|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-281 |
6.44e-105 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 334.55 E-value: 6.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 47 CYPATGDLLVGRadRLTASSTCGLNGPQPYCIVSHLQDEKKCFLCDSRRPFsardnpHSHRIQNVVTSFaPQRRAAWWQS 126
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSN-NGTNETWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 127 ENGIPA---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFpGVPLAPPRHW--DDVV 201
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 202 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVV 279
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 530372442 280 RG 281
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
41-281 |
3.07e-83 |
|
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: 273.08 E-value: 3.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 41 GCSRGSCYPATGDLLVGRadRLTASSTCGLNGPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpHSHRIQNVVTSFAPQR 119
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 120 RAaWWQSEN---GIPAVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWHVYRYFSYDCGADFPGVPLAPPR- 195
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 196 -HWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 273
Cdd:smart00136 151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 530372442 274 LYELVVRG 281
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 ... |
1727-1798 |
1.10e-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: 136.03 E-value: 1.10e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530372442 1727 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1798
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1449-1786 |
3.66e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEga 1528
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1529 dpdsiemvatRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQ 1608
Cdd:COG1196 305 ----------ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1609 AALEEAQRAQGIAQGAIRGAVADTRDTEQtlyQVQERMAGAERALSSAGERARQLDALLEALKLKRagnsLAASTAEETA 1688
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1689 GSAQGRAQEAEQLLRGPLGDQyQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGtyEENERALES 1768
Cdd:COG1196 448 AEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLRGLAG 524
|
330
....*....|....*...
gi 530372442 1769 KAAQLDGLEARMRSVLQA 1786
Cdd:COG1196 525 AVAVLIGVEAAYEAALEA 542
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
783-831 |
9.03e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 9.03e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 783 CQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGFGPTGCQAC 831
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
783-828 |
9.17e-16 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 72.73 E-value: 9.17e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 783 CQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGFGPTGC 828
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1462-1781 |
1.30e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1462 ELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVL 1541
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1542 ELsipasAEQIQHLAG----------AIAERVRSLADVDAILARTVGDVR--------RAEQLLQDARRARSWAEDEKQK 1603
Cdd:PRK02224 290 EL-----EEERDDLLAeaglddadaeAVEARREELEDRDEELRDRLEECRvaaqahneEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1604 AETVQAALEEAQRAQGIAQGAI--------------------RGAVADTRDT-EQTLYQVQERMAGAERALSSAGERARQ 1662
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIeeleeeieelrerfgdapvdLGNAEDFLEElREERDELREREAELEATLRTARERVEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1663 LDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRgPLGDQYQTVKALAERkAQGVLAAQARAEQLRDEARDLl 1742
Cdd:PRK02224 445 AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDL- 521
|
330 340 350
....*....|....*....|....*....|....*....
gi 530372442 1743 qaaqdkLQRLQELEGTYEENERALESKAAQLDGLEARMR 1781
Cdd:PRK02224 522 ------EELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
782-829 |
2.70e-15 |
|
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: 71.62 E-value: 2.70e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530372442 782 PCQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGF--GPTGCQ 829
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1793 |
1.23e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1201 VQDLAARTQRLEQRAQELQQTGVLGAfessfwhMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIGEATEHLTQLE 1280
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAE-------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1281 ADLTDVQD--------------------ENFNANHALSGL-----------ERDRLALNLTLRQLDQHL----------- 1318
Cdd:TIGR02168 482 RELAQLQArldslerlqenlegfsegvkALLKNQSGLSGIlgvlselisvdEGYEAAIEAALGGRLQAVvvenlnaakka 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1319 -DLLKHSN-----FLgAYDSIRHAHSQSAEAERRANTS--ALAVPSPVSNSASARHRTEALMD--AQKEDFNSkhmANQR 1388
Cdd:TIGR02168 562 iAFLKQNElgrvtFL-PLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPKLRKALSYLLGgvLVVDDLDN---ALEL 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1389 AlGKLSAHTHTLSLTDinELVcgapgdapcatspcggagcrdedgqpRCGGLSCNGAAATADLALGRARhtqaELQRALA 1468
Cdd:TIGR02168 638 A-KKLRPGYRIVTLDG--DLV--------------------------RPGGVITGGSAKTNSSILERRR----EIEELEE 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1469 EggsilsrVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDflnqegadpdsiemvatrvLELSIPAS 1548
Cdd:TIGR02168 685 K-------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-------------------LRKDLARL 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1549 AEQIQHLAGAIAERVRSLADVDAILARtvgdvrrAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGA 1628
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEE-------LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1629 VADTRDTEQtlyQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETagsaqgRAQEAEQLlrgplgd 1708
Cdd:TIGR02168 812 LTLLNEEAA---NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL------IEELESEL------- 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1709 qyqtVKALAERKAQgvlaaQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAIN 1788
Cdd:TIGR02168 876 ----EALLNERASL-----EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
....*
gi 530372442 1789 LQVQI 1793
Cdd:TIGR02168 947 EEYSL 951
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1479-1767 |
6.17e-14 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 77.56 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1479 ETRRQASEAQQRAQAALDKANASRGQV-EQANQELQELIQSVKDFLNQEGADPDsiemvatrvlELSIPASAEqiqhlag 1557
Cdd:NF041483 441 EARRLRGEAEQLRAEAVAEGERIRGEArREAVQQIEEAARTAEELLTKAKADAD----------ELRSTATAE------- 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1558 aiAERVRSLADVDAILARtvgdvRRAEQLLQDAR----RARSWAEDEkqkAETVQAALEEAqrAQGIAQGAIRGAVADTR 1633
Cdd:NF041483 504 --SERVRTEAIERATTLR-----RQAEETLERTRaeaeRLRAEAEEQ---AEEVRAAAERA--ARELREETERAIAARQA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1634 DTEQTLYQVQ----ERMAGAERALSSA---GERARQlDALLEALKLK-------RAGNSLAASTAE----ETAGSAQGRA 1695
Cdd:NF041483 572 EAAEELTRLHteaeERLTAAEEALADAraeAERIRR-EAAEETERLRteaaeriRTLQAQAEQEAErlrtEAAADASAAR 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1696 QEAEQL---LRGPLGDQYQTVKALAERKAQGVLA-AQARAEQLRDEARDLLQAAQDK-LQRLQELEGTY--------EEN 1762
Cdd:NF041483 651 AEGENVavrLRSEAAAEAERLKSEAQESADRVRAeAAAAAERVGTEAAEALAAAQEEaARRRREAEETLgsaraeadQER 730
|
....*
gi 530372442 1763 ERALE 1767
Cdd:NF041483 731 ERARE 735
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1444-1782 |
3.99e-13 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 75.25 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1444 GAAATADLALGRAR----------HTQAELQRALAEG--GSILSRVAETRRQASE----AQQRAQAALDKANASRGQVEQ 1507
Cdd:NF041483 204 SARAEAEAILRRARkdaerllnaaSTQAQEATDHAEQlrSSTAAESDQARRQAAElsraAEQRMQEAEEALREARAEAEK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1508 ANQELQEliQSVKDFLNQEGADPDSI----EMVATRVLEL-----SIPASAEQIQHLAGAIAERVRSLAdvdAILARTVG 1578
Cdd:NF041483 284 VVAEAKE--AAAKQLASAESANEQRTrtakEEIARLVGEAtkeaeALKAEAEQALADARAEAEKLVAEA---AEKARTVA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1579 DVRRAEQLlqdARRARSwAEDEKQKA-----ETVQAALEEAQR---------------AQGIAQGAIRGAVADTRDTEQT 1638
Cdd:NF041483 359 AEDTAAQL---AKAART-AEEVLTKAsedakATTRAAAEEAERirreaeaeadrlrgeAADQAEQLKGAAKDDTKEYRAK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1639 LYQVQE---RMAG-AERALSSA---GERARQlDALLEALKLKRAgnslAASTAEETAGSAQGRAQEaeqlLRGPLGDQYQ 1711
Cdd:NF041483 435 TVELQEearRLRGeAEQLRAEAvaeGERIRG-EARREAVQQIEE----AARTAEELLTKAKADADE----LRSTATAESE 505
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1712 TVKALA-------ERKAQGVLA-AQARAEQLRDEARDllQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRS 1782
Cdd:NF041483 506 RVRTEAierattlRRQAEETLErTRAEAERLRAEAEE--QAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHT 582
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1255-1767 |
8.36e-13 |
|
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: 74.10 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1255 TAQLVEATEELRRE-------IGEATEHLTQLEADLTDVQDENFNANHA-LSGLERDRLALNLTLRQLDQHLDllKHSNF 1326
Cdd:pfam12128 296 DDQWKEKRDELNGElsaadaaVAKDRSELEALEDQHGAFLDADIETAAAdQEQLPSWQSELENLEERLKALTG--KHQDV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1327 LGAYDSIRHAHSQSAEAERRANTSALAVpspvSNSASARHRT--EALMDAQKEDFNSKHMANQRALgKLSAHTHTLSLTD 1404
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRDIAGIKDKLAK----IREARDRQLAvaEDDLQALESELREQLEAGKLEF-NEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1405 INELVcgapgDAPCATSpcggagcrDEDGQPRCGGLSCNgaaaTADLALGRARHTQAELQRALaeggsilsRVAETRR-Q 1483
Cdd:pfam12128 449 LKLRL-----NQATATP--------ELLLQLENFDERIE----RAREEQEAANAEVERLQSEL--------RQARKRRdQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1484 ASEAQQRAQAALDkanasrgQVEQANQELQELI----QSVKDFLNQEGAD-PDSIEMVATRVLEL-------SIPASAEQ 1551
Cdd:pfam12128 504 ASEALRQASRRLE-------ERQSALDELELQLfpqaGTLLHFLRKEAPDwEQSIGKVISPELLHrtdldpeVWDGSVGG 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1552 IQHLAGaIAERVRSLaDVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAvad 1631
Cdd:pfam12128 577 ELNLYG-VKLDLKRI-DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA--- 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1632 tRDTEQTLYQVQERMAGA-----ERALSSAGERARQLDALLEALKLKRagnSLAASTAEETAGSAQGRAQEAEQLLRGPL 1706
Cdd:pfam12128 652 -RLDLRRLFDEKQSEKDKknkalAERKDSANERLNSLEAQLKQLDKKH---QAWLEEQKEQKREARTEKQAYWQVVEGAL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1707 GDQYQTVK-ALAERKAQgvlaAQARAEQLRDE-ARDLLQAAQDKlQRLQELEGTYEENERALE 1767
Cdd:pfam12128 728 DAQLALLKaAIAARRSG----AKAELKALETWyKRDLASLGVDP-DVIAKLKREIRTLERKIE 785
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1773 |
9.62e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.63 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RAR-HTQA----ELQRALAEGGSILSRvAETRRQASEAQQRAQAaldKANASRGQVEQAnqelqeLIQSVKDflnqegad 1529
Cdd:NF041483 158 RARtESQArrllDESRAEAEQALAAAR-AEAERLAEEARQRLGS---EAESARAEAEAI------LRRARKD-------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1530 pdsiemvATRVLElsipASAEQIQHlAGAIAERVRS--LADVDAILARTVGDVRRAEQLLQDA----RRARswAEDEKQK 1603
Cdd:NF041483 220 -------AERLLN----AASTQAQE-ATDHAEQLRSstAAESDQARRQAAELSRAAEQRMQEAeealREAR--AEAEKVV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1604 AETVQAALEEAQRAQGIAQGAIRGAvadtrdTEQTLYQVQERMAGAErALSSAGERARQlDALLEALKL-KRAGNSLAAS 1682
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1683 TAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQ----AAQD--KLQRLQELE 1756
Cdd:NF041483 358 AAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEqlkgAAKDdtKEYRAKTVE 437
|
330
....*....|....*..
gi 530372442 1757 gtYEENERALESKAAQL 1773
Cdd:NF041483 438 --LQEEARRLRGEAEQL 452
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1250-1782 |
9.79e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.63 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1250 TSAASTAQLVEATEELRREIGEATEHLTQLEADLTDVQDENfnanhalsglERDRlalnltlRQLDQHLDLLKHSnflgA 1329
Cdd:NF041483 562 TERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEA----------ERIR-------REAAEETERLRTE----A 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1330 YDSIRHAHSQS-AEAER-RANTSALAVPSPVSNSASA-RHRTEALMDAQKEDFNSKHMANQ-RALGKLSAHTHTlslTDI 1405
Cdd:NF041483 621 AERIRTLQAQAeQEAERlRTEAAADASAARAEGENVAvRLRSEAAAEAERLKSEAQESADRvRAEAAAAAERVG---TEA 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1406 NELVCGAPGDApcatspcggAGCRDEDGQprcgglSCNGAAATADLALGRARHTQAELqralaeggsilsrVAETRRQAS 1485
Cdd:NF041483 698 AEALAAAQEEA---------ARRRREAEE------TLGSARAEADQERERAREQSEEL-------------LASARKRVE 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1486 EAQQRAQAALDKANASRGQ-VEQANQELQELIQSVKDFlnQEGADpdsiEMVATrvLELSIPASAEQIQHLAGAIAERVR 1564
Cdd:NF041483 750 EAQAEAQRLVEEADRRATElVSAAEQTAQQVRDSVAGL--QEQAE----EEIAG--LRSAAEHAAERTRTEAQEEADRVR 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1565 SladvDAILARtvgdvrraEQLLQDARRARSWAEDEKQKAE-----TVQAALEEAQRAQgiaqgairgavADTRDTEQTL 1639
Cdd:NF041483 822 S----DAYAER--------ERASEDANRLRREAQEETEAAKalaerTVSEAIAEAERLR-----------SDASEYAQRV 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1640 -YQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAqEAEQLLRGPLGDQYQTVKALAE 1718
Cdd:NF041483 879 rTEASDTLASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARA-EAERLRDEARAEAERVRADAAA 957
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1719 RKAQGVLAAQARAEQLRDEARDLLQAAQdklqrlQELEGTYEENERALESKAAQLDGLEARMRS 1782
Cdd:NF041483 958 QAEQLIAEATGEAERLRAEAAETVGSAQ------QHAERIRTEAERVKAEAAAEAERLRTEARE 1015
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
521-562 |
3.58e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 3.58e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 530372442 521 PCDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFRP 562
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1095-1143 |
6.11e-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: 58.90 E-value: 6.11e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 1095 CACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDPGLQCHAC 1143
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1143-1190 |
6.73e-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: 58.90 E-value: 6.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530372442 1143 CDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGiFPACHPC 1190
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
831-879 |
8.19e-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: 8.19e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 831 CQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWGFPSCRPCVC 879
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
522-561 |
9.44e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 9.44e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530372442 522 CDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFR 561
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
469-520 |
2.06e-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: 57.75 E-value: 2.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 530372442 469 RCQCNARGTVPGStpCDPNSGSCYCKRLVTGRGCDRCLPGHWGLSHDLLGCR 520
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1037-1093 |
2.30e-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: 2.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1037 RCTCNLLGTNPQQCpspdqchcDPSSGQCPCLPNVQGPSCDRCAPNFWNLTS-GHGCQ 1093
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1142-1191 |
3.20e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 3.20e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530372442 1142 ACDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGIFPACHPCH 1191
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1038-1092 |
3.55e-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: 3.55e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1038 CTCNLLGTNPQQCpspdqchcDPSSGQCPCLPNVQGPSCDRCAPNFWNL--TSGHGC 1092
Cdd:pfam00053 1 CDCNPHGSLSDTC--------DPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1143-1187 |
7.80e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 7.80e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 1143 CDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGI-FPAC 1187
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1095-1140 |
8.95e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 8.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 1095 CACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDPGLQC 1140
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
410-467 |
9.35e-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: 55.82 E-value: 9.35e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 410 CDCDPMGSQdGGRCDSHddpalglvSGQCRCKEHVVGTRCQQCRDGFFGLSISDRLGC 467
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1038-1092 |
1.35e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.35e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1038 CTCNLLGTNPQQCpspdqchcDPSSGQCPCLPNVQGPSCDRCAPNFWNlTSGHGC 1092
Cdd:smart00180 1 CDCDPGGSASGTC--------DPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1775 |
1.59e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.31 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RARHTQAELQRALAEGGSILSRvAETRR---QASEAQQRAQAALDKANASRGQveQANQELQELIQSVKDFLNqegadpd 1531
Cdd:NF041483 79 RNAQIQADQLRADAERELRDAR-AQTQRilqEHAEHQARLQAELHTEAVQRRQ--QLDQELAERRQTVESHVN------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1532 siEMVATrvlelsipasAEQIqhlagaiaeRVRSLADvdailARTVGDVRRAE--QLLQDARrarswAEDEKQKAETVQA 1609
Cdd:NF041483 149 --ENVAW----------AEQL---------RARTESQ-----ARRLLDESRAEaeQALAAAR-----AEAERLAEEARQR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1610 ALEEAQRAQGIAQGAIRGAVADtrdteqtlyqvqermagAERALSSAGERARQLDALLEALKLKRAGNSLAA-STAEETA 1688
Cdd:NF041483 198 LGSEAESARAEAEAILRRARKD-----------------AERLLNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1689 GSAQGRAQEAEQLLRgplgdqyqtvkalaerkaqgvlAAQARAEQLRDEARDllQAAqdklQRLQELEGTYEENERALES 1768
Cdd:NF041483 261 RAAEQRMQEAEEALR----------------------EARAEAEKVVAEAKE--AAA----KQLASAESANEQRTRTAKE 312
|
....*..
gi 530372442 1769 KAAQLDG 1775
Cdd:NF041483 313 EIARLVG 319
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1094-1136 |
2.06e-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: 2.06e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530372442 1094 PCACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDP 1136
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
470-524 |
2.54e-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: 2.54e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 470 CQCNARGTVPGStpCDPNSGSCYCKRLVTGRGCDRCLPGHWGLSHDLlgcrPCDC 524
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
522-561 |
3.50e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.90 E-value: 3.50e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530372442 522 CDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFR 561
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
830-873 |
6.09e-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: 53.51 E-value: 6.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 530372442 830 ACQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWGFPS 873
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1244-1593 |
7.19e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1244 IVGARNTSAASTAQLVEATEELRREIGEATEHLTQLEADLTDVQDENFNANHALSGLERDRLALNLTLRQLDQHLD-LLK 1322
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1323 HSNFLGAYDSIRHAHSQSAEAERRANTSALAvpspvsNSASARHRTEALM---DAQKEDFNSKHMANQRALGKLSAHTHT 1399
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLE------EAEEELAEAEAEIeelEAQIEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1400 LSltdinelvcgapGDAPCATSPCGGAGCRDEDGQPRCGGLSCNGAAATADLAlgRARHTQAELQRALAEGGSILSRVAE 1479
Cdd:TIGR02168 815 LN------------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--SLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1480 TRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMvatrvlelsipasaeQIQHLAGAI 1559
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---------------RIDNLQERL 945
|
330 340 350
....*....|....*....|....*....|....*
gi 530372442 1560 AERVR-SLADVDAILARTVGDVRRAEQLLQDARRA 1593
Cdd:TIGR02168 946 SEEYSlTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
831-874 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 831 CQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWG--FPSC 874
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-513 |
1.20e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.20e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 530372442 470 CQCNARGTVPGStpCDPNSGSCYCKRLVTGRGCDRCLPGHWGLS 513
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
409-468 |
4.32e-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: 50.82 E-value: 4.32e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 409 SCDCDPMGSQdGGRCDSHddpalglvSGQCRCKEHVVGTRCQQCRDGFFGLSiSDRLGCR 468
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
986-1028 |
4.51e-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: 50.81 E-value: 4.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530372442 986 CECSGNIDPmdPDACDPHTGQCLrCLHHTEGPHCAHCKPGFHG 1028
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
876-921 |
4.54e-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: 50.82 E-value: 4.54e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 876 PCVCNGHAD---ECNTHTGACLgCRDHTGGEHCERCIAGFHGDPRLPYG 921
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
877-924 |
1.42e-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: 49.66 E-value: 1.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 530372442 877 CVCNGHA---DECNTHTGACLgCRDHTGGEHCERCIAGFHGDPRLPyGGQC 924
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
410-460 |
1.62e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 1.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 530372442 410 CDCDPMGSQDGgRCDSHddpalglvSGQCRCKEHVVGTRCQQCRDGFFGLS 460
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
986-1032 |
2.28e-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: 48.89 E-value: 2.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530372442 986 CECSGNIDPmdPDACDPHTGQCLrCLHHTEGPHCAHCKPGFHGQAAR 1032
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1445-1701 |
4.36e-07 |
|
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: 53.44 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLAlgRARHTQAE-LQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVkdfl 1523
Cdd:smart00283 17 AEELEELA--ERMEELSAsIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESS---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1524 nqegadpDSIEmvatRVLEL--SIpasAEQIQHLA--GAI---------------AERVRSLADvdailaRTvgdvrrae 1584
Cdd:smart00283 91 -------DEIG----EIVSVidDI---ADQTNLLAlnAAIeaarageagrgfavvADEVRKLAE------RS-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1585 qllQDArrarswAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMagaERALSSAGERARQLD 1664
Cdd:smart00283 143 ---AES------AKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSV---EEIADLVQEIAAATD 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 530372442 1665 ALLEALK-LKRAGNSLA------ASTAEETAGSAQGRAQEAEQL 1701
Cdd:smart00283 211 EQAAGSEeVNAAIDEIAqvtqetAAMSEEISAAAEELSGLAEEL 254
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
926-984 |
4.33e-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: 45.42 E-value: 4.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 926 PCPCPeGPGSQRHfatSCHQDeysqQIVCHCRAGYTGLRCEACAPGHFGDPSRPGGrCQ 984
Cdd:cd00055 1 PCDCN-GHGSLSG---QCDPG----TGQCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1445-1754 |
4.46e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQAELQRALAEGGsilsrvAETRRQASEAQQRAQAALDKANasrgqvEQANQELQEliqsvkdfln 1524
Cdd:NF041483 977 AAETVGSAQQHAERIRTEAERVKAEAA------AEAERLRTEAREEADRTLDEAR------KDANKRRSE---------- 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1525 qegadpdsiemVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRR-AEQLLQDAR-RARSWAEDEKQ 1602
Cdd:NF041483 1035 -----------AAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKeAERIVAEATvEGNSLVEKART 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1603 KAETVqaaLEEAQRaqgiAQGAIRGAVADTRD-TEQTLYQVQERmagAER----ALSSAGERArqlDALLEALKLKRAGn 1677
Cdd:NF041483 1104 DADEL---LVGARR----DATAIRERAEELRDrITGEIEELHER---ARResaeQMKSAGERC---DALVKAAEEQLAE- 1169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1678 slAASTAEETAGSAQGRA--------QEAEQLLRgplgdQYQTVKALAERKAQGVLA-AQARAEQLRDEARDLLqaaqDK 1748
Cdd:NF041483 1170 --AEAKAKELVSDANSEAskvriaavKKAEGLLK-----EAEQKKAELVREAEKIKAeAEAEAKRTVEEGKREL----DV 1238
|
....*.
gi 530372442 1749 LQRLQE 1754
Cdd:NF041483 1239 LVRRRE 1244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
986-1028 |
1.01e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 530372442 986 CECS--GNIDPmdpdACDPHTGQCLrCLHHTEGPHCAHCKPGFHG 1028
Cdd:smart00180 1 CDCDpgGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
953-983 |
1.50e-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: 43.88 E-value: 1.50e-05
10 20 30
....*....|....*....|....*....|.
gi 530372442 953 VCHCRAGYTGLRCEACAPGHFGDPSRPGGRC 983
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| 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 ... |
1701-1793 |
1.50e-05 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 46.15 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1701 LLRGPLGDQYQTVKAL-------AERKAQGVLAAQARAEQL----RDEARDLLQAAQDKLQRL-QELEG-TYEENERALE 1767
Cdd:pfam00430 19 FAWKPLGKVLDKRRELiadeiaeAEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIE 98
|
90 100
....*....|....*....|....*...
gi 530372442 1768 SKAAQLDGLEARMRSVL--QAINLQVQI 1793
Cdd:pfam00430 99 QAAAEIEQEKDRALAELrqQVVALAVQI 126
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
347-398 |
3.82e-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: 42.73 E-value: 3.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 347 CECHGH---THSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 398
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
927-976 |
4.02e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 4.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530372442 927 CPCPEGpgsqRHFATSCHQDeysqQIVCHCRAGYTGLRCEACAPGHFGDP 976
Cdd:smart00180 1 CDCDPG----GSASGTCDPD----TGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
347-399 |
4.27e-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: 42.73 E-value: 4.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372442 347 CECHGH---THSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 399
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-335 |
5.74e-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: 42.34 E-value: 5.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372442 283 CFCYGHAS---ECApapgapahaegMVHGACICKHNTRGLNCEQCQDFYRDLPWRP 335
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1466-1753 |
7.22e-05 |
|
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: 47.91 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1466 ALAEGGSILSRVAETRRQaSEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLnqEGADPDSIEMVATRVLElSI 1545
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1546 PASAEQIQHLAGAIAERVRSLaDVDAILARTVGDVRR---AEQLLQdarRARSWAEDEKQkaeTVQAALEEAQRAQGIAQ 1622
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDAL-DSQATYAGESGDQWRnpfAGGLLD---RVQEQLDDAKK---ISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1623 GAIRGAVAdtrDTEQTLYQVQERMAGAERALSSAGERA--RQLDALL---EALKLKRAGNSLA----------ASTAEET 1687
Cdd:NF012221 1685 QKVKDAVA---KSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1688 AGSAQGRAQEAEQ----------LLRGPLGDQYQTVKALAER----KAQGVLAAQAR-AEQLRDEARDLLQAAQDKLQRL 1752
Cdd:NF012221 1762 ANQAQADAKGAKQdesdkpnrqgAAGSGLSGKAYSVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNRL 1841
|
.
gi 530372442 1753 Q 1753
Cdd:NF012221 1842 Q 1842
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1256-1617 |
7.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1256 AQLVEATEELRREIGEATEHLTQLEADLTDVQDEnfnanHALSGLERDRLALNLTLRQLDQHLDLL--KHSNFLGAYDSI 1333
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELeeRLEELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1334 RHAHSQSAEAERRANTsALAVPSPVSNSASARHRTEAlmdaqkEDFNSKHMANQRALGKLSAHTHTLSlTDINELVCGAP 1413
Cdd:COG4717 166 EELEAELAELQEELEE-LLEQLSLATEEELQDLAEEL------EELQQRLAELEEELEEAQEELEELE-EELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1414 GDAPC------------ATSPCGGAGCRDEDGQP--RCGGLSCNGAAATADLALGRARH--------------------T 1459
Cdd:COG4717 238 AAALEerlkearlllliAAALLALLGLGGSLLSLilTIAGVLFLVLGLLALLFLLLAREkaslgkeaeelqalpaleelE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGG---------------------SILSRVAETRRQA--SEAQQRAQAALDKANAS-----RGQVEQAN-- 1509
Cdd:COG4717 318 EEELEELLAALGlppdlspeellelldrieelqELLREAEELEEELqlEELEQEIAALLAEAGVEdeeelRAALEQAEey 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1510 QELQELIQSVKDFLnqEGADPDSIEMVATRVLElSIPASAEQIQHLAGAIAERVRSL----ADVDAILAR--TVGDVRRA 1583
Cdd:COG4717 398 QELKEELEELEEQL--EELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELreelAELEAELEQleEDGELAEL 474
|
410 420 430
....*....|....*....|....*....|....
gi 530372442 1584 EQLLQDARRARSWAEDEKQKAETVQAALEEAQRA 1617
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
877-916 |
8.01e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 8.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530372442 877 CVCN--GHADE-CNTHTGACLgCRDHTGGEHCERCIAGFHGDP 916
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1691-1793 |
2.39e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1691 AQGRAQEAEQLLRGpLGDQYQTVKALAERKAQgVLAAQARAEQLRDEARDLLQAAQDKL---QRLQELEGTYEENERALE 1767
Cdd:COG1566 88 AEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQ-LAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDAAQAQLE 165
|
90 100
....*....|....*....|....*.
gi 530372442 1768 SKAAQLDGLEARMRSVLQAINLQVQI 1793
Cdd:COG1566 166 AAQAQLAQAQAGLREEEELAAAQAQV 191
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1680-1792 |
6.73e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 42.23 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1680 AASTAEETAGSAQGRAqEAEQLLrgplgDQYQTVKALAERKAQGVL-AAQARAEQLRDEARDLLQAAQDKLQRLQELEGT 1758
Cdd:PRK14475 43 AAKIQAELDEAQRLRE-EAQALL-----ADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERKIA 116
|
90 100 110
....*....|....*....|....*....|....
gi 530372442 1759 YEENERALESKAAQLDgLEARMRSVLQAINLQVQ 1792
Cdd:PRK14475 117 QAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1582-1617 |
7.65e-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: 40.36 E-value: 7.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530372442 1582 RAEQLLQDARRARSWAEDEKQKAE----TVQAALEEAQRA 1617
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
306-338 |
1.15e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|...
gi 530372442 306 VHGACICKHNTRGLNCEQCQDFYRDLPWRPAED 338
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
347-400 |
1.92e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 347 CECHG---HTHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 400
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1444-1512 |
2.95e-03 |
|
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: 38.43 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1444 GAAATADLAlgRARHTQAELQRALAeggSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQEL 1512
Cdd:NF040598 17 GCATTSDLE--NLQSQVQELDAKVD---QASSDAAAAQSRADEAAAKAEQAEAAANAAQQEADEANERA 80
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1504-1754 |
8.80e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1504 QVEQANQELQELIQSVKDFLNQE--GADPDSIEMVATR--VLELSIPASAEQIQHLAgAIAERVRSLADVDA-ILARTVG 1578
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTdyGDDLESVEALLKKheALEAELAAHEERVEALN-ELGEQLIEEGHPDAeEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1579 DVRRAEQLLQdarrarswaedekQKAETVQAALEEAQRAQGIAQgairgavaDTRDTEQtlyqvqeRMAGAERALSS--A 1656
Cdd:cd00176 83 ELNQRWEELR-------------ELAEERRQRLEEALDLQQFFR--------DADDLEQ-------WLEEKEAALASedL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1657 GERARQLDALLEALKlkragnslaasTAEETAGSAQGRAQEAEQLlrgplGDQYqtvkaLAERKAQGVLAAQARAEQLRD 1736
Cdd:cd00176 135 GKDLESVEELLKKHK-----------ELEEELEAHEPRLKSLNEL-----AEEL-----LEEGHPDADEEIEEKLEELNE 193
|
250
....*....|....*...
gi 530372442 1737 EARDLLQAAQDKLQRLQE 1754
Cdd:cd00176 194 RWEELLELAEERQKKLEE 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-281 |
6.44e-105 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 334.55 E-value: 6.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 47 CYPATGDLLVGRadRLTASSTCGLNGPQPYCIVSHLQDEKKCFLCDSRRPFsardnpHSHRIQNVVTSFaPQRRAAWWQS 126
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSN-NGTNETWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 127 ENGIPA---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFpGVPLAPPRHW--DDVV 201
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 202 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVV 279
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 530372442 280 RG 281
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
41-281 |
3.07e-83 |
|
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: 273.08 E-value: 3.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 41 GCSRGSCYPATGDLLVGRadRLTASSTCGLNGPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpHSHRIQNVVTSFAPQR 119
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 120 RAaWWQSEN---GIPAVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWHVYRYFSYDCGADFPGVPLAPPR- 195
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 196 -HWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 273
Cdd:smart00136 151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 530372442 274 LYELVVRG 281
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 ... |
1727-1798 |
1.10e-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: 136.03 E-value: 1.10e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530372442 1727 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1798
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 ... |
1728-1797 |
1.17e-26 |
|
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: 104.28 E-value: 1.17e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1728 QARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTC 1797
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1727-1797 |
1.30e-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: 92.92 E-value: 1.30e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530372442 1727 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTC 1797
Cdd:cd22300 2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1449-1786 |
3.66e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEga 1528
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1529 dpdsiemvatRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQ 1608
Cdd:COG1196 305 ----------ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1609 AALEEAQRAQGIAQGAIRGAVADTRDTEQtlyQVQERMAGAERALSSAGERARQLDALLEALKLKRagnsLAASTAEETA 1688
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1689 GSAQGRAQEAEQLLRGPLGDQyQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGtyEENERALES 1768
Cdd:COG1196 448 AEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLRGLAG 524
|
330
....*....|....*...
gi 530372442 1769 KAAQLDGLEARMRSVLQA 1786
Cdd:COG1196 525 AVAVLIGVEAAYEAALEA 542
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1200-1789 |
3.73e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1200 VVQDLAARTQRLE------QRAQELQQTGVLGAFESSFWHMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIGEAT 1273
Cdd:COG1196 194 ILGELERQLEPLErqaekaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1274 EHLTQLEADLTDVQDENFNANHALSGLERDRLALNLTLRQLDQHLDLLKHSN------FLGAYDSIRHAHSQSAEAERRA 1347
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleeeLEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1348 NTSALAVpspvSNSASARHRTEALMDA---QKEDFNSKHMANQRALGKLSAHTHTL--SLTDINELVCGAPGDApcatsp 1422
Cdd:COG1196 354 EEAEAEL----AEAEEALLEAEAELAEaeeELEELAEELLEALRAAAELAAQLEELeeAEEALLERLERLEEEL------ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1423 cggagcRDEDGQPRcgglscnGAAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASR 1502
Cdd:COG1196 424 ------EELEEALA-------ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1503 GQV---EQANQELQELIQSVKDFLN--------QEGADPDSIEMVATRVLELSIPAS------------AEQIQHLAGAI 1559
Cdd:COG1196 491 ARLlllLEAEADYEGFLEGVKAALLlaglrglaGAVAVLIGVEAAYEAALEAALAAAlqnivveddevaAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1560 AERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVAdtrdTEQTL 1639
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT----LAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1640 YQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLgDQYQTVKALAER 1719
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE-EERLEEELEEEA 725
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1720 KAQGVLAAQARAEQLRDEARDLLQAAQ----DKLQRLQELEgtyeeneraleskaAQLDGLEARMRSvLQAINL 1789
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEAleelPEPPDLEELE--------------RELERLEREIEA-LGPVNL 784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1452-1790 |
7.59e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.46 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQAELQRA---LAEggsILSRVAETRRQASEAQQ-----------RAQAALDKANASRGQVEQANQELQELIQ 1517
Cdd:COG1196 177 AERKLEATEENLERLediLGE---LERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1518 SVKDFLNQEgadpdsiemvatRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDArrarswa 1597
Cdd:COG1196 254 ELEELEAEL------------AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1598 EDEKQKAETVQAALEE--AQRAQGIAQGAIRGAVADT--RDTEQTLYQVQERMAGAERALSsagERARQLDALLEALKLK 1673
Cdd:COG1196 315 EERLEELEEELAELEEelEELEEELEELEEELEEAEEelEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1674 RAGNSLAASTAEETAGSAQGRAQEAEQLLRgplgdQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQ 1753
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEE-----ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 530372442 1754 ELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQ 1790
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1446-1792 |
5.75e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1446 AATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQ 1525
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1526 EgadpdsiemvatrvlelsipasAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSwaEDEKQKAE 1605
Cdd:COG1196 321 L----------------------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL--EAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1606 TVQAALEEAQRAQGIAQGAIRgAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAgnSLAASTAE 1685
Cdd:COG1196 377 AEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE--EAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1686 ETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDE------ARDLLQAAQDKLQRLQELEGTY 1759
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvkAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350
....*....|....*....|....*....|....*
gi 530372442 1760 EENERALESKAAQL--DGLEARMRSVLQAINLQVQ 1792
Cdd:COG1196 534 AAYEAALEAALAAAlqNIVVEDDEVAAAAIEYLKA 568
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
783-831 |
9.03e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 9.03e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 783 CQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGFGPTGCQAC 831
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
783-828 |
9.17e-16 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 72.73 E-value: 9.17e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 783 CQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGFGPTGC 828
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1462-1781 |
1.30e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1462 ELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVL 1541
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1542 ELsipasAEQIQHLAG----------AIAERVRSLADVDAILARTVGDVR--------RAEQLLQDARRARSWAEDEKQK 1603
Cdd:PRK02224 290 EL-----EEERDDLLAeaglddadaeAVEARREELEDRDEELRDRLEECRvaaqahneEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1604 AETVQAALEEAQRAQGIAQGAI--------------------RGAVADTRDT-EQTLYQVQERMAGAERALSSAGERARQ 1662
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIeeleeeieelrerfgdapvdLGNAEDFLEElREERDELREREAELEATLRTARERVEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1663 LDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRgPLGDQYQTVKALAERkAQGVLAAQARAEQLRDEARDLl 1742
Cdd:PRK02224 445 AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDL- 521
|
330 340 350
....*....|....*....|....*....|....*....
gi 530372442 1743 qaaqdkLQRLQELEGTYEENERALESKAAQLDGLEARMR 1781
Cdd:PRK02224 522 ------EELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
782-829 |
2.70e-15 |
|
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: 71.62 E-value: 2.70e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530372442 782 PCQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGF--GPTGCQ 829
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1793 |
1.23e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1201 VQDLAARTQRLEQRAQELQQTGVLGAfessfwhMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIGEATEHLTQLE 1280
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAE-------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1281 ADLTDVQD--------------------ENFNANHALSGL-----------ERDRLALNLTLRQLDQHL----------- 1318
Cdd:TIGR02168 482 RELAQLQArldslerlqenlegfsegvkALLKNQSGLSGIlgvlselisvdEGYEAAIEAALGGRLQAVvvenlnaakka 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1319 -DLLKHSN-----FLgAYDSIRHAHSQSAEAERRANTS--ALAVPSPVSNSASARHRTEALMD--AQKEDFNSkhmANQR 1388
Cdd:TIGR02168 562 iAFLKQNElgrvtFL-PLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPKLRKALSYLLGgvLVVDDLDN---ALEL 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1389 AlGKLSAHTHTLSLTDinELVcgapgdapcatspcggagcrdedgqpRCGGLSCNGAAATADLALGRARhtqaELQRALA 1468
Cdd:TIGR02168 638 A-KKLRPGYRIVTLDG--DLV--------------------------RPGGVITGGSAKTNSSILERRR----EIEELEE 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1469 EggsilsrVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDflnqegadpdsiemvatrvLELSIPAS 1548
Cdd:TIGR02168 685 K-------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-------------------LRKDLARL 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1549 AEQIQHLAGAIAERVRSLADVDAILARtvgdvrrAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGA 1628
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEE-------LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1629 VADTRDTEQtlyQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETagsaqgRAQEAEQLlrgplgd 1708
Cdd:TIGR02168 812 LTLLNEEAA---NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL------IEELESEL------- 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1709 qyqtVKALAERKAQgvlaaQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAIN 1788
Cdd:TIGR02168 876 ----EALLNERASL-----EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
....*
gi 530372442 1789 LQVQI 1793
Cdd:TIGR02168 947 EEYSL 951
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1491-1796 |
1.52e-14 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 79.29 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1491 AQAALDKANASRgQVEQANQELQELIQSVKDFLnqegadpdSIEMVA-TRVLELSIPA-SAEQIQHLAGAIAErvrslad 1568
Cdd:COG3206 96 LERVVDKLNLDE-DPLGEEASREAAIERLRKNL--------TVEPVKgSNVIEISYTSpDPELAAAVANALAE------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1569 vdAILARTVgDVRRAEqllqdARRARSWAEDE----KQKAETVQAALEEAQRAQGIAqgairgavadtrDTEQTLYQVQE 1644
Cdd:COG3206 160 --AYLEQNL-ELRREE-----ARKALEFLEEQlpelRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLLQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1645 RMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAE-----QLLRGPLGDQYQTVKALAER 1719
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEleaelAELSARYTPNHPDVIALRAQ 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1720 KAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQelegtyeENERALESKAAQLDGLEARMRSVLQAINLQVQIYNT 1796
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQ-------AQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1728-1797 |
3.05e-14 |
|
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: 69.18 E-value: 3.05e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1728 QARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTC 1797
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1452-1789 |
5.58e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.12 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQA--ALDKANASRGQVEQANQELQELIQSVKDFLNQegad 1529
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEER---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1530 pdsieMVATRVLELSIPASAEQIQHLAGAIAERVRSL-ADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQ 1608
Cdd:COG4717 155 -----LEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1609 AALEEAQRAQGIAQ--------GAIRGAVADTRDTEQTLYQVQERMAGAerALSSAG----------ERARQLDALLEAL 1670
Cdd:COG4717 230 EQLENELEAAALEErlkearllLLIAAALLALLGLGGSLLSLILTIAGV--LFLVLGllallflllaREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1671 KLKRAGNSLAASTAEETAgSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQgvLAAQARAEQLRDEARDLLQAAQ---- 1746
Cdd:COG4717 308 QALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAGvede 384
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530372442 1747 DKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINL 1789
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1479-1767 |
6.17e-14 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 77.56 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1479 ETRRQASEAQQRAQAALDKANASRGQV-EQANQELQELIQSVKDFLNQEGADPDsiemvatrvlELSIPASAEqiqhlag 1557
Cdd:NF041483 441 EARRLRGEAEQLRAEAVAEGERIRGEArREAVQQIEEAARTAEELLTKAKADAD----------ELRSTATAE------- 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1558 aiAERVRSLADVDAILARtvgdvRRAEQLLQDAR----RARSWAEDEkqkAETVQAALEEAqrAQGIAQGAIRGAVADTR 1633
Cdd:NF041483 504 --SERVRTEAIERATTLR-----RQAEETLERTRaeaeRLRAEAEEQ---AEEVRAAAERA--ARELREETERAIAARQA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1634 DTEQTLYQVQ----ERMAGAERALSSA---GERARQlDALLEALKLK-------RAGNSLAASTAE----ETAGSAQGRA 1695
Cdd:NF041483 572 EAAEELTRLHteaeERLTAAEEALADAraeAERIRR-EAAEETERLRteaaeriRTLQAQAEQEAErlrtEAAADASAAR 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1696 QEAEQL---LRGPLGDQYQTVKALAERKAQGVLA-AQARAEQLRDEARDLLQAAQDK-LQRLQELEGTY--------EEN 1762
Cdd:NF041483 651 AEGENVavrLRSEAAAEAERLKSEAQESADRVRAeAAAAAERVGTEAAEALAAAQEEaARRRREAEETLgsaraeadQER 730
|
....*
gi 530372442 1763 ERALE 1767
Cdd:NF041483 731 ERARE 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1437-1700 |
7.15e-14 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 75.64 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1437 CGGLSCNGAAATADLALGRAR----HTQAELQRALAEGGSILSRVAETRRQASEAQQR---AQAALDKANAsrgQVEQAN 1509
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQkelsELQAELEAAQAELDALQAELEELNEEYNELQAEleaLQAEIDKLQA---EIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1510 QELQELIQSVKDFLN---QEGADPDSIEMVATrvlelsipasaeqiqhlAGAIAERVRSLADVDAILARTVGDVRRAEQL 1586
Cdd:COG3883 79 AEIEERREELGERARalyRSGGSVSYLDVLLG-----------------SESFSDFLDRLSALSKIADADADLLEELKAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1587 LQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLyqvQERMAGAERALSSAGERARQLDAL 1666
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA---EAQLAELEAELAAAEAAAAAAAAA 218
|
250 260 270
....*....|....*....|....*....|....
gi 530372442 1667 LEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQ 1700
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1455-1788 |
8.06e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.73 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RARHTQAELQRALAEGG-SILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDF-LNQEGADPDS 1532
Cdd:COG4717 171 ELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAaLEERLKEARL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1533 IEMVATRVLELS--IPASAEQIQHLAGAIAERVRSLADVDAILArtvgdvRRAEQLLQDARRARSWAEDEKQKAETVQAA 1610
Cdd:COG4717 251 LLLIAAALLALLglGGSLLSLILTIAGVLFLVLGLLALLFLLLA------REKASLGKEAEELQALPALEELEEEELEEL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1611 LEEaqraQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAgERARQLDALLEAlklkragnslAASTAEETAGS 1690
Cdd:COG4717 325 LAA----LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAE----------AGVEDEEELRA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1691 AQGRAQEAEQL------LRGPLGDQYQTVKALAERKAQGVLAAQ-ARAEQLRDEARDLLQAAQDKL----QRLQELE--G 1757
Cdd:COG4717 390 ALEQAEEYQELkeeleeLEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELaeleAELEQLEedG 469
|
330 340 350
....*....|....*....|....*....|....
gi 530372442 1758 TYEENERALESKAAQLDGLE---ARMRSVLQAIN 1788
Cdd:COG4717 470 ELAELLQELEELKAELRELAeewAALKLALELLE 503
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1444-1782 |
3.99e-13 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 75.25 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1444 GAAATADLALGRAR----------HTQAELQRALAEG--GSILSRVAETRRQASE----AQQRAQAALDKANASRGQVEQ 1507
Cdd:NF041483 204 SARAEAEAILRRARkdaerllnaaSTQAQEATDHAEQlrSSTAAESDQARRQAAElsraAEQRMQEAEEALREARAEAEK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1508 ANQELQEliQSVKDFLNQEGADPDSI----EMVATRVLEL-----SIPASAEQIQHLAGAIAERVRSLAdvdAILARTVG 1578
Cdd:NF041483 284 VVAEAKE--AAAKQLASAESANEQRTrtakEEIARLVGEAtkeaeALKAEAEQALADARAEAEKLVAEA---AEKARTVA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1579 DVRRAEQLlqdARRARSwAEDEKQKA-----ETVQAALEEAQR---------------AQGIAQGAIRGAVADTRDTEQT 1638
Cdd:NF041483 359 AEDTAAQL---AKAART-AEEVLTKAsedakATTRAAAEEAERirreaeaeadrlrgeAADQAEQLKGAAKDDTKEYRAK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1639 LYQVQE---RMAG-AERALSSA---GERARQlDALLEALKLKRAgnslAASTAEETAGSAQGRAQEaeqlLRGPLGDQYQ 1711
Cdd:NF041483 435 TVELQEearRLRGeAEQLRAEAvaeGERIRG-EARREAVQQIEE----AARTAEELLTKAKADADE----LRSTATAESE 505
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1712 TVKALA-------ERKAQGVLA-AQARAEQLRDEARDllQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRS 1782
Cdd:NF041483 506 RVRTEAierattlRRQAEETLErTRAEAERLRAEAEE--QAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHT 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1561-1779 |
7.90e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1561 ERVRSLADVDAILARtVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAiRGAVADTRDT--EQT 1638
Cdd:COG4913 219 EEPDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAL-RLWFAQRRLEllEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1639 LYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAA--------STAEETAGSAQGRAQEAEQLLRGpLG-DQ 1709
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlereiERLERELEERERRRARLEALLAA-LGlPL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1710 YQTVKALAERKAQgvlaAQARAEQLRDEARDLLQAAQDKLQRLQELegtyeenERALESKAAQLDGLEAR 1779
Cdd:COG4913 376 PASAEEFAALRAE----AAALLEALEEELEALEEALAEAEAALRDL-------RRELRELEAEIASLERR 434
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1255-1767 |
8.36e-13 |
|
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: 74.10 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1255 TAQLVEATEELRRE-------IGEATEHLTQLEADLTDVQDENFNANHA-LSGLERDRLALNLTLRQLDQHLDllKHSNF 1326
Cdd:pfam12128 296 DDQWKEKRDELNGElsaadaaVAKDRSELEALEDQHGAFLDADIETAAAdQEQLPSWQSELENLEERLKALTG--KHQDV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1327 LGAYDSIRHAHSQSAEAERRANTSALAVpspvSNSASARHRT--EALMDAQKEDFNSKHMANQRALgKLSAHTHTLSLTD 1404
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRDIAGIKDKLAK----IREARDRQLAvaEDDLQALESELREQLEAGKLEF-NEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1405 INELVcgapgDAPCATSpcggagcrDEDGQPRCGGLSCNgaaaTADLALGRARHTQAELQRALaeggsilsRVAETRR-Q 1483
Cdd:pfam12128 449 LKLRL-----NQATATP--------ELLLQLENFDERIE----RAREEQEAANAEVERLQSEL--------RQARKRRdQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1484 ASEAQQRAQAALDkanasrgQVEQANQELQELI----QSVKDFLNQEGAD-PDSIEMVATRVLEL-------SIPASAEQ 1551
Cdd:pfam12128 504 ASEALRQASRRLE-------ERQSALDELELQLfpqaGTLLHFLRKEAPDwEQSIGKVISPELLHrtdldpeVWDGSVGG 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1552 IQHLAGaIAERVRSLaDVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAvad 1631
Cdd:pfam12128 577 ELNLYG-VKLDLKRI-DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA--- 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1632 tRDTEQTLYQVQERMAGA-----ERALSSAGERARQLDALLEALKLKRagnSLAASTAEETAGSAQGRAQEAEQLLRGPL 1706
Cdd:pfam12128 652 -RLDLRRLFDEKQSEKDKknkalAERKDSANERLNSLEAQLKQLDKKH---QAWLEEQKEQKREARTEKQAYWQVVEGAL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1707 GDQYQTVK-ALAERKAQgvlaAQARAEQLRDE-ARDLLQAAQDKlQRLQELEGTYEENERALE 1767
Cdd:pfam12128 728 DAQLALLKaAIAARRSG----AKAELKALETWyKRDLASLGVDP-DVIAKLKREIRTLERKIE 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1446-1793 |
3.48e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.91 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1446 AATADLALGRARHtQAELQRALAEGGSILSRVAETRRQASEAQQRA---QAALDKANASRGQVEQANQELQELIQSVKDF 1522
Cdd:PRK04863 265 ESTNYVAADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1523 LNQEGAdpdsIEMVATRVLELSiPASAEQIQHLAGAIAERVRSLADVDAI------LARTVGDVRRAEQLLQdaRRARSW 1596
Cdd:PRK04863 344 LRQQEK----IERYQADLEELE-ERLEEQNEVVEEADEQQEENEARAEAAeeevdeLKSQLADYQQALDVQQ--TRAIQY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1597 aedekQKAetvQAALEEAQRAQGIAQGAIRGA---VADTRDTEQtlyQVQERMAGAERALSSAGERARQLDALLEALKlk 1673
Cdd:PRK04863 417 -----QQA---VQALERAKQLCGLPDLTADNAedwLEEFQAKEQ---EATEELLSLEQKLSVAQAAHSQFEQAYQLVR-- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1674 RAGNSLAASTAEETAGSAQGRAQE----AEQL--LRGPLGDqyqtvkalaerkAQGVLAAQARAEQLRDEArdlLQAAQD 1747
Cdd:PRK04863 484 KIAGEVSRSEAWDVARELLRRLREqrhlAEQLqqLRMRLSE------------LEQRLRQQQRAERLLAEF---CKRLGK 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 530372442 1748 KLQRLQELEGTYEENERALESKAAQLDGLEARmRSVLQAINLQVQI 1793
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQA 593
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1773 |
9.62e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.63 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RAR-HTQA----ELQRALAEGGSILSRvAETRRQASEAQQRAQAaldKANASRGQVEQAnqelqeLIQSVKDflnqegad 1529
Cdd:NF041483 158 RARtESQArrllDESRAEAEQALAAAR-AEAERLAEEARQRLGS---EAESARAEAEAI------LRRARKD-------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1530 pdsiemvATRVLElsipASAEQIQHlAGAIAERVRS--LADVDAILARTVGDVRRAEQLLQDA----RRARswAEDEKQK 1603
Cdd:NF041483 220 -------AERLLN----AASTQAQE-ATDHAEQLRSstAAESDQARRQAAELSRAAEQRMQEAeealREAR--AEAEKVV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1604 AETVQAALEEAQRAQGIAQGAIRGAvadtrdTEQTLYQVQERMAGAErALSSAGERARQlDALLEALKL-KRAGNSLAAS 1682
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1683 TAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQ----AAQD--KLQRLQELE 1756
Cdd:NF041483 358 AAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEqlkgAAKDdtKEYRAKTVE 437
|
330
....*....|....*..
gi 530372442 1757 gtYEENERALESKAAQL 1773
Cdd:NF041483 438 --LQEEARRLRGEAEQL 452
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1250-1782 |
9.79e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.63 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1250 TSAASTAQLVEATEELRREIGEATEHLTQLEADLTDVQDENfnanhalsglERDRlalnltlRQLDQHLDLLKHSnflgA 1329
Cdd:NF041483 562 TERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEA----------ERIR-------REAAEETERLRTE----A 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1330 YDSIRHAHSQS-AEAER-RANTSALAVPSPVSNSASA-RHRTEALMDAQKEDFNSKHMANQ-RALGKLSAHTHTlslTDI 1405
Cdd:NF041483 621 AERIRTLQAQAeQEAERlRTEAAADASAARAEGENVAvRLRSEAAAEAERLKSEAQESADRvRAEAAAAAERVG---TEA 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1406 NELVCGAPGDApcatspcggAGCRDEDGQprcgglSCNGAAATADLALGRARHTQAELqralaeggsilsrVAETRRQAS 1485
Cdd:NF041483 698 AEALAAAQEEA---------ARRRREAEE------TLGSARAEADQERERAREQSEEL-------------LASARKRVE 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1486 EAQQRAQAALDKANASRGQ-VEQANQELQELIQSVKDFlnQEGADpdsiEMVATrvLELSIPASAEQIQHLAGAIAERVR 1564
Cdd:NF041483 750 EAQAEAQRLVEEADRRATElVSAAEQTAQQVRDSVAGL--QEQAE----EEIAG--LRSAAEHAAERTRTEAQEEADRVR 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1565 SladvDAILARtvgdvrraEQLLQDARRARSWAEDEKQKAE-----TVQAALEEAQRAQgiaqgairgavADTRDTEQTL 1639
Cdd:NF041483 822 S----DAYAER--------ERASEDANRLRREAQEETEAAKalaerTVSEAIAEAERLR-----------SDASEYAQRV 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1640 -YQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAqEAEQLLRGPLGDQYQTVKALAE 1718
Cdd:NF041483 879 rTEASDTLASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARA-EAERLRDEARAEAERVRADAAA 957
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1719 RKAQGVLAAQARAEQLRDEARDLLQAAQdklqrlQELEGTYEENERALESKAAQLDGLEARMRS 1782
Cdd:NF041483 958 QAEQLIAEATGEAERLRAEAAETVGSAQ------QHAERIRTEAERVKAEAAAEAERLRTEARE 1015
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1463-1796 |
1.40e-11 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 68.14 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1463 LQRALAEGGSIlsRVAETRRQASEAQQRAQAA-------LDKANASRGQVEQANQELQELIQSVKDFLNQEGADpdsiem 1535
Cdd:COG1538 6 IERALANNPDL--RAARARVEAARAQLRQARAgllpsqeLDLGGKRRARIEAAKAQAEAAEADLRAARLDLAAE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1536 VATRVLELSipASAEQIQHLAGAIAERVRSLADVDAILArtVGDVRRAEQLLQDARRARswaedekqkaetVQAALEEAQ 1615
Cdd:COG1538 78 VAQAYFDLL--AAQEQLALAEENLALAEELLELARARYE--AGLASRLDVLQAEAQLAQ------------ARAQLAQAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1616 RAQGIAQGAIRGAVADTRDTE----QTLYQVQERMAGAERALSSAGER-------ARQLDALLEALKLKRAGN----SLA 1680
Cdd:COG1538 142 AQLAQARNALALLLGLPPPAPldlpDPLPPLPPLPPSLPGLPSEALERrpdlraaEAQLEAAEAEIGVARAAFlpslSLS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1681 ASTAEETAGSAQGRAQEAEQL---LRGPLGDQYQTVKALAERKAQgVLAAQARAEQLRDEA----RDLLQAAQDKLQRLQ 1753
Cdd:COG1538 222 ASYGYSSSDDLFSGGSDTWSVglsLSLPLFDGGRNRARVRAAKAQ-LEQAEAQYEQTVLQAlqevEDALAALRAAREQLE 300
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530372442 1754 ELEGTYEENERALEskAAQLdGLEARMRSVLQAINLQVQIYNT 1796
Cdd:COG1538 301 ALEEALEAAEEALE--LARA-RYRAGLASLLDVLDAQRELLQA 340
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1460-1786 |
2.06e-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: 69.43 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGGSILSRVAETR----RQASEAQQRAQA---ALDKANASRGQVEQANQ----ELQELIQSVKDFlnqeGA 1528
Cdd:pfam01576 603 QKKFDQMLAEEKAISARYAEERdraeAEAREKETRALSlarALEEALEAKEELERTNKqlraEMEDLVSSKDDV----GK 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1529 DPDSIEMvATRVLELSIPASAEQIQHLAGAI--AE--RVRSLADVDAILAR------------------TVGDVRRAEQL 1586
Cdd:pfam01576 679 NVHELER-SKRALEQQVEEMKTQLEELEDELqaTEdaKLRLEVNMQALKAQferdlqardeqgeekrrqLVKQVRELEAE 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1587 LQDARRARSWAEDEKQKAET-------------------------VQAALEEAQRAQGIAQGAIRGAVADTRDTEQTL-- 1639
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELdlkeleaqidaankgreeavkqlkkLQAQMKDLQRELEEARASRDEILAQSKESEKKLkn 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1640 -----YQVQERMAGAERAlssagerARQLDALLEALklkragnslaastAEETAGSAQGRA---QEAEQL------LRGP 1705
Cdd:pfam01576 838 leaelLQLQEDLAASERA-------RRQAQQERDEL-------------ADEIASGASGKSalqDEKRRLeariaqLEEE 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1706 LGDQYQTVKALAE--RKAQ-------GVLAAQARAEQLRDEARDLLQAAQDKLQ-RLQELEGT----YEENERALESKAA 1771
Cdd:pfam01576 898 LEEEQSNTELLNDrlRKSTlqveqltTELAAERSTSQKSESARQQLERQNKELKaKLQEMEGTvkskFKSSIAALEAKIA 977
|
410
....*....|....*.
gi 530372442 1772 QL-DGLEARMRSVLQA 1786
Cdd:pfam01576 978 QLeEQLEQESRERQAA 993
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1457-1763 |
2.59e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.62 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1457 RHTQAELQRALAEggsiLSRV-----------AETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDfLNQ 1525
Cdd:COG4372 48 EQLREELEQAREE----LEQLeeeleqarselEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1526 EGADpdsiemvatrvLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAE-----DE 1600
Cdd:COG4372 123 ERQD-----------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldellKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1601 KQKAETVQAALEEAQRAQGIAQ-------------GAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALL 1667
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPrelaeelleakdsLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1668 EALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQD 1747
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLL 351
|
330
....*....|....*.
gi 530372442 1748 KLQRLQELEGTYEENE 1763
Cdd:COG4372 352 DNDVLELLSKGAEAGV 367
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1455-1772 |
3.02e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIE 1534
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1535 mVATRVLElsipasAEQIQHLAGAI----AERVRSLADVDAI-LARTVGDVRRAEQL--LQDARRArswaeDEKQKAETV 1607
Cdd:PTZ00121 1168 -EARKAED------AKKAEAARKAEevrkAEELRKAEDARKAeAARKAEEERKAEEArkAEDAKKA-----EAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1608 QAALEEAQRAQgiaqgairgavaDTRDTEQTLYQVQERMAG-AERALSSAGERARQLDALLEALKLKRAgNSLAASTAEE 1686
Cdd:PTZ00121 1236 KKDAEEAKKAE------------EERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAEEKKKA-DEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1687 TAGSAQGRAQE---AEQLLRGP--LGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQ-DKLQRLQELEGTYE 1760
Cdd:PTZ00121 1303 KADEAKKKAEEakkADEAKKKAeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADA 1382
|
330
....*....|..
gi 530372442 1761 ENERALESKAAQ 1772
Cdd:PTZ00121 1383 AKKKAEEKKKAD 1394
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1460-1754 |
3.50e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGGSILSRVAETRRQASEAQQ-------RAQAALDKANASRGQVEQANQELQELIQSVKdflnqegADPDS 1532
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-------NVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1533 IEMVATRV--LELSIPASAEQI----QHLAGA-IAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAE 1605
Cdd:TIGR02169 760 LKELEARIeeLEEDLHKLEEALndleARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1606 TVQAALEEAQRAQGIAQGAIRGAVADT----RDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAA 1681
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELeeelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1682 STAEETAGSAQGRAQEAEQLLRG---------PLGDQYQTVKALaERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRL 1752
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEdeeipeeelSLEDVQAELQRV-EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL 998
|
..
gi 530372442 1753 QE 1754
Cdd:TIGR02169 999 EE 1000
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
521-562 |
3.58e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 3.58e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 530372442 521 PCDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFRP 562
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1450-1792 |
6.07e-11 |
|
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: 68.06 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1450 DLALGrARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQeLQELIQSVKdflnqegAD 1529
Cdd:COG3096 285 ERALE-LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQ-------ED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1530 PDSIEmVATRVLELSIPASAEQiqhLAGAIAERVRSLADVDAI---LArtvgDVRRAEQLLQdaRRARSWaedekQKAet 1606
Cdd:COG3096 356 LEELT-ERLEEQEEVVEEAAEQ---LAEAEARLEAAEEEVDSLksqLA----DYQQALDVQQ--TRAIQY-----QQA-- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1607 VQAaLEEAQRAQGIAQGAIRGA---VADTRDTEQtlyQVQERMAGAERALSSAGERARQLDALLEALKlkragnSLAAST 1683
Cdd:COG3096 419 VQA-LEKARALCGLPDLTPENAedyLAAFRAKEQ---QATEEVLELEQKLSVADAARRQFEKAYELVC------KIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1684 AEETAGsaqgraQEAEQLLRgplgdQYQTVKALAERkAQGVLAAQARAEQL---RDEARDLLQ----------AAQDKLQ 1750
Cdd:COG3096 489 ERSQAW------QTARELLR-----RYRSQQALAQR-LQQLRAQLAELEQRlrqQQNAERLLEefcqrigqqlDAAEELE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530372442 1751 RLQ-ELEGTYEENERALESKAAQLdgleARMRSVLQAINLQVQ 1792
Cdd:COG3096 557 ELLaELEAQLEELEEQAAEAVEQR----SELRQQLEQLRARIK 595
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1095-1143 |
6.11e-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: 58.90 E-value: 6.11e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 1095 CACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDPGLQCHAC 1143
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1143-1190 |
6.73e-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: 58.90 E-value: 6.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530372442 1143 CDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGiFPACHPC 1190
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
831-879 |
8.19e-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: 8.19e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 831 CQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWGFPSCRPCVC 879
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
522-561 |
9.44e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 9.44e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530372442 522 CDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFR 561
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1462-1795 |
1.32e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 65.31 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1462 ELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVL 1541
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1542 ELSipasaEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQraqgiA 1621
Cdd:COG4372 112 ELQ-----EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE-----A 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1622 QGAIRGAVadtRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQL 1701
Cdd:COG4372 182 EQALDELL---KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1702 LRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKlqrLQELEGTYEENERALESKAAQLDGLEARMR 1781
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA---ALSLIGALEDALLAALLELAKKLELALAIL 335
|
330
....*....|....
gi 530372442 1782 SVLQAINLQVQIYN 1795
Cdd:COG4372 336 LAELADLLQLLLVG 349
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1447-1786 |
1.48e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1447 ATADLALGRARHTQAELQRALAEGG-----------SILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQEL 1515
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGlplpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1516 IQSVKdflnqegADPDSI--EMVATRVL---ELSIPAS-----AEQIQ----HLA--GAIaERV------------RSLA 1567
Cdd:COG4913 428 IASLE-------RRKSNIpaRLLALRDAlaeALGLDEAelpfvGELIEvrpeEERwrGAI-ERVlggfaltllvppEHYA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1568 D----VDAILARTVGDVRRAEQLLQDARR------------------ARSWAEDEKQ------KAETVQAaLEEAQRA-- 1617
Cdd:COG4913 500 AalrwVNRLHLRGRLVYERVRTGLPDPERprldpdslagkldfkphpFRAWLEAELGrrfdyvCVDSPEE-LRRHPRAit 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1618 -QG-IAQGAIRGAVADTRDTEQTLY----------QVQERMAGAERALSSAGERARQLDALLEAL-KLKRAGNSLAASTA 1684
Cdd:COG4913 579 rAGqVKGNGTRHEKDDRRRIRSRYVlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALqERREALQRLAEYSW 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1685 EET-AGSAQGRAQEAEQLLRgplgdqyqtvkALaeRKAQGVLAA-QARAEQLRDEARDLLQAAQDKLQRLQELEGTYEEN 1762
Cdd:COG4913 659 DEIdVASAEREIAELEAELE-----------RL--DASSDDLAAlEEQLEELEAELEELEEELDELKGEIGRLEKELEQA 725
|
410 420
....*....|....*....|....
gi 530372442 1763 ERALESKAAQLDGLEARMRSVLQA 1786
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRA 749
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1452-1773 |
1.68e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQAELQRALAEGGSILS----RVAETRRQASEAQQRA----------QAALDKANASRGQVEQANQELQE--- 1514
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEeadeQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIQYQQAVQALERakq 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1515 -------LIQSVKDFLNQEGADPDSiemVATRVLELsipasaEQIQHLAGAIAERvrsLADVDAILARTVGDVRRAEqll 1587
Cdd:PRK04863 429 lcglpdlTADNAEDWLEEFQAKEQE---ATEELLSL------EQKLSVAQAAHSQ---FEQAYQLVRKIAGEVSRSE--- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1588 qdarrARSWAEDEKQKAETVQAaleEAQRAQGIAQGairgavadTRDTEQTLYQVQErmagAERALSSAGERARQ----- 1662
Cdd:PRK04863 494 -----AWDVARELLRRLREQRH---LAEQLQQLRMR--------LSELEQRLRQQQR----AERLLAEFCKRLGKnldde 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1663 --LDALLEALKLKRAGNSLAASTAEETAGSAQgraQEAEQLlrgplGDQYQTVKAlaerKAQGVLAAQARAEQLRD---- 1736
Cdd:PRK04863 554 deLEQLQEELEARLESLSESVSEARERRMALR---QQLEQL-----QARIQRLAA----RAPAWLAAQDALARLREqsge 621
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530372442 1737 ---EARDLLQAAQDKLQRLQEL---EGTYEENERALESKAAQL 1773
Cdd:PRK04863 622 efeDSQDVTEYMQQLLERERELtveRDELAARKQALDEEIERL 664
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
469-520 |
2.06e-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: 57.75 E-value: 2.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 530372442 469 RCQCNARGTVPGStpCDPNSGSCYCKRLVTGRGCDRCLPGHWGLSHDLLGCR 520
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1447-1776 |
2.25e-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: 65.85 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1447 ATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALdkaNASRGQVEQANQELQELIQSVKDflnqe 1526
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLAN----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1527 gadpdsiemvatrvLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARswaEDEKQKAET 1606
Cdd:TIGR02168 314 --------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL---EELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1607 VQAALEEAQRAQgiaqgairgavadtRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALklkraGNSLAASTAEE 1686
Cdd:TIGR02168 377 LEEQLETLRSKV--------------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL-----LKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1687 TAGSAQGRAQEAEQLlrgpLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARdlLQAAQDKLQRLQELEGTYEENERAL 1766
Cdd:TIGR02168 438 LQAELEELEEELEEL----QEELERLEEALEELREELEEAEQALDAAERELAQ--LQARLDSLERLQENLEGFSEGVKAL 511
|
330
....*....|
gi 530372442 1767 ESKAAQLDGL 1776
Cdd:TIGR02168 512 LKNQSGLSGI 521
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1037-1093 |
2.30e-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: 2.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1037 RCTCNLLGTNPQQCpspdqchcDPSSGQCPCLPNVQGPSCDRCAPNFWNLTS-GHGCQ 1093
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1210-1792 |
2.57e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 65.76 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1210 RLEQRAQELQQTGVLGAFESSfwhMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIGEaTEHLTQLEADLTDVQDE 1289
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVKQQSS---IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1290 NFNANHALSGLERDR-LALNLTLRQLDQHLDLLkhsnflgaydsirHAHSQSAEAERRANTSALAVpSPVSNSASARHRt 1368
Cdd:TIGR00618 395 LQSLCKELDILQREQaTIDTRTSAFRDLQGQLA-------------HAKKQQELQQRYAELCAAAI-TCTAQCEKLEKI- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1369 EALMDAQKEDFNSKHMANQRALGKLSAHTHTLSLTDINELvcgapgdapcATSPCggagcrdedgqPRCGGLSCNGAAAT 1448
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL----------QEEPC-----------PLCGSCIHPNPARQ 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALG-------RARHTQAELQRALA----EGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELiq 1517
Cdd:TIGR00618 519 DIDNPGpltrrmqRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL-- 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1518 svKDFLNQEGADPDSIEMVATRVLELSIPASAEQ--IQHLaGAIAERvrsLADVDAILARTvgdvrrAEQLLQDARR--A 1593
Cdd:TIGR00618 597 --QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHL-QQCSQE---LALKLTALHAL------QLTLTQERVRehA 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1594 RSWAEDEKQKAETVQAALEEAQ-RAQGIaqgairgavadTRDTEqTLYQVQERMAGAERALSSAGERARQLDALLEALKL 1672
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQKMQsEKEQL-----------TYWKE-MLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1673 KRAGNSlaaSTAEETAGSAQgrAQEAEQLlrgplgdqyqtvKALAERKAQGVLAAQArAEQLRDEardllqaaqdklqrL 1752
Cdd:TIGR00618 733 DLAARE---DALNQSLKELM--HQARTVL------------KARTEAHFNNNEEVTA-ALQTGAE--------------L 780
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 530372442 1753 QELEGTYEENERALESKAAQLDGLEARMR----SVLQAINLQVQ 1792
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCE 824
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1142-1191 |
3.20e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 3.20e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530372442 1142 ACDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGIFPACHPCH 1191
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1038-1092 |
3.55e-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: 3.55e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1038 CTCNLLGTNPQQCpspdqchcDPSSGQCPCLPNVQGPSCDRCAPNFWNL--TSGHGC 1092
Cdd:pfam00053 1 CDCNPHGSLSDTC--------DPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1445-1792 |
3.57e-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: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEA-QQRAQAALDKANASRGQVEQANQELQELIQSVKDFL 1523
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1524 NQegadpdsiemvaTRVLELSIPASAEQIQHLAGAIAERvrsLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEK-- 1601
Cdd:COG4913 366 AL------------LAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIas 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1602 ---------QKAETVQAALEEA---------------------QRAQGIAQGAIRG-------------AVA---DTRDT 1635
Cdd:COG4913 431 lerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltllvppehyaAALrwvNRLHL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1636 EQTL-YQ---------------------------------VQERMA---------------GAERALSSAG-----ERAR 1661
Cdd:COG4913 511 RGRLvYErvrtglpdperprldpdslagkldfkphpfrawLEAELGrrfdyvcvdspeelrRHPRAITRAGqvkgnGTRH 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1662 QLD----------------ALLEALKLKRAgnslaasTAEETAGSAQGRAQEAEQLLrgplgDQYQTVKALAERKAQ--- 1722
Cdd:COG4913 591 EKDdrrrirsryvlgfdnrAKLAALEAELA-------ELEEELAEAEERLEALEAEL-----DALQERREALQRLAEysw 658
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1723 ---GVLAAQARAEQLRDEaRDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQ 1792
Cdd:COG4913 659 deiDVASAEREIAELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1461-1790 |
4.58e-10 |
|
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: 64.81 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1461 AELQRALAEggsILSRVAETRRQAS---EAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPD------ 1531
Cdd:pfam01576 218 TDLQEQIAE---LQAQIAELRAQLAkkeEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNkaekqr 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1532 ---SIEMVATRV-LELSIPASAEQ----------IQHLAGAIAERVRS----LADVDAILARTVGDVrrAEQLLQdARRA 1593
Cdd:pfam01576 295 rdlGEELEALKTeLEDTLDTTAAQqelrskreqeVTELKKALEEETRSheaqLQEMRQKHTQALEEL--TEQLEQ-AKRN 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1594 RSWAEDEKQKAETVQAALEEAQRaqgiaqgAIRGAVADT----RDTEQTLYQVQERMAGAERALSSAGERARQLDALLEA 1669
Cdd:pfam01576 372 KANLEKAKQALESENAELQAELR-------TLQQAKQDSehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1670 LklkragnslaASTAEETAGSAQGRAQEAEQllrgpLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQ------ 1743
Cdd:pfam01576 445 V----------SSLLNEAEGKNIKLSKDVSS-----LESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEqleeee 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 530372442 1744 AAQDKLQR-LQELEGTYEENERALESKAAQLDGLEA---RMRSVLQAINLQ 1790
Cdd:pfam01576 510 EAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEEgkkRLQRELEALTQQ 560
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1460-1793 |
4.88e-10 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 64.29 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGgSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKdflnqegadpdsiemvatr 1539
Cdd:COG3064 2 QEALEEKAAEA-AAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1540 vlelsipasAEQIQHLAGAIAERVRSLADVDAilARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQR--- 1616
Cdd:COG3064 62 ---------AEAEQRAAELAAEAAKKLAEAEK--AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkae 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1617 --AQGIAQGAiRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGR 1694
Cdd:COG3064 131 eeAKRKAEEE-RKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1695 AQEAEQLLRgpLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLD 1774
Cdd:COG3064 210 AAADAALLA--LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAG 287
|
330
....*....|....*....
gi 530372442 1775 GLEARMRSVLQAINLQVQI 1793
Cdd:COG3064 288 LAAAAAGLVLDDSAALAAE 306
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1729-1798 |
5.06e-10 |
|
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: 57.07 E-value: 5.06e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1729 ARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1798
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1443-1755 |
7.00e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.59 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1443 NGAAATADLALGRARhtqAELQRALAEGGSILSRVAEtRRQASEAQQR-------AQAALDKAnasrgqveQANQELQEL 1515
Cdd:COG3096 367 EEVVEEAAEQLAEAE---ARLEAAEEEVDSLKSQLAD-YQQALDVQQTraiqyqqAVQALEKA--------RALCGLPDL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1516 -IQSVKDFLNQEGADPDSIEmvaTRVLELSipasaeqiQHLAGAIAERvRSLADVDAILARTVGDVRR------AEQLLQ 1588
Cdd:COG3096 435 tPENAEDYLAAFRAKEQQAT---EEVLELE--------QKLSVADAAR-RQFEKAYELVCKIAGEVERsqawqtARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1589 DARRARSWAedekQKAETVQAALEEA-------QRAQGIAQG---AIRGAVADTRDTEQTLYQVQERMAGAERALSSAGE 1658
Cdd:COG3096 503 RYRSQQALA----QRLQQLRAQLAELeqrlrqqQNAERLLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1659 RARQLDALLEALKLKRAGNS------LAASTAEEtagsaQGRAQEAEQLLRGPLGDQY--QTVKALAERKAQGVLAAQAR 1730
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAarapawLAAQDALE-----RLREQSGEALADSQEVTAAmqQLLEREREATVERDELAARK 653
|
330 340
....*....|....*....|....*
gi 530372442 1731 aEQLRDEARDLLQAAQDKLQRLQEL 1755
Cdd:COG3096 654 -QALESQIERLSQPGGAEDPRLLAL 677
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1143-1187 |
7.80e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 7.80e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 1143 CDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGI-FPAC 1187
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1475-1769 |
8.89e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1475 SRVAETRRQASEAQQRAQAAldKANASRgQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPAS----AE 1550
Cdd:PTZ00121 1205 ARKAEEERKAEEARKAEDAK--KAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearkAD 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1551 QIQHlagaiAERVRSLADvdailARTVGDVRRAEQLLQDARRARSW------AEDEKQKAETVQAALEEAQRAQGIAQGA 1624
Cdd:PTZ00121 1282 ELKK-----AEEKKKADE-----AKKAEEKKKADEAKKKAEEAKKAdeakkkAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1625 IRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALK-----LKRAGNSLAASTAEETAGSAQGRAQE-- 1697
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKkaeedKKKADELKKAAAAKKKADEAKKKAEEkk 1431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1698 -AEQLLRgplgdqyqtvKALAERKAQgvlAAQARAEQLRdEARDLLQAAQDKlQRLQELEGTYEENERALESK 1769
Cdd:PTZ00121 1432 kADEAKK----------KAEEAKKAD---EAKKKAEEAK-KAEEAKKKAEEA-KKADEAKKKAEEAKKADEAK 1489
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1095-1140 |
8.95e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 8.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 1095 CACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDPGLQC 1140
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
410-467 |
9.35e-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: 55.82 E-value: 9.35e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 410 CDCDPMGSQdGGRCDSHddpalglvSGQCRCKEHVVGTRCQQCRDGFFGLSISDRLGC 467
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1038-1092 |
1.35e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.35e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1038 CTCNLLGTNPQQCpspdqchcDPSSGQCPCLPNVQGPSCDRCAPNFWNlTSGHGC 1092
Cdd:smart00180 1 CDCDPGGSASGTC--------DPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1455-1775 |
1.59e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.31 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RARHTQAELQRALAEGGSILSRvAETRR---QASEAQQRAQAALDKANASRGQveQANQELQELIQSVKDFLNqegadpd 1531
Cdd:NF041483 79 RNAQIQADQLRADAERELRDAR-AQTQRilqEHAEHQARLQAELHTEAVQRRQ--QLDQELAERRQTVESHVN------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1532 siEMVATrvlelsipasAEQIqhlagaiaeRVRSLADvdailARTVGDVRRAE--QLLQDARrarswAEDEKQKAETVQA 1609
Cdd:NF041483 149 --ENVAW----------AEQL---------RARTESQ-----ARRLLDESRAEaeQALAAAR-----AEAERLAEEARQR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1610 ALEEAQRAQGIAQGAIRGAVADtrdteqtlyqvqermagAERALSSAGERARQLDALLEALKLKRAGNSLAA-STAEETA 1688
Cdd:NF041483 198 LGSEAESARAEAEAILRRARKD-----------------AERLLNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1689 GSAQGRAQEAEQLLRgplgdqyqtvkalaerkaqgvlAAQARAEQLRDEARDllQAAqdklQRLQELEGTYEENERALES 1768
Cdd:NF041483 261 RAAEQRMQEAEEALR----------------------EARAEAEKVVAEAKE--AAA----KQLASAESANEQRTRTAKE 312
|
....*..
gi 530372442 1769 KAAQLDG 1775
Cdd:NF041483 313 EIARLVG 319
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1460-1772 |
1.86e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGGSILSRVAETRRQA-----SEAQQRAQAALDKANASRgQVEQANQELQELIQSVKDFLNQEGADPDSIE 1534
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAaekkkEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1535 MV-----ATRVLELSIPASAEQIQHLAGAIAERVRSLADvdaiLARTVGDVRRAEQLLQDARRARSwAEDEKQKAETVQA 1609
Cdd:PTZ00121 1423 AKkkaeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKK-ADEAKKKAEEAKK 1497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1610 ALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAEralSSAGERARQLDALLEALKLKRA---GNSLAASTAEE 1686
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE---AKKAEEKKKADELKKAEELKKAeekKKAEEAKKAEE 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1687 TAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQgvlaaQAR-AEQLRDEARDLLQAAQDKLQRLQELEGTYEENERA 1765
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-----EAKkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
....*..
gi 530372442 1766 LESKAAQ 1772
Cdd:PTZ00121 1650 EELKKAE 1656
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1094-1136 |
2.06e-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: 2.06e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530372442 1094 PCACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDP 1136
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
470-524 |
2.54e-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: 2.54e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 470 CQCNARGTVPGStpCDPNSGSCYCKRLVTGRGCDRCLPGHWGLSHDLlgcrPCDC 524
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
522-561 |
3.50e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.90 E-value: 3.50e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530372442 522 CDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFR 561
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1574-1788 |
3.77e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1574 ART-VGDVRRAEQLLQDARRARSWAEDEK----------QKAETVQAALE--EAQRAQGIAQgaiRGAVADTRDT----- 1635
Cdd:PRK02224 174 ARLgVERVLSDQRGSLDQLKAQIEEKEEKdlherlngleSELAELDEEIEryEEQREQARET---RDEADEVLEEheerr 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1636 ------EQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGnslAASTAEETAGSAQGRAQEAEQL------LR 1703
Cdd:PRK02224 251 eeletlEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD---LLAEAGLDDADAEAVEARREELedrdeeLR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1704 GPLGDQYQTVKAL---AERKAQGVLAAQARAEQLRDEARDL---LQAAQDKLQ----RLQELEGTYEENERALESKAAQL 1773
Cdd:PRK02224 328 DRLEECRVAAQAHneeAESLREDADDLEERAEELREEAAELeseLEEAREAVEdrreEIEELEEEIEELRERFGDAPVDL 407
|
250
....*....|....*
gi 530372442 1774 DGLEARMRSVLQAIN 1788
Cdd:PRK02224 408 GNAEDFLEELREERD 422
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1445-1701 |
4.45e-09 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 61.19 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLAlGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDfln 1524
Cdd:COG0840 273 AASAEELA-AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1525 qegadpdsiemVATRVLELSipASAEQIQHLAGAI-------------------------------AERVRSLA------ 1567
Cdd:COG0840 349 -----------TAETIEELG--ESSQEIGEIVDVIddiaeqtnllalnaaieaarageagrgfavvADEVRKLAersaea 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1568 --DVDAILARTVGDVRRAEQLlqdARRARSWAEDEKQKAETVQAALEEaqraqgiaqgaIRGAVADTRDteqtlyQVQER 1645
Cdd:COG0840 416 tkEIEELIEEIQSETEEAVEA---MEEGSEEVEEGVELVEEAGEALEE-----------IVEAVEEVSD------LIQEI 475
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1646 MAGAERALSSAGERAR---QLDALLEAlklkragnslAASTAEETAGSAQGRAQEAEQL 1701
Cdd:COG0840 476 AAASEEQSAGTEEVNQaieQIAAAAQE----------NAASVEEVAAAAEELAELAEEL 524
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1636-1780 |
5.51e-09 |
|
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: 55.69 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1636 EQTLYQVQERMAGAERALSSAGERARQLDAllealKLKRagnslaastAEETAGSAQGRAQEAEQLLRgplgdqyqtvkA 1715
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEE-----ERRQ---------AEEEAERLEQKRQEAEEEKE-----------R 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1716 LAERKAqgvlAAQARAEQLRDEARdllqAAQDKLQRLQElegtyEENERALESKAAQLDGLEARM 1780
Cdd:pfam20492 67 LEESAE----MEAEEKEQLEAELA----EAQEEIARLEE-----EVERKEEEARRLQEELEEARE 118
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
830-873 |
6.09e-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: 53.51 E-value: 6.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 530372442 830 ACQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWGFPS 873
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1264-1789 |
6.16e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 61.41 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1264 ELRREIGEAtehltqLEADLTDVQDENFN--ANHALSGLERDRLA-LNLT--------------LRQLDQHLDLLKHSNF 1326
Cdd:COG3899 667 ALHRRIARA------LEARGPEPLEERLFelAHHLNRAGERDRAArLLLRaarralargayaeaLRYLERALELLPPDPE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1327 LGAYDSIRHAHsqsAEAERRAntsalavpspvSNSASARHRTEALMDAQkedfnskhmaNQRALGKLSAHTHTLSLTDIN 1406
Cdd:COG3899 741 EEYRLALLLEL---AEALYLA-----------GRFEEAEALLERALAAR----------ALAALAALRHGNPPASARAYA 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1407 ELVCGAPGDAPCATSPCGGAGCRDEDGQPRCGGLSCNGAAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASE 1486
Cdd:COG3899 797 NLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1487 AQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRsl 1566
Cdd:COG3899 877 AAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAAL-- 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1567 advDAILARTVGDVRRAEQLLQDARRARSWAEDEkqkAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERM 1646
Cdd:COG3899 955 ---AAALALAAAAAAAAAAALAAAAAAAAAAAAA---AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALA 1028
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1647 AGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLA 1726
Cdd:COG3899 1029 AAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALA 1108
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1727 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINL 1789
Cdd:COG3899 1109 AALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALAL 1171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1244-1593 |
7.19e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1244 IVGARNTSAASTAQLVEATEELRREIGEATEHLTQLEADLTDVQDENFNANHALSGLERDRLALNLTLRQLDQHLD-LLK 1322
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1323 HSNFLGAYDSIRHAHSQSAEAERRANTSALAvpspvsNSASARHRTEALM---DAQKEDFNSKHMANQRALGKLSAHTHT 1399
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLE------EAEEELAEAEAEIeelEAQIEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1400 LSltdinelvcgapGDAPCATSPCGGAGCRDEDGQPRCGGLSCNGAAATADLAlgRARHTQAELQRALAEGGSILSRVAE 1479
Cdd:TIGR02168 815 LN------------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--SLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1480 TRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMvatrvlelsipasaeQIQHLAGAI 1559
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---------------RIDNLQERL 945
|
330 340 350
....*....|....*....|....*....|....*
gi 530372442 1560 AERVR-SLADVDAILARTVGDVRRAEQLLQDARRA 1593
Cdd:TIGR02168 946 SEEYSlTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1550-1779 |
7.57e-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: 60.08 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1550 EQIQHLAGAIAERVRSL----ADVDAILartvgdvRRAEQLLQDARRARSwaedEKQKAETVQAALEEAQraqgiaqGAI 1625
Cdd:pfam19220 6 ELLRVRLGEMADRLEDLrslkADFSQLI-------EPIEAILRELPQAKS----RLLELEALLAQERAAY-------GKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1626 RGAVADTRDteqtlyqvqeRMAGAERALSSAGERARQLDALLEalKLKRAGNSLAASTAEETA--GSAQGR-AQEAEQll 1702
Cdd:pfam19220 68 RRELAGLTR----------RLSAAEGELEELVARLAKLEAALR--EAEAAKEELRIELRDKTAqaEALERQlAAETEQ-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1703 RGPLGDQyqtVKALAERkAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQ-----------ELEGTYEENERALESKAA 1771
Cdd:pfam19220 134 NRALEEE---NKALREE-AQAAEKALQRAEGELATARERLALLEQENRRLQalseeqaaelaELTRRLAELETQLDATRA 209
|
....*...
gi 530372442 1772 QLDGLEAR 1779
Cdd:pfam19220 210 RLRALEGQ 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1463-1788 |
9.76e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1463 LQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQEL-------------IQSVKDFLNQ-EGA 1528
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeleeleaeleeLREELEKLEKlLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1529 DPDSIEMVATRV---------------------LELSIPASAEQIQHLAGAIAERVRSL-ADVDAILARTVGDVRRAEQL 1586
Cdd:COG4717 128 LPLYQELEALEAelaelperleeleerleelreLEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1587 LQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQ--------GAIRGAVADTRDTEQTLYQVQERMAGAerALSSAG- 1657
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearllLLIAAALLALLGLGGSLLSLILTIAGV--LFLVLGl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1658 ---------ERARQLDALLEALKLKRAGNSLAASTAEETAgSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQgvLAAQ 1728
Cdd:COG4717 286 lallflllaREKASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1729 ARAEQLRDEARDLLQAAQ-----------DKLQRLQELEGTYEENERALESKA---------AQLDGLEARMRSVLQAIN 1788
Cdd:COG4717 363 LQLEELEQEIAALLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLgeleelleaLDEEELEEELEELEEELE 442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1201-1795 |
1.03e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1201 VQDLAARTQRLEQRAQELQQtgVLGAFEssFWHMQEKLgivqgivgarntsaastAQLVEATEELRREIGEATEHLTQLE 1280
Cdd:COG4913 257 IRELAERYAAARERLAELEY--LRAALR--LWFAQRRL-----------------ELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1281 ADLTDVQDENFNANHALSGLERDRLA-LNLTLRQLDQHLDLLKHsnflgaydsirhahsQSAEAERRANTsaLAVPSPVS 1359
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERER---------------RRARLEALLAA--LGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1360 NSASARHRTEAlmDAQKEDFNSKHMANQRALGKLSAhthtlSLTDINElvcgapgdapcatspcggagcrdedgqprcgg 1439
Cdd:COG4913 379 AEEFAALRAEA--AALLEALEEELEALEEALAEAEA-----ALRDLRR-------------------------------- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1440 lscngaaatadlalgRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAAL----------DKANASRGQVEQA- 1508
Cdd:COG4913 420 ---------------ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELpfvgelievrPEEERWRGAIERVl 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1509 -NQEL-----QELIQSVKDFLNQ---------EGADPDSIEMVATRVLELSIpasAEQIQHLAGAIAERVRSL--ADVDA 1571
Cdd:COG4913 485 gGFALtllvpPEHYAAALRWVNRlhlrgrlvyERVRTGLPDPERPRLDPDSL---AGKLDFKPHPFRAWLEAElgRRFDY 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1572 ILARTVGDVRRAEQ----------------------------LLQDARRARSWAEDEKQKAEtvqAALEEAQRAQGIAQG 1623
Cdd:COG4913 562 VCVDSPEELRRHPRaitragqvkgngtrhekddrrrirsryvLGFDNRAKLAALEAELAELE---EELAEAEERLEALEA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1624 AIrgavaDTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALklkRAGNS-LAAstAEETAGSAQGRAQEAEQLL 1702
Cdd:COG4913 639 EL-----DALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL---DASSDdLAA--LEEQLEELEAELEELEEEL 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1703 RGplgdqyqtvkalAERKAQGVLAAQARAEQLRDEARDLLQAAQD--KLQRLQELEGTY-EENERALESK-----AAQLD 1774
Cdd:COG4913 709 DE------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDlaRLELRALLEERFaAALGDAVERElrenlEERID 776
|
650 660
....*....|....*....|.
gi 530372442 1775 GLEARMRSVLQAINLQVQIYN 1795
Cdd:COG4913 777 ALRARLNRAEEELERAMRAFN 797
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
831-874 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 831 CQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWG--FPSC 874
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1789 |
1.11e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1581 RRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGER- 1659
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1660 ARQLDALLEALKLKRAGNSLAASTAEETAGSA-------QGRAQEAEQLlRGPLGDQYQTVKALAERKAQ------GVLA 1726
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaPARREQAEEL-RADLAELAALRAELEAERAEleallaELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1727 AQARAEQLRDEARDLLQAAQDKL----QRLQELegtyEENERALESKAAQLDGLEARMRSVLQAINL 1789
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELaelaAELAEL----QQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-513 |
1.20e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.20e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 530372442 470 CQCNARGTVPGStpCDPNSGSCYCKRLVTGRGCDRCLPGHWGLS 513
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1460-1782 |
1.69e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEggsiLSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQ-------ELQELIQSVKDFLNQEGADPDS 1532
Cdd:PTZ00121 1297 KAEEKKKADE----AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKaaeaakaEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1533 IEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVdaiLARTVGDVRRAEQLLQDARRARSWAE-----DEKQKAETV 1607
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKADEakkkaEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1608 QAALEEAQRAQGIAQGAirgavADTRDTEQTLYQVQERMAgAERALSSAGERARQLDALLEALKLKRAGNSlaASTAEET 1687
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKA-----EEAKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADEAKKAAEAKKKADE--AKKAEEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1688 AGSAQGR----AQEAEQLLRGPLGDQYQTVKALAE-RKAQGVLAAQA--RAEQLRDEA-RDLLQAAQDKLQRLQELEGTY 1759
Cdd:PTZ00121 1522 KKADEAKkaeeAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEakKAEEDKNMAlRKAEEAKKAEEARIEEVMKLY 1601
|
330 340
....*....|....*....|....*
gi 530372442 1760 EENE--RALESKAAQldglEARMRS 1782
Cdd:PTZ00121 1602 EEEKkmKAEEAKKAE----EAKIKA 1622
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1730-1797 |
2.66e-08 |
|
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: 52.36 E-value: 2.66e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1730 RAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTC 1797
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1453-1796 |
3.04e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1453 LGRARhtqAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANAsrgQVEQANQELQELIQSvkdfLNQEGADPDS 1532
Cdd:COG4372 8 VGKAR---LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREELEQLEEE----LEQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1533 IEmvatrvlelsipasaEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALE 1612
Cdd:COG4372 78 LE---------------EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1613 EAQRAQgiaqgairgaVADTRDTEQTLYQVQERMAGAERALSSAGERA--RQLDALLEALKLKRAGNSLAASTAEETAGS 1690
Cdd:COG4372 143 SEIAER----------EEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1691 AQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEska 1770
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE--- 289
|
330 340
....*....|....*....|....*.
gi 530372442 1771 AQLDGLEARMRSVLQAINLQVQIYNT 1796
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALED 315
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1445-1787 |
3.15e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 58.51 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLA--LGRARHTQAELQRALAEGGSILSRVAET------------RRQASEAQQRA-QAALDKANASRGQVEQAN 1509
Cdd:COG3064 69 AELAAEAAkkLAEAEKAAAEAEKKAAAEKAKAAKEAEAaaaaekaaaaaeKEKAEEAKRKAeEEAKRKAEEERKAAEAEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1510 QELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQD 1589
Cdd:COG3064 149 AAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1590 ARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERAlssAGERARQLDALLEA 1669
Cdd:COG3064 229 SREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAA---AAGLVLDDSAALAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1670 LKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKL 1749
Cdd:COG3064 306 ELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEE 385
|
330 340 350
....*....|....*....|....*....|....*...
gi 530372442 1750 QRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAI 1787
Cdd:COG3064 386 AAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1477-1791 |
3.43e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1477 VAETRRQASEAQQRAQAALDKanasrgQVEQANQELQELIQSVKDFLNQEGadpdsiemvatrvlelsIPASAEQIQHLA 1556
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNG-----------------LVDLSEEAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1557 GAIAErvrsladvdailartvgdvrrAEQLLQDARRARSWAedekqkaetvQAALEEAQRAQGIAQGAIRGAVADT--RD 1634
Cdd:COG3206 219 QQLSE---------------------LESQLAEARAELAEA----------EARLAALRAQLGSGPDALPELLQSPviQQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1635 TEQTLYQVQERMAGAERALSSAGERARQLDALLEALKlkragnslaastaeetagsaQGRAQEAEQLlrgplgdqyqtvk 1714
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR--------------------AQLQQEAQRI------------- 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1715 aLAERKAQgVLAAQARAEQLRDEardlLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQV 1791
Cdd:COG3206 315 -LASLEAE-LEALQAREASLQAQ----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1482-1777 |
3.71e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1482 RQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEG--ADPDSIEmvatRVLELSipASAEQIQHLAGAI 1559
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANllADETLAD----RLEELR--EELDAAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1560 AERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAEtvqaALEE-AQRAQGIAQGAIRGAVADTRDTEQT 1638
Cdd:COG3096 913 QQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF----ALSEvVQRRPHFSYEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1639 LyqvQERMAGAERALSSAGERARQldallealklkragnslaastaeetagsAQGRAQEAEQL---LRGPLGDQYQTVKA 1715
Cdd:COG3096 989 L---RARLEQAEEARREAREQLRQ----------------------------AQAQYSQYNQVlasLKSSRDAKQQTLQE 1037
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1716 LAER-KAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLE 1777
Cdd:COG3096 1038 LEQElEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
409-468 |
4.32e-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: 50.82 E-value: 4.32e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 409 SCDCDPMGSQdGGRCDSHddpalglvSGQCRCKEHVVGTRCQQCRDGFFGLSiSDRLGCR 468
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
986-1028 |
4.51e-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: 50.81 E-value: 4.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530372442 986 CECSGNIDPmdPDACDPHTGQCLrCLHHTEGPHCAHCKPGFHG 1028
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
876-921 |
4.54e-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: 50.82 E-value: 4.54e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530372442 876 PCVCNGHAD---ECNTHTGACLgCRDHTGGEHCERCIAGFHGDPRLPYG 921
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1542-1754 |
5.11e-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: 56.66 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1542 ELSIPASAEQIQHLAGAIaervrsladVDAILArTVGD-VRRAEQLLQ-DARRARSwaedEKQKAEtvqAALEEAQRAQG 1619
Cdd:pfam00529 13 RVVVSGNAKAVQPQVSGI---------VTRVLV-KEGDrVKAGDVLFQlDPTDYQA----ALDSAE---AQLAKAQAQVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1620 IAQGAIRGAVAdtrdTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGnslAASTAEETAGSAQgRAQEAE 1699
Cdd:pfam00529 76 RLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR---RRVLAPIGGISRE-SLVTAG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1700 QLLRgplgDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQE 1754
Cdd:pfam00529 148 ALVA----QAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1598-1787 |
6.42e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1598 EDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSA----GERARQLdallealklK 1673
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelGERARAL---------Y 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1674 RAGNSLaaSTAEETAGSaqgraQEAEQLLrgplgDQYQTVKALAERKA---QGVLAAQARAEQLRDEARDLLQAAQDKLQ 1750
Cdd:COG3883 97 RSGGSV--SYLDVLLGS-----ESFSDFL-----DRLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 530372442 1751 RLQELEgtyEENERALESKAAQLDGLEARMRSVLQAI 1787
Cdd:COG3883 165 ELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1475-1754 |
9.40e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1475 SRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQeliqsvkdflNQEGADPDSIEMVATRVLELSIPASAEQIQh 1554
Cdd:TIGR02794 22 SLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKK----------PAAKKEQERQKKLEQQAEEAEKQRAAEQAR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1555 lagaIAERVRSLADVDAIlartvgdvRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRD 1634
Cdd:TIGR02794 91 ----QKELEQRAAAEKAA--------KQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1635 TEQtlyqvQERMAGAERALSSAGERARQldallEALKLKRAGNSLAASTAEETAGSAQGRAQEaeqllrgplgdqyqtvK 1714
Cdd:TIGR02794 159 KAA-----AEAKKKAEEAKKKAEAEAKA-----KAEAEAKAKAEEAKAKAEAAKAKAAAEAAA----------------K 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530372442 1715 ALAERKAQGVLAAQARAEQLrdEARDLLQAAQDKLQRLQE 1754
Cdd:TIGR02794 213 AEAEAAAAAAAEAERKADEA--ELGDIFGLASGSNAEKQG 250
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1445-1793 |
9.62e-08 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 56.95 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLN 1524
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1525 QEGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKA 1604
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1605 ETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAG-AERALSSA---------GERARQLDALLEALK--- 1671
Cdd:COG0840 176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERiAEGDLTVRidvdskdeiGQLADAFNRMIENLRelv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1672 --LKRAGNSLAAStAEETAGSAQGRAQEAEQLLrgplgDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKL 1749
Cdd:COG0840 256 gqVRESAEQVASA-SEELAASAEELAAGAEEQA-----ASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530372442 1750 QRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQI 1793
Cdd:COG0840 330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDI 373
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
877-924 |
1.42e-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: 49.66 E-value: 1.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 530372442 877 CVCNGHA---DECNTHTGACLgCRDHTGGEHCERCIAGFHGDPRLPyGGQC 924
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
410-460 |
1.62e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 1.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 530372442 410 CDCDPMGSQDGgRCDSHddpalglvSGQCRCKEHVVGTRCQQCRDGFFGLS 460
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1483-1796 |
2.11e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.22 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1483 QASEAQQRAQAALDKANASRGQVEQANQ---ELQELIQSVKDFLNQEGADPDSIE-------------MVATRVLELSIP 1546
Cdd:PRK10929 45 EIVEALQSALNWLEERKGSLERAKQYQQvidNFPKLSAELRQQLNNERDEPRSVPpnmstdaleqeilQVSSQLLEKSRQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1547 ASAEQiqhlagaiaERVRSLADVDAILArtvgdvrraeQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIR 1626
Cdd:PRK10929 125 AQQEQ---------DRAREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1627 GAVADTRDTEQ-TLYQVQE--RMagaeRAlSSAGERARQLDALLEALKlkragNSLaastaeetagSAQgRAQEAEQLLr 1703
Cdd:PRK10929 186 KALVDELELAQlSANNRQElaRL----RS-ELAKKRSQQLDAYLQALR-----NQL----------NSQ-RQREAERAL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1704 gplgdqyqtvkalaerkaqgvlaaqARAEQLRDEARDLLQAAQDKLQRLQELegtyeenERALESKAAQLDGLEARMRsv 1783
Cdd:PRK10929 244 -------------------------ESTELLAEQSGDLPKSIVAQFKINREL-------SQALNQQAQRMDLIASQQR-- 289
|
330
....*....|....*.
gi 530372442 1784 lQAIN--LQV-QIYNT 1796
Cdd:PRK10929 290 -QAASqtLQVrQALNT 304
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1476-1732 |
2.14e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 55.37 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1476 RVAETRRQASE-AQQRAQAALdkanASRGQVEQANQELQELiqsvkdflNQEGADPDSIEMVatrvLELSIPASAEQIQH 1554
Cdd:PRK07735 6 DLEDLKKEAARrAKEEARKRL----VAKHGAEISKLEEENR--------EKEKALPKNDDMT----IEEAKRRAAAAAKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1555 LAGAIAERVRsladvDAILARTVGDVRRAEQLLQDARRARSwAEDEKQKAETVQAALEE----AQRAQGIAQGAIRGAVA 1630
Cdd:PRK07735 70 KAAALAKQKR-----EGTEEVTEEEKAKAKAKAAAAAKAKA-AALAKQKREGTEEVTEEekaaAKAKAAAAAKAKAAALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1631 DTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEE-------TAGSAQGRA-----QEA 1698
Cdd:PRK07735 144 KQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEkakakakAAAAAKAKAaalakQKA 223
|
250 260 270
....*....|....*....|....*....|....
gi 530372442 1699 EQLlRGPLGDQYQTVKALAERKAQGVLAAQARAE 1732
Cdd:PRK07735 224 SQG-NGDSGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1452-1681 |
2.25e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 53.29 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQAelqRALAEGGSILSRVAETRRQASEAQQRAQAALDKANasrgqveqanqelqeliqsvkdflnqegadpd 1531
Cdd:COG1842 38 DLVEARQALA---QVIANQKRLERQLEELEAEAEKWEEKARLALEKGR-------------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1532 siEMVATRVLelsipasaEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDArrarswaedeKQKAETVqAAL 1611
Cdd:COG1842 83 --EDLAREAL--------ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEL----------KAKKDTL-KAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1612 EEAQRAQGIAQGAIRGavADTRDTEQTLYQVQERMAGAERALSSAGERARQ--LDALLEALKLKRAGNS-LAA 1681
Cdd:COG1842 142 AKAAKAQEKVNEALSG--IDSDDATSALERMEEKIEEMEARAEAAAELAAGdsLDDELAELEADSEVEDeLAA 212
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
986-1032 |
2.28e-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: 48.89 E-value: 2.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530372442 986 CECSGNIDPmdPDACDPHTGQCLrCLHHTEGPHCAHCKPGFHGQAAR 1032
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1631-1783 |
3.91e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1631 DTRDTEQTLYQVQERMA---GAERALSSAGERARQLDALLE-ALKLKRAGNSLAASTAEETAGSAQgRAQEAEQLLRGPL 1706
Cdd:COG4913 219 EEPDTFEAADALVEHFDdleRAHEALEDAREQIELLEPIRElAERYAAARERLAELEYLRAALRLW-FAQRRLELLEAEL 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1707 GDQYQTVKALAERKAQgvlaAQARAEQLRDEARDLLQA-AQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSV 1783
Cdd:COG4913 298 EELRAELARLEAELER----LEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1583-1792 |
4.06e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1583 AEQLLQDaRRARSWAEDEKQKAETVQAALEEA-QRAQGIAQGAIRGAVADTRDTEQTlyQVQERMAGAERALSSAGERAR 1661
Cdd:COG3064 1 AQEALEE-KAAEAAAQERLEQAEAEKRAAAEAeQKAKEEAEEERLAELEAKRQAEEE--AREAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1662 QLDallealKLKRAGNSLAASTAEETAGSaqgrAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDL 1741
Cdd:COG3064 78 KLA------EAEKAAAEAEKKAAAEKAKA----AKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530372442 1742 LQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQ 1792
Cdd:COG3064 148 AAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1445-1701 |
4.36e-07 |
|
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: 53.44 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLAlgRARHTQAE-LQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVkdfl 1523
Cdd:smart00283 17 AEELEELA--ERMEELSAsIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESS---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1524 nqegadpDSIEmvatRVLEL--SIpasAEQIQHLA--GAI---------------AERVRSLADvdailaRTvgdvrrae 1584
Cdd:smart00283 91 -------DEIG----EIVSVidDI---ADQTNLLAlnAAIeaarageagrgfavvADEVRKLAE------RS-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1585 qllQDArrarswAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMagaERALSSAGERARQLD 1664
Cdd:smart00283 143 ---AES------AKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSV---EEIADLVQEIAAATD 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 530372442 1665 ALLEALK-LKRAGNSLA------ASTAEETAGSAQGRAQEAEQL 1701
Cdd:smart00283 211 EQAAGSEeVNAAIDEIAqvtqetAAMSEEISAAAEELSGLAEEL 254
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1455-1787 |
4.82e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1455 RARHTQAEL-QRALAEggsilsrvAETRRQASEAQQRAqaALDKANASRGQVEQANQELQEliQSVKDFLNQEgadpdsi 1533
Cdd:COG3064 23 AEKRAAAEAeQKAKEE--------AEEERLAELEAKRQ--AEEEAREAKAEAEQRAAELAA--EAAKKLAEAE------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1534 emvatrvlelsipASAEQIQHLAGAIAERVRSLADVDAilartvgdvrRAEQLLQDARRARswAEDEKQKAETvQAALEE 1613
Cdd:COG3064 84 -------------KAAAEAEKKAAAEKAKAAKEAEAAA----------AAEKAAAAAEKEK--AEEAKRKAEE-EAKRKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1614 AQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQG 1693
Cdd:COG3064 138 EEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1694 RAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQL 1773
Cdd:COG3064 218 ALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVL 297
|
330
....*....|....
gi 530372442 1774 DGLEARMRSVLQAI 1787
Cdd:COG3064 298 DDSAALAAELLGAV 311
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1519-1782 |
5.10e-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: 55.07 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1519 VKDFLNQEGADPDSIEMV----ATRVLELSIPASAEQIQHLAGaIAERVRSLADVDAILARTVGDVRRAEQLLQDARRAR 1594
Cdd:TIGR02169 122 IHDFLAAAGIYPEGYNVVlqgdVTDFISMSPVERRKIIDEIAG-VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1595 SWAEDEKQKAETVQAALEEAQRAQG-IAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEAL--K 1671
Cdd:TIGR02169 201 ERLRREREKAERYQALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1672 LKRAG----NSLAASTAEETAGSAQGRAQEAEQLLRgplgdqyqtVKALAERKAQGVL-----------------AAQAR 1730
Cdd:TIGR02169 281 IKDLGeeeqLRVKEKIGELEAEIASLERSIAEKERE---------LEDAEERLAKLEAeidkllaeieelereieEERKR 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 530372442 1731 AEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRS 1782
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1475-1694 |
5.15e-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: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1475 SRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRV--LELSIPASAEQI 1552
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeLEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1553 QHLAGAIAERVRSL-----ADVDAIL--ARTVGDVRRAEQLLQ-----DARRARSWAED------EKQKAETVQAALEEA 1614
Cdd:COG4942 100 EAQKEELAELLRALyrlgrQPPLALLlsPEDFLDAVRRLQYLKylapaRREQAEELRADlaelaaLRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1615 QRAQGIAQGAIRGAVAdtrDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAgnSLAASTAEETAGSAQGR 1694
Cdd:COG4942 180 LAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA--AAAERTPAAGFAALKGK 254
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1478-1740 |
9.23e-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: 51.92 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1478 AETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFlnqegadPDSIEMVATRVLELSIPASAEQIQHLAG 1557
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDA-------PAELRELRQELAALQAKAEAAPKEILAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1558 aiaervRSLADVDAILARTVGDvrraeqlLQDARRARSWAEDEKQKAET----VQAALEEAQRAQGiaqgAIRGAVADTR 1633
Cdd:pfam12795 78 ------LSLEELEQRLLQTSAQ-------LQELQNQLAQLNSQLIELQTrperAQQQLSEARQRLQ----QIRNRLNGPA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1634 DTEQTLYQVQERMAGAERALssagerarqLDALLEALKLKRAGNS----LAASTAEETAgsAQGRAQEAE-QLLRGPLGD 1708
Cdd:pfam12795 141 PPGEPLSEAQRWALQAELAA---------LKAQIDMLEQELLSNNnrqdLLKARRDLLT--LRIQRLEQQlQALQELLNE 209
|
250 260 270
....*....|....*....|....*....|..
gi 530372442 1709 QYQtvkALAERkaqgvlaAQARAEQLRDEARD 1740
Cdd:pfam12795 210 KRL---QEAEQ-------AVAQTEQLAEEAAG 231
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1531-1798 |
9.55e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1531 DSIEMVATRVLELSIPASAE------QIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDA-------------- 1590
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKaelltlRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShayltqkreaqeeq 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1591 ---RRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIR-----GAVADTRDTEQTLYQ-VQERMAGAERALSSAGERAR 1661
Cdd:TIGR00618 256 lkkQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahiKAVTQIEQQAQRIHTeLQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1662 QLDALLEALKLkragnslaastaEETAGSAQGR-AQEAEQllrgPLGDQYQTVKALAERkaQGVLAAQaraeQLRDEARD 1740
Cdd:TIGR00618 336 QQSSIEEQRRL------------LQTLHSQEIHiRDAHEV----ATSIREISCQQHTLT--QHIHTLQ----QQKTTLTQ 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530372442 1741 LLQAAQDKLQRLQELEGTYEenERALESKAAQLDGLEARMRSVLQ---AINLQVQIYNTCQ 1798
Cdd:TIGR00618 394 KLQSLCKELDILQREQATID--TRTSAFRDLQGQLAHAKKQQELQqryAELCAAAITCTAQ 452
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1579-1782 |
1.45e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1579 DVRRAEQLLQDARR------ARSWAEDEkqkaetvQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERA 1652
Cdd:PRK04863 808 DVQKLQRLHQAFSRfigshlAVAFEADP-------EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1653 LSSA--------GERARQLDALLEALK-----LKRAGNSL------AASTAEETAGSAQGRAQ--EAEQLLRgplgDQYQ 1711
Cdd:PRK04863 881 LPRLnlladetlADRVEEIREQLDEAEeakrfVQQHGNALaqlepiVSVLQSDPEQFEQLKQDyqQAQQTQR----DAKQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1712 TVKALAE----------RKAQGVLAA-----------QARAEQLRDEARDLLQAAQDKL----QRLQELEGTYE------ 1760
Cdd:PRK04863 957 QAFALTEvvqrrahfsyEDAAEMLAKnsdlneklrqrLEQAEQERTRAREQLRQAQAQLaqynQVLASLKSSYDakrqml 1036
|
250 260
....*....|....*....|....
gi 530372442 1761 -ENERALESKAAQLD-GLEARMRS 1782
Cdd:PRK04863 1037 qELKQELQDLGVPADsGAEERARA 1060
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1446-1793 |
1.47e-06 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 53.27 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1446 AATADLALGRARHTQAELQRALAEggsilsrvaetRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQ 1525
Cdd:COG2203 337 ADQAAIAIERARLYEALEAALAAL-----------LQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1526 EGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAE 1605
Cdd:COG2203 406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1606 TVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAE 1685
Cdd:COG2203 486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1686 ETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERA 1765
Cdd:COG2203 566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645
|
330 340
....*....|....*....|....*...
gi 530372442 1766 LESKAAQLDGLEARMRSVLQAINLQVQI 1793
Cdd:COG2203 646 LALALASLVLLRALLATELDLILDSSLL 673
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1443-1792 |
1.67e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 52.72 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1443 NGAAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDF 1522
Cdd:COG0840 108 ALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1523 LNQEGADPDSIEMVATRVLELSIPASAEQIQHLA----------------GAIAERVRSLADVdaiLARTVGDVRR---- 1582
Cdd:COG0840 188 LLALVALAIILALLLSRSITRPLRELLEVLERIAegdltvridvdskdeiGQLADAFNRMIEN---LRELVGQVREsaeq 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1583 ----AEQLLQDARRARSWAEDEKQKAETVQAALEE--------AQRAQGIAQGAIRgAVADTRDTEQTLYQVQERMAGAE 1650
Cdd:COG0840 265 vasaSEELAASAEELAAGAEEQAASLEETAAAMEElsatvqevAENAQQAAELAEE-ASELAEEGGEVVEEAVEGIEEIR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1651 RALSSAGERARQLDallealklKRAGN-----SLAASTAEET-------------AGSaQGR-----AQEaeqllrgplg 1707
Cdd:COG0840 344 ESVEETAETIEELG--------ESSQEigeivDVIDDIAEQTnllalnaaieaarAGE-AGRgfavvADE---------- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1708 dqyqtVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAI 1787
Cdd:COG0840 405 -----VRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAAS 479
|
....*
gi 530372442 1788 NLQVQ 1792
Cdd:COG0840 480 EEQSA 484
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1449-1790 |
1.78e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALGRARHTQAELQRALAEG--GSILSRVAETRRQASEAQQR---AQAALDKANASRGQVEQANQELQELIQSVKDFL 1523
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEGqlQELQARLSESERQRAELAEKlskLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1524 NqegadpDSIEMVatrvlelsipaSAEQIQHLAgaIAERVRSLADVDAIL---------ARtvgdvRRAEQLLQDARRAR 1594
Cdd:pfam01576 471 Q------DTQELL-----------QEETRQKLN--LSTRLRQLEDERNSLqeqleeeeeAK-----RNVERQLSTLQAQL 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1595 SwaeDEKQKAETVQAALEEAQRAQGIAQgairgavadtRDTEQTLYQVQERMAGAERaLSSAGERARQ-LDALLEALKLK 1673
Cdd:pfam01576 527 S---DMKKKLEEDAGTLEALEEGKKRLQ----------RELEALTQQLEEKAAAYDK-LEKTKNRLQQeLDDLLVDLDHQ 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1674 RagnSLAAST-----------AEETAGSAQgRAQE---AEQLLRgplgdQYQTvKALA-ERKAQGVLAAQARAE----QL 1734
Cdd:pfam01576 593 R---QLVSNLekkqkkfdqmlAEEKAISAR-YAEErdrAEAEAR-----EKET-RALSlARALEEALEAKEELErtnkQL 662
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530372442 1735 RDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLE--------ARMR-SV-LQAINLQ 1790
Cdd:pfam01576 663 RAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEdelqatedAKLRlEVnMQALKAQ 728
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1449-1680 |
2.30e-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: 50.45 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALGRARHTQAEL---QRALAEggsilsRVAETRRQASEAQQRAQAALDKANasrgqveqanqelQELIQSVkdflnq 1525
Cdd:pfam04012 34 MQSELVKARQALAQTiarQKQLER------RLEQQTEQAKKLEEKAQAALTKGN-------------EELAREA------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1526 egadpdsiemvatrvlelsipasAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDArrarswaedeKQKAE 1605
Cdd:pfam04012 89 -----------------------LAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL----------KAKKN 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1606 TVQAAlEEAQRAQGIAQGAIRGavADTRDTEQTLYQVQERMAGAERALSSAGERA--RQLDALLEALKLKRAGNSLA 1680
Cdd:pfam04012 136 LLKAR-LKAAKAQEAVQTSLGS--LSTSSATDSFERIEEKIEEREARADAAAELAsaVDLDAKLEQAGIQMEVSEDV 209
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1473-1787 |
2.59e-06 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 52.50 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1473 ILSRVAEtrrQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASAEQI 1552
Cdd:COG2203 332 LLEALAD---QAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLD 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1553 QHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADT 1632
Cdd:COG2203 409 AADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALL 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1633 RDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQT 1712
Cdd:COG2203 489 LLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLL 568
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1713 VKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAI 1787
Cdd:COG2203 569 LLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALL 643
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1532-1778 |
2.85e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 50.87 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1532 SIEMVATRVLELSIPASAEQIQhlaGAIAER-VRSLA-DVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQA 1609
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQ---IEILEKeLSSLAqETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1610 ALEEAqraqgiaqgairgavadtrdTEQTLYQVQERMAGAERALSSAGERArqlDALLEALKLKRAGNSLAASTAEETAg 1689
Cdd:pfam06008 97 NIKEI--------------------NEKVATLGENDFALPSSDLSRMLAEA---QRMLGEIRSRDFGTQLQNAEAELKA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1690 sAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQgvlaaqaRAEQLRDeARDLLQAAQDKLQRLQELEGTYEENERALESK 1769
Cdd:pfam06008 153 -AQDLLSRIQTWFQSPQEENKALANALRDSLAE-------YEAKLSD-LRELLREAAAKTRDANRLNLANQANLREFQRK 223
|
....*....
gi 530372442 1770 AAQLDGLEA 1778
Cdd:pfam06008 224 KEEVSEQKN 232
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1558-1744 |
3.72e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1558 AIAERVRSLADVDAILARTVGDVRRAEQLLQDARRArswAEDEKQKAET-VQAALEEAQRAQGIAQGAIRGAVADTRDTE 1636
Cdd:COG1842 31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAE---AEKWEEKARLaLEKGREDLAREALERKAELEAQAEALEAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1637 QTLYQVQERMAGAERALSSAGERARQ----LDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQllrgplgDQYQT 1712
Cdd:COG1842 108 AQLEEQVEKLKEALRQLESKLEELKAkkdtLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIE-------EMEAR 180
|
170 180 190
....*....|....*....|....*....|..
gi 530372442 1713 VKALAERKAQGVLAAQARAEQLRDEARDLLQA 1744
Cdd:COG1842 181 AEAAAELAAGDSLDDELAELEADSEVEDELAA 212
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1581-1782 |
3.97e-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: 50.03 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1581 RRAEQLLQDARRArswaedeKQKAETVQAALEEAQRAqgiAQGAIRG-AVADTRDTEqtlyqVQERMAGAERALSSAGER 1659
Cdd:pfam00261 43 RRIQLLEEELERT-------EERLAEALEKLEEAEKA---ADESERGrKVLENRALK-----DEEKMEILEAQLKEAKEI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1660 ARQLDALLE--ALKLKRAGNSLaaSTAEETAGSAQGRAQEAEQLLRGpLGDQYQTVKALAERKAQgvlaaqaRAEQLRDE 1737
Cdd:pfam00261 108 AEEADRKYEevARKLVVVEGDL--ERAEERAELAESKIVELEEELKV-VGNNLKSLEASEEKASE-------REDKYEEQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530372442 1738 ARDLlqaaQDKLQrlqELEGTYEENERALESKAAQLDGLEARMRS 1782
Cdd:pfam00261 178 IRFL----TEKLK---EAETRAEFAERSVQKLEKEVDRLEDELEA 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1445-1788 |
4.16e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQAELQRALAEggsilSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELiqsvkdfln 1524
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELE-----DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL--------- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1525 QEGADPDSIEMVATRVL----ELSIPASAEQIQHLAGAIA--------------------ERVRS-LADVDAILARTVGD 1579
Cdd:PRK02224 362 REEAAELESELEEAREAvedrREEIEELEEEIEELRERFGdapvdlgnaedfleelreerDELRErEAELEATLRTARER 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1580 VRRAEQLL------------QDARRARSWAEDEKQKAE-------------TVQAALEEAQRAQGIAQGAIRgaVADTRD 1634
Cdd:PRK02224 442 VEEAEALLeagkcpecgqpvEGSPHVETIEEDRERVEEleaeledleeeveEVEERLERAEDLVEAEDRIER--LEERRE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1635 T-EQTLYQVQERMAGAERALSSAGERARQLDALLEAlklKRAgnslAASTAEETAGSAQGRA-----------QEAEQL- 1701
Cdd:PRK02224 520 DlEELIAERRETIEEKRERAEELRERAAELEAEAEE---KRE----AAAEAEEEAEEAREEVaelnsklaelkERIESLe 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1702 -------LRGPLGDQYQ------------------TVKALAERKAQ--------GVLAAQA---RAEQLRD--------- 1736
Cdd:PRK02224 593 rirtllaAIADAEDEIErlrekrealaelnderreRLAEKRERKREleaefdeaRIEEAREdkeRAEEYLEqveekldel 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1737 -EARDLLQ----AAQDKLQRLQELEGTYEENE------RALESKAAQLDGLEARMRSVLQAIN 1788
Cdd:PRK02224 673 rEERDDLQaeigAVENELEELEELRERREALEnrvealEALYDEAEELESMYGDLRAELRQRN 735
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1476-1700 |
4.27e-06 |
|
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: 49.99 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1476 RVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSvkdfLNQEGADPDsiEMVATRVLELSIPASAEQIQHL 1555
Cdd:pfam12795 17 KLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAE--AAPKEILASLSLEELEQRLLQT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1556 AGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDT 1635
Cdd:pfam12795 91 SAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLEQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530372442 1636 E-------QTLYQVQermagaeRALssAGERARQLDALLEAlkLKRAGNSLAASTAEETAGSAQGRAQEAEQ 1700
Cdd:pfam12795 171 EllsnnnrQDLLKAR-------RDL--LTLRIQRLEQQLQA--LQELLNEKRLQEAEQAVAQTEQLAEEAAG 231
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
926-984 |
4.33e-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: 45.42 E-value: 4.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 926 PCPCPeGPGSQRHfatSCHQDeysqQIVCHCRAGYTGLRCEACAPGHFGDPSRPGGrCQ 984
Cdd:cd00055 1 PCDCN-GHGSLSG---QCDPG----TGQCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1445-1754 |
4.46e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQAELQRALAEGGsilsrvAETRRQASEAQQRAQAALDKANasrgqvEQANQELQEliqsvkdfln 1524
Cdd:NF041483 977 AAETVGSAQQHAERIRTEAERVKAEAA------AEAERLRTEAREEADRTLDEAR------KDANKRRSE---------- 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1525 qegadpdsiemVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRR-AEQLLQDAR-RARSWAEDEKQ 1602
Cdd:NF041483 1035 -----------AAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKeAERIVAEATvEGNSLVEKART 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1603 KAETVqaaLEEAQRaqgiAQGAIRGAVADTRD-TEQTLYQVQERmagAER----ALSSAGERArqlDALLEALKLKRAGn 1677
Cdd:NF041483 1104 DADEL---LVGARR----DATAIRERAEELRDrITGEIEELHER---ARResaeQMKSAGERC---DALVKAAEEQLAE- 1169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1678 slAASTAEETAGSAQGRA--------QEAEQLLRgplgdQYQTVKALAERKAQGVLA-AQARAEQLRDEARDLLqaaqDK 1748
Cdd:NF041483 1170 --AEAKAKELVSDANSEAskvriaavKKAEGLLK-----EAEQKKAELVREAEKIKAeAEAEAKRTVEEGKREL----DV 1238
|
....*.
gi 530372442 1749 LQRLQE 1754
Cdd:NF041483 1239 LVRRRE 1244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1460-1722 |
5.16e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANaSRGQVEQANQELQELIQSVKdfLNQEgadpdsiEMVATR 1539
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE-KKMKAEEAKKAEEAKIKAEE--LKKA-------EEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1540 VLELSIPASAEQIQhlagaiAERVRSLADVDAIlaRTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQG 1619
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK------AEELKKAEEENKI--KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1620 IAqgaiRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDallEALKLKRAGNSLAASTAEETAGSAQGRaQEAE 1699
Cdd:PTZ00121 1707 LK----KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIR-KEKE 1778
|
250 260
....*....|....*....|...
gi 530372442 1700 QLLRGPLGDQYQTVKALAERKAQ 1722
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1445-1787 |
5.22e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.18 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQA--ELQRALAEGGSILSRVAETRRQASEAQQRAQAAldkANASRgQVEQANQELqeliqsvkdf 1522
Cdd:pfam05701 120 VAAKAQLEVAKARHAAAvaELKSVKEELESLRKEYASLVSERDIAIKRAEEA---VSASK-EIEKTVEEL---------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1523 lnqegadpdSIEMVATR-VLELSipasaeqiqHLAGAIAERVRsladVDAILARTVG------DVRRAEQLLQDARRARS 1595
Cdd:pfam05701 186 ---------TIELIATKeSLESA---------HAAHLEAEEHR----IGAALAREQDklnwekELKQAEEELQRLNQQLL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1596 WAEDEKQKAETVQAAL----------------EEAQRAQG--IAQGAIRGAVADTRDteqtlyQVQERMAGAERALSSag 1657
Cdd:pfam05701 244 SAKDLKSKLETASALLldlkaelaaymesklkEEADGEGNekKTSTSIQAALASAKK------ELEEVKANIEKAKDE-- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1658 erARQLDALLEALK--LKRAGNSLAASTAEETAGSAQGRAQEAE-QLLRGPLGDQYQTVKALAERKAQgvLAAQ-ARAEQ 1733
Cdd:pfam05701 316 --VNCLRVAAASLRseLEKEKAELASLRQREGMASIAVSSLEAElNRTKSEIALVQAKEKEAREKMVE--LPKQlQQAAQ 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1734 LRDEARDLLQAAQDklqrlqELEGTYEENERAlesKAAqLDGLEARMRSVLQAI 1787
Cdd:pfam05701 392 EAEEAKSLAQAARE------ELRKAKEEAEQA---KAA-ASTVESRLEAVLKEI 435
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1478-1788 |
5.63e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1478 AETRRQASEAQQRAQAALDKANASRGQVEQAN---QELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASAEQIQH 1554
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLkkqQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1555 LAGAIAERVRSLADVDAILArtvgdvrRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGaIRGAVADTRD 1634
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRA-------KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS-IREISCQQHT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1635 TEQTLYQVQERMAGAERALSSAGERARQLDAL---LEALKLKRA---GNSLAASTAEETagsaqgrAQEAEQLLRGPLGD 1708
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatIDTRTSAFRdlqGQLAHAKKQQEL-------QQRYAELCAAAITC 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1709 QYQTVKAlaeRKAQGVLAAQA---RAEQLRDEARDLLQAAQDK------LQRLQELEGTYEENERALESKAAQLDGLEAR 1779
Cdd:TIGR00618 450 TAQCEKL---EKIHLQESAQSlkeREQQLQTKEQIHLQETRKKavvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
....*....
gi 530372442 1780 MRSVLQAIN 1788
Cdd:TIGR00618 527 TRRMQRGEQ 535
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1472-1681 |
6.16e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 49.72 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1472 SILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKdFLNQEGADPDSIEmvatrvlelsIPASAEQ 1551
Cdd:pfam06008 58 ELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVA-TLGENDFALPSSD----------LSRMLAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1552 IQHLAGAIAERvrslaDVDAILARTVGDVRRAEQLLQdarRARSWAEDEKQKAETVQAALEE--AQRAQGI--AQGAIRG 1627
Cdd:pfam06008 127 AQRMLGEIRSR-----DFGTQLQNAEAELKAAQDLLS---RIQTWFQSPQEENKALANALRDslAEYEAKLsdLRELLRE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1628 AVADTRDTEQTLYQVQERMagaeRALSSAGERARQLDALLEALkLKRAGNSLAA 1681
Cdd:pfam06008 199 AAAKTRDANRLNLANQANL----REFQRKKEEVSEQKNQLEET-LKTARDSLDA 247
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1482-1664 |
6.46e-06 |
|
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: 50.11 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1482 RQASEAQQRAQAALDKAnasRGQVEQANQELQELiQSVKDFLNQEGADPDSIEmVATRVLELSIPASAEQIQhLAGAIAE 1561
Cdd:pfam00529 54 TDYQAALDSAEAQLAKA---QAQVARLQAELDRL-QALESELAISRQDYDGAT-AQLRAAQAAVKAAQAQLA-QAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1562 RVRSLADVDAILARTvgdvrraeqlLQDARRARswaedekqkaETVQAALEEAQRAQGIAQGAIRGAVADT-RDTEQTLY 1640
Cdd:pfam00529 128 RRRVLAPIGGISRES----------LVTAGALV----------AQAQANLLATVAQLDQIYVQITQSAAENqAEVRSELS 187
|
170 180
....*....|....*....|....
gi 530372442 1641 QVQERMAGAERALSSAGERARQLD 1664
Cdd:pfam00529 188 GAQLQIAEAEAELKLAKLDLERTE 211
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1558-1754 |
7.14e-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: 48.91 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1558 AIAERVRSLADVDAILARTVGDVRRAEQLL-QDARRARSWaEDEKQKA------ETVQAALEEAQRAQGIAQGairgava 1630
Cdd:pfam04012 30 AIRDMQSELVKARQALAQTIARQKQLERRLeQQTEQAKKL-EEKAQAAltkgneELAREALAEKKSLEKQAEA------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1631 dtrdtEQTLYQVQERM-AGAERALSSAGERARQLDALLEALKLkRAGNSLAASTAEETAGSAqgRAQEAEQLLrgplgDQ 1709
Cdd:pfam04012 102 -----LETQLAQQRSAvEQLRKQLAALETKIQQLKAKKNLLKA-RLKAAKAQEAVQTSLGSL--STSSATDSF-----ER 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530372442 1710 YQTvkALAERKAQGVLAAQARAEQLRDEARDLLQA----AQDKLQRLQE 1754
Cdd:pfam04012 169 IEE--KIEEREARADAAAELASAVDLDAKLEQAGIqmevSEDVLARLKA 215
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1195-1786 |
9.43e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1195 GDWDRVVQDLAARTQRLEQRAQEL-QQTGVLGAFESSFWHMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIG--- 1270
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELeELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEvve 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1271 EATEHLTQLEADLTDVQDEnfnanhalsgleRDRLALNLTLRQldQHLDLLKHSNflGAYdsiRHAHSQSAEAERRANTS 1350
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEE------------VDSLKSQLADYQ--QALDVQQTRA--IQY---QQAVQALEKARALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1351 ALAVPSPVSNSASARHR----TEALMDA-QKEDFNSKHmANQralgklsaHTHTLsltdinELVCGAPGDAPcatspcgg 1425
Cdd:COG3096 433 DLTPENAEDYLAAFRAKeqqaTEEVLELeQKLSVADAA-RRQ--------FEKAY------ELVCKIAGEVE-------- 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1426 agcRDEdgqprcgglscngAAATADLALGRARHTQAELQRA------LAEGGSILSRVAETRRQASEAQQRAQAALDKAN 1499
Cdd:COG3096 490 ---RSQ-------------AWQTARELLRRYRSQQALAQRLqqlraqLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1500 ASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASA-----EQIQHLAGAIAERVRSLADVDAILA 1574
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQ 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1575 RTVGDVR-----------RAEQLLQDARR--ARSWAEDEK--QKAETVQA----------ALEEA--------QRAQGIA 1621
Cdd:COG3096 634 QLLEREReatverdelaaRKQALESQIERlsQPGGAEDPRllALAERLGGvllseiyddvTLEDApyfsalygPARHAIV 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1622 ---QGAIRGAVADTRDTEQTLYQVQ-------------ERMAGA------ERALSSA--------GERARQldALLEALK 1671
Cdd:COG3096 714 vpdLSAVKEQLAGLEDCPEDLYLIEgdpdsfddsvfdaEELEDAvvvklsDRQWRYSrfpevplfGRAARE--KRLEELR 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1672 LKRAGnslaasTAEETAGSAQGR------AQEAEQLLRGPL-----GDQYQTVKALAERK--AQGVLAAQARAEQLRDEA 1738
Cdd:COG3096 792 AERDE------LAEQYAKASFDVqklqrlHQAFSQFVGGHLavafaPDPEAELAALRQRRseLERELAQHRAQEQQLRQQ 865
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 530372442 1739 RDLLQAAQDKLQRLQELEGTYEEneralESKAAQLDGLEARMRSVLQA 1786
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANLLAD-----ETLADRLEELREELDAAQEA 908
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
986-1028 |
1.01e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 530372442 986 CECS--GNIDPmdpdACDPHTGQCLrCLHHTEGPHCAHCKPGFHG 1028
Cdd:smart00180 1 CDCDpgGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1462-1769 |
1.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1462 ELQRALAEGGSI--LSRVAETRRQASEAQQRAQAAlDKANASRGQVEQAnQELQELIQSVKDFLNQEGADPDSIEmvATR 1539
Cdd:PTZ00121 1409 ELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEE--AKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1540 VLELSipASAEQIQHLAGAI--AERVRSLADVdailARTVGDVRRAEQL--LQDARRArswaeDEKQKAETVQAAlEEAQ 1615
Cdd:PTZ00121 1485 ADEAK--KKAEEAKKKADEAkkAAEAKKKADE----AKKAEEAKKADEAkkAEEAKKA-----DEAKKAEEKKKA-DELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1616 RAQGIAQGAIRGAVADTRDTEQTLYQVQERmagAERALSSAGERARQLDALLEALKLKRAGNslAASTAEETAGSAQGRA 1695
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRK---AEEAKKAEEARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1696 QEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLR-------DEARDLLQAAQDKLQRLQELEGTYEENERALES 1768
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeedkKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
.
gi 530372442 1769 K 1769
Cdd:PTZ00121 1708 K 1708
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1561-1792 |
1.24e-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: 50.44 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1561 ERVRSLADVDAILARtVGDVRR---------------AEQL--LQDARRARSWA------EDEKQKAETVQAALEEAQRA 1617
Cdd:TIGR02168 176 ETERKLERTRENLDR-LEDILNelerqlkslerqaekAERYkeLKAELRELELAllvlrlEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1618 QGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAgnslaasTAEETAGSAQGRAQE 1697
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA-------NLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1698 AEQLLrgplgDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLE 1777
Cdd:TIGR02168 328 LESKL-----DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250
....*....|....*
gi 530372442 1778 ARMRSVLQAINLQVQ 1792
Cdd:TIGR02168 403 ERLEARLERLEDRRE 417
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1603-1747 |
1.46e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 49.87 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1603 KAETVQAALEEAQRAQGIAQGAIRGAvADTRDTeqtlyqvqerMAGAERALSSAGERARQLD---ALLEAlKLKRAGNSL 1679
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAA-DEAKTA----------AAAAAREAAPLKASLRKLErakARADA-ELKRADKAL 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1680 AASTAEETAGSAQGRAQEAEQLLrGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQD 1747
Cdd:PRK12472 249 AAAKTDEAKARAEERQQKAAQQA-AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATD 315
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
953-983 |
1.50e-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: 43.88 E-value: 1.50e-05
10 20 30
....*....|....*....|....*....|.
gi 530372442 953 VCHCRAGYTGLRCEACAPGHFGDPSRPGGRC 983
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| 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 ... |
1701-1793 |
1.50e-05 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 46.15 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1701 LLRGPLGDQYQTVKAL-------AERKAQGVLAAQARAEQL----RDEARDLLQAAQDKLQRL-QELEG-TYEENERALE 1767
Cdd:pfam00430 19 FAWKPLGKVLDKRRELiadeiaeAEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIE 98
|
90 100
....*....|....*....|....*...
gi 530372442 1768 SKAAQLDGLEARMRSVL--QAINLQVQI 1793
Cdd:pfam00430 99 QAAAEIEQEKDRALAELrqQVVALAVQI 126
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1536-1782 |
1.57e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1536 VATRVLELSIPASAE-QIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDArrarswaedeKQKAETVQAALEEA 1614
Cdd:COG3883 1 ALALALAAPTPAFADpQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL----------QAELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1615 QRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAG-----ERARQLD-------ALLEALKlkragnslaas 1682
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESfsdflDRLSALSkiadadaDLLEELK----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1683 taeetagSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQgVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEEN 1762
Cdd:COG3883 140 -------ADKAELEAKKAELEAKLAELEALKAELEAAKAE-LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
250 260
....*....|....*....|
gi 530372442 1763 ERALESKAAQLDGLEARMRS 1782
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAAAA 231
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
1444-1774 |
1.60e-05 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 50.08 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1444 GAAATADLALGRAR-HTQAELQRALaeggsilsrVAETRRQASEAQQRAQAALDKANA-------------SRGQVEQAN 1509
Cdd:TIGR02917 245 EAEKHADALLKKAPnSPLAHYLKAL---------VDFQKKNYEDARETLQDALKSAPEylpalllagaseyQLGNLEQAY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1510 QELQeliqsvkDFLNQEGADPDSIEMVATRVLELSIPASAEqiqhlagAIAERVRSLADVDA----ILARTV---GDVRR 1582
Cdd:TIGR02917 316 QYLN-------QILKYAPNSHQARRLLASIQLRLGRVDEAI-------ATLSPALGLDPDDPaalsLLGEAYlalGDFEK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1583 AEQLLQDARrarswaedeKQKAETVQAALEEAQRAqgIAQGAIRGAVADTRDTEQTLYQvqerMAGAERALSSAGERARQ 1662
Cdd:TIGR02917 382 AAEYLAKAT---------ELDPENAAARTQLGISK--LSQGDPSEAIADLETAAQLDPE----LGRADLLLILSYLRSGQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1663 LDALLEALKLKRAGNSLAASTAEETAGSAQGR--AQEAEQLLRGPLGDQYQTVKALAE-----RKAQGVLAAQARAEQLR 1735
Cdd:TIGR02917 447 FDKALAAAKKLEKKQPDNASLHNLLGAIYLGKgdLAKAREAFEKALSIEPDFFPAAANlaridIQEGNPDDAIQRFEKVL 526
|
330 340 350
....*....|....*....|....*....|....*....
gi 530372442 1736 DEARDLLQAAQdKLQRLQELEGTYEENERALEsKAAQLD 1774
Cdd:TIGR02917 527 TIDPKNLRAIL-ALAGLYLRTGNEEEAVAWLE-KAAELN 563
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1461-1771 |
1.88e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.64 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1461 AELQrALAEggSILSRVAETRRQASEAQQRAQAALDKANAS----RGQVEQANQELQEL---IQSVKDFLNQEGADPDSI 1533
Cdd:pfam05701 264 AELA-AYME--SKLKEEADGEGNEKKTSTSIQAALASAKKEleevKANIEKAKDEVNCLrvaAASLRSELEKEKAELASL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1534 ---EMVAtrvlelSIPASAEQiqhlagaiAERVRSLADVDAILARTVGDVRRAEQL---LQDARRArswAEDEKQKAetv 1607
Cdd:pfam05701 341 rqrEGMA------SIAVSSLE--------AELNRTKSEIALVQAKEKEAREKMVELpkqLQQAAQE---AEEAKSLA--- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1608 QAALEEAQRAQGIAQGAIRGAVAdtrdTEQTLYQVQERM----AGAERALSSAgerarqlDALLEALKLKRAGNSLAAS- 1682
Cdd:pfam05701 401 QAAREELRKAKEEAEQAKAAAST----VESRLEAVLKEIeaakASEKLALAAI-------KALQESESSAESTNQEDSPr 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1683 ----TAEETAgSAQGRAQEAEQLLRgplgdqyqtvKALAERKAQgvlAAQARAEQLRDEARdLLQAAQDKLQRLQELEGT 1758
Cdd:pfam05701 470 gvtlSLEEYY-ELSKRAHEAEELAN----------KRVAEAVSQ---IEEAKESELRSLEK-LEEVNREMEERKEALKIA 534
|
330
....*....|...
gi 530372442 1759 YEENERALESKAA 1771
Cdd:pfam05701 535 LEKAEKAKEGKLA 547
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1635-1781 |
1.90e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 47.75 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1635 TEQTLYQVQERMAGAERALSSAGERARQLDALLEALKL---KRAGNSLAASTA--EETAGSAQGRAQEAEQLLRGpLGDQ 1709
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEqakKLEEKAQAALTKgnEELAREALAEKKSLEKQAEA-LETQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1710 YQTVKALAErKAQGVLAA-QARAEQLRDEARDLLqaAQDKLQRLQE-LEGTY-----EENERALESKAAQLDGLEARMR 1781
Cdd:pfam04012 106 LAQQRSAVE-QLRKQLAAlETKIQQLKAKKNLLK--ARLKAAKAQEaVQTSLgslstSSATDSFERIEEKIEEREARAD 181
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1557-1753 |
3.09e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.12 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1557 GAIAERVRSL-ADVDAILAR---TVGDVRRAEQLLqdarrARSWAEDEKQKAETVQAALEEAQrAQGIAQGAIRGAVADT 1632
Cdd:COG1566 39 GRVEARVVTVaAKVSGRVTEvlvKEGDRVKKGQVL-----ARLDPTDLQAALAQAEAQLAAAE-AQLARLEAELGAEAEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1633 RDTEQTLYQVQERMAGAERALssagERARQLDAllealklKRAGNSLAASTAEETAGSAQGRAQEAEQllrgplgdQYQT 1712
Cdd:COG1566 113 AAAEAQLAAAQAQLDLAQREL----ERYQALYK-------KGAVSQQELDEARAALDAAQAQLEAAQA--------QLAQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 530372442 1713 VKALAERKAQgVLAAQARAEQLRDEardlLQAAQDKLQRLQ 1753
Cdd:COG1566 174 AQAGLREEEE-LAAAQAQVAQAEAA----LAQAELNLARTT 209
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1444-1745 |
3.26e-05 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 47.98 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1444 GAAATAD--LALGRARHTQAE--LQRALAEGGS-ILSRVAetrrqASEAqqrAQAaldkanasRGQVEQANQELQELIQS 1518
Cdd:COG3071 16 LLAALLEglLALAEGRYARAEklLSKAAEHSEApLLAYLL-----AARA---AQA--------LGDYERRDEYLAQALEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1519 vkdflnqegaDPDSIEMVATRVLELSIpasaeQIQHLAGAiaervrsLADVDAILARTVGDVRRAEQLLQDARRARSWAE 1598
Cdd:COG3071 80 ----------APEAELAVLLTRAELLL-----DQGQAEQA-------LATLEALRAGAPRHPQVLRLLLQAYRQLGDWEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1599 dekqkaetVQAALEEAQRAQGIaqgairgavadtrdtEQTLYQVQERMAGAERaLSSAGERARQLDALLEAL-KLKRAGN 1677
Cdd:COG3071 138 --------LLELLPALRKHKAL---------------SAEEAQALERRAYLGL-LRQAARDAEALKALWKALpRAERRDP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1678 SLAASTAEetAGSAQGRAQEAEQLLRGPLGDQYQT--VKALAERKAQGVLAAQARAE----------------------- 1732
Cdd:COG3071 194 ELAAAYAR--ALIALGDHDEAERLLREALKRQWDPrlVRLYGRLQGGDPAKQLKRAEkwlkkhpndpdlllalgrlclrn 271
|
330
....*....|...
gi 530372442 1733 QLRDEARDLLQAA 1745
Cdd:COG3071 272 QLWGKAREYLEAA 284
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1603-1772 |
3.31e-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: 48.30 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1603 KAETVQAALEEAQRAQgiaqgaIRGAVADTRDTEQ-TLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAgnslaa 1681
Cdd:TIGR02794 39 QAVLVDPGAVAQQANR------IQQQKKPAAKKEQeRQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1682 stAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQElegtyEE 1761
Cdd:TIGR02794 107 --AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA-----EA 179
|
170
....*....|..
gi 530372442 1762 NERAL-ESKAAQ 1772
Cdd:TIGR02794 180 KAKAEaEAKAKA 191
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
347-398 |
3.82e-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: 42.73 E-value: 3.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 347 CECHGH---THSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 398
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1452-1793 |
3.83e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 48.65 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGA--- 1528
Cdd:COG2203 152 AALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGail 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1529 --DPDS--IEMVATRVLELSIPASAEQIQHLAGAIAERVRSL----ADVDAILARTVGDVRRAEQ--------LLQD--- 1589
Cdd:COG2203 232 lvDEDGgeLELVAAPGLPEEELGRLPLGEGLAGRALRTGEPVvvndASTDPRFAPSLRELLLALGirsllcvpLLVDgrl 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1590 -------ARRARSWAEDEKQKAETV---------QAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERAL 1653
Cdd:COG2203 312 igvlalySKEPRAFTEEDLELLEALadqaaiaieRARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLAL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1654 SSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQ 1733
Cdd:COG2203 392 LLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELL 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1734 LRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQI 1793
Cdd:COG2203 472 VLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAA 531
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
927-976 |
4.02e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 4.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530372442 927 CPCPEGpgsqRHFATSCHQDeysqQIVCHCRAGYTGLRCEACAPGHFGDP 976
Cdd:smart00180 1 CDCDPG----GSASGTCDPD----TGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1588-1781 |
4.04e-05 |
|
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: 46.02 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1588 QDARRARS-WAEDEKQKAETVQAALE-EAQRAQGIAQgairgavaDTRDTEQTLYQVQERMAGAERALSSAGERARQLDA 1665
Cdd:pfam05335 30 AAARQVKNqLADKALQAAKAAEAALAgKQQIVEQLEQ--------ELREAEAVVQEESASLQQSQANANAAQRAAQQAQQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1666 LLEALKlkragNSLAAstAEETAGSAQGRAQEAEQllrgplgdqyqtvkALAErKAQGVLAAQARAEQLrdeARDLLQAA 1745
Cdd:pfam05335 102 QLEALT-----AALKA--AQANLENAEQVAAGAQQ--------------ELAE-KTQLLEAAKKRVERL---QRQLAEAR 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 530372442 1746 QDklqrlqelegtYEENERALE--SKAAQldglEARMR 1781
Cdd:pfam05335 157 AD-----------LEKTKKAAYkaACAAV----EAKQK 179
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1584-1754 |
4.14e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.10 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1584 EQLLQDARRARSWAEDEKQKA-ETVQAALEEAqraqgiaqgaiRGAVADTRDTEQTlyQVQERMAGAERALSSAGER--- 1659
Cdd:pfam01442 18 EQLGPVAQELVDRLEKETEALrERLQKDLEEV-----------RAKLEPYLEELQA--KLGQNVEELRQRLEPYTEElrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1660 --ARQLDALLEALKLKRAGnslAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVlaaqarAEQLRDE 1737
Cdd:pfam01442 85 rlNADAEELQEKLAPYGEE---LRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEV------QAQLSQR 155
|
170
....*....|....*..
gi 530372442 1738 ARDLLQAAQDKLQRLQE 1754
Cdd:pfam01442 156 LQELREKLEPQAEDLRE 172
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
347-399 |
4.27e-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: 42.73 E-value: 4.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372442 347 CECHGH---THSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 399
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-335 |
5.74e-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: 42.34 E-value: 5.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530372442 283 CFCYGHAS---ECApapgapahaegMVHGACICKHNTRGLNCEQCQDFYRDLPWRP 335
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1483-1753 |
6.75e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 46.64 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1483 QASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQegadpdsiemvATRVLelsipASAEQIQHLAGAIAER 1562
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK-----------ATQTL-----AKAQQVNAESERTLGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1563 VRSLADvdAIlartVGDVRRAEQLLQDArrARSWAEDEKQKAETVQAALEEAQRAQGIaqgaIRGavadtRDTEQTLYQV 1642
Cdd:pfam06008 84 AKELAE--AI----KNLIDNIKEINEKV--ATLGENDFALPSSDLSRMLAEAQRMLGE----IRS-----RDFGTQLQNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1643 QERMAGAERALSSAGERAR----QLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRgplgdqyQTVKAL-- 1716
Cdd:pfam06008 147 EAELKAAQDLLSRIQTWFQspqeENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNL-------ANQANLre 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 530372442 1717 AERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQ 1753
Cdd:pfam06008 220 FQRKKEEVSEQKNQLEETLKTARDSLDAANLLLQEID 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1580-1787 |
6.77e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1580 VRRAEQLLQDARRARSWAEDEKQKAETV---QAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERM-AGAERALSS 1655
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQanrEAEEAELEQEREIETARIAEAEAELAKKKAEERREAETArAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1656 AGERA-RQLDALLEALKLKRagnslaastaeetagsaQGRAQEAEQLlrgplgdqyqtvKALAERKAQGVLAAQARAEQL 1734
Cdd:COG2268 271 AEANAeREVQRQLEIAERER-----------------EIELQEKEAE------------REEAELEADVRKPAEAEKQAA 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1735 RDEARdlLQAAQDKLQRLQELEGTYEENEraleskAAQLDGLEARMRSVLQAI 1787
Cdd:COG2268 322 EAEAE--AEAEAIRAKGLAEAEGKRALAE------AWNKLGDAAILLMLIEKL 366
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1466-1753 |
7.22e-05 |
|
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: 47.91 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1466 ALAEGGSILSRVAETRRQaSEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLnqEGADPDSIEMVATRVLElSI 1545
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1546 PASAEQIQHLAGAIAERVRSLaDVDAILARTVGDVRR---AEQLLQdarRARSWAEDEKQkaeTVQAALEEAQRAQGIAQ 1622
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDAL-DSQATYAGESGDQWRnpfAGGLLD---RVQEQLDDAKK---ISGKQLADAKQRHVDNQ 1684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1623 GAIRGAVAdtrDTEQTLYQVQERMAGAERALSSAGERA--RQLDALL---EALKLKRAGNSLA----------ASTAEET 1687
Cdd:NF012221 1685 QKVKDAVA---KSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1688 AGSAQGRAQEAEQ----------LLRGPLGDQYQTVKALAER----KAQGVLAAQAR-AEQLRDEARDLLQAAQDKLQRL 1752
Cdd:NF012221 1762 ANQAQADAKGAKQdesdkpnrqgAAGSGLSGKAYSVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNRL 1841
|
.
gi 530372442 1753 Q 1753
Cdd:NF012221 1842 Q 1842
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1256-1617 |
7.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1256 AQLVEATEELRREIGEATEHLTQLEADLTDVQDEnfnanHALSGLERDRLALNLTLRQLDQHLDLL--KHSNFLGAYDSI 1333
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELeeRLEELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1334 RHAHSQSAEAERRANTsALAVPSPVSNSASARHRTEAlmdaqkEDFNSKHMANQRALGKLSAHTHTLSlTDINELVCGAP 1413
Cdd:COG4717 166 EELEAELAELQEELEE-LLEQLSLATEEELQDLAEEL------EELQQRLAELEEELEEAQEELEELE-EELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1414 GDAPC------------ATSPCGGAGCRDEDGQP--RCGGLSCNGAAATADLALGRARH--------------------T 1459
Cdd:COG4717 238 AAALEerlkearlllliAAALLALLGLGGSLLSLilTIAGVLFLVLGLLALLFLLLAREkaslgkeaeelqalpaleelE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1460 QAELQRALAEGG---------------------SILSRVAETRRQA--SEAQQRAQAALDKANAS-----RGQVEQAN-- 1509
Cdd:COG4717 318 EEELEELLAALGlppdlspeellelldrieelqELLREAEELEEELqlEELEQEIAALLAEAGVEdeeelRAALEQAEey 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1510 QELQELIQSVKDFLnqEGADPDSIEMVATRVLElSIPASAEQIQHLAGAIAERVRSL----ADVDAILAR--TVGDVRRA 1583
Cdd:COG4717 398 QELKEELEELEEQL--EELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELreelAELEAELEQleEDGELAEL 474
|
410 420 430
....*....|....*....|....*....|....
gi 530372442 1584 EQLLQDARRARSWAEDEKQKAETVQAALEEAQRA 1617
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1546-1793 |
7.92e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1546 PASAEQIQHLAGAIAERVRSLADVDAILARTV---GDVRRAEQLLQDarRARSWAED---------EKQKAETVQAALEE 1613
Cdd:pfam12128 175 ESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILeddGVVPPKSRLNRQ--QVEHWIRDiqaiagimkIRPEFTKLQQEFNT 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1614 AQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEaLKLKRAGNSLAASTAEETAGSAQG 1693
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN-GELSAADAAVAKDRSELEALEDQH 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1694 R----------AQEAEQL--LRGPLGDQYQTVKALAErKAQGVLAAQARAEQLRDEArdllqaAQDKLQRL-QELEGTYE 1760
Cdd:pfam12128 332 GafldadietaAADQEQLpsWQSELENLEERLKALTG-KHQDVTAKYNRRRSKIKEQ------NNRDIAGIkDKLAKIRE 404
|
250 260 270
....*....|....*....|....*....|...
gi 530372442 1761 ENERALESKAAQLDGLEARMRSVLQAINLQVQI 1793
Cdd:pfam12128 405 ARDRQLAVAEDDLQALESELREQLEAGKLEFNE 437
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
877-916 |
8.01e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 8.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530372442 877 CVCN--GHADE-CNTHTGACLgCRDHTGGEHCERCIAGFHGDP 916
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1633-1790 |
1.10e-04 |
|
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: 45.79 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1633 RDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALK---------LKRAGNSLAASTAEETagSAQGRAQEAEQLLr 1703
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNrriqlleeeLERTEERLAEALEKLE--EAEKAADESERGR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1704 gplgdqyqtvKALAERKAQG-----VLAAQAR-AEQLRDEARDLLQAAQDKLQRLQ-ELEGTyEENERALESKAAQldgL 1776
Cdd:pfam00261 81 ----------KVLENRALKDeekmeILEAQLKeAKEIAEEADRKYEEVARKLVVVEgDLERA-EERAELAESKIVE---L 146
|
170
....*....|....
gi 530372442 1777 EARMRSVLQaiNLQ 1790
Cdd:pfam00261 147 EEELKVVGN--NLK 158
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1571-1698 |
1.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 46.79 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1571 AILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGA--VADTRDTEQTLYQVQERMAG 1648
Cdd:PRK12472 187 AAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRAdkALAAAKTDEAKARAEERQQK 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530372442 1649 AERAlssAGERARQLDALLEALKLKRAgnslAASTAEETAGSAQGRAQEA 1698
Cdd:PRK12472 267 AAQQ---AAEAATQLDTAKADAEAKRA----AAAATKEAAKAAAAKKAET 309
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
1528-1771 |
1.40e-04 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 46.89 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1528 ADPDSIEMVA-TRVLELSIpasaeqiqhlaGAIAERVrsladVDAILA-RTVGD--VRRAEQLLQDARRArswaedekqk 1603
Cdd:pfam04632 118 ADPEAIFDIAvARVSEISL-----------GILCAAL-----VSALVFpRSVGPalRARLRARLRDALRL---------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1604 aetVQAALEEAQRAQGIAQGAIRgAVADTRDTEQTLYQV---QERMAGAERALSSAgeRARQLDALLEALKLKRAGNSLA 1680
Cdd:pfam04632 172 ---AAAALAGAPGAEAFEAARLR-LAADILALEALRSHAafeSPRGRARARALRRL--LARMLALLPRLRSLARLLARLR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1681 ASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERkaqgVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYE 1760
Cdd:pfam04632 246 TEGAGTVPELAALLDELAAWEAALAAEALQAALAALRAR----LRALRPALPLDFDTAAELLARLADLLAELAEALASCR 321
|
250
....*....|.
gi 530372442 1761 ENERALESKAA 1771
Cdd:pfam04632 322 ALRHPIAQGAR 332
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1476-1777 |
1.62e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1476 RVAETRRQASEAQQR-AQAALDKanasrgqveqanQELQELIQSVKDFLNQEGA---DPDSiemvatrvlelsipasAEQ 1551
Cdd:PRK04863 787 RIEQLRAEREELAERyATLSFDV------------QKLQRLHQAFSRFIGSHLAvafEADP----------------EAE 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1552 IQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWA---EDEK--QKAETVQAALEEAQRA------QGI 1620
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnllADETlaDRVEEIREQLDEAEEAkrfvqqHGN 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1621 AQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQL----------------------DALLEAL--KLKRAg 1676
Cdd:PRK04863 919 ALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALtevvqrrahfsyedaaemlaknSDLNEKLrqRLEQA- 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1677 nSLAASTAEETAGSAQGRAQEAEQL---LRGPLGDQYQTVKALAER-KAQGVLA---AQARAEQLRDEARDLLQAAQdkl 1749
Cdd:PRK04863 998 -EQERTRAREQLRQAQAQLAQYNQVlasLKSSYDAKRQMLQELKQElQDLGVPAdsgAEERARARRDELHARLSANR--- 1073
|
330 340
....*....|....*....|....*...
gi 530372442 1750 QRLQELEGTYEENERALESKAAQLDGLE 1777
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1461-1773 |
1.66e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1461 AELQRALAEGGSILSRVAETRRQasEAQQRAQAALDKANAS-RGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATR 1539
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1540 VLELSIP-ASAEQIQhlagaiAERVRS-LADVDAILARTVGDVRRAEQLLQDARRARswaedeKQKAETVQAALEEAQRA 1617
Cdd:pfam12128 334 FLDADIEtAAADQEQ------LPSWQSeLENLEERLKALTGKHQDVTAKYNRRRSKI------KEQNNRDIAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1618 qgIAQGAIRGAVADTRDTEQTLYQVQERMagaERALSSAGERARQLDALLEALKLKragnsLAASTAEETAGSAQGRAQE 1697
Cdd:pfam12128 402 --IREARDRQLAVAEDDLQALESELREQL---EAGKLEFNEEEYRLKSRLGELKLR-----LNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530372442 1698 AEQLLRGPLGDQYQTVKALAErkaqgvlaAQARAEQLRDEARDLLQAAQdklQRLQELEGTYEENERALESKAAQL 1773
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQS--------ELRQARKRRDQASEALRQAS---RRLEERQSALDELELQLFPQAGTL 536
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1547-1753 |
1.70e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 46.52 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1547 ASAEQIQHLAGAIAERVRSLADVDAILAR---TVGDVRRAEQLLQDARRARSWAEDEKQKAetVQAALEEAqrAQGIAQG 1623
Cdd:pfam13779 407 ALIEQRRRLALDRENRPRVARALDALTLApeeFGPDAGVYLGLRSALARLELARSDEALDE--VADLLWEL--ALRIEDG 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1624 AIRGAVADTRDTEQTLYQVQERMAGAEralssagERARQLDALLEAL-KLKRAgnsLAAstaeetagsaqgRAQEAEQLL 1702
Cdd:pfam13779 483 DLSDAERRLRAAQERLSEALERGASDE-------EIAKLMQELREALdDYMQA---LAE------------QAQQNPQDL 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1703 RGPLGDQYQTV--KALAE--RKAQGvLAAQARaeqlRDEARDLLQAAQDKLQRLQ 1753
Cdd:pfam13779 541 QQPDDPNAQEMtqQDLQRmlDRIEE-LARSGR----RAEAQQMLSQLQQMLENLQ 590
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1444-1628 |
1.80e-04 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 45.42 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1444 GAAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANA--SRGQVEQANQ-------ELQE 1514
Cdd:COG4223 36 TAALEARLAALRAALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAARAAALalAAAALRAAVErgqpfaaELAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1515 LIQSVKDFLNQEGADPDSIEMVATRV-LELSIPASAEQI---QHLAGAIAE-------------RVRSLA-----DVDAI 1572
Cdd:COG4223 116 LEALAPDAPALAALAAFAATGVPTLAaLRAEFPAAARAAlaaARAPEADASwldrllafarslvTVRRVGpvegdDPDAI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1573 LAR-----TVGDVRRA----EQLLQDARRArswAEDEKQKAETVQAALEEAQRAQGIAQGAIRGA 1628
Cdd:COG4223 196 LARaeaalAAGDLAGAlaelEALPEAAQAA---AAPWIAKAEARLAADAALQALAAQALAALGGA 257
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1489-1789 |
2.16e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1489 QRAQAALDKANASRGQVEqANQELQELiQSVKDFLNQEGADPDSIEMVATRVLELS---------IPASAEQIQHLAGAI 1559
Cdd:COG0497 48 GRADASLVRHGADKAEVE-AVFDLSDD-PPLAAWLEENGLDLDDGELILRREISADgrsrafingRPVTLSQLRELGELL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1560 --------------AERVRSLadVDAI--LARTVGDVRRAEQLLQDARRA----RSWAEDEKQKAETVQAALEE------ 1613
Cdd:COG0497 126 vdihgqhehqslldPDAQREL--LDAFagLEELLEEYREAYRAWRALKKEleelRADEAERARELDLLRFQLEEleaaal 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1614 --------AQRAQGIAQGA-IRGAVADTRdteQTLYQ----VQERMAGAERALSSAGERARQLDALLEAlkLKRAGNSL- 1679
Cdd:COG0497 204 qpgeeeelEEERRRLSNAEkLREALQEAL---EALSGgeggALDLLGQALRALERLAEYDPSLAELAER--LESALIELe 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1680 -AASTAEETAGSAQ---GRAQEAEQLLrgplgdqyQTVKALAeRK----AQGVLAaqaraeqLRDEARDLLQAAQDKLQR 1751
Cdd:COG0497 279 eAASELRRYLDSLEfdpERLEEVEERL--------ALLRRLA-RKygvtVEELLA-------YAEELRAELAELENSDER 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 530372442 1752 LQELEGTYEENERALESKAAQL--------DGLEARMRSVLQAINL 1789
Cdd:COG0497 343 LEELEAELAEAEAELLEAAEKLsaarkkaaKKLEKAVTAELADLGM 388
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1691-1793 |
2.39e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1691 AQGRAQEAEQLLRGpLGDQYQTVKALAERKAQgVLAAQARAEQLRDEARDLLQAAQDKL---QRLQELEGTYEENERALE 1767
Cdd:COG1566 88 AEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQ-LAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDAAQAQLE 165
|
90 100
....*....|....*....|....*.
gi 530372442 1768 SKAAQLDGLEARMRSVLQAINLQVQI 1793
Cdd:COG1566 166 AAQAQLAQAQAGLREEEELAAAQAQV 191
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1487-1755 |
2.41e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 46.13 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1487 AQQRAQAALDKANASRgqVEQANQELqeLIQSvkdflnqEGADPDSIEMVATRVL--ELSIPASAEQIQHLAGAIAERVR 1564
Cdd:pfam13779 409 IEQRRRLALDRENRPR--VARALDAL--TLAP-------EEFGPDAGVYLGLRSAlaRLELARSDEALDEVADLLWELAL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1565 SLADvdailartvGDVRRAEQLLQDARRA-----RSWAEDE--KQKAETVQAALEE-----AQRAQGIAQGAIRGA---- 1628
Cdd:pfam13779 478 RIED---------GDLSDAERRLRAAQERlsealERGASDEeiAKLMQELREALDDymqalAEQAQQNPQDLQQPDdpna 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1629 -VADTRDTEQTLYQVQE-----RMAGAERALSsagerarQLDALLEALKLKRAGNSLAASTAE---------ETAGSAQG 1693
Cdd:pfam13779 549 qEMTQQDLQRMLDRIEElarsgRRAEAQQMLS-------QLQQMLENLQAGQPQQQQQQGQSEmqqamdelgDLLREQQQ 621
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1694 -------RAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQEL 1755
Cdd:pfam13779 622 lldetfrQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEEL 690
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1609-1786 |
2.47e-04 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 44.65 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1609 AALEEAQRAQGiAQGAIRGAVADTRDT--EQTLYQVQERMAGAERALSSAGERARQLDAllEALKLKRAGNSLAASTAEE 1686
Cdd:COG4223 24 AALEAAPAAAA-ATAALEARLAALRAAlaAAREAVAAAAAAALEARLAALEAKAAAPEA--EAAAAARAAALALAAAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1687 TAgSAQGRAQEAE-QLLRGPLGDQyQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAqdklqrlqelegtyeeneRA 1765
Cdd:COG4223 101 AA-VERGQPFAAElAALEALAPDA-PALAALAAFAATGVPTLAALRAEFPAAARAALAAA------------------RA 160
|
170 180
....*....|....*....|.
gi 530372442 1766 LESKAAQLDGLEARMRSVLQA 1786
Cdd:COG4223 161 PEADASWLDRLLAFARSLVTV 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1449-1599 |
2.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAA---LDKANASRGQVEQANQELQELIQSVKDFLNQ 1525
Cdd:COG4913 659 DEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELeeeLDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1526 --EGADPDSIEMVATRVLELSIPASAEQIQHlagAIAERVRSLAdvdailartvGDVRRAEQLLQDARRA--RSWAED 1599
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE---NLEERIDALR----------ARLNRAEEELERAMRAfnREWPAE 803
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1637-1788 |
3.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1637 QTLYQVQERmagaERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLrgplgdqyQTVKAL 1716
Cdd:COG1579 7 RALLDLQEL----DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------EEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1717 AER--KAQGVL--------------AAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARM 1780
Cdd:COG1579 75 IKKyeEQLGNVrnnkeyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*...
gi 530372442 1781 RSVLQAIN 1788
Cdd:COG1579 155 EAELEELE 162
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1452-1670 |
3.21e-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: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQ----AELQRALAEGGSILsRVAETRRQASEAQQRAQAALDKAnasrgQVEQANQELQEliqsVKDFLNQEG 1527
Cdd:COG2268 188 ALGRRKIAEiirdARIAEAEAERETEI-AIAQANREAEEAELEQEREIETA-----RIAEAEAELAK----KKAEERREA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1528 adpDSIEMVATRVLELsipASAEQIQHLAGAIaERVRSLADVDAILARtvgdVRRAEQLLQDARRARswAEDEKQKAETV 1607
Cdd:COG2268 258 ---ETARAEAEAAYEI---AEANAEREVQRQL-EIAEREREIELQEKE----AEREEAELEADVRKP--AEAEKQAAEAE 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530372442 1608 QAALEEAQRAQGIAQGairgavadtrdteqtlyQVQERMAGAERALSSAGErarqLDALLEAL 1670
Cdd:COG2268 325 AEAEAEAIRAKGLAEA-----------------EGKRALAEAWNKLGDAAI----LLMLIEKL 366
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1450-1614 |
3.34e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1450 DLALGRARHTQAELQRALAEggsILSRVAETRRQASEAQQRAQAALDKANASRGQVEQAN------QELQELIQSVKDF- 1522
Cdd:COG1579 16 DSELDRLEHRLKELPAELAE---LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyEEQLGNVRNNKEYe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1523 -LNQEgadpdsIEMVATRVLELSipasaEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARrarswAEDEK 1601
Cdd:COG1579 93 aLQKE------IESLKRRISDLE-----DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL-----AELEA 156
|
170
....*....|...
gi 530372442 1602 QKAEtVQAALEEA 1614
Cdd:COG1579 157 ELEE-LEAEREEL 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1599-1792 |
3.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1599 DEKQKAETVQAALEEAQRAQGIaqgaiRGAVADTRDTEQTLyqvqERMAGAERALSSAGERARQLDALLEALKLKRAgns 1678
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA-----HEALEDAREQIELL----EPIRELAERYAAARERLAELEYLRAALRLWFA--- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1679 laastaeetagsaQGRAQEAEQLLRGpLGDQYQTVKALAERKAQGVLAAQARAEQLRDEAR----DLLQAAQDKLQRLQE 1754
Cdd:COG4913 287 -------------QRRLELLEAELEE-LRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLER 352
|
170 180 190
....*....|....*....|....*....|....*...
gi 530372442 1755 LEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQ 1792
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1453-1541 |
3.92e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 42.99 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1453 LGRA-RHTQAELQRALAEGGSILSRvAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLnqegadPD 1531
Cdd:PRK14473 58 LANAkRDYEAELAKARQEAAKIVAQ-AQERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQI------AD 130
|
90
....*....|
gi 530372442 1532 SIEMVATRVL 1541
Cdd:PRK14473 131 LVTLTASRVL 140
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1547-1774 |
6.42e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1547 ASAEQIQHLagaiaervRSLADVDAILARTVGDVRRAEQLLQDARRARswaEDEKQKAETVQAALEEAQRAQGIAQGAIR 1626
Cdd:COG1579 1 AMPEDLRAL--------LDLQELDSELDRLEHRLKELPAELAELEDEL---AALEARLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1627 gavadtrdteqtlyQVQERMAGAERALSSAGErARQLDAL---LEALKLKRagnslaaSTAEETAGSAQGRAQEAEqllr 1703
Cdd:COG1579 70 --------------EVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRI-------SDLEDEILELMERIEELE---- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530372442 1704 gplgdqyqtvkalaerkaqgvlAAQARAEQLRDEARDLLQAAQDKLQ-RLQELEGTYEENERALESKAAQLD 1774
Cdd:COG1579 124 ----------------------EELAELEAELAELEAELEEKKAELDeELAELEAELEELEAEREELAAKIP 173
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1488-1779 |
6.44e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 44.28 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1488 QQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQ--EGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRS 1565
Cdd:pfam15070 28 QQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQaaVPPAEEEQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1566 LADVDAILARTVgdvrrAEQ---LLQDARRARSW---AEDEKQKAETVQaaleeAQRAqgiaqgAIRGAVADTRDTEQTL 1639
Cdd:pfam15070 108 QVQDNEQLSRLN-----QEQeqrLLELERAAERWgeqAEDRKQILEDMQ-----SDRA------TISRALSQNRELKEQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1640 YQVQE---RMAGAERALSSA--------GERARQLDALLEAL-KLKRagnslaasTAEETAGSAQGRAQEAEQLL----- 1702
Cdd:pfam15070 172 AELQNgfvKLTNENMELTSAlqseqhvkKELAKKLGQLQEELgELKE--------TLELKSQEAQSLQEQRDQYLahlqq 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1703 -----------RGPLGDQY----QTVKALAERKAQGVLAAQARAEQLRdEARDLLQAAQDKLQRLQ--------ELEG-- 1757
Cdd:pfam15070 244 yvaayqqlaseKEELHKQYllqtQLMDRLQHEEVQGKVAAEMARQELQ-ETQERLEALTQQNQQLQaqlsllanPGEGdg 322
|
330 340
....*....|....*....|....
gi 530372442 1758 --TYEENERALESKAAQLDGLEAR 1779
Cdd:pfam15070 323 leSEEEEEEAPRPSLSIPEDFESR 346
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1680-1792 |
6.73e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 42.23 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1680 AASTAEETAGSAQGRAqEAEQLLrgplgDQYQTVKALAERKAQGVL-AAQARAEQLRDEARDLLQAAQDKLQRLQELEGT 1758
Cdd:PRK14475 43 AAKIQAELDEAQRLRE-EAQALL-----ADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERKIA 116
|
90 100 110
....*....|....*....|....*....|....
gi 530372442 1759 YEENERALESKAAQLDgLEARMRSVLQAINLQVQ 1792
Cdd:PRK14475 117 QAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1582-1617 |
7.65e-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: 40.36 E-value: 7.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530372442 1582 RAEQLLQDARRARSWAEDEKQKAE----TVQAALEEAQRA 1617
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1202-1377 |
8.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1202 QDLAARTQRLEQRAQELQQTG--------VLGAfeSSFwhmQEKLGIVQgivgARNTSAASTAQLVEATEELRREIGEAT 1273
Cdd:COG3883 79 AEIEERREELGERARALYRSGgsvsyldvLLGS--ESF---SDFLDRLS----ALSKIADADADLLEELKADKAELEAKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1274 EHLTQLEADLTDVQDEnfnANHALSGLERDRLALNLTLRQLDQHLDLLKhsnflgayDSIRHAHSQSAEAERRANTSALA 1353
Cdd:COG3883 150 AELEAKLAELEALKAE---LEAAKAELEAQQAEQEALLAQLSAEEAAAE--------AQLAELEAELAAAEAAAAAAAAA 218
|
170 180
....*....|....*....|....
gi 530372442 1354 VPSPVSNSASARHRTEALMDAQKE 1377
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1644-1784 |
8.89e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1644 ERMAGAERALSSAGeraRQLDALLEALKLKRAGN-SLAASTAEETAGsaqGRAQEAEQ-LLRGpLGDQYQTVKALAERKA 1721
Cdd:PRK09039 46 REISGKDSALDRLN---SQIAELADLLSLERQGNqDLQDSVANLRAS---LSAAEAERsRLQA-LLAELAGAGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 1722 QGVLAAQARAEQLRDEAR---DLLQAAQDKLQR-LQELEGTYEENERALESKAAQLDGLEARMRSVL 1784
Cdd:PRK09039 119 GELAQELDSEKQVSARALaqvELLNQQIAALRRqLAALEAALDASEKRDRESQAKIADLGRRLNVAL 185
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1648-1744 |
9.02e-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: 40.50 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1648 GAERALSSAGERARQLDALLE-ALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQ-GVL 1725
Cdd:pfam16999 2 VSSRLLSELAEREAALDQQIEaARKEAEREVEAAEAEAARILREAEAKAKALQAEYRQELAAETARIREEARARAEaEAQ 81
|
90 100
....*....|....*....|
gi 530372442 1726 AAQARAEQ-LRDEARDLLQA 1744
Cdd:pfam16999 82 AVRTRAEGrLQQAVELILRA 101
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1452-1613 |
9.19e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1452 ALGRARHTQAELQRALAEggsilsrvaeTRRQASEAQQRAQAALDKANasrgqvEQANQELQELIQSVKDFlnqegadpd 1531
Cdd:COG0711 39 GLAEAERAKEEAEAALAE----------YEEKLAEARAEAAEIIAEAR------KEAEAIAEEAKAEAEAE--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1532 siemvATRVLElsipASAEQIQhlagaiAERVRSLADVDAILARTVgdVRRAEQLLQDArrarswAEDEKQKAeTVQAAL 1611
Cdd:COG0711 94 -----AERIIA----QAEAEIE------QERAKALAELRAEVADLA--VAIAEKILGKE------LDAAAQAA-LVDRFI 149
|
..
gi 530372442 1612 EE 1613
Cdd:COG0711 150 AE 151
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1581-1622 |
9.28e-04 |
|
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: 39.28 E-value: 9.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530372442 1581 RRAEQLLQDARRARSWAEDEKQKA----ETVQAALEEAQRAQGIAQ 1622
Cdd:pfam11839 8 SKADQAEQDAAAAQSAADSAKAKAdeaaARANAAEAAAEEAQQAAE 53
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1451-1703 |
1.09e-03 |
|
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: 42.79 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1451 LALGRARHTQAELQRALAeggsILSRVAETRRQASEAQQ-------------RAQAALDKANASRGQVEQANQELQELIQ 1517
Cdd:COG2956 46 LALGNLYRRRGEYDRAIR----IHQKLLERDPDRAEALLelaqdylkaglldRAEELLEKLLELDPDDAEALRLLAEIYE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1518 SVKDFlnqegadPDSIEmVATRVLELSiPASAeQIQHLAGAIAERvrsladvdailartVGDVRRAEQLLQDARRARswa 1597
Cdd:COG2956 122 QEGDW-------EKAIE-VLERLLKLG-PENA-HAYCELAELYLE--------------QGDYDEAIEALEKALKLD--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1598 edekQKAETVQAALEEAQRAQGIAQGAIRgAVADTRDTEQTLYQVQERMAGAERALssaGERARQLDALLEALKLKrAGN 1677
Cdd:COG2956 175 ----PDCARALLLLAELYLEQGDYEEAIA-ALERALEQDPDYLPALPRLAELYEKL---GDPEEALELLRKALELD-PSD 245
|
250 260
....*....|....*....|....*.
gi 530372442 1678 SLAASTAEETAgsAQGRAQEAEQLLR 1703
Cdd:COG2956 246 DLLLALADLLE--RKEGLEAALALLE 269
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1449-1739 |
1.14e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1449 ADLALGRARHTQAElqRALAEGGSILSRVAETRRQASEAQQRAQAALDKAN-------ASRgqVEQANQELQELiQSVKD 1521
Cdd:PRK04863 837 AELRQLNRRRVELE--RALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetlADR--VEEIREQLDEA-EEAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1522 FLNQEGA--------------DPDSIEMVATRVLElsipasAEQIQHLAgaiAERVRSLADVDA------------ILAR 1575
Cdd:PRK04863 912 FVQQHGNalaqlepivsvlqsDPEQFEQLKQDYQQ------AQQTQRDA---KQQAFALTEVVQrrahfsyedaaeMLAK 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1576 TVG-------DVRRAEQLLQDARRARSWAEDEKQKAETVQAAL------------EEAQRAQGI----AQGAIRGAVADT 1632
Cdd:PRK04863 983 NSDlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLkssydakrqmlqELKQELQDLgvpaDSGAEERARARR 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1633 RDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKragnslaASTAEETAGSAQGRAQEAEQLLR-----GPL- 1706
Cdd:PRK04863 1063 DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD-------YHEMREQVVNAKAGWCAVLRLVKdngveRRLh 1135
|
330 340 350
....*....|....*....|....*....|....*...
gi 530372442 1707 --GDQYQTVKALAER--KAQGVLA-AQARAEQLRDEAR 1739
Cdd:PRK04863 1136 rrELAYLSADELRSMsdKALGALRlAVADNEHLRDVLR 1173
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
306-338 |
1.15e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|...
gi 530372442 306 VHGACICKHNTRGLNCEQCQDFYRDLPWRPAED 338
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1445-1751 |
1.16e-03 |
|
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: 42.79 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1445 AAATADLALGRARHTQAELQRALAEggsiLSRVAETRRQASEAQqraqAALDKANASRGQVEQANQELQELIQS------ 1518
Cdd:COG2956 6 AAALGWYFKGLNYLLNGQPDKAIDL----LEEALELDPETVEAH----LALGNLYRRRGEYDRAIRIHQKLLERdpdrae 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1519 -----VKDFLNQEgaDPDSIEMVATRVLELSiPASAEQIQHLAgAIAERVRSLAdvDAILArtvgdvrrAEQLLQDA-RR 1592
Cdd:COG2956 78 allelAQDYLKAG--LLDRAEELLEKLLELD-PDDAEALRLLA-EIYEQEGDWE--KAIEV--------LERLLKLGpEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1593 ARSWAE--DEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRdteqtLYQVQERMAGAERALSSAGERARQLDALLEAL 1670
Cdd:COG2956 144 AHAYCElaELYLEQGDYDEAIEALEKALKLDPDCARALLLLAE-----LYLEQGDYEEAIAALERALEQDPDYLPALPRL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1671 klkragnslaastaeETAGSAQGRAQEAEQLLRgplgdqyqtvKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQ 1750
Cdd:COG2956 219 ---------------AELYEKLGDPEEALELLR----------KALELDPSDDLLLALADLLERKEGLEAALALLERQLR 273
|
.
gi 530372442 1751 R 1751
Cdd:COG2956 274 R 274
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1447-1670 |
1.34e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 43.64 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1447 ATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQE 1526
Cdd:COG2203 1 LLSVLALALAREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1527 GADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARtvgdvRRAEQLLQDARRARSWAEDEKQKAET 1606
Cdd:COG2203 81 IDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARL-----LDLLLLGLGGRLRGVVLRGLRSAALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1607 VQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEAL 1670
Cdd:COG2203 156 LSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELA 219
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
1533-1681 |
1.38e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 43.05 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1533 IEMVATRVLELSI--PASAEQIQHLAG-AIAERVRSLAD-VDAILARTVGDVRRAEQLLQDArrarswaeDEKQKAETVQ 1608
Cdd:PRK12402 169 IPPIRSRCLPLFFraPTDDELVDVLESiAEAEGVDYDDDgLELIAYYAGGDLRKAILTLQTA--------ALAAGEITME 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1609 AALEEAQR------AQGIAQGAIRGAVADTRDTEQTLyQVQERMAGAEralssagerarQLDALLEALKLKRAGNSLAA 1681
Cdd:PRK12402 241 AAYEALGDvgtdevIESLLDAAEAGDFTDARKTLDDL-LIDEGLSGGE-----------VLEELLRVARSRYRGDNLAR 307
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1561-1781 |
1.60e-03 |
|
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: 42.60 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1561 ERVRSL------ADVDAILARTVGDV-RRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQgiaqgAIRGAvadtr 1633
Cdd:pfam13868 6 DELRELnskllaAKCNKERDAQIAEKkRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE-----RKRYR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1634 dteQTLY-QVQERmagaeralssagERARQLDA---LLEALKLKRAgnsLAASTAEETAgSAQGRAQEAEQLLRgplgDQ 1709
Cdd:pfam13868 76 ---QELEeQIEER------------EQKRQEEYeekLQEREQMDEI---VERIQEEDQA-EAEEKLEKQRQLRE----EI 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530372442 1710 YQTVKALAERKAQgvlaaqaRAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMR 1781
Cdd:pfam13868 133 DEFNEEQAEWKEL-------EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1551-1731 |
1.68e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1551 QIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEkqkAETVQAALEEAQRAQGIAQGA------ 1624
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGNVRNNkeyeal 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1625 ---IRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAgNSLAASTAEETAgsAQGRAQEAEQL 1701
Cdd:COG1579 95 qkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEE--LEAEREELAAK 171
|
170 180 190
....*....|....*....|....*....|
gi 530372442 1702 LRGPLGDQYQTVKalAERKAQGVLAAQARA 1731
Cdd:COG1579 172 IPPELLALYERIR--KRKNGLAVVPVEGGA 199
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
347-400 |
1.92e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530372442 347 CECHG---HTHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 400
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1462-1563 |
2.44e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.93 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1462 ELQRALAEGGSILSRV-AETRRQASEAQQRAQAALD--KANASRGQVEQANQELQELIQSVKDFLNqegadpDSIEMVAT 1538
Cdd:PRK06669 82 ELLKKTDEASSIIEKLqMQIEREQEEWEEELERLIEeaKAEGYEEGYEKGREEGLEEVRELIEQLN------KIIEKLIK 155
|
90 100
....*....|....*....|....*
gi 530372442 1539 RVLELsIPASAEQIQHLAGAIAERV 1563
Cdd:PRK06669 156 KREEI-LESSEEEIVELALDIAKKV 179
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1465-1578 |
2.49e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 42.70 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1465 RALAE-----GGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDF--LNQEGADP-----DS 1532
Cdd:COG0840 406 RKLAErsaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVsdLIQEIAAAseeqsAG 485
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530372442 1533 IEMVATRVLELSipASAEQIQHLAGAIAERVRSLADVDAILARTVG 1578
Cdd:COG0840 486 TEEVNQAIEQIA--AAAQENAASVEEVAAAAEELAELAEELQELVS 529
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1548-1791 |
2.53e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1548 SAEQIQHLAGAIAERvRSLADVDAILartVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRaqGIAQ-GAIR 1626
Cdd:PRK11281 37 TEADVQAQLDALNKQ-KLLEAEDKLV---QQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA--ELEAlKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1627 GAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALK--LKRAGNSLAAstaeetagsAQGRAQEAEQLLRG 1704
Cdd:PRK11281 111 DEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQtqPERAQAALYA---------NSQRLQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1705 PLGDQY-----QTVKALAERKAQGVLAAQARAE-----QLRD---EARDLLQAAQDKLQR----LQEL---------EGT 1758
Cdd:PRK11281 182 GKVGGKalrpsQRVLLQAEQALLNAQNDLQRKSlegntQLQDllqKQRDYLTARIQRLEHqlqlLQEAinskrltlsEKT 261
|
250 260 270
....*....|....*....|....*....|...
gi 530372442 1759 YEENERALESKAAQLDGLEARMrsvlQAINLQV 1791
Cdd:PRK11281 262 VQEAQSQDEAARIQANPLVAQE----LEINLQL 290
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1565-1744 |
2.70e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1565 SLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQ---------GAIRGAVADTRDT 1635
Cdd:pfam00529 66 QLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarrrvlAPIGGISRESLVT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1636 EQTLY-QVQERMAGAERALSSAGERARQLDA-LLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEqlLRGPL-GdqyqT 1712
Cdd:pfam00529 146 AGALVaQAQANLLATVAQLDQIYVQITQSAAeNQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE--IRAPVdG----T 219
|
170 180 190
....*....|....*....|....*....|..
gi 530372442 1713 VKALAERKAQGVLAAQARAEQLRDEARDLLQA 1744
Cdd:pfam00529 220 VAFLSVTVDGGTVSAGLRLMFVVPEDNLLVPG 251
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
905-984 |
2.78e-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: 40.07 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 905 CERCIAGFHGDPRLPYGgqCRPC-PCPEGPGSQRHFATSCHQDEysqqiVCHCRAGYT-------GLRCEACAPGHFGDP 976
Cdd:cd13406 36 CSPCEPGFYNEAVNYEP--CKPCtQCNQRSGSEEKQKCTKTSDT-----VCRCRPGTQpldsykpGVDCVPCPPGHFSRG 108
|
....*...
gi 530372442 977 SrpGGRCQ 984
Cdd:cd13406 109 D--NQACK 114
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
1602-1737 |
2.89e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 39.57 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1602 QKAETvqaALEEAQRAQGIAQGAIRGAvadtrdtEQTLYQVQERMAGAERALSSAGERARQ--LDALLEALKLKRagNSL 1679
Cdd:pfam02050 1 DEAAR---ELAEAQRELQQAEEKLEEL-------QQYRAEYQQQLSGAGQGISAAELRNYQafISQLDEAIAQQQ--QEL 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1680 AASTAEETAgsAQGRAQEAEQllrgplgdQYQTVKALAERKAQGVLAAQARAEQLR-DE 1737
Cdd:pfam02050 69 AQAEAQVEK--AREEWQEARQ--------ERKSLEKLREREKKEERKEQNRREQKQlDE 117
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1444-1512 |
2.95e-03 |
|
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: 38.43 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530372442 1444 GAAATADLAlgRARHTQAELQRALAeggSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQEL 1512
Cdd:NF040598 17 GCATTSDLE--NLQSQVQELDAKVD---QASSDAAAAQSRADEAAAKAEQAEAAANAAQQEADEANERA 80
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1692-1785 |
3.27e-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: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1692 QGRAQEAEQLLrgplgdqyQTVKALAErKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKaa 1771
Cdd:cd16269 177 QSKEAEAEAIL--------QADQALTE-KEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK-- 245
|
90
....*....|....
gi 530372442 1772 qldgLEARMRSVLQ 1785
Cdd:cd16269 246 ----MEEERENLLK 255
|
|
| DUF6781 |
pfam20572 |
Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. ... |
1583-1751 |
3.45e-03 |
|
Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 223 and 298 amino acids in length.
Pssm-ID: 466721 Cd Length: 213 Bit Score: 40.71 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1583 AEQLLQDARRARSWAEDEKQKA--ETVQAALEEA--------QRAQGIAQGAIRGA-VADTRDTEQTLYQVqerMAGAER 1651
Cdd:pfam20572 8 QDALIDEFSQAVAGQGEALREAvrDATLRALQGReltlknirQVLKAVTEGASQGAnAARGGEVEALLKQA---VAGLDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1652 ALSSAGErARQLdALLEALK---------LKRAGNSLAA--STAEETAGSAqgrAQEAEQLLRGPLGD------------ 1708
Cdd:pfam20572 85 ALLKAAE-ASRL-ALEEAVDqgaafseqdLKKALDDLEKleDTFFDTLRKA---AKSAGGPLKGPWGDlldhlkrsgtdt 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1709 -----------QYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQR 1751
Cdd:pfam20572 160 gaqaraaveqlAAQLQAALREGRAAGSRAARALADSYAALASGVLIGLSEALQP 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1649-1793 |
3.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1649 AERAlssagERARQLDALLEALKLKRAGNSLAAstaeetagsAQGRAQEAEQLLrgplgdqyqtvkALAERKAQGVLAAQ 1728
Cdd:COG1196 209 AEKA-----ERYRELKEELKELEAELLLLKLRE---------LEAELEELEAEL------------EELEAELEELEAEL 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530372442 1729 ARAEQLRDEARDLLQAAQDKLQRLQelegtyeENERALESKAAQLDglEARMRSVLQAINLQVQI 1793
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLE--QDIARLEERRRELEERL 318
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1696-1787 |
3.95e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.32 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1696 QEAEQLLRgplgdqyQTVKALAErkAQGVLA-AQARAEQLRDEARDLLQAAqdklqRLQELEGTYEENERALESKAAQLD 1774
Cdd:PRK07352 60 KEAEERLR-------QAAQALAE--AQQKLAqAQQEAERIRADAKARAEAI-----RAEIEKQAIEDMARLKQTAAADLS 125
|
90
....*....|....*....
gi 530372442 1775 GLEARM------RSVLQAI 1787
Cdd:PRK07352 126 AEQERViaqlrrEAAELAI 144
|
|
| 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 ... |
1476-1588 |
4.39e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1476 RVAETRRQASEAQQRAQAALDKAnasRGQVEQANQELQELIQSVKDFLNQEGADpdsiemvatrvLELSIPASAEQIQHL 1555
Cdd:pfam00430 34 LIADEIAEAEERRKDAAAALAEA---EQQLKEARAEAQEIIENAKKRAEKLKEE-----------IVAAAEAEAERIIEQ 99
|
90 100 110
....*....|....*....|....*....|....*..
gi 530372442 1556 AGA--IAERVRSLADvdaiLARTVGD--VRRAEQLLQ 1588
Cdd:pfam00430 100 AAAeiEQEKDRALAE----LRQQVVAlaVQIAEKLLE 132
|
|
| DUF3375 |
pfam11855 |
Protein of unknown function (DUF3375); This family of proteins are functionally ... |
1472-1790 |
4.61e-03 |
|
Protein of unknown function (DUF3375); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 479 to 499 amino acids in length.
Pssm-ID: 463373 Cd Length: 469 Bit Score: 41.47 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1472 SILSRV--AETRR-QASEAQQRAQAALDKANASRGQVE---QANQELQELIQS--VKDFLNQEGADPdsiemvatrVLEL 1543
Cdd:pfam11855 22 AFLRRVfdEGNRRvPAEDLHERLEDDLEELREEEGEEAlpqSARDYLRDWAKEgwLRRRYDPGSDEE---------VYEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1544 SiPASAEQIQHLAGA--------------IAERVRSLA---DVDAilartvgDVRRAEqlLQdARRARSWAEDEKQKAET 1606
Cdd:pfam11855 93 T-PAAEKALRFVARLderrfvatesrlntVFDALRQLAegtEPDP-------EERLAE--LE-AEIAEIDAEIDRLRAGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1607 VQAALEEAQ--RAQGIAQGAiRGAVADTRDTEQTLYQ----VQERMAGAERalsSAGERarqLDALLEAlklkragnsla 1680
Cdd:pfam11855 162 VPELDDTQAleRAREILQLA-RELPADFRRVEDEFRQldreLRERIIDWDG---SRGEV---LEELFDG----------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1681 astAEETAGSAQGRAQEA-EQLLRGP-----LGDQYQTVkaLAERKAQGVLAAQARaeQLRDEARDLLQAAQDKLQRLQE 1754
Cdd:pfam11855 224 ---YDALADSDQGRSFEAfWDLLMDPerqaeLDELLDTV--LSRPFARGLDADQRR--FLRRLHRDLLEAGEEVQRTRRR 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530372442 1755 LE---------GTYEENERALEskaaQLDGLEARMRSVLQAINLQ 1790
Cdd:pfam11855 297 LSrslrrfvrsQAFLEDRRVDR----LLREAEALALALRDAPPAD 337
|
|
| 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 ... |
1627-1750 |
4.88e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1627 GAVADTRDT--EQTLYQVQERMAGAERALSSAgeRARQLDALLEALKLKRAGNSLAASTAEETAGSAqgrAQEAEQLLrg 1704
Cdd:pfam00430 25 GKVLDKRREliADEIAEAEERRKDAAAALAEA--EQQLKEARAEAQEIIENAKKRAEKLKEEIVAAA---EAEAERII-- 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530372442 1705 plgdqyqtvkalaERKAQGVLAAQARA-EQLRDEARDL-LQAAQDKLQ 1750
Cdd:pfam00430 98 -------------EQAAAEIEQEKDRAlAELRQQVVALaVQIAEKLLE 132
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
1658-1789 |
4.96e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 39.27 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1658 ERARQLDALLEALKLKRA------GNSLAASTAEETAGSAQGRAQEAEQLlrgplgdqyQTVKALAERKAQGVLAAQARA 1731
Cdd:pfam05130 9 EELELLEELLELLEEEQEalkagdIEALEELTEEKQELLQKLAQLEKERR---------ELLAELGLSPEEATLSELLAK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1732 EQLRDEARDLLQAAQDKLQRLQELEgtyEENERAleskaaqldgLEARMRSVLQAINL 1789
Cdd:pfam05130 80 EEEDPELRELWQELLELLERLKELN---ELNGEL----------IEQSLEFNNRSLNI 124
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1583-1794 |
4.99e-03 |
|
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: 41.06 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1583 AEQLLQDARRARswAEDEK---QKAETVQAALEEAQRAQgiaqgairgavadtrdTEQTLYQVQERMAgAERALSSAGER 1659
Cdd:pfam13868 100 REQMDEIVERIQ--EEDQAeaeEKLEKQRQLREEIDEFN----------------EEQAEWKELEKEE-EREEDERILEY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1660 ARQLDALLEALKLKRAGNSLAastaeetagsaqgRAQEAEQLLRgplgDQYQTVKALAERKAqgVLAAQARAEQLRDEAR 1739
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEE-------------KEREIARLRA----QQEKAQDEKAERDE--LRAKLYQEEQERKERQ 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1740 DLLQAAQDKLQRLQELEGTYEE---NERALESKAAQLDglEARMRSVLQAINLQVQIY 1794
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEqieLKERRLAEEAERE--EEEFERMLRKQAEDEEIE 277
|
|
| DUF4398 |
pfam14346 |
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. ... |
1443-1508 |
5.31e-03 |
|
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: 37.62 E-value: 5.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530372442 1443 NGAAATADLALGRARHTQAELQRALAEGgsilsRVAETRRQASEAQQRAQAALDKANA--SRGQVEQA 1508
Cdd:pfam14346 16 DGAAQYAPLELKRARDALAKAEAAMAEK-----DYEKARHLAYLAEADAELAEAKARAakAEAAAAQA 78
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1461-1514 |
5.72e-03 |
|
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: 36.97 E-value: 5.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530372442 1461 AELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQE 1514
Cdd:pfam11839 1 AQVEELQSKADQAEQDAAAAQSAADSAKAKADEAAARANAAEAAAEEAQQAAEE 54
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1525-1789 |
8.17e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.00 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1525 QEGADPDSI-EMVATRVLELSipasAEQIQHL-AGAIAERVRSLADVDAILARTVGDVRRAeqlLQDARRARSWAEDEKQ 1602
Cdd:COG3899 568 AALALPDTVvDLLAARLDRLP----PAARRVLrLAAVLGRRFDLELLAAVLGLSEAELAAA---LEELVAAGLLVPRGDA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1603 KAETV--------QAALE---EAQRAQG---IAQgAIRGAVADTRDTEQT-----LYQVQERmAGAERALSSAGERARQL 1663
Cdd:COG3899 641 GGGRYrfrhdlvrEAAYAslpPEERRALhrrIAR-ALEARGPEPLEERLFelahhLNRAGER-DRAARLLLRAARRALAR 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1664 DALLEALK-LKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPlgdqyqtvkALAERKAQGVLAAQARAEQLRDEARDLL 1742
Cdd:COG3899 719 GAYAEALRyLERALELLPPDPEEEYRLALLLELAEALYLAGRF---------EEAEALLERALAARALAALAALRHGNPP 789
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 530372442 1743 QAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINL 1789
Cdd:COG3899 790 ASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNL 836
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1711-1782 |
8.27e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1711 QTVKA---LAE---RKAQGVLAaQARAEQLRDEARdlLQAAQDKLQRLQEL-------EGTYEENERALESKAAQLDGLE 1777
Cdd:COG0845 43 DRVKKgqvLARldpPDLQAALA-QAQAQLAAAQAQ--LELAKAELERYKALlkkgavsQQELDQAKAALDQAQAALAAAQ 119
|
....*
gi 530372442 1778 ARMRS 1782
Cdd:COG0845 120 AALEQ 124
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1504-1754 |
8.80e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1504 QVEQANQELQELIQSVKDFLNQE--GADPDSIEMVATR--VLELSIPASAEQIQHLAgAIAERVRSLADVDA-ILARTVG 1578
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTdyGDDLESVEALLKKheALEAELAAHEERVEALN-ELGEQLIEEGHPDAeEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1579 DVRRAEQLLQdarrarswaedekQKAETVQAALEEAQRAQGIAQgairgavaDTRDTEQtlyqvqeRMAGAERALSS--A 1656
Cdd:cd00176 83 ELNQRWEELR-------------ELAEERRQRLEEALDLQQFFR--------DADDLEQ-------WLEEKEAALASedL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530372442 1657 GERARQLDALLEALKlkragnslaasTAEETAGSAQGRAQEAEQLlrgplGDQYqtvkaLAERKAQGVLAAQARAEQLRD 1736
Cdd:cd00176 135 GKDLESVEELLKKHK-----------ELEEELEAHEPRLKSLNEL-----AEEL-----LEEGHPDADEEIEEKLEELNE 193
|
250
....*....|....*...
gi 530372442 1737 EARDLLQAAQDKLQRLQE 1754
Cdd:cd00176 194 RWEELLELAEERQKKLEE 211
|
|
| |
