREQVGDQyqtv 1715
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKK------AEELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK---- 1756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1716 RALAERKAEgvlaAQARAEQLRDEARGLLQAAQDK--LQRLQELEGTYEENERELEV 1770
Cdd:PTZ00121 1757 KKIAHLKKE----EEKKAEEIRKEKEAVIEEELDEedEKRRMEVDKKIKDIFDNFAN 1809
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1555-1776 |
1.76e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1555 IQRLASEIAERVRSLADVDTILahtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG--AV 1632
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1633 VDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaasTAEETAGSAQSRAREAEKLREQvgDQY 1712
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-----------ELEAELAELQEELEELLEQLSL--ATE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1713 QTVRALAERKAEgvlaAQARAEQLRDEarglLQAAQDKLQRLQElEGTYEENERELEVKAAQLD 1776
Cdd:COG4717 192 EELQDLAEELEE----LQQRLAELEEE----LEEAQEELEELEE-ELEQLENELEAAALEERLK 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1522-1784 |
1.98e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1522 VKDFLSQEGADPDSIEMV----ATRVLDISIPASPEQIQRLASeIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRAR 1597
Cdd:TIGR02169 122 IHDFLAAAGIYPEGYNVVlqgdVTDFISMSPVERRKIIDEIAG-VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1598 SRAEGERQKAETVQAALEEAQRAQGAAQ-GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL--K 1674
Cdd:TIGR02169 201 ERLRREREKAERYQALLKEKREYEGYELlKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1675 LKRAG----NSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKA--------EGVLAAQA-RAEQLRDEAR 1741
Cdd:TIGR02169 281 IKDLGeeeqLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKllaeieelEREIEEERkRRDKLTEEYA 360
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958794729 1742 GLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1784
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1514-1795 |
2.64e-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: 56.00 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1514 ELRELIQNVKDFLSQEGADpdsIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTM---GDVRRAEQL- 1589
Cdd:pfam12128 143 EYRSIIQNDRTLLGRERVE---LRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILeddGVVPPKSRLn 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1590 -------LQDAQrARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASER 1662
Cdd:pfam12128 220 rqqvehwIRDIQ-AIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1663 ARQLHALLEaLKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQ-----YQTVRALAERKAEGVLAAQARAEQLR 1737
Cdd:pfam12128 299 WKEKRDELN-GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQeqlpsWQSELENLEERLKALTGKHQDVTAKY 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1738 DEARGLL-QAAQDKLQRL-QELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1795
Cdd:pfam12128 378 NRRRSKIkEQNNRDIAGIkDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNE 437
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1554-1756 |
2.68e-07 |
|
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: 53.39 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRLASEIAErvrsladvdtiLAHtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgairgavv 1633
Cdd:COG1579 11 DLQELDSELDR-----------LEH------RLKELPAELAELEDELAALEARLEAAKTELEDLEKEI------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1634 dtKNTEQTLQQVQERMAGTEQSLNSASErARQLHAL---LEALKLKRagnslaaSTAEEtagsaqsRAREAEKLREQVGD 1710
Cdd:COG1579 62 --KRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRI-------SDLED-------EILELMERIEELEE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958794729 1711 QYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE 1756
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1488-1789 |
3.00e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1488 EEAQQRAQAALDKANASRGQVEQANQELRELIQNVkDFLSQEGADPDSIEMVATRVLDI-------SIPASPEQIQRLAS 1560
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYegyellkEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 EIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQrARSRAEGERQKAEtVQAALEEAQRAQGAAQGAIRGAvvdtkntEQ 1640
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEK-------ER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1641 TLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaastaeetagsaqsrareaeKLREQVGDQY---QTVRA 1717
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEER----------------------------KRRDKLTEEYaelKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1718 LAERKAEGVLAAQARA-----------EQLRDEaRGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLDGLEARMRSV 1785
Cdd:TIGR02169 368 DLRAELEEVDKEFAETrdelkdyreklEKLKRE-INELKRELDRLQeELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
....
gi 1958794729 1786 LQAI 1789
Cdd:TIGR02169 447 ALEI 450
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1588-1790 |
3.24e-07 |
|
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: 53.46 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1588 QLLQDAQRARSRAEGERQKAETVQAALEEA------QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASE 1661
Cdd:pfam12795 20 QDLQQALSLLDKIDASKQRAAAYQKALDDApaelreLRQELAALQAKAEAAPKEILASLSLEELEQRLLQTSAQLQELQN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1662 RARQLHALLEALklkragnslaaSTAEETAGSAQSRAREA-EKLREQVGDQYQTVRALAErkaEGVLAAQARAEQLRDEA 1740
Cdd:pfam12795 100 QLAQLNSQLIEL-----------QTRPERAQQQLSEARQRlQQIRNRLNGPAPPGEPLSE---AQRWALQAELAALKAQI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1741 RgLLQAAQDKLQRLQELegtyeeNERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:pfam12795 166 D-MLEQELLSNNNRQDL------LKARRDLLTLRIQRLEQQLQALQELLN 208
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
880-927 |
3.90e-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: 3.90e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 880 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 927
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1534-1790 |
4.14e-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: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1534 DSIEMVATRVLDIS------IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDA-------------- 1593
Cdd:TIGR00618 176 DQYTQLALMEFAKKkslhgkAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShayltqkreaqeeq 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1594 ---QRARSRAEGERQKAETVQAALEEAQRA-----QGAAQGAIRGAVVDT-KNTEQTLQQVQERMA-------------- 1650
Cdd:TIGR00618 256 lkkQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIeQQAQRIHTELQSKMRsrakllmkraahvk 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1651 ---------GTEQSLNSASERAR--------------QLHALLEALK--------LKRAGNSLAASTAEETAGSAQ---- 1695
Cdd:TIGR00618 336 qqssieeqrRLLQTLHSQEIHIRdahevatsireiscQQHTLTQHIHtlqqqkttLTQKLQSLCKELDILQREQATidtr 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 -----------SRAREAEKLREQVGDQYQ-----TVRALAERKAEGVLAAQA---RAEQLRDEARGLLQAAQDK------ 1750
Cdd:TIGR00618 416 tsafrdlqgqlAHAKKQQELQQRYAELCAaaitcTAQCEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKavvlar 495
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958794729 1751 LQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:TIGR00618 496 LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1596-1794 |
4.89e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1596 ARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKl 1675
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1676 kragnslaastaeetagsaQSRAREAEKLREQVGDQYQTVRALAER---KAEGVLAAQARAEQLRDEARGLLQAAQDKLQ 1752
Cdd:COG4942 97 -------------------AELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958794729 1753 RLQELEgtyeENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1794
Cdd:COG4942 158 DLAELA----ALRAELEAERAELEALLAELEEERAALEALKA 195
|
|
| 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 1958794729 879 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 924
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1769 |
7.09e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQ--ELRELIQNVK-DFL--SQEGADPDSIEMVATRvldisipAS 1551
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKaDEAkkAEEAKKADEAKKAEEK-------KK 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1552 PEQIQRlASEI--AERVRSLADVDTILAHTMGDVRRAEQLLQdAQRARSRA------EGERQKAETVQAALEEAQRAQga 1623
Cdd:PTZ00121 1548 ADELKK-AEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKK-AEEARIEEvmklyeEEKKMKAEEAKKAEEAKIKAE-- 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1624 aqgAIRGAVVDTKNTEQTLQQVQERMagteqslnsasERARQLHALLEALKLKragnslaastAEETAGSAQSRAREAEK 1703
Cdd:PTZ00121 1624 ---ELKKAEEEKKKVEQLKKKEAEEK-----------KKAEELKKAEEENKIK----------AAEEAKKAEEDKKKAEE 1679
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1704 LREQVGDQYQTVRALAERKAEGVLAAQAR---AEQLRdEARGLLQAAQDKLQRLQELEGTYEENERELE 1769
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKkkeAEEKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1732-1799 |
7.44e-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: 7.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1732 RAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1799
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1455-1754 |
8.61e-07 |
|
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: 53.75 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1455 ALGRARHTQAELQRALVEGGGILSRVSETR----RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEG 1530
Cdd:pfam07888 88 ELRQSREKHEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1531 ADPDSiemvaTRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQR--------------A 1596
Cdd:pfam07888 168 EEEAE-----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleelrsL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1597 RSRAEGERQKAETVQAALEE--AQRAQGAA---QGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERAR-QLHALL 1670
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSmaAQRDRTQAelhQARLQAA-------QLTLQLADASLALREGRARWAQERETlQQSAEA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1671 E---ALKLKRAGNSLAASTAEETAGSAQSR---AREAEKLREQVGdqyQTVRALAERKAeGVLAAQARAEQLRDEARGLL 1744
Cdd:pfam07888 316 DkdrIEKLSAELQRLEERLQEERMEREKLEvelGREKDCNRVQLS---ESRRELQELKA-SLRVAQKEKEQLQAEKQELL 391
|
330
....*....|
gi 1958794729 1745 QAAQDKLQRL 1754
Cdd:pfam07888 392 EYIRQLEQRL 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1514-1790 |
1.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1514 ELRELIQNVKDFLSQEgadpdsiemvatrvldisipaspEQIQRLASEIAERvrsladvdtiLAHTMGDVRRAEQLLQDA 1593
Cdd:PRK03918 173 EIKRRIERLEKFIKRT-----------------------ENIEELIKEKEKE----------LEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1594 QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ------SLNSASERARQLH 1667
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKA---------EGVLAAQARAEQLRD 1738
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKK 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1739 EARGLlqaAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:PRK03918 380 RLTGL---TPEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1453-1665 |
1.18e-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: 51.46 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1453 DLALGRARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegad 1532
Cdd:COG1579 16 DSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1533 pdsiemvatrvldISipaSPEQIQRLASEIAervrSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEGERQKAETVQA 1612
Cdd:COG1579 85 -------------VR---NNKEYEALQKEIE----SLK-------------RRISDLEDEILELMERIEELEEELAELEA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1613 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGT-EQSLNSASERARQ 1665
Cdd:COG1579 132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYERIRK 185
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1660-1794 |
1.28e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1660 SERARQLHALLEALKLKRAGNSLAAstAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDE 1739
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1740 ARGLLQAAQDKLQRLQELEgtyeENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1794
Cdd:COG1196 297 LARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELE 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1545-1774 |
1.31e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1545 DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE--AQRA-- 1620
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelGERAra 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1621 ---QGAAQGAIrGAVVDTKNTEQTLQQVQermagteqSLNSASERARQLhalLEALKLKRAGNSLAASTAEETAGSAQSR 1697
Cdd:COG3883 95 lyrSGGSVSYL-DVLLGSESFSDFLDRLS--------ALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1698 AREAEKLREQVgdqyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1774
Cdd:COG3883 163 KAELEAAKAEL----EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1553-1790 |
1.50e-06 |
|
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: 51.52 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEgerQKAETVQAALEEAQRAQGAAQGAIRGA- 1631
Cdd:smart00283 7 EEIAAGAEEQAEELEELA-------------ERMEELSASIEEVAANAD---EIAATAQSAAEAAEEGREAVEDAITAMd 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1632 --VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ-----LHALLEAlklKRAGNS------LAA---STAEETAGSAQ 1695
Cdd:smart00283 71 qiREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQtnllaLNAAIEA---ARAGEAgrgfavVADevrKLAERSAESAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 SRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRD------EARGLLQ-----------AAQDKLQRLQELE 1758
Cdd:smart00283 148 EIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEivdsveEIADLVQeiaaatdeqaaGSEEVNAAIDEIA 227
|
250 260 270
....*....|....*....|....*....|..
gi 1958794729 1759 GTYEENERELEVKAAQLDGLEARMRSVLQAIN 1790
Cdd:smart00283 228 QVTQETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1585-1784 |
1.60e-06 |
|
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: 51.18 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1585 RAEQLLQDAQRARSRAEGERQKAETVQAAL--------EEAQRAQG--------------AAQGAIRGavvdTKNTEQTL 1642
Cdd:pfam00261 12 EAEERLKEAMKKLEEAEKRAEKAEAEVAALnrriqlleEELERTEErlaealekleeaekAADESERG----RKVLENRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1643 QQVQERMAGTEQSLNSASERARQLHALLE--ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAE 1720
Cdd:pfam00261 88 LKDEEKMEILEAQLKEAKEIAEEADRKYEevARKLVVVEGDL--ERAEERAELAESKIVELEEELKVVGNNLKSLEASEE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1721 rkaegvlAAQARAEQLRDEARgLLQAaqdklqRLQELEGTYEENERELEVKAAQLDGLEARMRS 1784
Cdd:pfam00261 166 -------KASEREDKYEEQIR-FLTE------KLKEAETRAEFAERSVQKLEKEVDRLEDELEA 215
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1584-1783 |
1.64e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1584 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgAIRGAvvdtknteQTL-QQVQERmagteqslnsasER 1662
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE-----RKRYR--------QELeEQIEER------------EQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1663 ARQLhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVgDQYQtvRALAERKaegvlaaQARAEQLRDEARG 1742
Cdd:pfam13868 88 KRQE-EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI-DEFN--EEQAEWK-------ELEKEEEREEDER 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958794729 1743 LLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1783
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
|
|
| 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 1958794729 1452 ADLALGRARHTQAEL---QRALVEgggilsRVSETRRQAEEAQQRAQAALDKanasrgqveqANQEL-RELIQnvkdfls 1527
Cdd:pfam04012 34 MQSELVKARQALAQTiarQKQLER------RLEQQTEQAKKLEEKAQAALTK----------GNEELaREALA------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 qegadpdsiemvatrvldisipaspeQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKA 1607
Cdd:pfam04012 91 --------------------------EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL----------KAKK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1608 ETVQAAlEEAQRAQGAAQGAIRGAvvDTKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALLEALKLKRAGNSLA 1683
Cdd:pfam04012 135 NLLKAR-LKAAKAQEAVQTSLGSL--STSSATDSFERIEEKIEEREARADAAAELAsaVDLDAKLEQAGIQMEVSEDV 209
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1492-1791 |
1.67e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 52.77 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1492 QRAQAALDKANASRGQVEqANQELRELiQNVKDFLSQEGADPDSIEMVATRVLDIS---------IPASPEQIQRLAS-- 1560
Cdd:COG0497 48 GRADASLVRHGADKAEVE-AVFDLSDD-PPLAAWLEENGLDLDDGELILRREISADgrsrafingRPVTLSQLRELGEll 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 -EI-----------AERVRSL----ADVDTILAhtmgDVRRAEQLLQDAQRARSRAEGE----RQKAETVQAALEE---- 1616
Cdd:COG0497 126 vDIhgqhehqslldPDAQRELldafAGLEELLE----EYREAYRAWRALKKELEELRADeaerARELDLLRFQLEEleaa 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1617 -----------AQRAQGAAQGAIRgavvdtknteQTLQQVQERMAGTEQS----LNSAS---ERARQLHALLEALkLKRA 1678
Cdd:COG0497 202 alqpgeeeeleEERRRLSNAEKLR----------EALQEALEALSGGEGGaldlLGQALralERLAEYDPSLAEL-AERL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1679 GNSLAAstAEETAGSAQSRAREAE----KLrEQVGDQYQTVRALAeRK----AEGVLaaqARAEQLRDEarglLQAAQDK 1750
Cdd:COG0497 271 ESALIE--LEEAASELRRYLDSLEfdpeRL-EEVEERLALLRRLA-RKygvtVEELL---AYAEELRAE----LAELENS 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1751 LQRLQELEGTYEENERELEVKAAQL--------DGLEARMRSVLQAINL 1791
Cdd:COG0497 340 DERLEELEAELAEAEAELLEAAEKLsaarkkaaKKLEKAVTAELADLGM 388
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1605-1772 |
1.79e-06 |
|
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: 49.95 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1605 QKAETVQAAL----EEAQRAQGAAQGAIRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASERARQ-LHALLEALKlKRAG 1679
Cdd:pfam01442 11 TYAEELQEQLgpvaQELVDRLEKETEALRERL--QKDLEEVRAKLEPYLEELQAKLGQNVEELRQrLEPYTEELR-KRLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1680 NSLAASTA--EETAGSAQSRAREA-EKLREQVGdqyqtvrALAERKAEGVlaaQARAEQLRDEARGLLQAAQDKL-QRLQ 1755
Cdd:pfam01442 88 ADAEELQEklAPYGEELRERLEQNvDALRARLA-------PYAEELRQKL---AERLEELKESLAPYAEEVQAQLsQRLQ 157
|
170
....*....|....*..
gi 1958794729 1756 ELEGTYEENERELEVKA 1772
Cdd:pfam01442 158 ELREKLEPQAEDLREKL 174
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1476-1709 |
1.80e-06 |
|
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: 51.52 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1476 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1553
Cdd:smart00283 2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRA--------------RSRAEGERQ 1605
Cdd:smart00283 75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARAgeagrgfavvadevRKLAERSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1606 KAETVQAALEEAQRAQGAAQGAIRGA-------VVDTKNTEQTLQQVQERMAGTEQSL----NSASERARQLHALLEALK 1674
Cdd:smart00283 145 SAKEIESLIKEIQEETNEAVAAMEESsseveegVELVEETGDALEEIVDSVEEIADLVqeiaAATDEQAAGSEEVNAAID 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1958794729 1675 LKRAGNSLAASTAEETAGSAQSRAREAEKLREQVG 1709
Cdd:smart00283 225 EIAQVTQETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1484-1734 |
1.85e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 52.29 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1484 RRQAEEAQQRAQAALdkanASRGQVEQANQELreliQNVKDFLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIA 1563
Cdd:PRK07735 12 KEAARRAKEEARKRL----VAKHGAEISKLEE----ENREKEKALPKNDDMTIE---------------EAKRRAAAAAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1564 ERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-EGERQKAETVQAALEE--AQRAQGAAQGAIRGAVVDTKNTEQ 1640
Cdd:PRK07735 69 AKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAaALAKQKREGTEEVTEEekAAAKAKAAAAAKAKAAALAKQKRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1641 TLQQVQERMAGTEQSL--NSASERARQLHALLEALKLKRAGNSLAASTAEETA-----GSAQSRAREAEKLREQV----- 1708
Cdd:PRK07735 149 GTEEVTEEEEETDKEKakAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAkakakAAAAAKAKAAALAKQKAsqgng 228
|
250 260
....*....|....*....|....*...
gi 1958794729 1709 --GDQYQTVRALAERKAEGVLAAQARAE 1734
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1448-1795 |
1.85e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 52.72 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 QEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ-------SLNSASER---ARQLHALLEALK--- 1674
Cdd:COG0840 176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgdltvriDVDSKDEIgqlADAFNRMIENLRelv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1675 --LKRAGNSLAAStAEETAGSAQSRAREAEKLREQVgdqyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQ 1752
Cdd:COG0840 256 gqVRESAEQVASA-SEELAASAEELAAGAEEQAASL----EETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGE 330
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958794729 1753 RLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1795
Cdd:COG0840 331 VVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDI 373
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1482-1795 |
1.95e-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: 52.59 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1482 ETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvKDFLSQEGADPDSIEMVATRvldisipaspEQIQRLASE 1561
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQ--AQEAANRQREKEKERYKRDR----------EQWERQRRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1562 IAERVrslADVDTILAHTMGDVRRAEQLLQDAQRARsraegerqkaetvqAALEEAQRAQGAAQGAirgAVVDTKNTEQT 1641
Cdd:pfam07888 78 LESRV---AELKEELRQSREKHEELEEKYKELSASS--------------EELSEEKDALLAQRAA---HEARIRELEED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1642 LQQVQERMAGTEQSLNSASERARQLHALL-------EALKLKragnsLAASTAE---------ETAGSAQSRAREAEKLR 1705
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRkeeeaerKQLQAK-----LQQTEEElrslskefqELRNSLAQRDTQVLQLQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1706 EQVGDQYQTVRALAERKAEgvlaaqarAEQLRDEARGLlqaaQDklqRLQELEGTYEENERELEVKAAQLDGLEARM-RS 1784
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAE--------NEALLEELRSL----QE---RLNASERKVEGLGEELSSMAAQRDRTQAELhQA 277
|
330
....*....|.
gi 1958794729 1785 VLQAINLQVQI 1795
Cdd:pfam07888 278 RLQAAQLTLQL 288
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1590-1749 |
1.98e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1590 LQDAQRARSRAEGERQKAETVQAalEEAQRAQGAAQgairgavvdtknteQTLQQV-QERMAGTEQslNSASERARQLHA 1668
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQA--EELQQKQAAEQ--------------ERLKQLeKERLAAQEQ--KKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1669 L----LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAE-QLRDEARGL 1743
Cdd:PRK09510 129 LkqkqAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAK 208
|
....*.
gi 1958794729 1744 LQAAQD 1749
Cdd:PRK09510 209 KKAAAE 214
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1684-1794 |
2.34e-06 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 49.55 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1684 ASTAEETAGSAQSRAREAEKLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELEG 1759
Cdd:PRK14475 36 AGALDAYAAKIQAELDEAQRLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERKI 115
|
90 100 110
....*....|....*....|....*....|....*
gi 1958794729 1760 TYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1794
Cdd:PRK14475 116 AQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1485-1794 |
2.52e-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: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1485 RQAEEAQQRAQ--AALDKANASRGQVEQANQELRELiqnvKDFLSQEG--ADPDSIEMvatRVLDISIPASPEQIQRLAS 1560
Cdd:pfam05622 160 RNAEYMQRTLQleEELKKANALRGQLETYKRQVQEL----HGKLSEESkkADKLEFEY---KKLEEKLEALQKEKERLII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1561 E---------------IAERVRSLADVDTILAHTMGDVRRAE-----------QLLQDAQRARSRAEG-ERQKAETVQAA 1613
Cdd:pfam05622 233 ErdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEimpaeirekliRLQHENKMLRLGQEGsYRERLTELQQL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1614 LEEAQRAQGAAQGAIRgavvdtKNTEQ--TLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAASTA-- 1687
Cdd:pfam05622 313 LEDANRRKNELETQNR------LANQRilELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHleKLHEAQSELQKKKEqi 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1688 EETAGSAQSR-AREAEKLREQVGDQYQTVRALAER------KAEGVLAA-QARAEQLR-DEARGLLQAAQDKLQRLQELE 1758
Cdd:pfam05622 387 EELEPKQDSNlAQKIDELQEALRKKDEDMKAMEERykkyveKAKSVIKTlDPKQNPASpPEIQALKNQLLEKDKKIEHLE 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1759 GTYEEN--ERELEVK-----------AAQLDGLEARmrsvLQAINLQVQ 1794
Cdd:pfam05622 467 RDFEKSklQREQEEKlivtawynmgmALHRKAIEER----LAGLSSPGQ 511
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1479-1780 |
2.88e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.96 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKdfLSQEGADPDSIEMVATRVLDISipASPEQIQRL 1558
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK--AEAEQRAAELAAEAAKKLAEAE--KAAAEAEKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1559 ASEIAERVRSLADVDTIL--AHTMGDVRRAEQLLQDAQR-ARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:COG3064 93 AAAEKAKAAKEAEAAAAAekAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHAllEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTV 1715
Cdd:COG3064 173 RAAAGAAAALVAAAAAAVEAADTAAAAAAALAA--AAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEE 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1716 RALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA 1780
Cdd:COG3064 251 AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEE 315
|
|
| 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 1958794729 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 1958794729 989 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1452-1780 |
3.06e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1452 ADLALGRARHTQAELQRALVEG--GGILSRVSETRRQAEEAQQR---AQAALDKANASRGQVEQAN-------------- 1512
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEGqlQELQARLSESERQRAELAEKlskLQSELESVSSLLNEAEGKNiklskdvsslesql 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1513 QELRELIQ-------NVKDFLSQEGADPDSI------EMVATRVLDisipaspEQIQRLASEIAERVRSLADVDTILaht 1579
Cdd:pfam01576 471 QDTQELLQeetrqklNLSTRLRQLEDERNSLqeqleeEEEAKRNVE-------RQLSTLQAQLSDMKKKLEEDAGTL--- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1580 mgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQ---TLQQVQ---ERMAGTE 1653
Cdd:pfam01576 541 -------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsNLEKKQkkfDQMLAEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1654 QSLNS--ASERARqlhallealklkragnslAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRAL-AE---------- 1720
Cdd:pfam01576 614 KAISAryAEERDR------------------AEAEAREKETRALSLARALEEALEAKEELERTNKQLrAEmedlvsskdd 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1721 --------RKAEGVLAAQA-----RAEQLRDEarglLQAAQDKLQRLQ------------ELEGTYEENE--RELEVKaa 1773
Cdd:pfam01576 676 vgknvhelERSKRALEQQVeemktQLEELEDE----LQATEDAKLRLEvnmqalkaqferDLQARDEQGEekRRQLVK-- 749
|
....*..
gi 1958794729 1774 QLDGLEA 1780
Cdd:pfam01576 750 QVRELEA 756
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1553-1781 |
3.21e-06 |
|
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: 51.61 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIAERVRSL----ADVDTILahtmgdvRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRaqgaaqgai 1628
Cdd:pfam19220 6 ELLRVRLGEMADRLEDLrslkADFSQLI-------EPIEAILRELPQAKSRLLELEALLAQERAAYGKLRR--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1629 rgavvdtknteqTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTAEETAgsaqsRAREAEKLREQV 1708
Cdd:pfam19220 70 ------------ELAGLTRRLSAAEGELEELVARLAKLEAALR--EAEAAKEELRIELRDKTA-----QAEALERQLAAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1709 GDQYQTV----RALAERkAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ-----------ELEGTYEENERELEVKAA 1773
Cdd:pfam19220 131 TEQNRALeeenKALREE-AQAAEKALQRAEGELATARERLALLEQENRRLQalseeqaaelaELTRRLAELETQLDATRA 209
|
....*...
gi 1958794729 1774 QLDGLEAR 1781
Cdd:pfam19220 210 RLRALEGQ 217
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1612-1784 |
4.13e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1612 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAS--------ERARQLHALLEALK-----LKRA 1678
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetlaDRVEEIREQLDEAEeakrfVQQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1679 GNSLAAstAEETAGSAQSRAREAEKLREQV-------GDQYQTVRALAE----------RKAEGVLAA-----------Q 1730
Cdd:PRK04863 917 GNALAQ--LEPIVSVLQSDPEQFEQLKQDYqqaqqtqRDAKQQAFALTEvvqrrahfsyEDAAEMLAKnsdlneklrqrL 994
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1731 ARAEQLRDEARGLLQAAQDKL----QRLQELEGTYE-------ENERELEVKAAQLD-GLEARMRS 1784
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQAQLaqynQVLASLKSSYDakrqmlqELKQELQDLGVPADsGAEERARA 1060
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1583-1787 |
4.50e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1583 VRRAEQLLQDAQrarsrAEGERQKA-ETVQAALEEAQRAQGAAQgairgavvdtknteqtlQQVQERMAGTEQSLNSASE 1661
Cdd:TIGR02794 74 EQQAEEAEKQRA-----AEQARQKElEQRAAAEKAAKQAEQAAK-----------------QAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1662 RARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQyqtvRALAERKAEGVlAAQARAEQLRDEAR 1741
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEAKAKAE-EAKAKAEAAKAKAA 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958794729 1742 gllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ 1787
Cdd:TIGR02794 207 ---AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1459-1795 |
4.95e-06 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 51.73 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1459 ARHTQAELQRAlvegggilsRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEM 1538
Cdd:COG2203 337 ADQAAIAIERA---------RLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1539 VATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEqLLQDAQRARSRAEGERQKAETVQAALEEAQ 1618
Cdd:COG2203 408 DAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLL-LALAELELLEILELLVLLAVILLALALLAA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1619 RAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA 1698
Cdd:COG2203 487 LLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGV 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1699 REAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGL 1778
Cdd:COG2203 567 LLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRL 646
|
330
....*....|....*..
gi 1958794729 1779 EARMRSVLQAINLQVQI 1795
Cdd:COG2203 647 ALALASLVLLRALLATE 663
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1452-1734 |
7.02e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.84 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1452 ADLALGRARHtqaelQRALVEG-GGILSRVSETRRQAEEAQQrAQAALDKANASRGQVEQANQELRELIQNVkdflsqEG 1530
Cdd:COG0497 133 EHQSLLDPDA-----QRELLDAfAGLEELLEEYREAYRAWRA-LKKELEELRADEAERARELDLLRFQLEEL------EA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1531 ADPDSIEMVAtrvLDisipaspEQIQRLASeiAERVRSLADvdTILAHTMGDVRRAEQLLQDAQRARSRAEGERQK---- 1606
Cdd:COG0497 201 AALQPGEEEE---LE-------EERRRLSN--AEKLREALQ--EALEALSGGEGGALDLLGQALRALERLAEYDPSlael 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1607 AETVQAALEEAQRAQGAAQGAIRGAVVDtkntEQTLQQVQERMAgteqSLNSAserARQLHALLEAL--KLKRAGNSLAA 1684
Cdd:COG0497 267 AERLESALIELEEAASELRRYLDSLEFD----PERLEEVEERLA----LLRRL---ARKYGVTVEELlaYAEELRAELAE 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1685 STAEETagsaqsrarEAEKLREQVGDQYQTVRALAE------RKAEGVLAAQARAE 1734
Cdd:COG0497 336 LENSDE---------RLEELEAELAEAEAELLEAAEklsaarKKAAKKLEKAVTAE 382
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1491-1784 |
7.73e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1491 QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE----M--VATR---VLDISIPASPEQIQ---RL 1558
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRdlkdMldVKERkinVLQKKIENLQEQLRdkdKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1559 ASEIAERVRSL----ADVDTILAhTMgdvrraEQLLQDAQRARSRAEGERQKAEtvQAALEEAQRAQGaaqgairgavvD 1634
Cdd:pfam10174 417 LAGLKERVKSLqtdsSNTDTALT-TL------EEALSEKERIIERLKEQRERED--RERLEELESLKK-----------E 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQL--HALLEALKLKRAGNSLAASTAEETAGSAQSR----AREAEKLREQV 1708
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLKkahnAEEAVRTNPEI 556
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1709 GDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1784
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1449-1795 |
1.00e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 50.58 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1449 AATADLALGRARHTQAELQRALvegggilsrvsETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1528
Cdd:COG2203 337 ADQAAIAIERARLYEALEAALA-----------ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1529 EGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADV-DTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG2203 406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDeEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG2203 486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1688 EETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERE 1767
Cdd:COG2203 566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645
|
330 340
....*....|....*....|....*...
gi 1958794729 1768 LEVKAAQLDGLEARMRSVLQAINLQVQI 1795
Cdd:COG2203 646 LALALASLVLLRALLATELDLILDSSLL 673
|
|
| 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 1958794729 1480 VSETRRQAEEAQQ-RAQAALDKANASR--GQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDisipASPEQIQ 1556
Cdd:pfam06008 53 AQETEELQKKATQtLAKAQQVNAESERtlGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLS----RMLAEAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1557 RLASEIAERvrslaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQK-AETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:pfam06008 129 RMLGEIRSR-----DFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAlANALRDSLAEYEAKLSDLRELLREAAAKT 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1636 KNTEQTLQQVQERMagteQSLNSASERARQLHALLEALkLKRAGNSLAA 1684
Cdd:pfam06008 204 RDANRLNLANQANL----REFQRKKEEVSEQKNQLEET-LKTARDSLDA 247
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1585-1796 |
1.24e-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: 49.53 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1585 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgAIRGAVV-----DTKNTEQTLQQVQERMAGTEQSlNSA 1659
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQERE-QMDEIVEriqeeDQAEAEEKLEKQRQLREEIDEF-NEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1660 SERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQ---VGDQYQTVRALAERkaEGVLAAQARAEQL 1736
Cdd:pfam13868 139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlRAQQEKAQDEKAER--DELRAKLYQEEQE 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1737 RDEARGLLQAAQDKLQRLQELEGTYEE---NERELEVKAAQLDglEARMRSVLQAINLQVQIY 1796
Cdd:pfam13868 217 RKERQKEREEAEKKARQRQELQQAREEqieLKERRLAEEAERE--EEEFERMLRKQAEDEEIE 277
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1585-1782 |
1.49e-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: 49.07 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1585 RAEQLLQDAQRARsRAEGERQKAETVQAalEEAQRAQGAAQgairgavVDTKNTEQTLQQVQErmagteqslnsasERAR 1664
Cdd:TIGR02794 51 QANRIQQQKKPAA-KKEQERQKKLEQQA--EEAEKQRAAEQ-------ARQKELEQRAAAEKA-------------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1665 QLHALLEALKLKRAgnslaastAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLL 1744
Cdd:TIGR02794 108 EQAAKQAEEKQKQA--------EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958794729 1745 QAAQDKLQRLQE------LEGTYEENERELEVKAAQLDGLEARM 1782
Cdd:TIGR02794 180 KAKAEAEAKAKAeeakakAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1612-1788 |
1.51e-05 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 48.51 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1612 AALEEAQRAQGA-AQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEET 1690
Cdd:COG4223 24 AALEAAPAAAAAtAALEARLAALRAALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAA-RAAALALAAAALRAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1691 AGSAQSRAREAEKLREQVGDQyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAqdklqrlqelegtyeeneRELEV 1770
Cdd:COG4223 103 VERGQPFAAELAALEALAPDA-PALAALAAFAATGVPTLAALRAEFPAAARAALAAA------------------RAPEA 163
|
170
....*....|....*...
gi 1958794729 1771 KAAQLDGLEARMRSVLQA 1788
Cdd:COG4223 164 DASWLDRLLAFARSLVTV 181
|
|
| 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 1958794729 350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| 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 1958794729 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 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1452 ADLALGRARHTQAELQ---RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1528
Cdd:COG4913 659 DEIDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1529 --EGADPDSIEMVATRVLDISIPASPEQIQRlasEIAERVRSLAdvdtilahtmGDVRRAEQLLQDAQRA-RSRAEGERQ 1605
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE---NLEERIDALR----------ARLNRAEEELERAMRAfNREWPAETA 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1606 KAETVQAALEEAQR------AQG--AAQGAIRGAVvdTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEAL 1673
Cdd:COG4913 806 DLDADLESLPEYLAlldrleEDGlpEYEERFKELL--NENSIEFVADLLSKL---RRAIREIKERIDPLNDSLKRI 876
|
|
| 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 1958794729 956 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 986
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1586-1789 |
1.97e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1586 AEQLLQDAQRARsrAEgERQKAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERARQ 1665
Cdd:COG3096 290 LRRELFGARRQL--AE-EQYRLVEMARELEELSARESDLEQDYQAAS-DHLNLVQTALRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1666 LHALLEALKLKRAgnslaasTAEETAGSAQSrarEAEKLREQVGDqYQT------VRALAERKAegvLAAQARAEQLRDE 1739
Cdd:COG3096 366 QEEVVEEAAEQLA-------EAEARLEAAEE---EVDSLKSQLAD-YQQaldvqqTRAIQYQQA---VQALEKARALCGL 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1740 ARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1789
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV 481
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-338 |
1.97e-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: 1.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1477-1647 |
2.34e-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: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1477 LSRVSETR-RQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvatrvldisipaSPEQI 1555
Cdd:pfam07321 4 LLRVKHLReDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAW--------------------------------RPQEE 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRLASEIAERVRSLADVDTILaHTMGDVRRAEQLL-QDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAIRGAVVD 1634
Cdd:pfam07321 52 QRLYAEIQGKLVLLKELEKVK-QQVALLRENEADLeKQVAEARQQLEAEREALRQARQALAEARRAV--EKFAELVRLVQ 128
|
170
....*....|...
gi 1958794729 1635 TKntEQTLQQVQE 1647
Cdd:pfam07321 129 AE--ELRQQERQE 139
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1647-1775 |
2.43e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1647 ERMAGTEQSLNsasERARQLHALLEALKLKRAGNslaaSTAEETAGSAQSRAREAEKLREQVGDQY---QTVRALAERKA 1723
Cdd:PRK09039 46 REISGKDSALD---RLNSQIAELADLLSLERQGN----QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRA 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1724 EGVLAAQARAEQLRDEARG---LLQ----AAQDKLQRLQELEGTYEENERELEVKAAQL 1775
Cdd:PRK09039 119 GELAQELDSEKQVSARALAqveLLNqqiaALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1489-1773 |
2.73e-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: 49.19 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1489 EAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRS 1568
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1569 LADVDTILahtmgdVRRAEQLLQDAQRARSRAEGERQKA--ETVQAALEEAQRAQGAAQGAIRGAVVDT-KNTEQTLQQV 1645
Cdd:COG5185 352 LTENLEAI------KEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEEL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1646 QERMAGTEQSLNSASERARQLHALLEAlKLKRAGNSLAASTAEETAGSAQSRAREAEKLREQVGDQYQTVRALaerkaeg 1725
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNELISELNK-VMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL------- 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958794729 1726 vlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTyEENERELEVKAA 1773
Cdd:COG5185 498 ----KATLEKLRAKLERQLEGVRSKLDQVAESLKD-FMRARGYAHILA 540
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1476-1774 |
2.88e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1476 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISipaspEQI 1555
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR-----EEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRLASEIAERVRSLADVDTIlahtmgdVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAirgavVDT 1635
Cdd:COG1340 95 DELRKELAELNKAGGSIDKL-------RKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKN-----EKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaastaeetagsaqsraREAEKLREQVgDQYQtv 1715
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELY------------------------KEADELRKEA-DELH-- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1716 ralaerkaEGVLAAQARAEQLRDEarglLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1774
Cdd:COG1340 216 --------KEIVEAQEKADELHEE----IIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1479-1788 |
2.94e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1479 RVSETRRQAEEAQQR-AQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-IQ 1556
Cdd:PRK04863 787 RIEQLRAEREELAERyATLSFDV------------QKLQRLHQAFSRFIGSH--------------LAVAFEADPEAeLR 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1557 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRA------QGAAQ 1625
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladETLADRVEEIREQLDEAEEAkrfvqqHGNAL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1626 GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLE---ALKLKRAGNSLAASTA--------EETAGSA 1694
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrraHFSYEDAAEMLAKNSDlneklrqrLEQAEQE 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1695 QSRAREAEKLREQVGDQYQTVRA------------LAERKAE----GVLA---AQARAEQLRDEARGLLQAAQdklQRLQ 1755
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQYNQVLAslkssydakrqmLQELKQElqdlGVPAdsgAEERARARRDELHARLSANR---SRRN 1077
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958794729 1756 ELEGTYEENERELE-----VKAAQLDGLEARmRSVLQA 1788
Cdd:PRK04863 1078 QLEKQLTFCEAEMDnltkkLRKLERDYHEMR-EQVVNA 1114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1607-1790 |
3.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1607 AETVQAALEEAQRAQGAAQGAIRGavvdtKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnSLAAST 1686
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQG-----RKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEE--ELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1687 AEETAgsAQSRAREAEKLrEQVGDQYQTVRALAERKAEGvlaaQARAEQLRDEarglLQAAQDKLQRLQELEGTYEENER 1766
Cdd:COG4717 109 AELEE--LREELEKLEKL-LQLLPLYQELEALEAELAEL----PERLEELEER----LEELRELEEELEELEAELAELQE 177
|
170 180
....*....|....*....|....*
gi 1958794729 1767 ELEVKAAQLD-GLEARMRSVLQAIN 1790
Cdd:COG4717 178 ELEELLEQLSlATEEELQDLAEELE 202
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1636-1783 |
3.44e-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: 46.98 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKL---KRAGNSLAASTA--EETAGSAQSRAREAEKLREQVGD 1710
Cdd:pfam04012 25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEqakKLEEKAQAALTKgnEELAREALAEKKSLEKQAEALET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1711 QYQTVRALAErKAEGVLAA-QARAEQLRDEARGLLqaAQDKLQRLQE-LEGTY-----EENERELEVKAAQLDGLEARMR 1783
Cdd:pfam04012 105 QLAQQRSAVE-QLRKQLAAlETKIQQLKAKKNLLK--ARLKAAKAQEaVQTSLgslstSSATDSFERIEEKIEEREARAD 181
|
|
| 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 1958794729 930 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 979
Cdd:smart00180 1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1452-1790 |
3.59e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1452 ADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA-----QAAL----DKANASRGQVEQANQELRELIQNV 1522
Cdd:pfam12128 651 ARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQldkkhQAWLeeqkEQKREARTEKQAYWQVVEGALDAQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1523 KDFLSQE--------GADPDSIEMVATRVLDiSIPASPEQIQRLASEIAERVRSLADVdtilAHTMGDVRRAEQLLQDA- 1593
Cdd:pfam12128 731 LALLKAAiaarrsgaKAELKALETWYKRDLA-SLGVDPDVIAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETw 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1594 ----QRARSRAEGERQKAETVQ---AALEEAQRAQGAA----QGAIRGAVVDTKNTEQTLQQVQERMA------GTEQSL 1656
Cdd:pfam12128 806 lqrrPRLATQLSNIERAISELQqqlARLIADTKLRRAKlemeRKASEKQQVRLSENLRGLRCEMSKLAtlkedaNSEQAQ 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1657 NSASERARQlhalLEALKLKRAGNSLAASTAEE------TAGSAQSRAREAEKLREQvgDQYQT---VRALAERKAEGVL 1727
Cdd:pfam12128 886 GSIGERLAQ----LEDLKLKRDYLSESVKKYVEhfknviADHSGSGLAETWESLREE--DHYQNdkgIRLLDYRKLVPYL 959
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1728 A--AQARAEQ----LRDEARGLLQAAQDKLQRLQELEGTYEENEREL--EVKA-AQLDGL---EARMRSVLQAIN 1790
Cdd:pfam12128 960 EqwFDVRVPQsimvLREQVSILGVDLTEFYDVLADFDRRIASFSRELqrEVGEeAFFEGVsesAVRIRSKVSELE 1034
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1484-1797 |
4.09e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1484 RRQAEEAQQRA-QAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEI 1562
Cdd:COG3064 119 KEKAEEAKRKAeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1563 AERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL 1642
Cdd:COG3064 199 AAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1643 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEET--AGSAQSRAREAEKLREQVGDQYQTVRALAE 1720
Cdd:COG3064 279 VVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGAlvVRGGGAASLEAALSLLAAGAAAAAAGAGAL 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1721 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1797
Cdd:COG3064 359 ATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVA 435
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1478-1756 |
4.68e-05 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 46.97 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1478 SRVSETRRQAEEAQQRAqAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvATRVLDISIPASPEQIQR 1557
Cdd:COG4223 7 AAVAELPAQLTALEQRL-AALEAAPAAAAATAALEARLAAL---------------------RAALAAAREAVAAAAAAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1558 LASEIAErvrsladvdtilahtmgdvrraeqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQG------AIRGA 1631
Cdd:COG4223 65 LEARLAA-------------------------LEAKAAAPEAEAAAAARAAALALAAAALRAAVERGQPfaaelaALEAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1632 VVDtknteqtlQQVQERMAGTEQS-LNSASERARQLHALLEALklkragnsLAASTAEETAGSAQSRAREAekLREQVgd 1710
Cdd:COG4223 120 APD--------APALAALAAFAATgVPTLAALRAEFPAAARAA--------LAAARAPEADASWLDRLLAF--ARSLV-- 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958794729 1711 qyqTVRALAERKAEGVLAAQARAEQ-LRdeaRGLLQAAQDKLQRLQE 1756
Cdd:COG4223 180 ---TVRRVGPVEGDDPDAILARAEAaLA---AGDLAGALAELEALPE 220
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1432-1757 |
5.48e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 48.06 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1432 RDEDGQprcgglgcSGAAATADLALGRARHTQaELQRALVEgggilsrvsetrrqaeeaqQRAQAALDKANASRgqveqA 1511
Cdd:pfam13779 379 TDGAGQ--------EGRSEPLEIRLPERRFSD-PLARALIE-------------------QRRRLALDRENRPR-----V 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1512 NQELRELIqnvkdfLSQEGADPDSIEMVATRVL--DISIPASPEQIQRLAS---EIAERVRSladvdtilahtmGDVRRA 1586
Cdd:pfam13779 426 ARALDALT------LAPEEFGPDAGVYLGLRSAlaRLELARSDEALDEVADllwELALRIED------------GDLSDA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1587 EQLLQDAQRARSRA------EGERQK-AETVQAALEE-----AQRAQGAAQGAIRGAVVDTK-NTEQTLQQVQERMAgtE 1653
Cdd:pfam13779 488 ERRLRAAQERLSEAlergasDEEIAKlMQELREALDDymqalAEQAQQNPQDLQQPDDPNAQeMTQQDLQRMLDRIE--E 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1654 QSLNSASERARQlhaLLEAlkLKRAGNSLAASTAEETAGSAQSRAREA-----EKLREQ--------------------- 1707
Cdd:pfam13779 566 LARSGRRAEAQQ---MLSQ--LQQMLENLQAGQPQQQQQQGQSEMQQAmdelgDLLREQqqlldetfrqlqqqggqqqgq 640
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1708 VGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQEL 1757
Cdd:pfam13779 641 PGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEEL 690
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1582-1734 |
5.72e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1582 DVRRAEQLLQdaQRARSRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdtkntEQTLQQVQERMAGTEQSLNSASE 1661
Cdd:PRK09510 73 SAKRAEEQRK--KKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-------------EQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1662 RARQlhalLEALKLK-----RAGNSLAASTAEETAGSAQSRAR---EAEKLREQVGDQYQTVRALAERKAEGVLAAQARA 1733
Cdd:PRK09510 138 AAKA----AAAAKAKaeaeaKRAAAAAKKAAAEAKKKAEAEAAkkaAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
.
gi 1958794729 1734 E 1734
Cdd:PRK09510 214 E 214
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
1564-1784 |
7.13e-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: 46.24 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1564 ERVRSLADVDTILaHTMGDVRRAEqlLQDAQrarsrAEGERQKAETVQAALEE--AQRAQGAAQ----------GAIRGA 1631
Cdd:pfam16591 3 ERSDRMTDISQLN-DTLTDLRIAR--LQYML-----SNGDATAAQAVQKKLDElkQQLQQLKTTftspenvrllQEQLQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1632 VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastAEETAGSAQSRAreAEKLREQV-GD 1710
Cdd:pfam16591 75 IQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTP--------EADSRRAAQYQA--ISELKRQVqMA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1711 QYQtVRA-LAERKAEGVLAAQARAEQLRDEARGLLQA-AQDKLQRLQELE---GTYEENERELEVKAAQLDGLEARMRS 1784
Cdd:pfam16591 145 RYQ-VRGyTFTPNEDSEQAAYQQLDAALASLDQLRQAlAGDPGAALQQLTsalQGYRDALDTFKAAVAAIEQARQEMTS 222
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1532-1750 |
7.41e-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: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1532 DPDSIEMVATRV-LDISIPASPEQ-----IQRLASE-----IAERVRSLADVDTILAHTmgDVRRAEQLLQDAQRARSRA 1600
Cdd:TIGR02794 44 DPGAVAQQANRIqQQKKPAAKKEQerqkkLEQQAEEaekqrAAEQARQKELEQRAAAEK--AAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1601 EGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL--QQVQERMAGTEQSLNSASERARQlhALLEALKLKra 1678
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEAEAK--AKAEEAKAK-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1679 gnslaASTAEETAGS-AQSRAREAEKLREqvgdqyqtvRALAERKAE-------GVLAAQARAEQLRDEARGLLQAAQDK 1750
Cdd:TIGR02794 198 -----AEAAKAKAAAeAAAKAEAEAAAAA---------AAEAERKADeaelgdiFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1584-1625 |
7.44e-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: 7.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958794729 1584 RRAEQLLQDAQRARSRAEGERQKA----ETVQAALEEAQRAQGAAQ 1625
Cdd:pfam11839 8 SKADQAEQDAAAAQSAADSAKAKAdeaaARANAAEAAAEEAQQAAE 53
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1583-1756 |
7.74e-05 |
|
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: 45.90 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1583 VRRAEQLLQDAQRARS--RAEGERQKAETVQAALEEAQRA----QGAAQGAIRGAVVDTKNTEQTLQQVQER-------M 1649
Cdd:cd00176 16 LSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERvealNELGEQLIEEGHPDAEEIQERLEELNQRweelrelA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1650 AGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEETAGSAQSRAREAEKLREQVgDQYQTVRALAERKAEGVLA 1728
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADDLEQwLEEKEAALASEDLGKDLESVEELLKKHKELEEEL-EAHEPRLKSLNELAEELLE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958794729 1729 A---------QARAEQLRDEARGLLQAAQDKLQRLQE 1756
Cdd:cd00176 175 EghpdadeeiEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1576-1794 |
8.52e-05 |
|
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: 47.74 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1576 LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAE---TVQAALEEAQRAqgaaqgaIRGAVVDTKNTEqtLQQVQERMAGT 1652
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAErykELKAELRELELA-------LLVLRLEELREE--LEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1653 EQSLNSASERARQLHALLEALKLKRagnslaastaeetagsaQSRAREAEKLREQVGDQYQTVRALAERKAEgvlaAQAR 1732
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEV-----------------SELEEEIEELQKELYALANEISRLEQQKQI----LRER 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1733 AEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARM---RSVLQAINLQVQ 1794
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeelEAELEELESRLE 375
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1613-1775 |
8.75e-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: 46.76 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1613 ALEEAQRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMAGT----EQSLNSASERARQLHA--LLEALKLKRAGNSLAAs 1685
Cdd:TIGR02794 22 SLYHSVKPEPGGGAEIIQAVlVDPGAVAQQANRIQQQKKPAakkeQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1686 taEETAGSAQSRAREAEKLREQVGDQYQtvRALAERKAegvlAAQARAEQ-LRDEARGllQAAQDKLQRLQE---LEGTY 1761
Cdd:TIGR02794 101 --EKAAKQAEQAAKQAEEKQKQAEEAKA--KQAAEAKA----KAEAEAERkAKEEAAK--QAEEEAKAKAAAeakKKAEE 170
|
170
....*....|....
gi 1958794729 1762 EENERELEVKAAQL 1775
Cdd:TIGR02794 171 AKKKAEAEAKAKAE 184
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1571-1769 |
8.93e-05 |
|
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: 45.81 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1571 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1650
Cdd:cd07596 1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1651 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKLREQVGDQYQTV-------RALAER 1721
Cdd:cd07596 71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDDRADALLTLQSLkkdlaskKAQLEK 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958794729 1722 KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1769
Cdd:cd07596 136 LKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1637-1783 |
9.08e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1637 NTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREA-EKLREQVGdqyqtv 1715
Cdd:COG1842 23 DPEKMLDQAIRDM---EEDLVEARQALAQVIANQKRLERQLE-------ELEAEAEKWEEKARLAlEKGREDLA------ 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1716 RALAERKAEgvlaAQARAEQLRdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMR 1783
Cdd:COG1842 87 REALERKAE----LEAQAEALE-AQLAQLEEQVEKLKEaLRQLESKLEELKAKKDTLKARAKAAKAQEK 150
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1589-1781 |
9.44e-05 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 47.27 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1589 LLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEqSLNSASerarQLHA 1668
Cdd:PRK15374 13 YTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDAARE-KLSSEG----QLTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1669 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAekLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRDEARGLLQ 1745
Cdd:PRK15374 88 LLGKLMTLLGDVSLSQLESRLAVWQAMIESQKE--MGIQVSKEFQTALGEAQeatDLYEASIKKTDTAKSVYDAAEKKLT 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958794729 1746 AAQDKLQRLQELEGTYEENERELEVKAAqlDGLEAR 1781
Cdd:PRK15374 166 QAQNKLQSLDPADPGYAQAEAAVEQAGK--EATEAK 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1696-1797 |
9.82e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 SRAREA-EKLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKLQRLQELEgtyEENERELEVKAA 1773
Cdd:COG4913 238 ERAHEAlEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLELLEAEL---EELRAELARLEA 309
|
90 100
....*....|....*....|....*
gi 1958794729 1774 QLDGLEARMRSVLQAI-NLQVQIYN 1797
Cdd:COG4913 310 ELERLEARLDALREELdELEAQIRG 334
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1477-1788 |
1.01e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1477 LSRVSETRRQA-------EEAQQRAQAA-LDKANASRGQVEQANQELRELIQNVKDFLSQEgadpdsiemvatrvldisi 1548
Cdd:COG3096 245 LEAIRVTQSDRdlfkhliTEATNYVAADyMRHANERRELSERALELRRELFGARRQLAEEQ------------------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1549 paspEQIQRLASEIAERVRSLADVDTilahtmgDVRRAE---QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQ 1625
Cdd:COG3096 306 ----YRLVEMARELEELSARESDLEQ-------DYQAASdhlNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1626 GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG-SAQSRAREAE-- 1702
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDyLAAFRAKEQQat 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1703 ----KLREQVGD------QYQTVRALAERKAEGVLAAQA--RAEQLRDEARGLlqaaQDKLQRLQELEGTYEENERELEV 1770
Cdd:COG3096 455 eevlELEQKLSVadaarrQFEKAYELVCKIAGEVERSQAwqTARELLRRYRSQ----QALAQRLQQLRAQLAELEQRLRQ 530
|
330 340
....*....|....*....|.
gi 1958794729 1771 KAA---QLDGLEARMRSVLQA 1788
Cdd:COG3096 531 QQNaerLLEEFCQRIGQQLDA 551
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
1607-1764 |
1.08e-04 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 45.31 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1607 AETVQAALEEAQRAQGAAQGAIRGA---VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ-----LHALLEAlklKRA 1678
Cdd:cd11386 18 AETSQQAAELAEKGREAAEDAINQMnqiDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQtnllaLNAAIEA---ARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1679 GNS------LAA---STAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQ----------ARAEQLRDE 1739
Cdd:cd11386 95 GEAgrgfavVADevrKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEetgrafeeivASVEEVADG 174
|
170 180
....*....|....*....|....*
gi 1958794729 1740 ARGLLQAAQDKLQRLQELEGTYEEN 1764
Cdd:cd11386 175 IQEISAATQEQSASTQEIAAAVEEI 199
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
1605-1739 |
1.12e-04 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 43.42 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1605 QKAETvqaALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRagNSL 1682
Cdd:pfam02050 1 DEAAR---ELAEAQRELQQAEEKLE-------ELQQYRAEYQQQLSGAGQGISAAELRNYQafISQLDEAIAQQQ--QEL 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1683 AASTAEetagsaQSRAREAEKLREQvgdQYQTVRALAERKAEGVLAAQARAEQLR-DE 1739
Cdd:pfam02050 69 AQAEAQ------VEKAREEWQEARQ---ERKSLEKLREREKKEERKEQNRREQKQlDE 117
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1504-1722 |
1.43e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1504 SRGQVEQANQELreliqNVKDFLSQEGADP-------DSIE--------MVATR------VLDISIPA-SPEQIQRLA-- 1559
Cdd:COG3524 84 SRDAVERLDAEL-----DLRAHYSRPGIDPlsrldpdASIEdlykyyrrRVKVEydstsgIITLEVRAfDPEDAQAIAea 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1560 ----SE-----IAERVRSladvDTIlAHTMGDVRRAEQLLQDAQRARSRAegeRQKAETVQAAleeaqrAQGAAQGAIRG 1630
Cdd:COG3524 159 llaeSEelvnqLSERARE----DAV-RFAEEEVERAEERLRDAREALLAF---RNRNGILDPE------ATAEALLQLIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1631 AVVDTKNTEQT-LQQVQERMAGTEQSLNSASERARQLHALLEALKLK----RAGNSLAASTAE-ETagsAQSRAREAEKL 1704
Cdd:COG3524 225 TLEGQLAELEAeLAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARltgaSGGDSLASLLAEyER---LELEREFAEKA 301
|
250
....*....|....*...
gi 1958794729 1705 REQVGDQYQTVRALAERK 1722
Cdd:COG3524 302 YTSALAALEQARIEAARQ 319
|
|
| 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 ... |
1641-1733 |
1.89e-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: 43.07 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1641 TLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAqsrAREAEKLREQVGDQYQTVRALAE 1720
Cdd:pfam00430 38 EIAEAEERRKDAAAALAEAEQQLKE--ARAEAQEIIENAKKRAEKLKEEIVAAA---EAEAERIIEQAAAEIEQEKDRAL 112
|
90
....*....|...
gi 1958794729 1721 RKAEGVLAAQARA 1733
Cdd:pfam00430 113 AELRQQVVALAVQ 125
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1606-1749 |
1.93e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 46.02 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1606 KAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERArqlhallEAlKLKRAGNSLAAS 1685
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAAD-EAKTAAAAAAREAAPLKASLRKLERAKARA-------DA-ELKRADKALAAA 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1686 TAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQD 1749
Cdd:PRK12472 252 KTDEAKARAEERQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATD 315
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1587-1756 |
1.96e-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: 44.67 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1587 EQLLQDAQR--ARSRAEGERQKAETVQ------AALEEAQRAQGAAQGAIrgavvdTKNTEQTLQQVQERMAGTEQSLNS 1658
Cdd:pfam04012 28 EQAIRDMQSelVKARQALAQTIARQKQlerrleQQTEQAKKLEEKAQAAL------TKGNEELAREALAEKKSLEKQAEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1659 ASERARQLHALLEALK------------LKRAGNSLAA--STA------EETAG--SAQSRAREAEKLREQVGDQYQTVR 1716
Cdd:pfam04012 102 LETQLAQQRSAVEQLRkqlaaletkiqqLKAKKNLLKArlKAAkaqeavQTSLGslSTSSATDSFERIEEKIEEREARAD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958794729 1717 ALAERKAEGVLAAQARAEQLRDEargllqAAQDKLQRLQE 1756
Cdd:pfam04012 182 AAAELASAVDLDAKLEQAGIQME------VSEDVLARLKA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1448-1668 |
2.26e-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: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1448 AAATADLALGRARHTQAELQRALVEGggILSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIqnvkdfls 1527
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEA--ELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLD-------- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1528 qegadpdsiemvatrvldisipASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA 1607
Cdd:COG4913 682 ----------------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---QDRL 736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1608 ETVQAALEEAQRAQGAAQgaiRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1668
Cdd:COG4913 737 EAAEDLARLELRALLEER---FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1566-1783 |
2.28e-04 |
|
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: 45.10 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1566 VRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAAL----EEAQRAQGAAQGAIRGAVVDTKNTEQT 1641
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELsslaQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1642 LQQVQERMAGTEQSlnsaserARQLHALLE-ALKLKRAGNSLAASTAEETAGSAQSRareaekLREQVGDQYQTVRALAE 1720
Cdd:pfam06008 81 LGHAKELAEAIKNL-------IDNIKEINEkVATLGENDFALPSSDLSRMLAEAQRM------LGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794729 1721 rkaegvlaaqaraEQLrDEARGLLQAAQDKLQRLQELEGTYEENERE-LEVKAAQLDGLEARMR 1783
Cdd:pfam06008 148 -------------AEL-KAAQDLLSRIQTWFQSPQEENKALANALRDsLAEYEAKLSDLRELLR 197
|
|
| DUF4398 |
pfam14346 |
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. ... |
1446-1511 |
2.57e-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: 2.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1446 SGAAATADLALGRARHTQAELQRALVEGggilsRVSETRRQAEEAQQRAQAALDKANA--SRGQVEQA 1511
Cdd:pfam14346 16 DGAAQYAPLELKRARDALAKAEAAMAEK-----DYEKARHLAYLAEADAELAEAKARAakAEAAAAQA 78
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1548-1704 |
2.69e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 45.63 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1548 IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEgerqkaetvqAALEEAQRAQGAAQga 1627
Cdd:PRK12472 185 LAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARAD----------AELKRADKALAAAK-- 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1628 irgavvdtknTEQTLQQVQERMAGTEQslnSASERARQLHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEKL 1704
Cdd:PRK12472 253 ----------TDEAKARAEERQQKAAQ---QAAEAATQLDTAKADAEAKRA----AAAATKEAAKAAAAKKAETAKA 312
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1554-1795 |
2.82e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRLAS-EIAERVRSLADVDTILAHTMGDVRRAEQLLQDA----QRARSR-----AEGE-RQKA-ETVQAALEEAQRAQ 1621
Cdd:COG3206 86 QIEILKSrPVLERVVDKLNLDEDPLGEEASREAAIERLRKNltvePVKGSNvieisYTSPdPELAaAVANALAEAYLEQN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1622 GAAQgairgavvdTKNTEQTLQQVQERMAGTEQSLNSASERARQLhallealklkRAGNSLAASTAEETAGSAQSrarea 1701
Cdd:COG3206 166 LELR---------REEARKALEFLEEQLPELRKELEEAEAALEEF----------RQKNGLVDLSEEAKLLLQQL----- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1702 eklrEQVGDQYQTVRALAErkaegvlAAQARAEQLRDEARGLLQAA---------QDKLQRLQELEGTYEENEREL---- 1768
Cdd:COG3206 222 ----SELESQLAEARAELA-------EAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYtpnh 290
|
250 260 270
....*....|....*....|....*....|
gi 1958794729 1769 -EVKA--AQLDGLEARMRSVLQAINLQVQI 1795
Cdd:COG3206 291 pDVIAlrAQIAALRAQLQQEAQRILASLEA 320
|
|
| 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 1958794729 1455 ALGRARHTQ----AELQRALVEGGGILsRVSETRRQAEEAQQRAQAALDKAnasrgQVEQANQELRELIQNVKdfLSQEG 1530
Cdd:COG2268 188 ALGRRKIAEiirdARIAEAEAERETEI-AIAQANREAEEAELEQEREIETA-----RIAEAEAELAKKKAEER--REAET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1531 AdpdsiEMVATRVLDISIPASPEQIQRLAsEIAERVRSLAdvdtiLAHtmgdvRRAEQLLQDAQRA-RSRAEGERQKAET 1609
Cdd:COG2268 260 A-----RAEAEAAYEIAEANAEREVQRQL-EIAEREREIE-----LQE-----KEAEREEAELEADvRKPAEAEKQAAEA 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTE----------QTLQQVQERMA 1650
Cdd:COG2268 324 EAEAEAEAIRAKGLAEAEGKRALAEAWNKLgdaaillmliEKLPEIAEAAA 374
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1445-1789 |
2.90e-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: 45.81 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1445 CSGAAATADLALGRARHTQAELQRALVEGGGIL-------------------SRVSETRRQAEEAQQRAQAAL----DKA 1501
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLrlapDKL 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1502 NASRGQVEQANQELRELI------QNVKDFLSQEgadpdsiemvatrvldisIPASPEQIQRLASEIAERVRSLADVDTI 1575
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLglapgrQSIIDLKEKE------------------IPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1576 LAHTMGDVRRAEQLLQDAqrarsraegerQKAETVQAALEEAQR--AQGAAQgairgavVDTKNTEQTLQQVQERMAGTE 1653
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDV-----------TIMERFQMELKDVERkiAQQAAK-------LQGSDLDRTVQQVNQEKQEKQ 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1654 QSLNSASERARQLHALLEalklkragnslaasTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQA-- 1731
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQ--------------DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSli 901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794729 1732 -RAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVK----AAQLDGLEARMRSVLQAI 1789
Cdd:TIGR00606 902 rEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKvndiKEKVKNIHGYMKDIENKI 964
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1585-1620 |
2.97e-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: 2.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958794729 1585 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1620
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1482-1792 |
3.00e-04 |
|
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: 44.91 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1482 ETRRQAEEAQQRAQAALDKANAsRGQVEQANQ--ELRELIQNVKDFLSQEGadpdsiemvatRVLDISIPASPEQIQRLA 1559
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERK-RYRQELEEQieEREQKRQEEYEEKLQER-----------EQMDEIVERIQEEDQAEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1560 SEIAERVRsladvdtilaHTMGDVRRAEQLLQDA---QRARSRAEGER------QKAETvQAALEEAQRAQGAAQgairg 1630
Cdd:pfam13868 119 EEKLEKQR----------QLREEIDEFNEEQAEWkelEKEEEREEDERileylkEKAER-EEEREAEREEIEEEK----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1631 avvdtknteqtlQQVQERMAgTEQslnsasERARQLHALLEALKLKRAgnslaastAEETAgsAQSRAREAEKlreqvgd 1710
Cdd:pfam13868 183 ------------EREIARLR-AQQ------EKAQDEKAERDELRAKLY--------QEEQE--RKERQKEREE------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1711 qyqtvralAERKAEGVLA-AQARAEQLRDEARGL-LQAAQDK------LQRLQELegtyEENERELEVKAAQLDglEARM 1782
Cdd:pfam13868 227 --------AEKKARQRQElQQAREEQIELKERRLaEEAEREEeefermLRKQAED----EEIEQEEAEKRRMKR--LEHR 292
|
330
....*....|
gi 1958794729 1783 RSVLQAINLQ 1792
Cdd:pfam13868 293 RELEKQIEER 302
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1577-1759 |
3.13e-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: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1577 AHTMGDVRRAEQLLqdaQRARSRAEGERQKAETVQAaleEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSL 1656
Cdd:COG3071 60 AQALGDYERRDEYL---AQALELAPEAELAVLLTRA---ELLLDQGQAEQAL-----------ATLEALRAGAPRHPQVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1657 NSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREA--EKLREQVGDQYQTVRAL-----AERKAEGVLAA 1729
Cdd:COG3071 123 RLLLQAYRQLGDWEELLELLPALRKHKALSAEE----AQALERRAylGLLRQAARDAEALKALWkalprAERRDPELAAA 198
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958794729 1730 QARA-EQLRD--EARGLLQAAQDK------LQRLQELEG 1759
Cdd:COG3071 199 YARAlIALGDhdEAERLLREALKRqwdprlVRLYGRLQG 237
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
1663-1780 |
3.24e-04 |
|
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: 43.03 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1663 ARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKlrEQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRDE 1739
Cdd:pfam16535 1 AGQLTLLLGNLMSLLGEVSLSQLESRIAAWKAMQEAQQQKG--LELSDEFQTALSEAEeatDAYEKAINKLKNAKSKAKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958794729 1740 ARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA 1780
Cdd:pfam16535 79 AEKKIDQAQTRLQSLAPDSPGKAKLEAAEQQAGIKKDALQA 119
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1562-1758 |
3.33e-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: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1562 IAErVRSLADVDTILAHTMGDVRRAEQ--------LLQDAQRAR---SRAEGERQKAEtvQAALEEAQRAQGAAQgairg 1630
Cdd:COG2268 194 IAE-IIRDARIAEAEAERETEIAIAQAnreaeeaeLEQEREIETariAEAEAELAKKK--AEERREAETARAEAE----- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1631 avvdtknteqtlQQVQERMAGTEQSLNSASERARQLHALleALKLKRAgnslaastaeetagsAQSRAREAEKLREQVGD 1710
Cdd:COG2268 266 ------------AAYEIAEANAEREVQRQLEIAEREREI--ELQEKEA---------------EREEAELEADVRKPAEA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958794729 1711 QYQTVRALAERKAEGVLA---AQARAEQLRDEARGLLQAAQDKLQRLQELE 1758
Cdd:COG2268 317 EKQAAEAEAEAEAEAIRAkglAEAEGKRALAEAWNKLGDAAILLMLIEKLP 367
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1649-1782 |
3.46e-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: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1649 MAGTEQSLNSASERARQLHALLEALK--LKRAGNSLAastaeETAGSAQSRAREAEKLREQVGDQYQTVRAlAERKAEGV 1726
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQAIRDMQseLVKARQALA-----QTIARQKQLERRLEQQTEQAKKLEEKAQA-ALTKGNEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1727 LAAQA--RAEQLRDEARGL------LQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARM 1782
Cdd:pfam04012 84 LAREAlaEKKSLEKQAEALetqlaqQRSAVEQLRKqLAALETKIQQLKAKKNLLKARLKAAKAQE 148
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1484-1756 |
3.60e-04 |
|
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: 44.91 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1484 RRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflsQEgadpdsiemvatRVLDisipaspEQIQRLASEIA 1563
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EE------------REED-------ERILEYLKEKA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1564 ERVRSladvdtilahtmgdvRRAEQLLQDAQRARSRAE-GERQ-KAETVQAALEE--AQRAQgaaqgairgAVVDTKNTE 1639
Cdd:pfam13868 166 EREEE---------------REAEREEIEEEKEREIARlRAQQeKAQDEKAERDElrAKLYQ---------EEQERKERQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1640 QTLQQVQERMAgTEQSLNSASERARQLHALLEALKLKRA---GNSLAASTAEEtagsAQSRAREAEKLREQVGDQYQTVR 1716
Cdd:pfam13868 222 KEREEAEKKAR-QRQELQQAREEQIELKERRLAEEAEREeeeFERMLRKQAED----EEIEQEEAEKRRMKRLEHRRELE 296
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958794729 1717 ALAERKAEgvLAAQARAEQlRDEARGLLQAAQDKLQRLQE 1756
Cdd:pfam13868 297 KQIEEREE--QRAAEREEE-LEEGERLREEEAERRERIEE 333
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1458-1757 |
3.98e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.64 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1458 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnASRGQVEQANQE--LRELIQNVKDFLSQEGADPDS 1535
Cdd:pfam15558 71 KARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERA-RQEAEQRKQCQEqrLKEKEEELQALREQNSLQLQE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1536 IEMVATRVLDISIPASPEQIQrlASEIAERVRSLAdvdtiLAHTMGDVRRAEQLLqdaqrARSRAEGERQKAETVQAALE 1615
Cdd:pfam15558 150 RLEEACHKRQLKEREEQKKVQ--ENNLSELLNHQA-----RKVLVDCQAKAEELL-----RRLSLEQSLQRSQENYEQLV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1616 EaQRAQGAAQGAIRgavvdtknTEQTLQQVQERmagTEQSlnsasERARQLH----ALLEALKLKRAgNSLAASTAEETA 1691
Cdd:pfam15558 218 E-ERHRELREKAQK--------EEEQFQRAKWR---AEEK-----EEERQEHkealAELADRKIQQA-RQVAHKTVQDKA 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794729 1692 gsaqSRAREAEKLREQVGdqyqtvRALAErKAEgvlaaqaRAEQLRdeARGLLQAAQDKLQRLQEL 1757
Cdd:pfam15558 280 ----QRARELNLEREKNH------HILKL-KVE-------KEEKCH--REGIKEAIKKKEQRSEQI 325
|
|
| 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 1958794729 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 ... |
1469-1753 |
4.27e-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: 45.60 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1469 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1548
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1549 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1625
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1626 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALleaLKLKRAgnSLAASTAEETAGSAQSRareaek 1703
Cdd:NF012221 1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDAL---AKQNEA--QQAESDANAAANDAQSR------ 1750
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1704 lreqvGDQYQTvralaerkaegvlAAQARAEQLRDEARGLLQAAQDKLQR 1753
Cdd:NF012221 1751 -----GEQDAS-------------AAENKANQAQADAKGAKQDESDKPNR 1782
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1454-1713 |
4.65e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 43.95 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1454 LALGRARHTQAELQRALvegggilsRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvkdflsqegADP 1533
Cdd:COG2956 46 LALGNLYRRRGEYDRAI--------RIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE----------LDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1534 DSIEmVATRVLDISipaspEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1611
Cdd:COG2956 108 DDAE-ALRLLAEIY-----EQEGDWekAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1612 AALEEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEET 1690
Cdd:COG2956 182 LLLAELYLEQGDYEEAI-----------AALERALEQDPDYLPALPRLAELYEKLGDPEEALElLRKALELDPSDDLLLA 250
|
250 260
....*....|....*....|...
gi 1958794729 1691 AGSAQSRAREAEKLREQVGDQYQ 1713
Cdd:COG2956 251 LADLLERKEGLEAALALLERQLR 273
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1618-1789 |
5.74e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1618 QRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMagtEQSLNSASERAR---QLHALLEALKLKRAgnsLAASTAEETAGS 1693
Cdd:PTZ00491 643 ERTRDSLQKSVQLAIeITTKSQEAAARHQAELL---EQEARGRLERQKmhdKAKAEEQRTKLLEL---QAESAAVESSGQ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1694 AQSRAR-EAEKlreqvgdqyqtvrALAERKAEgVLAAQARAEQLRDEARGLLqaaqDKLQRLQELEGTYEENERELEV-K 1771
Cdd:PTZ00491 717 SRAEALaEAEA-------------RLIEAEAE-VEQAELRAKALRIEAEAEL----EKLRKRQELELEYEQAQNELEIaK 778
|
170
....*....|....*....
gi 1958794729 1772 AAQLDGLEA-RMRSVLQAI 1789
Cdd:PTZ00491 779 AKELADIEAtKFERIVEAL 797
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1556-1645 |
6.55e-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: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1556 QRLASEIAERVRSLAD-VDTILAHTMGDVRRAEQ----LLQDAQ----------RARSRAEGERQKAETVQAALEEAQRA 1620
Cdd:pfam16999 4 SRLLSELAEREAALDQqIEAARKEAEREVEAAEAeaarILREAEakakalqaeyRQELAAETARIREEARARAEAEAQAV 83
|
90 100
....*....|....*....|....*
gi 1958794729 1621 QGAAQGAIRGAVvdtkntEQTLQQV 1645
Cdd:pfam16999 84 RTRAEGRLQQAV------ELILRAV 102
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1485-1660 |
6.62e-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: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1485 RQAEEA-QQRAQAAL---------DKA-NASRGQVeqaNQELRELIQnvkdflsqEGADPDSIEMVATRVLDISIPaspE 1553
Cdd:COG0330 102 ENAEEAlRQLAESALrevigkmtlDEVlSTGRDEI---NAEIREELQ--------EALDPYGIEVVDVEIKDIDPP---E 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1554 QIQRlaseiaervrsladvdtilahTMGDVRRAEQllqDAQRARSRAEGERQKAETVqaALEEAQR----AQGAAQGAIR 1629
Cdd:COG0330 168 EVQD---------------------AMEDRMKAER---EREAAILEAEGYREAAIIR--AEGEAQRaiieAEAYREAQIL 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958794729 1630 GAVVDTKNTEQTLQQ-------VQERMAGT-EQSLNSAS 1660
Cdd:COG0330 222 RAEGEAEAFRIVAEAysaapfvLFYRSLEAlEEVLSPNS 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1585-1774 |
6.69e-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: 44.35 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1585 RAEQLLQDAQRA-----RSRAEGERqKAETVQAALEEAqraqgaaqgairgavVDTKNTEQT-LQQVQERMAGTEQSLNS 1658
Cdd:pfam05557 10 RLSQLQNEKKQMelehkRARIELEK-KASALKRQLDRE---------------SDRNQELQKrIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1659 ASERARQLHALLEALKLKRAGNSLAASTAEETA----GSAQSRAREAEKLREQVGDQYQTVRALAERKAEGVLAAQaRAE 1734
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVIsclkNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958794729 1735 QLRDEarglLQAAQDKL----QRLQELEgtYE---ENERELEVKAAQ 1774
Cdd:pfam05557 153 QLRQN----LEKQQSSLaeaeQRIKELE--FEiqsQEQDSEIVKNSK 193
|
|
| 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 1958794729 1469 ALVEGGGILSRVSETRRQAEEAQqrAQAALDKAnasRGQVEQANQELRELiQNVKDFLSQEGADPDSIEmVATRVLDISI 1548
Cdd:pfam00529 40 DRVKAGDVLFQLDPTDYQAALDS--AEAQLAKA---QAQVARLQAELDRL-QALESELAISRQDYDGAT-AQLRAAQAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1549 PASPEQIQrLASEIAERVRSLADVDTILAHTMGDVRRaeqLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAI 1628
Cdd:pfam00529 113 KAAQAQLA-QAQIDLARRRVLAPIGGISRESLVTAGA---LVAQAQANLLATVAQLDQIYVQITQSAAENQAE--VRSEL 186
|
170 180
....*....|....*....|....*
gi 1958794729 1629 RGAVVDTKNTEQTLQQVQERMAGTE 1653
Cdd:pfam00529 187 SGAQLQIAEAEAELKLAKLDLERTE 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1789 |
1.08e-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: 43.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1682 LAASTAEETAGSAQSRAREAEKLREQVgDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDklqRLQELEGTY 1761
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAEL 85
|
90 100
....*....|....*....|....*...
gi 1958794729 1762 EENERELEVKAAQLDGLEARMRSVLQAI 1789
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRAL 113
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1588-1790 |
1.16e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1588 QLLQDAQRARSRAEGERQKAETVQAALEEAQRaQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASErarqlh 1667
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA-ELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQN------ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1668 ALLEAlklkragNSLAAS--TAEETAGSAQSRAREaeklREQvgdqyQTVRALAERKAEGvlaaqaraEQLRDEARGLLQ 1745
Cdd:PRK11281 143 DLAEY-------NSQLVSlqTQPERAQAALYANSQ----RLQ-----QIRNLLKGGKVGG--------KALRPSQRVLLQ 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794729 1746 A------AQDKLQRlQELEG-----TYEENERELevKAAQLDGLEaRMRSVLQ-AIN 1790
Cdd:PRK11281 199 AeqallnAQNDLQR-KSLEGntqlqDLLQKQRDY--LTARIQRLE-HQLQLLQeAIN 251
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1699-1794 |
1.18e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1699 REAE----KLREQVGDQyQTVRALAERKAEgvlAAQARAEQLRDEARGLLQAAQDKL-----QRLQELEGTYEENERELE 1769
Cdd:COG1842 33 RDMEedlvEARQALAQV-IANQKRLERQLE---ELEAEAEKWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA 108
|
90 100
....*....|....*....|....*
gi 1958794729 1770 vkaaQLDGLEARMRSVLQAINLQVQ 1794
Cdd:COG1842 109 ----QLEEQVEKLKEALRQLESKLE 129
|
|
| 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 1958794729 350 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 403
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1605-1762 |
1.23e-03 |
|
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: 43.51 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1605 QKAETVQAAleEAQRAQGAAQGAIRGAVVDTKnTEQTLQQVQERMAGTEQSLNsaseRARQLHALLEALKLKRAgnSLAA 1684
Cdd:pfam15070 1 QLMESLKQL--QTERDQYAENLKEEGAVWQQK-MQQLSEQVRTLREEKERSVS----QVQELETSLAELKNQAA--VPPA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1685 STAEETAGSAQSRAR---EAEKLREQVGDqyqtvralaerkaegvLAAQARAeQLRDEArGLLQAAQDKLQRLQELEGTY 1761
Cdd:pfam15070 72 EEEQPPAGPSEEEQRlqeEAEQLQKELEA----------------LAGQLQA-QVQDNE-QLSRLNQEQEQRLLELERAA 133
|
.
gi 1958794729 1762 E 1762
Cdd:pfam15070 134 E 134
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1535-1749 |
1.68e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1535 SIEMVATRVLDISIPASPEQIQRLASEIAERVRSLA-------DVDTILAHTMGDVRRAEQL---LQ--DAQRARSRAEG 1602
Cdd:PRK09039 35 TVFVVAQFFLSREISGKDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQalLAELAGAGAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1603 ERQKAETVQA-ALEEAQRAQGAAQgairgavVDTKNteQTLQQVQERMAGTEQSLNSASERARQLHALLEALklkraGNS 1681
Cdd:PRK09039 115 EGRAGELAQElDSEKQVSARALAQ-------VELLN--QQIAALRRQLAALEAALDASEKRDRESQAKIADL-----GRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1682 LAASTAEETAGSAQSRAREAEKLREQVGDQyQTVRALAER---KAEgVLAAQARAE-------QLRDEARGLLQAAQD 1749
Cdd:PRK09039 181 LNVALAQRVQELNRYRSEFFGRLREILGDR-EGIRIVGDRfvfQSE-VLFPTGSAElnpegqaEIAKLAAALIELAKE 256
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
1660-1791 |
1.84e-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: 40.43 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1660 SERARQLHALLEALKLKRA------GNSLAASTAEETAGSAQsrAREAEKLREQVgdqyqtVRALAERKAEGVLAAQARA 1733
Cdd:pfam05130 8 EEELELLEELLELLEEEQEalkagdIEALEELTEEKQELLQK--LAQLEKERREL------LAELGLSPEEATLSELLAK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794729 1734 EQLRDEARGLLQAAQDKLQRLQELEgtyEENeRELevkaaqldgLEARMRSVLQAINL 1791
Cdd:pfam05130 80 EEEDPELRELWQELLELLERLKELN---ELN-GEL---------IEQSLEFNNRSLNI 124
|
|
| 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 ... |
1719-1795 |
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 1958794729 1719 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1790
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121
|
....*
gi 1958794729 1791 LQVQI 1795
Cdd:pfam00430 122 LAVQI 126
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1553-1650 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQ------RARSRAEGERQKAETVQAALEEAQRAQGAAQG 1626
Cdd:COG0711 31 ERQEKIADGLAEAERAKEEAEAALA-------EYEEKLAEARaeaaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEA 103
|
90 100
....*....|....*....|....
gi 1958794729 1627 AIRGAVvdtkntEQTLQQVQERMA 1650
Cdd:COG0711 104 EIEQER------AKALAELRAEVA 121
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1478-1789 |
2.31e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1478 SRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ-EGADPDSIEMVATRVLDISIPASPEQIQ 1556
Cdd:PRK10246 304 AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEhDRFRQWNNELAGWRAQFSQQTSDREQLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1557 RLASEIAERVRSLADV-DTILAHTMGDVRRAEqllqdAQRARSRAegERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:PRK10246 384 QWQQQLTHAEQKLNALpAITLTLTADEVAAAL-----AQHAEQRP--LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1636 KNTEQTLQQVQERMAGTEQSLNSAS---ERARQLHALLEALKLKRAGNS--LAASTAEE--------TAGSAQSRAREAE 1702
Cdd:PRK10246 457 TQRNAALNEMRQRYKEKTQQLADVKticEQEARIKDLEAQRAQLQAGQPcpLCGSTSHPaveayqalEPGVNQSRLDALE 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1703 KLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQD-------KLQRLQELEG---TYEENEREL---- 1768
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAvcaslniTLQPQDDIQPwldAQEEHERQLrlls 616
|
330 340
....*....|....*....|...
gi 1958794729 1769 --EVKAAQLDGLEARMRSVLQAI 1789
Cdd:PRK10246 617 qrHELQGQIAAHNQQIIQYQQQI 639
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1553-1797 |
2.68e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQ----RLASEIaERVRSLADVDTILAhtmgdvRRAEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQGAI 1628
Cdd:pfam00038 4 EQLQelndRLASYI-DKVRFLEQQNKLLE------TKISELRQKKGAEPSRLY------SLYEKEIEDLRRQLDTLTVER 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1629 RGAVVDTKNTEQTLQQVQERMAgTEQSLNSASERA-----RQLHAL-LEALKLKRAGNSLAastaEETAgsAQSRAREAE 1702
Cdd:pfam00038 71 ARLQLELDNLRLAAEDFRQKYE-DELNLRTSAENDlvglrKDLDEAtLARVDLEAKIESLK----EELA--FLKKNHEEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1703 --KLREQVGDQYQTV-----------RALAERKAE-GVLAA----------QARAEQLRDEARGLLQAAQDKLQRLQELE 1758
Cdd:pfam00038 144 vrELQAQVSDTQVNVemdaarkldltSALAEIRAQyEEIAAknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELR 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958794729 1759 GTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1797
Cdd:pfam00038 224 RTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQ 262
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1695-1759 |
2.92e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 40.29 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1695 QSRAREAEKLREQVGD---QYQTVRALAERKAEGVLA--------------AQAR--AEQLRDEARGllQAAQDKLQRLQ 1755
Cdd:PRK14473 45 EESLRDAEKVREQLANakrDYEAELAKARQEAAKIVAqaqeraraqeaeiiAQARreAEKIKEEARA--QAEQERQRMLS 122
|
....
gi 1958794729 1756 ELEG 1759
Cdd:PRK14473 123 ELKS 126
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1456-1544 |
2.94e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 40.29 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1456 LGRA-RHTQAELQRALVEGGGILSRVSEtRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSqegadpD 1534
Cdd:PRK14473 58 LANAkRDYEAELAKARQEAAKIVAQAQE-RARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIA------D 130
|
90
....*....|
gi 1958794729 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 |
3.07e-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: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1563 AERVRSLADVDTILAHTmgdVRRAEQLLQDAQRarsraEGERQKAETVQAALEEAQRAQgAAQGAirGAVVDtknTEQTL 1642
Cdd:TIGR02499 6 AEDLAALAQAQAILAAA---RQRAEAILADAEE-----EAEASRQLGYEQGLEQFWQEA-AAQLA--EWQQE---AEQLE 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958794729 1643 QQVQERMAG-----TEQSLNSASERARQLHALLEALKLKR 1677
Cdd:TIGR02499 72 ASLEERLAElvlqaLEQILGEYDEPERLVRLLRQLLRAVA 111
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1553-1674 |
3.08e-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: 39.10 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1553 EQIQRL---ASEIAERVRSLADVDTilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgaiR 1629
Cdd:pfam18595 9 EELAELerkARELQAKIDALQVVEK-------DLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEIEL-------R 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958794729 1630 GAVVDTKNTEQTLQQVQERMAGTEQslnSASERARQLHALLEALK 1674
Cdd:pfam18595 75 ELERREERLQRQLENAQEKLERLRE---QAEEKREAAQARLEELR 116
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1719-1787 |
3.39e-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: 3.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794729 1719 AERKAEgvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKaaqldgLEARMRSVLQ 1787
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 1958794729 309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| F-BAR_FCHSD |
cd07654 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ... |
1589-1751 |
3.89e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153338 [Multi-domain] Cd Length: 264 Bit Score: 41.03 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1589 LLQDAQR-ARSRAEGERQKAETVQAALEEAQRAQGAAQGAI------RGAVVDTKNTEQTLQQVQERMAGTEQSLNSASE 1661
Cdd:cd07654 20 LLEDIRTySQKKAAIEREYGQALQKLASQFLKREWPGSGELkpeddrSGYTVWGAWLEGLDAVAQSRQNRCEAYRRYISE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1662 RARQLHALLEaLKLKRAGNSLAASTAEetagsAQSRAREAEKLREQVGDQYQtVRALAERKAEGVLAAQARAEQLRDEAR 1741
Cdd:cd07654 100 PAKTGRSAKE-QQLKKCTEQLQRAQAE-----VQQTVRELSKSRKTYFEREQ-VAHLAREKAADVQAREARSDLSIFQSR 172
|
170
....*....|
gi 1958794729 1742 GLLQAAQDKL 1751
Cdd:cd07654 173 TSLQKASVKL 182
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
1642-1767 |
4.80e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 39.07 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1642 LQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAAS--TAEETAgsaqsrareaEKLREQvgdqyqtvralA 1719
Cdd:COG3599 29 LDEVAEDYERLIRENKELKEKLEELEEELE--EYRELEETLQKTlvVAQETA----------EEVKEN-----------A 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958794729 1720 ERKAEGVLA-AQARAEQLRDEARgllqaaqdklQRLQELEGTYEENERE 1767
Cdd:COG3599 86 EKEAELIIKeAELEAEKIIEEAQ----------EKARKIVREIEELKRQ 124
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1447-1747 |
5.00e-03 |
|
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: 41.05 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1447 GAAATAD--LALGRARHTQAE--LQRAlvegggilsrvsetrrqAEEAQQRAQAALDKANAS--RGQVEQANQELRELIQ 1520
Cdd:COG3071 16 LLAALLEglLALAEGRYARAEklLSKA-----------------AEHSEAPLLAYLLAARAAqaLGDYERRDEYLAQALE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1521 NvkdflsqegaDPDSIEMVAtrvldisipaspeqiqrlaseiaervrsladvdtilahtmgdVRRAEQLLQ--DAQRARS 1598
Cdd:COG3071 79 L----------APEAELAVL------------------------------------------LTRAELLLDqgQAEQALA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1599 RAEGERQKA---ETVQAALEEAQRAQGAAQGAI--------RGAVvdtknTEQTLQQVQERMAgtEQSLNSASERARQLH 1667
Cdd:COG3071 107 TLEALRAGAprhPQVLRLLLQAYRQLGDWEELLellpalrkHKAL-----SAEEAQALERRAY--LGLLRQAARDAEALK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1668 ALLEAL-KLKRAGNSLAASTAEetAGSAQSRAREAEK-LREQVGDQYQT--VRALAERKAEGVLAAQARAE--------- 1734
Cdd:COG3071 180 ALWKALpRAERRDPELAAAYAR--ALIALGDHDEAERlLREALKRQWDPrlVRLYGRLQGGDPAKQLKRAEkwlkkhpnd 257
|
330 340
....*....|....*....|....*..
gi 1958794729 1735 --------------QLRDEARGLLQAA 1747
Cdd:COG3071 258 pdlllalgrlclrnQLWGKAREYLEAA 284
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1634-1788 |
5.10e-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: 40.51 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1634 DTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALklkragnslaastaeetagsAQSRAREAEKLREQVGD--- 1710
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL--------------------IEEGHPDAEEIQERLEElnq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1711 QYQTVRALAERKAEGVLAAQARAEQLRD------------------EARGLLQAAQDKLQRLQELegtyeenERELEVKA 1772
Cdd:cd00176 87 RWEELRELAEERRQRLEEALDLQQFFRDaddleqwleekeaalaseDLGKDLESVEELLKKHKEL-------EEELEAHE 159
|
170
....*....|....*.
gi 1958794729 1773 AQLDGLEARMRSVLQA 1788
Cdd:cd00176 160 PRLKSLNELAEELLEE 175
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1583-1724 |
5.27e-03 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 39.30 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1583 VRRAEQLLQDAQRARSRAEGERQKAEtvQAALEEAQRAQGAAQGAIrgavVDTKNTEQTLQQV---QERMAGTEQSLNSA 1659
Cdd:pfam07321 19 VKRQEQALAAARAAHQQAQASLQDYR--AWRPQEEQRLYAEIQGKL----VLLKELEKVKQQVallRENEADLEKQVAEA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794729 1660 serARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKLREQVGDQYQTVRALAERKAE 1724
Cdd:pfam07321 93 ---RQQLEAEREALRQARQ--------------ALAEARRAVEKFAELVRLVQAEELRQQERQEE 140
|
|
| DUF6468 |
pfam20072 |
Domain of unknown function (DUF6468); This domain of unknown function is found in ... |
1646-1729 |
5.29e-03 |
|
Domain of unknown function (DUF6468); This domain of unknown function is found in uncharacterized proteins predominantly from Alphaproteobacteria but it is also present in some sequences from eukaryotes. This domain is approximately 75 amino acids in length.
Pssm-ID: 437904 Cd Length: 76 Bit Score: 37.53 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1646 QERMAGTEQSLNSASERARqlhALLEALKlkragnslaaSTAEETAGSAQSRAREAEKLREQVGDQYQTVRALAERKAEG 1725
Cdd:pfam20072 5 RDELRALIAELNEATERAE---RAIAGLR----------ATAEEAGRTLGERLEKAEALRDELAFLVERGEALADRLEAI 71
|
....
gi 1958794729 1726 VLAA 1729
Cdd:pfam20072 72 VRAA 75
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
908-987 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 908 CERCIAGFHGDPRLPYGgqCRPC-PCPEGPGSQRHFATSCHRDgysqqIVCHCRAGYT-------GLRCEACAPGHFGDP 979
Cdd:cd13406 36 CSPCEPGFYNEAVNYEP--CKPCtQCNQRSGSEEKQKCTKTSD-----TVCRCRPGTQpldsykpGVDCVPCPPGHFSRG 108
|
....*...
gi 1958794729 980 SkpGGRCQ 987
Cdd:cd13406 109 D--NQACK 114
|
|
| 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 1958794729 1476 ILSRVSETRRQAEEAQQRAQAAL---DKANASRGQVEqanQELRELIQN------VKDFLSQ------------EGAD-P 1533
Cdd:pfam07793 459 FEEFLERERRRAELAEQRTVDAAegrERLELARQQAA---DELEQRLAGrplpevVREFLRQawsdvlaltylrHGEDsE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1534 DSIEMVAT------RVLDISIPASPEQIQRLASEIAERVRS-LADVdtilAHTMGDVRRAEQLLQDAQRARSRAEGERQK 1606
Cdd:pfam07793 536 EWQEALATaddlvwSVSPKPTAEERARLLALLPELLKRLRQgLASI----GYDPDESEAFFKELEALHAAAFRAKAAALA 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794729 1607 AETVQAALEEAQRAQGAaqgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSAS-ERARQLH 1667
Cdd:pfam07793 612 AALKAAAAKPAPAAAPA-------SPVEAEEEEALLGADAPPLAVVASPEDDAYlAQARALP 666
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1640-1777 |
6.42e-03 |
|
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: 41.20 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1640 QTLQQVQERmagteqsLNSASERARQLHALLEALKLKRAGNSLAASTAEETA---------------------GSAQSRA 1698
Cdd:pfam15070 288 QELQETQER-------LEALTQQNQQLQAQLSLLANPGEGDGLESEEEEEEAprpslsipedfesreamvaffNSALAQA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1699 R-EAEKLREQVGDQYQTVRALAERKAEG-------VLAAQARAEQLRDEARGLLQAAQDKLQ-RLQEL-EGTYEENER-- 1766
Cdd:pfam15070 361 EeERAELRRQLKEQKRRCRRLAQQAAPAqeepeheAHAPGTGGDSVPVEVHQALQVAMEKLQsRFTELmQEKADLKERve 440
|
170
....*....|.
gi 1958794729 1767 ELEVKAAQLDG 1777
Cdd:pfam15070 441 ELEHRCIQLSG 451
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1639-1776 |
7.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1639 EQTLQQVQERMAGTEQSLNsaserarQLHALLEALKLKragnslaastAEETAGSAQSRAREAEKLREQVGDQYQtvrAL 1718
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEKLN-------ELIASLEELERE----------LEQKAEEAEALLKEAEKLKEELEEKKE---KL 560
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1719 AERKAEGVLAAQARAEQLRDEARgllQAAQDKLQRLQELE--GTYEENERELEVKAAQLD 1776
Cdd:PRK00409 561 QEEEDKLLEEAEKEAQQAIKEAK---KEADEIIKELRQLQkgGYASVKAHELIEARKRLN 617
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1620-1783 |
8.88e-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: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1620 AQGAAQGAIrgAVVDTKNT--EQTLQQVQERMAgteqslnsasERARQlhallealklkragnslAASTAEET-AGSAQ- 1695
Cdd:pfam05335 10 AQKAAQEAK--AANDAQAAaaEAAARQVKNQLA----------DKALQ-----------------AAKAAEAAlAGKQQi 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794729 1696 -----SRAREAEKLREQVGDQYQTvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDklqRLQELEGTYEENERELEV 1770
Cdd:pfam05335 61 veqleQELREAEAVVQEESASLQQ----SQANANAAQRAAQQAQQQLEALTAALKAAQA---NLENAEQVAAGAQQELAE 133
|
170
....*....|...
gi 1958794729 1771 KAAQLDglEARMR 1783
Cdd:pfam05335 134 KTQLLE--AAKKR 144
|
|
| |
