|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
20-248 |
9.68e-84 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 272.31 E-value: 9.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 20 ACSRGACYPPVGDLLVGRtrFLRASSTCGLTKPETYCTQ--YGEWQMKCCKCDSRQPHnyYSHRVENVASSSGP--MRWW 95
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNPR--RSHPAENLTDGNNPnnPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 96 QSQNDVNP---VSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSsDFGKTWRVYQYLAADCTSTFPRVRQGRPQS--WQD 170
Cdd:smart00136 77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITKgnEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 171 VRCQSLPQRPNaRLNGGKVQLNLMDLVSGIP-ATQSQKIQEVGEITNLRVNFTRLAPVPQRGYH-----PPSAYYAVSQL 244
Cdd:smart00136 156 VICTSEYSDIV-PLEGGEIAFSLLEGRPSATdFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDdrpevTRRYYYAISDI 234
|
....
gi 189083719 245 RLQG 248
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
26-248 |
3.14e-58 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 200.50 E-value: 3.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 26 CYPPVGDLLVGRTrfLRASSTCGLTKPETYCTQygEWQM---KCCKCDSRQPHNyySHRVENVASSSG--PMRWWQSQND 100
Cdd:pfam00055 1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCIL--SGLEggkKCFICDSRDPHN--SHPPSNLTDSNNgtNETWWQSETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 101 VNP---VSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSW-QDVRC--- 173
Cdd:pfam00055 75 VIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVICtse 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 174 QSLPqRPnarLNGGKVQLNLMDLVSGIP-ATQSQKIQEVGEITNLRVNFTRLA--PVPQRGYHP--PSAYYAVSQLRLQG 248
Cdd:pfam00055 155 YSDI-SP---LTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtlGDELLDDPSvlRKYYYAISDISVGG 230
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1102-1172 |
4.90e-36 |
|
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: 130.64 E-value: 4.90e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083719 1102 GARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK 1172
Cdd:cd22303 1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
379-428 |
1.04e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 69.30 E-value: 1.04e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 379 CECDPDGAVpGAPCDPVTGQCVCKEHVQGERCDLCKPGFTGLTYANPQGC 428
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
379-428 |
5.28e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.25 E-value: 5.28e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 379 CECDPDGAVPGApCDPVTGQCVCKEHVQGERCDLCKPGFTGltyANPQGC 428
Cdd:smart00180 1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
378-429 |
1.59e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 1.59e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 189083719 378 SCECDPDGAVPGApCDPVTGQCVCKEHVQGERCDLCKPGFTGLTyANPQGCH 429
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
534-576 |
6.96e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 6.96e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 189083719 534 CDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYP 576
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
533-582 |
1.72e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 1.72e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 533 ACDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACH 582
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
431-478 |
2.15e-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: 59.67 E-value: 2.15e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 431 CDCNILGSRRDmPCDEESGRCLCLPNVVGPKCDQCAPYHWKLA--SGQGC 478
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
534-571 |
2.61e-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: 59.67 E-value: 2.61e-11
10 20 30
....*....|....*....|....*....|....*...
gi 189083719 534 CDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGY 571
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
430-479 |
2.76e-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: 2.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 189083719 430 RCDCNILGSRRDmPCDEESGRCLCLPNVVGPKCDQCAPYHWKLAS-GQGCE 479
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
431-478 |
8.83e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.09 E-value: 8.83e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 189083719 431 CDCNILGSRrDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKlASGQGC 478
Cdd:smart00180 1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1092 |
5.60e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 838 QLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDvrrtRLLIQQVRdfltdpdtdaATIQEVSEAVL 917
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQ----------AEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 918 ALwlPTDSATVLQKMNEIQAIAARLpnvdlvLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEA 997
Cdd:COG1196 299 RL--EQDIARLEERRRELEERLEEL------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 998 QDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEG 1077
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250
....*....|....*
gi 189083719 1078 FERIKQKYAELKDRL 1092
Cdd:COG1196 451 EAELEEEEEALLELL 465
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
481-534 |
6.78e-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: 55.44 E-value: 6.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 189083719 481 CACDPHNSLSPQCNQFTGQCPCREGFGGLMCSaaairQCPDRTYGDVATGCRAC 534
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
481-531 |
7.52e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 7.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 189083719 481 CACDPHNSLSPQCNQFTGQCPCREGFGGLMCSaaairQCPDRTYGDVATGC 531
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
480-532 |
2.16e-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: 54.28 E-value: 2.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 480 PCACDPHNSLSPQCNQFTGQCPCREGFGGLMCSaaairQCPDRTYGD--VATGCR 532
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
844-1071 |
5.19e-09 |
|
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: 58.45 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 844 AQLQRTRQMIRAAEESASQIQSSAQRLET------QVSASRSQMEEDVRRTRLLIQQ----VRDFLTDPDTDAATIQEVS 913
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEElsasieEVAANADEIAATAQSAAEAAEEgreaVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 914 EAVLALwlpTDSATVLQKMNE-IQAIAarlpnvdlvlSQTkqDI---------ARA--------------RRL----QAE 965
Cdd:smart00283 81 SAVEEL---EESSDEIGEIVSvIDDIA----------DQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 966 AEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLrpaEKLVTSMTKQ---LGDFWTR 1042
Cdd:smart00283 146 AKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQaagSEEVNAA 222
|
250 260
....*....|....*....|....*....
gi 189083719 1043 MEELRHQARQQGAEAVQAQQLAEGASEQA 1071
Cdd:smart00283 223 IDEIAQVTQETAAMSEEISAAAEELSGLA 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
834-1158 |
7.70e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEdvRRTRLL-----IQQVRDFLTDPDTDAAT 908
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--RREEIEeleeeIEELRERFGDAPVDLGN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 909 IQEVSEAVLAlwlptdsatvlqkmnEIQAIAARLPNVDLVLSQTKQDIARARRLQAE------------------AEEAR 970
Cdd:PRK02224 410 AEDFLEELRE---------------ERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 971 SRAHAVEGQVEDvvgnLRQGTVALQEAQDTMQgtsrSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQA 1050
Cdd:PRK02224 475 ERVEELEAELED----LEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1051 RQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELfGETMEMMDRMKDME 1130
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL-REKREALAELNDER 625
|
330 340 350
....*....|....*....|....*....|
gi 189083719 1131 LELLRGSQAimlRSADLTGL--EKRVEQIR 1158
Cdd:PRK02224 626 RERLAEKRE---RKRELEAEfdEARIEEAR 652
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
249-304 |
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: 50.43 E-value: 4.54e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 189083719 249 SCFCHGHAD---RCAPKPGasagpstavqvhdVCVCQHNTAGPNCERCAPFYNNRPWRP 304
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTG-------------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
951-1127 |
1.05e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 50.83 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 951 QTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQE-AQDTMQGTSRSL--------RLIQDRVAEVQQV 1021
Cdd:pfam04012 26 MLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEkAQAALTKGNEELarealaekKSLEKQAEALETQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1022 LRPAEKLVTSMTKQLGDFWTRMEELRHQ-----ARQQGAEAVQAQQLAEGASEQAlSAQEGFERIKQKYAELKDRLGQSS 1096
Cdd:pfam04012 106 LAQQRSAVEQLRKQLAALETKIQQLKAKknllkARLKAAKAQEAVQTSLGSLSTS-SATDSFERIEEKIEEREARADAAA 184
|
170 180 190
....*....|....*....|....*....|.
gi 189083719 1097 MLGEQGARIQSVKtEAEELFGETMEMMDRMK 1127
Cdd:pfam04012 185 ELASAVDLDAKLE-QAGIQMEVSEDVLARLK 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1158 |
1.05e-06 |
|
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: 53.14 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 838 QLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRtrlliqqvrdfltdpdtdaatIQEVSEAVL 917
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE---------------------IEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 918 ALwlptdSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARR----LQAEAEEARSRAHAVEGQVEDVVGNLRQGTVA 993
Cdd:TIGR02168 292 AL-----ANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 994 LQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQ------QLAEGA 1067
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqaELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1068 SEQAlSAQEGFERIKQKYAELKDRLGQSSmlgeqgARIQSVKTEAEELFGEtMEMMDRMKDMELELLRGSQAIMLRSADL 1147
Cdd:TIGR02168 447 EELE-ELQEELERLEEALEELREELEEAE------QALDAAERELAQLQAR-LDSLERLQENLEGFSEGVKALLKNQSGL 518
|
330
....*....|..
gi 189083719 1148 TGLEKRV-EQIR 1158
Cdd:TIGR02168 519 SGILGVLsELIS 530
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
250-307 |
8.77e-06 |
|
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: 8.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 250 CFCHGHADRcapkpgasagPSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEG 307
Cdd:pfam00053 1 CDCNPHGSL----------SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
847-1128 |
1.56e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.44 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 847 QRTRQMIRAAEESASQIQSSAQRLETQ----VSASRSQMEEDVRRTRLLIQQVRDFL-TD-------PDTDAATI----Q 910
Cdd:NF041483 764 RRATELVSAAEQTAQQVRDSVAGLQEQaeeeIAGLRSAAEHAAERTRTEAQEEADRVrSDayaererASEDANRLrreaQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 911 EVSEAVLALWLPTdsatvlqkMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGqvedvvGNLRQG 990
Cdd:NF041483 844 EETEAAKALAERT--------VSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADARED------ANRIRS 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 991 TVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSmtkqlgdfwtRMEELRHQARQQGAEAV-QAQQLAEGASE 1069
Cdd:NF041483 910 DAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAER----------VRADAAAQAEQLIAEATgEAERLRAEAAE 979
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 189083719 1070 QALSAQEGFERIKQKYAELKdrlgqssmlgeqgariQSVKTEAEELFGETMEMMDRMKD 1128
Cdd:NF041483 980 TVGSAQQHAERIRTEAERVK----------------AEAAAEAERLRTEAREEADRTLD 1022
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
316-366 |
3.24e-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: 42.34 E-value: 3.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 189083719 316 CDCNGH---SETCHFdpavfaasqgaYGGVCDnCRDHTEGKNCERCQLHYFRNR 366
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
315-369 |
3.45e-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: 3.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 315 RCDCNGH---SETCHFDpavfaasqgayGGVCDnCRDHTEGKNCERCQLHYFRNRRPG 369
Cdd:cd00055 1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
862-1076 |
5.30e-05 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 45.69 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 862 QIQSSAQrletQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLalwlptdsatvlQKMNEIQAIAAR 941
Cdd:cd11386 2 ELSASIE----EVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAV------------SAVEELEESSAE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 942 LPNVdlvlSQTKQDIAR-----ArrLQAEAEEAR----SRAHAVegqVEDVVGNLrqgtvalqeAQDTMQGT---SRSLR 1009
Cdd:cd11386 66 IGEI----VEVIDDIAEqtnllA--LNAAIEAARageaGRGFAV---VADEVRKL---------AEESAEAAkeiEELIE 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083719 1010 LIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQgaeAVQAQQLAEGASEQALSAQE 1076
Cdd:cd11386 128 EIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEV---ADGIQEISAATQEQSASTQE 191
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
620-1160 |
6.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 620 LASRILDAKSKIEQIRAVLSSPAVT--------EQEVAQVASAILSLRRTLQGLQLDLPLEEETLSLPRDLESLDRSFNg 691
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSL- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 692 llTMYQRKREQFEKISSADPSGAFRMLSTAYEQsaqaaqqvsdssrlLDQLRDSRREAERLVR-------QAGGGGGTGS 764
Cdd:TIGR00606 496 --TETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--------------LNHHTTTRTQMEMLTKdkmdkdeQIRKIKSRHS 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 765 PKLVALRLEMSSLPDLTPTFNKLCGNSRQMActpiscpgelcpqdngtacgSRCRGVLPRAGGAFLMAGQVAEQLRGFNA 844
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTR--------------------DRLAKLNKELASLEQNKNHINNELESKEE 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 845 QLQRTRQMIRAAEeSASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQV---------------RDFLTD-------- 901
Cdd:TIGR00606 620 QLSSYEDKLFDVC-GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFItqltdenqsccpvcqRVFQTEaelqefis 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 902 ---------PDTDAATIQEVS------EAVLALwLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRL---- 962
Cdd:TIGR00606 699 dlqsklrlaPDKLKSTESELKkkekrrDEMLGL-APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgti 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 963 QAEAEEARSRAHAV------EGQVEDVVGNLRQGTVALQ--EAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTK 1034
Cdd:TIGR00606 778 MPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1035 QLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAE-LKDRLGQSSMLGEQGARIQSVKTE-- 1111
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdSPLETFLEKDQQEKEELISSKETSnk 937
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 1112 -AEELFGETMEMMDR----MKDMELELLRGSQ-AIMLRSADLTGLEKRVEQIRDH 1160
Cdd:TIGR00606 938 kAQDKVNDIKEKVKNihgyMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKH 992
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
278-302 |
1.46e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 1.46e-04
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
316-369 |
2.39e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 2.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 189083719 316 CDCNG---HSETCHFDpavfaasqgayGGVCDnCRDHTEGKNCERCQLHYFRNRRPG 369
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
834-1139 |
3.47e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSA-QRLETQVSASRSQMEEdvrRTRLLIQQVRDFLTDPDTDAATIQEV 912
Cdd:NF041483 255 QAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQ---RTRTAKEEIARLVGEATKEAEALKAE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 913 SEAVLA------------------LWLPTDSATVLQKmneiqaiAARlpNVDLVLSQTKQDiARAR-----------RLQ 963
Cdd:NF041483 332 AEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKATtraaaeeaeriRRE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 964 AEAEEARSRAHAVE------GQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRliQDRVAE------------VQQV---L 1022
Cdd:NF041483 402 AEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirgearreaVQQIeeaA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1023 RPAEKLV-----------------------------TSMTKQLGDfwtRMEELRHQARQQGAEAV-QAQQLAEGASEQAL 1072
Cdd:NF041483 480 RTAEELLtkakadadelrstataeservrteaieraTTLRRQAEE---TLERTRAEAERLRAEAEeQAEEVRAAAERAAR 556
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083719 1073 SAQEGFER-IKQKYAELKDRLGQ-----SSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQA 1139
Cdd:NF041483 557 ELREETERaIAARQAEAAEELTRlhteaEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQA 629
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
626-980 |
3.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 626 DAKSKIEQIRAVLSSPAVTEQEVAQVASAILsLRRTLQGLQLDlpleEETLSLPRDLESLDRSFNGLLTMYQRKREQFEK 705
Cdd:COG3206 65 SSDVLLSGLSSLSASDSPLETQIEILKSRPV-LERVVDKLNLD----EDPLGEEASREAAIERLRKNLTVEPVKGSNVIE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 706 IS--SADPSGAFRM---LSTAYEQSaQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGgggtgspKLVALRLEmsslpdl 780
Cdd:COG3206 140 ISytSPDPELAAAVanaLAEAYLEQ-NLELRREEARKALEFLEEQLPELRKELEEAEA-------ALEEFRQK------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 781 tptfNKLcgnsrqmactpISCPGElcpqdngtacgsrcrgvlpraggaflmAGQVAEQLRGFNAQLQRTRQMIRAAEESA 860
Cdd:COG3206 205 ----NGL-----------VDLSEE---------------------------AKLLLQQLSELESQLAEARAELAEAEARL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 861 SQIQS----------------SAQRLETQVSASRSQMEE----------DVRRTRLLIQQVRDFLtdpDTDAATIQEVSE 914
Cdd:COG3206 243 AALRAqlgsgpdalpellqspVIQQLRAQLAELEAELAElsarytpnhpDVIALRAQIAALRAQL---QQEAQRILASLE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 915 AVLALwLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARR----LQAEAEEARSRAHAVEGQV 980
Cdd:COG3206 320 AELEA-LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyesLLQRLEEARLAEALTVGNV 388
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
833-1126 |
5.46e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 833 GQVAEQ-LRgfNAQLQrTRQMIRAAEESASQIQSSAQRL--ETQVSASRSQME---EDVRRTRLLIQQVRDfltdpdtDA 906
Cdd:NF041483 71 GYQAEQlLR--NAQIQ-ADQLRADAERELRDARAQTQRIlqEHAEHQARLQAElhtEAVQRRQQLDQELAE-------RR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 907 ATIQ-EVSEAVLalWlptdsATVLQKMNEIQAiaARLpnVDLVLSQTKQDIARAR------------RLQAEAEEARSRA 973
Cdd:NF041483 141 QTVEsHVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 974 HAVEGQV-EDVVGNLRQGTVALQEAqdtmqgTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQ 1052
Cdd:NF041483 210 EAILRRArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEK 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 1053 QGAEAVQ--AQQL--AEGASEQalsaqegfeRIKQKYAELkdrlgqSSMLGEQGARIQSVKTEAEELFGETMEMMDRM 1126
Cdd:NF041483 284 VVAEAKEaaAKQLasAESANEQ---------RTRTAKEEI------ARLVGEATKEAEALKAEAEQALADARAEAEKL 346
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
20-248 |
9.68e-84 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 272.31 E-value: 9.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 20 ACSRGACYPPVGDLLVGRtrFLRASSTCGLTKPETYCTQ--YGEWQMKCCKCDSRQPHnyYSHRVENVASSSGP--MRWW 95
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNPR--RSHPAENLTDGNNPnnPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 96 QSQNDVNP---VSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSsDFGKTWRVYQYLAADCTSTFPRVRQGRPQS--WQD 170
Cdd:smart00136 77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITKgnEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 171 VRCQSLPQRPNaRLNGGKVQLNLMDLVSGIP-ATQSQKIQEVGEITNLRVNFTRLAPVPQRGYH-----PPSAYYAVSQL 244
Cdd:smart00136 156 VICTSEYSDIV-PLEGGEIAFSLLEGRPSATdFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDdrpevTRRYYYAISDI 234
|
....
gi 189083719 245 RLQG 248
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
26-248 |
3.14e-58 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 200.50 E-value: 3.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 26 CYPPVGDLLVGRTrfLRASSTCGLTKPETYCTQygEWQM---KCCKCDSRQPHNyySHRVENVASSSG--PMRWWQSQND 100
Cdd:pfam00055 1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCIL--SGLEggkKCFICDSRDPHN--SHPPSNLTDSNNgtNETWWQSETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 101 VNP---VSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSW-QDVRC--- 173
Cdd:pfam00055 75 VIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVICtse 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 174 QSLPqRPnarLNGGKVQLNLMDLVSGIP-ATQSQKIQEVGEITNLRVNFTRLA--PVPQRGYHP--PSAYYAVSQLRLQG 248
Cdd:pfam00055 155 YSDI-SP---LTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtlGDELLDDPSvlRKYYYAISDISVGG 230
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1102-1172 |
4.90e-36 |
|
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: 130.64 E-value: 4.90e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083719 1102 GARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK 1172
Cdd:cd22303 1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1102-1171 |
7.69e-24 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 95.81 E-value: 7.69e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1102 GARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATC 1171
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
379-428 |
1.04e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 69.30 E-value: 1.04e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 379 CECDPDGAVpGAPCDPVTGQCVCKEHVQGERCDLCKPGFTGLTYANPQGC 428
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
379-428 |
5.28e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.25 E-value: 5.28e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 379 CECDPDGAVPGApCDPVTGQCVCKEHVQGERCDLCKPGFTGltyANPQGC 428
Cdd:smart00180 1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
378-429 |
1.59e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 1.59e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 189083719 378 SCECDPDGAVPGApCDPVTGQCVCKEHVQGERCDLCKPGFTGLTyANPQGCH 429
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
534-576 |
6.96e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 6.96e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 189083719 534 CDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYP 576
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
533-582 |
1.72e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 1.72e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 533 ACDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACH 582
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
431-478 |
2.15e-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: 59.67 E-value: 2.15e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 189083719 431 CDCNILGSRRDmPCDEESGRCLCLPNVVGPKCDQCAPYHWKLA--SGQGC 478
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
534-571 |
2.61e-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: 59.67 E-value: 2.61e-11
10 20 30
....*....|....*....|....*....|....*...
gi 189083719 534 CDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGY 571
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
430-479 |
2.76e-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: 2.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 189083719 430 RCDCNILGSRRDmPCDEESGRCLCLPNVVGPKCDQCAPYHWKLAS-GQGCE 479
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
431-478 |
8.83e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.09 E-value: 8.83e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 189083719 431 CDCNILGSRrDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKlASGQGC 478
Cdd:smart00180 1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1092 |
5.60e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 838 QLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDvrrtRLLIQQVRdfltdpdtdaATIQEVSEAVL 917
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQ----------AEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 918 ALwlPTDSATVLQKMNEIQAIAARLpnvdlvLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEA 997
Cdd:COG1196 299 RL--EQDIARLEERRRELEERLEEL------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 998 QDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEG 1077
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250
....*....|....*
gi 189083719 1078 FERIKQKYAELKDRL 1092
Cdd:COG1196 451 EAELEEEEEALLELL 465
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
481-534 |
6.78e-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: 55.44 E-value: 6.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 189083719 481 CACDPHNSLSPQCNQFTGQCPCREGFGGLMCSaaairQCPDRTYGDVATGCRAC 534
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
481-531 |
7.52e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 7.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 189083719 481 CACDPHNSLSPQCNQFTGQCPCREGFGGLMCSaaairQCPDRTYGDVATGC 531
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
480-532 |
2.16e-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: 54.28 E-value: 2.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 480 PCACDPHNSLSPQCNQFTGQCPCREGFGGLMCSaaairQCPDRTYGD--VATGCR 532
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
834-1109 |
2.81e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVsasrSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVS 913
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL----ARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 914 EAvlalwlptDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVA 993
Cdd:COG1196 333 EE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 994 LQEAQDTMQGtsRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLgdfwtrmEELRHQARQQGAEAVQAQQLAEGASEQALS 1073
Cdd:COG1196 405 LEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALE-------EAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270
....*....|....*....|....*....|....*.
gi 189083719 1074 AQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVK 1109
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
844-1071 |
5.19e-09 |
|
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: 58.45 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 844 AQLQRTRQMIRAAEESASQIQSSAQRLET------QVSASRSQMEEDVRRTRLLIQQ----VRDFLTDPDTDAATIQEVS 913
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEElsasieEVAANADEIAATAQSAAEAAEEgreaVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 914 EAVLALwlpTDSATVLQKMNE-IQAIAarlpnvdlvlSQTkqDI---------ARA--------------RRL----QAE 965
Cdd:smart00283 81 SAVEEL---EESSDEIGEIVSvIDDIA----------DQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 966 AEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLrpaEKLVTSMTKQ---LGDFWTR 1042
Cdd:smart00283 146 AKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQaagSEEVNAA 222
|
250 260
....*....|....*....|....*....
gi 189083719 1043 MEELRHQARQQGAEAVQAQQLAEGASEQA 1071
Cdd:smart00283 223 IDEIAQVTQETAAMSEEISAAAEELSGLA 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
834-1158 |
7.70e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEdvRRTRLL-----IQQVRDFLTDPDTDAAT 908
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--RREEIEeleeeIEELRERFGDAPVDLGN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 909 IQEVSEAVLAlwlptdsatvlqkmnEIQAIAARLPNVDLVLSQTKQDIARARRLQAE------------------AEEAR 970
Cdd:PRK02224 410 AEDFLEELRE---------------ERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 971 SRAHAVEGQVEDvvgnLRQGTVALQEAQDTMQgtsrSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQA 1050
Cdd:PRK02224 475 ERVEELEAELED----LEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1051 RQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELfGETMEMMDRMKDME 1130
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL-REKREALAELNDER 625
|
330 340 350
....*....|....*....|....*....|
gi 189083719 1131 LELLRGSQAimlRSADLTGL--EKRVEQIR 1158
Cdd:PRK02224 626 RERLAEKRE---RKRELEAEfdEARIEEAR 652
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
833-1082 |
3.05e-08 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 57.72 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 833 GQVAEQLRGFNAQLQRTRQMIR--------AAEESASQIQSSAQRLETQ------VSASRSQMEEDVRRTRLLIQQVRDF 898
Cdd:COG0840 238 GQLADAFNRMIENLRELVGQVResaeqvasASEELAASAEELAAGAEEQaasleeTAAAMEELSATVQEVAENAQQAAEL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 899 LTDPDTDAATIQEVSEAVLALW--LPTDSATVLQKMNEIQAIAARLPN-VDLVlsqtkQDI---------------ARA- 959
Cdd:COG0840 318 AEEASELAEEGGEVVEEAVEGIeeIRESVEETAETIEELGESSQEIGEiVDVI-----DDIaeqtnllalnaaieaARAg 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 960 -------------RRLqAE-----AEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEV--- 1018
Cdd:COG0840 393 eagrgfavvadevRKL-AErsaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVsdl 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 1019 -QQVLRPAEKLVTSmTKQLGdfwTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIK 1082
Cdd:COG0840 472 iQEIAAASEEQSAG-TEEVN---QAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFK 532
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
249-304 |
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: 50.43 E-value: 4.54e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 189083719 249 SCFCHGHAD---RCAPKPGasagpstavqvhdVCVCQHNTAGPNCERCAPFYNNRPWRP 304
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTG-------------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
616-1116 |
8.78e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 616 EDRGLASRILDAKSKIEQIRAVLSSPAVTEQEVAQVASAILSLRRTLQGLQLDL---PLEEETLSLPRDLESLDRSFNGL 692
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 693 LTMYQRKREQFEKISSAdpSGAFRMLSTAYEQ-----SAQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGgggtgspKL 767
Cdd:COG4717 152 EERLEELRELEEELEEL--EAELAELQEELEElleqlSLATEEELQDLAEELEELQQRLAELEEELEEAQE-------EL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 768 VALRLEMSSLPDLTPTFNKLcgNSRQMACTPISCPGELCPQDngTACGSRCRGVLPRAGGAFLMAGQVAEQLRGFNAQLQ 847
Cdd:COG4717 223 EELEEELEQLENELEAAALE--ERLKEARLLLLIAAALLALL--GLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 848 RTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLalwlptdsat 927
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 928 vlqkMNEIQAIAARLpNVDlvlsqTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQdtmqgtsrs 1007
Cdd:COG4717 369 ----EQEIAALLAEA-GVE-----DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--------- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1008 lrlIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAE--GASEQALSAQEGFERIKQKY 1085
Cdd:COG4717 430 ---LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAElrELAEEWAALKLALELLEEAR 506
|
490 500 510
....*....|....*....|....*....|.
gi 189083719 1086 AELKDRlgqssmlgeqgaRIQSVKTEAEELF 1116
Cdd:COG4717 507 EEYREE------------RLPPVLERASEYF 525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-1158 |
1.14e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 593 REQALRF----GRLRNATASLWsgpGLEDRGLASRILDAKSKIEQIRAVLsspAVTEQEVAQVASAILSLRRTLQGLQLD 668
Cdd:COG1196 209 AEKAERYrelkEELKELEAELL---LLKLRELEAELEELEAELEELEAEL---EELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 669 L-PLEEETLSLPRDLESLDRSFNGLLTMYQRKREQFEKISSADPSGAFRmLSTAYEQSAQAAQQVSDSSRLLDQLRDSRR 747
Cdd:COG1196 283 LeEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 748 EAERLVRQAGGgggtgspKLVALRLEMSSLpdltptfnklcgNSRQMActpiscpgelcPQDNGTACGSRCRGVLPRAGG 827
Cdd:COG1196 362 EAEEALLEAEA-------ELAEAEEELEEL------------AEELLE-----------ALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 828 AFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDfLTDPDTDAA 907
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-LLEELAEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 908 TIQEVSEAVLALWLPTDSATVLQKMNEIQ-----------------------AIAARLPNV---------DLVLSQTKQD 955
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayeaaleaALAAALQNIvveddevaaAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 956 IARARRLQAEAEEARS--RAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMT 1033
Cdd:COG1196 571 AGRATFLPLDKIRARAalAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1034 KQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAE 1113
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 189083719 1114 ELfgETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIR 1158
Cdd:COG1196 731 EA--EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
828-1086 |
3.95e-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: 53.61 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 828 AFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQM---EEDVRRTRLLIQQVRDFLTDPDT 904
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 905 DAATIQ---EVSEAVLALWLPTdsatvLQKMNeiqaiaaRLPNVDLVLSQT--KQDIARARRLQAEAEEARSRAHAVEGQ 979
Cdd:COG4942 91 EIAELRaelEAQKEELAELLRA-----LYRLG-------RQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 980 VEDvvgnLRQGTVALQEAQDTMQgtsRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQ 1059
Cdd:COG4942 159 LAE----LAALRAELEAERAELE---ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|....*..
gi 189083719 1060 AQQLAEGASEQALSAqeGFERIKQKYA 1086
Cdd:COG4942 232 LEAEAAAAAERTPAA--GFAALKGKLP 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
832-1162 |
5.51e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 832 AGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSAsrsqmEEDVRRTRLLIQQVRDFLTDPDTDAATIQE 911
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 912 VSEAVLAlwLPTDSATVLQKMNEIQAIAARLPNVDLV-LSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQG 990
Cdd:COG4717 158 LRELEEE--LEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 991 TVALQEAQD---------------TMQGTSRSLRLIQDRVAEVQQ-VLRPAEKLVTSMTKQLGDFWTRMEELRHQARQqg 1054
Cdd:COG4717 236 LEAAALEERlkearlllliaaallALLGLGGSLLSLILTIAGVLFlVLGLLALLFLLLAREKASLGKEAEELQALPAL-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1055 aEAVQAQQLAEGASEQALSAQEGFERIKQKY---AELKDRLGQSSMLGEQgARIQSVKTEAEELFGET------------ 1119
Cdd:COG4717 314 -EELEEEELEELLAALGLPPDLSPEELLELLdriEELQELLREAEELEEE-LQLEELEQEIAALLAEAgvedeeelraal 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 189083719 1120 ------MEMMDRMKDME--LELLRGSQAIMLRSADLTGLEKRVEQIRDHIN 1162
Cdd:COG4717 392 eqaeeyQELKEELEELEeqLEELLGELEELLEALDEEELEEELEELEEELE 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
692-1172 |
8.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 692 LLTMYQRKREQFEKISSADPSGAFRMLSTAYEQSAQAAQQVSDSSRLLDQLRDSRREAERLVRQAGggggtgspKLVALR 771
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE--------ELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 772 LEMSSLPDLTPTFNKLCGNSRQMActpiscpgelcpqdngtacgsrcrgvlpraggaflmagQVAEQLRGFNAQLQRTRQ 851
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELA--------------------------------------ELPERLEELEERLEELRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 852 M---IRAAEESASQIQSSAQRLETQVSASR----SQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLALWLPTD 924
Cdd:COG4717 161 LeeeLEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 925 SATVLQKMNEIQAIAARLpnvdLVLSQTKQDIARARRLQAEAeearsrAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGT 1004
Cdd:COG4717 241 LEERLKEARLLLLIAAAL----LALLGLGGSLLSLILTIAGV------LFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1005 SRSLRLIQDRVAEVQQVLRPAEKLVTSMT-------KQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASE------QA 1071
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELlelldriEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelrAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1072 LSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQS---VKTEAEELFGETMEMMDRMKDMELELLRGSQAI--MLRSAD 1146
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELeqLEEDGE 470
|
490 500
....*....|....*....|....*.
gi 189083719 1147 LTGLEKRVEQIRDHINGRVLYYATCK 1172
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWAALK 496
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
828-1108 |
9.00e-07 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 53.10 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 828 AFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAA 907
Cdd:COG0840 77 ALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 908 TIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQ--TKQDIARARRLQAEAEEARSR--AHAVEGQVEDV 983
Cdd:COG0840 157 AAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALllSRSITRPLRELLEVLERIAEGdlTVRIDVDSKDE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 984 VGNLRQgtvALQEAQDTMQGTSRSLRLIQDRVAE-VQQVLRPAEKLVTSMTKQ---LGDFWTRMEELRHQARQQGAEAVQ 1059
Cdd:COG0840 237 IGQLAD---AFNRMIENLRELVGQVRESAEQVASaSEELAASAEELAAGAEEQaasLEETAAAMEELSATVQEVAENAQQ 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 189083719 1060 AQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSS----MLGEQGARIQSV 1108
Cdd:COG0840 314 AAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAetieELGESSQEIGEI 366
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
951-1127 |
1.05e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 50.83 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 951 QTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQE-AQDTMQGTSRSL--------RLIQDRVAEVQQV 1021
Cdd:pfam04012 26 MLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEkAQAALTKGNEELarealaekKSLEKQAEALETQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1022 LRPAEKLVTSMTKQLGDFWTRMEELRHQ-----ARQQGAEAVQAQQLAEGASEQAlSAQEGFERIKQKYAELKDRLGQSS 1096
Cdd:pfam04012 106 LAQQRSAVEQLRKQLAALETKIQQLKAKknllkARLKAAKAQEAVQTSLGSLSTS-SATDSFERIEEKIEEREARADAAA 184
|
170 180 190
....*....|....*....|....*....|.
gi 189083719 1097 MLGEQGARIQSVKtEAEELFGETMEMMDRMK 1127
Cdd:pfam04012 185 ELASAVDLDAKLE-QAGIQMEVSEDVLARLK 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1158 |
1.05e-06 |
|
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: 53.14 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 838 QLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRtrlliqqvrdfltdpdtdaatIQEVSEAVL 917
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE---------------------IEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 918 ALwlptdSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARR----LQAEAEEARSRAHAVEGQVEDVVGNLRQGTVA 993
Cdd:TIGR02168 292 AL-----ANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 994 LQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQ------QLAEGA 1067
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqaELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1068 SEQAlSAQEGFERIKQKYAELKDRLGQSSmlgeqgARIQSVKTEAEELFGEtMEMMDRMKDMELELLRGSQAIMLRSADL 1147
Cdd:TIGR02168 447 EELE-ELQEELERLEEALEELREELEEAE------QALDAAERELAQLQAR-LDSLERLQENLEGFSEGVKALLKNQSGL 518
|
330
....*....|..
gi 189083719 1148 TGLEKRV-EQIR 1158
Cdd:TIGR02168 519 SGILGVLsELIS 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
834-1075 |
1.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEdvrRTRLLIQQVRDFLTDpDTDAATIQEVS 913
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARALYRS-GGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 914 EAvlalwlpTDSATVLQKMNeiqaiaarlpNVDLVLSQTKQDIARARRLQAEAEEARSrahavegQVEDVVGNLRQGTVA 993
Cdd:COG3883 110 GS-------ESFSDFLDRLS----------ALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 994 LQEAQDTMQGTsrslrliqdrVAEvqqvlrpAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALS 1073
Cdd:COG3883 166 LEAAKAELEAQ----------QAE-------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
..
gi 189083719 1074 AQ 1075
Cdd:COG3883 229 AA 230
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
936-1166 |
1.21e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 936 QAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRV 1015
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1016 AEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQS 1095
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083719 1096 --SMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVL 1166
Cdd:COG4372 184 alDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
821-1135 |
1.31e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 821 VLPRAggaFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLT 900
Cdd:pfam07888 25 VVPRA---ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 901 DPDTDAATIQEVSEAVLALW------------LPTDSATVLQKMNEIQAIAARLPN-VDLVLSQTKQDIARARRLQAEAE 967
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLaqraahearireLEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 968 EARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAE----------VQQVLRPAEKLVTSMTKQLG 1037
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1038 DFWTR----MEELrHQARQQGAEAvqAQQLAegasEQALSAQEGferiKQKYAELKDRLGQSSMLGEQgaRIQSVKTE-- 1111
Cdd:pfam07888 262 SMAAQrdrtQAEL-HQARLQAAQL--TLQLA----DASLALREG----RARWAQERETLQQSAEADKD--RIEKLSAElq 328
|
330 340
....*....|....*....|....*
gi 189083719 1112 -AEELFGEtmEMMDRMKdMELELLR 1135
Cdd:pfam07888 329 rLEERLQE--ERMEREK-LEVELGR 350
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
909-1164 |
2.27e-06 |
|
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: 51.98 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 909 IQEVSEAVLALwlpTDSATVLQKmnEIQAIAARLPNVDLVLSQTKQDIARARR----LQAEAEEARSRAHAVEGQVEDVV 984
Cdd:TIGR02168 679 IEELEEKIEEL---EEKIAELEK--ALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 985 GNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDF--------------WTRMEELRHQA 1050
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltllneeaanlRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1051 RQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRL-GQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDM 1129
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270
....*....|....*....|....*....|....*..
gi 189083719 1130 E--LELLRGSQAIMlrSADLTGLEKRVEQIRDHINGR 1164
Cdd:TIGR02168 914 RreLEELREKLAQL--ELRLEGLEVRIDNLQERLSEE 948
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
820-1163 |
4.93e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 820 GVLPRAGgafLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFL 899
Cdd:COG4372 17 GLRPKTG---ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 900 TDPDTDAATIQEVSEAvlalwlptdsATVLQKmnEIQAIAARLPNVDLVLSQTKQDIArarRLQAEAEEARSRAHAVEGQ 979
Cdd:COG4372 94 AELAQAQEELESLQEE----------AEELQE--ELEELQKERQDLEQQRKQLEAQIA---ELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 980 VEdvvgNLRQGTVALQEAQDTMqgtsrslrLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARqqgaEAVQ 1059
Cdd:COG4372 159 LE----SLQEELAALEQELQAL--------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE----ELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1060 AQQLAEGASEQALSAQEGFERiKQKYAELKDRLGQSSMLGEQGARIQsVKTEAEELFGETMEMMDRMKDMELELLRGSQA 1139
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALE-LEEDKEELLEEVILKEIEELELAIL-VEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
330 340
....*....|....*....|....
gi 189083719 1140 IMLRSADLTGLEKRVEQIRDHING 1163
Cdd:COG4372 301 LLNLAALSLIGALEDALLAALLEL 324
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
958-1159 |
5.91e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 958 RARRLQAEAEE------------ARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPA 1025
Cdd:COG1196 214 RYRELKEELKEleaellllklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1026 EKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQS-SMLGEQGAR 1104
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeEALLEAEAE 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 1105 IQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRD 1159
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
956-1114 |
6.81e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 956 IARARRLQAEAEEARSRAHAVEGQVEDVvgnLRQG-----TVALQEAQDtmqgtsrslrlIQDRVAEVQQVLRPAEKLVT 1030
Cdd:COG1842 50 IANQKRLERQLEELEAEAEKWEEKARLA---LEKGredlaREALERKAE-----------LEAQAEALEAQLAQLEEQVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1031 SMTKQLGDFWTRMEELRHQ-----ARQQGAEA-VQAQQLAEGASEQalSAQEGFERIKQK------YAELKDRLGQSSML 1098
Cdd:COG1842 116 KLKEALRQLESKLEELKAKkdtlkARAKAAKAqEKVNEALSGIDSD--DATSALERMEEKieemeaRAEAAAELAAGDSL 193
|
170
....*....|....*.
gi 189083719 1099 GEQGARIQSvKTEAEE 1114
Cdd:COG1842 194 DDELAELEA-DSEVED 208
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1104-1171 |
8.02e-06 |
|
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: 44.65 E-value: 8.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 1104 RIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATC 1171
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
250-307 |
8.77e-06 |
|
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: 8.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 250 CFCHGHADRcapkpgasagPSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEG 307
Cdd:pfam00053 1 CDCNPHGSL----------SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
847-1128 |
1.56e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.44 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 847 QRTRQMIRAAEESASQIQSSAQRLETQ----VSASRSQMEEDVRRTRLLIQQVRDFL-TD-------PDTDAATI----Q 910
Cdd:NF041483 764 RRATELVSAAEQTAQQVRDSVAGLQEQaeeeIAGLRSAAEHAAERTRTEAQEEADRVrSDayaererASEDANRLrreaQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 911 EVSEAVLALWLPTdsatvlqkMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGqvedvvGNLRQG 990
Cdd:NF041483 844 EETEAAKALAERT--------VSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADARED------ANRIRS 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 991 TVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSmtkqlgdfwtRMEELRHQARQQGAEAV-QAQQLAEGASE 1069
Cdd:NF041483 910 DAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAER----------VRADAAAQAEQLIAEATgEAERLRAEAAE 979
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 189083719 1070 QALSAQEGFERIKQKYAELKdrlgqssmlgeqgariQSVKTEAEELFGETMEMMDRMKD 1128
Cdd:NF041483 980 TVGSAQQHAERIRTEAERVK----------------AEAAAEAERLRTEAREEADRTLD 1022
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
820-1039 |
1.92e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 47.79 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 820 GVLPRAGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRL---ETQVSASRSQMEEDVRRTRLLIQQVR 896
Cdd:pfam06008 9 GALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELqkkATQTLAKAQQVNAESERTLGHAKELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 897 DFLTDPDtdaATIQEVSEAVLALWLPTD---SATVLQKMNEIQAIAARLPNVDLVLSQT--KQDIARARRLQAEAEEARS 971
Cdd:pfam06008 89 EAIKNLI---DNIKEINEKVATLGENDFalpSSDLSRMLAEAQRMLGEIRSRDFGTQLQnaEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 972 RAHA----VEGQVEDVVGN-----------LRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQvlrpaEKLVTSMT-KQ 1035
Cdd:pfam06008 166 SPQEenkaLANALRDSLAEyeaklsdlrelLREAAAKTRDANRLNLANQANLREFQRKKEEVSE-----QKNQLEETlKT 240
|
....
gi 189083719 1036 LGDF 1039
Cdd:pfam06008 241 ARDS 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
858-1162 |
2.61e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 858 ESASQIQSSAQRLETQVS--ASRSQMEEDVRRTRLliqqVRDFLTDPDTDAATIQEVSEAVlalwlptdSATVLQKMNEI 935
Cdd:COG3206 71 SGLSSLSASDSPLETQIEilKSRPVLERVVDKLNL----DEDPLGEEASREAAIERLRKNL--------TVEPVKGSNVI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 936 Q--------AIAARLPN------VDLVLSQTKQDIARARR-LQAEAEEARSRAHAVEGQVEDvvgnLRQ--GTVALQEaq 998
Cdd:COG3206 139 EisytspdpELAAAVANalaeayLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEE----FRQknGLVDLSE-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 999 dTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDfwtrmeelrhqarqqgaeavqaqqlaEGASEQALSAQEGF 1078
Cdd:COG3206 213 -EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS--------------------------GPDALPELLQSPVI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1079 ERIKQKYAELKDRLGQ-SSMLGEQGARIQSVKTEAEELfgetmemmDRMKDMELELLRGSQAIMLRSAD--LTGLEKRVE 1155
Cdd:COG3206 266 QQLRAQLAELEAELAElSARYTPNHPDVIALRAQIAAL--------RAQLQQEAQRILASLEAELEALQarEASLQAQLA 337
|
....*..
gi 189083719 1156 QIRDHIN 1162
Cdd:COG3206 338 QLEARLA 344
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
316-366 |
3.24e-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: 42.34 E-value: 3.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 189083719 316 CDCNGH---SETCHFdpavfaasqgaYGGVCDnCRDHTEGKNCERCQLHYFRNR 366
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
315-369 |
3.45e-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: 3.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 315 RCDCNGH---SETCHFDpavfaasqgayGGVCDnCRDHTEGKNCERCQLHYFRNRRPG 369
Cdd:cd00055 1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
850-1091 |
3.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 850 RQMI---RAAEESASQIQSSAQRLEtqvsASRSQMEEDVRRTRLLIQqvrdfltdpdtdaatIQEVSEAVLALWlptdsa 926
Cdd:COG4913 214 REYMleePDTFEAADALVEHFDDLE----RAHEALEDAREQIELLEP---------------IRELAERYAAAR------ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 927 tvlQKMNEIQAIAARLPnvdLVLSQTKQDIARAR---------RLQAEAEEARSRAHAVEGQVEDVVGNLRQ-GTVALQE 996
Cdd:COG4913 269 ---ERLAELEYLRAALR---LWFAQRRLELLEAEleelraelaRLEAELERLEARLDALREELDELEAQIRGnGGDRLEQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 997 AQDTMQGTSRSLRLIQDRVAEVQQVLRPAEkLVTSMTKQlgDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQE 1076
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALG-LPLPASAE--EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
250
....*....|....*
gi 189083719 1077 GFERIKQKYAELKDR 1091
Cdd:COG4913 420 ELRELEAEIASLERR 434
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
862-1076 |
5.30e-05 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 45.69 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 862 QIQSSAQrletQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLalwlptdsatvlQKMNEIQAIAAR 941
Cdd:cd11386 2 ELSASIE----EVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAV------------SAVEELEESSAE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 942 LPNVdlvlSQTKQDIAR-----ArrLQAEAEEAR----SRAHAVegqVEDVVGNLrqgtvalqeAQDTMQGT---SRSLR 1009
Cdd:cd11386 66 IGEI----VEVIDDIAEqtnllA--LNAAIEAARageaGRGFAV---VADEVRKL---------AEESAEAAkeiEELIE 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083719 1010 LIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQgaeAVQAQQLAEGASEQALSAQE 1076
Cdd:cd11386 128 EIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEV---ADGIQEISAATQEQSASTQE 191
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
620-1160 |
6.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 620 LASRILDAKSKIEQIRAVLSSPAVT--------EQEVAQVASAILSLRRTLQGLQLDLPLEEETLSLPRDLESLDRSFNg 691
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSL- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 692 llTMYQRKREQFEKISSADPSGAFRMLSTAYEQsaqaaqqvsdssrlLDQLRDSRREAERLVR-------QAGGGGGTGS 764
Cdd:TIGR00606 496 --TETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--------------LNHHTTTRTQMEMLTKdkmdkdeQIRKIKSRHS 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 765 PKLVALRLEMSSLPDLTPTFNKLCGNSRQMActpiscpgelcpqdngtacgSRCRGVLPRAGGAFLMAGQVAEQLRGFNA 844
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTR--------------------DRLAKLNKELASLEQNKNHINNELESKEE 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 845 QLQRTRQMIRAAEeSASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQV---------------RDFLTD-------- 901
Cdd:TIGR00606 620 QLSSYEDKLFDVC-GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFItqltdenqsccpvcqRVFQTEaelqefis 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 902 ---------PDTDAATIQEVS------EAVLALwLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRL---- 962
Cdd:TIGR00606 699 dlqsklrlaPDKLKSTESELKkkekrrDEMLGL-APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgti 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 963 QAEAEEARSRAHAV------EGQVEDVVGNLRQGTVALQ--EAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTK 1034
Cdd:TIGR00606 778 MPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1035 QLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAE-LKDRLGQSSMLGEQGARIQSVKTE-- 1111
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdSPLETFLEKDQQEKEELISSKETSnk 937
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 1112 -AEELFGETMEMMDR----MKDMELELLRGSQ-AIMLRSADLTGLEKRVEQIRDH 1160
Cdd:TIGR00606 938 kAQDKVNDIKEKVKNihgyMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKH 992
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
834-1165 |
6.62e-05 |
|
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: 47.48 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFltdpdtdaatIQEVS 913
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL----------QRELE 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 914 EAVLAlwlpTDSATVLQKMNEiqaiaARLPNVDLVLSQTKQDIARARRLQAEAEEARSrahavegQVEDVVGNLRQGTVA 993
Cdd:pfam01576 816 EARAS----RDEILAQSKESE-----KKLKNLEAELLQLQEDLAASERARRQAQQERD-------ELADEIASGASGKSA 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 994 LQEAQdtmqgtsrslRLIQDRVAEVQQVLRpAEKLVTSMTKQlgdfwtrmeelRHQARQQGAEAVQAQQLAEGASEQAL- 1072
Cdd:pfam01576 880 LQDEK----------RRLEARIAQLEEELE-EEQSNTELLND-----------RLRKSTLQVEQLTTELAAERSTSQKSe 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1073 SAQEGFERIKQkyaELKDRLGQ--SSMLGEQGARIQSVKTEAEELfGETMEMMDRMKDMELELLRGSQA----IMLRSAD 1146
Cdd:pfam01576 938 SARQQLERQNK---ELKAKLQEmeGTVKSKFKSSIAALEAKIAQL-EEQLEQESRERQAANKLVRRTEKklkeVLLQVED 1013
|
330 340
....*....|....*....|...
gi 189083719 1147 ltglEKRV-EQIRDHI---NGRV 1165
Cdd:pfam01576 1014 ----ERRHaDQYKDQAekgNSRM 1032
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
834-1164 |
7.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVS 913
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 914 EAVLALwlpTDSATVLQKmnEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSR--AHAVEGQVEDVVGNLRQGT 991
Cdd:COG4372 122 KERQDL---EQQRKQLEA--QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 992 VALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSmtkqLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQA 1071
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS----ALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1072 LSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELFG----ETMEMMDRMKDMELELLRGSQAIMLRSADL 1147
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLaallELAKKLELALAILLAELADLLQLLLVGLLD 352
|
330
....*....|....*..
gi 189083719 1148 TGLEKRVEQIRDHINGR 1164
Cdd:COG4372 353 NDVLELLSKGAEAGVAD 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
956-1159 |
8.25e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 956 IARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDtmqgtsrSLRLIQDRVAEVQQVLRPAEKLVTSMTKQ 1035
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1036 LgdfwtrmeelRHQARQQGAEAVQAQQLAE---GASEQALSAQEGFERIKQKYAELKDRLGQSSmlgeqgARIQSVKTEA 1112
Cdd:COG1196 304 I----------ARLEERRRELEERLEELEEelaELEEELEELEEELEELEEELEEAEEELEEAE------AELAEAEEAL 367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 189083719 1113 EELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRD 1159
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
831-1089 |
8.61e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 831 MAGQVAEQL-RGFNAQLQRTRQmiRAAEESASQIQSSAQRLETQVSASRSQMEeDVRRTRLLIQqvrdfltdpdtdaati 909
Cdd:COG3206 149 LAAAVANALaEAYLEQNLELRR--EEARKALEFLEEQLPELRKELEEAEAALE-EFRQKNGLVD---------------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 910 qevseavlalwLPTDSATVLQKMNEIQAiaarlpnvDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQ 989
Cdd:COG3206 210 -----------LSEEAKLLLQQLSELES--------QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 990 GTVALQEAQDTMQGTS-------RSLR-----LIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEA 1057
Cdd:COG3206 271 QLAELEAELAELSARYtpnhpdvIALRaqiaaLRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260 270
....*....|....*....|....*....|..
gi 189083719 1058 VQAQQLaegaSEQALSAQEGFERIKQKYAELK 1089
Cdd:COG3206 351 AELRRL----EREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
841-1085 |
1.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 841 GFNA--QLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQmeedvrrtRLLIQQVRDFLTDpDTDAATIQEvseavla 918
Cdd:COG4913 605 GFDNraKLAALEAELAELEEELAEAEERLEALEAELDALQER--------REALQRLAEYSWD-EIDVASAER------- 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 919 lwlptdsaTVLQKMNEIQAIaaRLPNVDLvlsqtkqdiaraRRLQAEAEEARSRAHAVEGQvedvvgnlrqgtvaLQEAQ 998
Cdd:COG4913 669 --------EIAELEAELERL--DASSDDL------------AALEEQLEELEAELEELEEE--------------LDELK 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 999 DTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVtsmtkQLGDFWtRMEELRHQARQQGAEAVQAQQLA---EGASEQALSAQ 1075
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLA-----RLELRA-LLEERFAAALGDAVERELRENLEeriDALRARLNRAE 786
|
250
....*....|
gi 189083719 1076 EGFERIKQKY 1085
Cdd:COG4913 787 EELERAMRAF 796
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
278-302 |
1.46e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 1.46e-04
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
834-1057 |
1.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQ--RTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVrdfltdpDTDAATIQE 911
Cdd:COG3206 186 ELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-------GSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 912 VSEavlalwlptdSATVLQKMNEIQAIAARLpnvDLVLSQTKQDIARARRLQAEAEEARSRahaVEGQVEDVVGNLRQGT 991
Cdd:COG3206 259 LLQ----------SPVIQQLRAQLAELEAEL---AELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083719 992 VALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEA 1057
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
835-1135 |
1.82e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 835 VAEQLRGFNAQLQRTRQMIRAAEESASQIQSsaqrletQVSASRSQMEEDVRRTRLLIQQVRDFltdpDTDAATIQEVSE 914
Cdd:COG1340 41 LAEKRDELNAQVKELREEAQELREKRDELNE-------KVKELKEERDELNEKLNELREELDEL----RKELAELNKAGG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 915 avlalwlptdSATVLQKmnEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARsRAHAVEGQVEDVVGNLRQgtvaL 994
Cdd:COG1340 110 ----------SIDKLRK--EIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAK-KALEKNEKLKELRAELKE----L 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 995 QEAQDTmqgtsrslrlIQDRVAE-VQQvlrpAEKLVTSMTKQLGdfwtRMEELRHQARQQGAEAVQAQQLAEGASEQALS 1073
Cdd:COG1340 173 RKEAEE----------IHKKIKElAEE----AQELHEEMIELYK----EADELRKEADELHKEIVEAQEKADELHEEIIE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083719 1074 AQEGFERIKQKYAELKDRLGQSSMlGEQGARIQSVKTEAEELF--GETMEMMDRMKDMELELLR 1135
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKR-EKEKEELEEKAEEIFEKLkkGEKLTTEELKLLQKSGLLE 297
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
936-1157 |
2.21e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 936 QAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVeGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRL--IQD 1013
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLL-KQLRARIEELRAQEAVLEETQERINRARKAAPLaaHIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1014 RVAEV-QQVLRPAEKLVTSMTKqlgdfwtrmeelRHQARQQGAEAVQAQQ--LAEGASEQALSAQEgfERIKQKYAELKD 1090
Cdd:TIGR00618 301 AVTQIeQQAQRIHTELQSKMRS------------RAKLLMKRAAHVKQQSsiEEQRRLLQTLHSQE--IHIRDAHEVATS 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083719 1091 RLGQSSmlgEQGARIQSVKTEAEELfgETMEMMDRMKDMELELLRGSQAimlrSADLTGLEKRVEQI 1157
Cdd:TIGR00618 367 IREISC---QQHTLTQHIHTLQQQK--TTLTQKLQSLCKELDILQREQA----TIDTRTSAFRDLQG 424
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
316-369 |
2.39e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 2.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 189083719 316 CDCNG---HSETCHFDpavfaasqgayGGVCDnCRDHTEGKNCERCQLHYFRNRRPG 369
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
930-1162 |
2.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 930 QKMNEIQAIAARLPnvdlvlsQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLR 1009
Cdd:PRK03918 204 EVLREINEISSELP-------ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1010 LIQDRVAEVQQvLRPAEKLVTSMTKQLGDF---WTRMEELRHQARQQgAEAVQAQ-QLAEGASEQALSAQEGFERIKQKY 1085
Cdd:PRK03918 277 ELEEKVKELKE-LKEKAEEYIKLSEFYEEYldeLREIEKRLSRLEEE-INGIEERiKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1086 AELKDRLGQSSMLGEQGARIQSVKT-----EAEELFGETMEMMDRMKDMELELLRGSQAImlrsadlTGLEKRVEQIRDH 1160
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARI-------GELKKEIKELKKA 427
|
..
gi 189083719 1161 IN 1162
Cdd:PRK03918 428 IE 429
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
834-1139 |
3.47e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSA-QRLETQVSASRSQMEEdvrRTRLLIQQVRDFLTDPDTDAATIQEV 912
Cdd:NF041483 255 QAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQ---RTRTAKEEIARLVGEATKEAEALKAE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 913 SEAVLA------------------LWLPTDSATVLQKmneiqaiAARlpNVDLVLSQTKQDiARAR-----------RLQ 963
Cdd:NF041483 332 AEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKATtraaaeeaeriRRE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 964 AEAEEARSRAHAVE------GQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRliQDRVAE------------VQQV---L 1022
Cdd:NF041483 402 AEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirgearreaVQQIeeaA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1023 RPAEKLV-----------------------------TSMTKQLGDfwtRMEELRHQARQQGAEAV-QAQQLAEGASEQAL 1072
Cdd:NF041483 480 RTAEELLtkakadadelrstataeservrteaieraTTLRRQAEE---TLERTRAEAERLRAEAEeQAEEVRAAAERAAR 556
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083719 1073 SAQEGFER-IKQKYAELKDRLGQ-----SSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQA 1139
Cdd:NF041483 557 ELREETERaIAARQAEAAEELTRlhteaEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQA 629
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
894-1092 |
3.57e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.20 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 894 QVRDFLTDPDTDAATIQEVSEAVLALWLPTDSATV---LQKMNEIQA-IAARLPNVDLVLSQTKQdiaRARRLQAEAEEA 969
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVealLKKHEALEAeLAAHEERVEALNELGEQ---LIEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 970 RSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQgTSRSLRLIQDRVAEVQQVL--RPAEKLVTSMTKQLGDFWTRMEELR 1047
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALasEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 189083719 1048 -HQARQQGAEAvQAQQLAEGASEQALSA-QEGFERIKQKYAELKDRL 1092
Cdd:cd00176 157 aHEPRLKSLNE-LAEELLEEGHPDADEEiEEKLEELNERWEELLELA 202
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
831-1098 |
3.61e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 44.26 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 831 MAGQVAE---QLRGFNAQLQRTRQMIRAAEESASQIQssaQRLETQVSAsrsqmEEDVRRTRLLIQQVRDFLTDpdtdAA 907
Cdd:COG1538 74 LAAEVAQayfDLLAAQEQLALAEENLALAEELLELAR---ARYEAGLAS-----RLDVLQAEAQLAQARAQLAQ----AE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 908 TIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQ---DIARARRLQAEAEEARSRAHA--------- 975
Cdd:COG1538 142 AQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALErrpDLRAAEAQLEAAEAEIGVARAaflpslsls 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 976 ----VEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLiqdRVAEVQQvlrpaEKLVTSMTKQLgdfwtrmEELRHQAR 1051
Cdd:COG1538 222 asygYSSSDDLFSGGSDTWSVGLSLSLPLFDGGRNRARV---RAAKAQL-----EQAEAQYEQTV-------LQALQEVE 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 189083719 1052 QQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYaelkdRLGQSSML 1098
Cdd:COG1538 287 DALAALRAAREQLEALEEALEAAEEALELARARY-----RAGLASLL 328
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
946-1122 |
3.81e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 946 DLVLSQTKQDIARarrLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSL----RLIQDRVAEVQQV 1021
Cdd:COG3883 15 DPQIQAKQKELSE---LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1022 LR----------PAEKLVTSmtKQLGDFWTRMEELRHQARQQGA---EAVQAQQLAEGASEQALSAQEGFERIKQKYAEL 1088
Cdd:COG3883 92 ARalyrsggsvsYLDVLLGS--ESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|....
gi 189083719 1089 KDRLGQSsmLGEQGARIQSVKTEAEELFGETMEM 1122
Cdd:COG3883 170 KAELEAQ--QAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
626-980 |
3.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 626 DAKSKIEQIRAVLSSPAVTEQEVAQVASAILsLRRTLQGLQLDlpleEETLSLPRDLESLDRSFNGLLTMYQRKREQFEK 705
Cdd:COG3206 65 SSDVLLSGLSSLSASDSPLETQIEILKSRPV-LERVVDKLNLD----EDPLGEEASREAAIERLRKNLTVEPVKGSNVIE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 706 IS--SADPSGAFRM---LSTAYEQSaQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGgggtgspKLVALRLEmsslpdl 780
Cdd:COG3206 140 ISytSPDPELAAAVanaLAEAYLEQ-NLELRREEARKALEFLEEQLPELRKELEEAEA-------ALEEFRQK------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 781 tptfNKLcgnsrqmactpISCPGElcpqdngtacgsrcrgvlpraggaflmAGQVAEQLRGFNAQLQRTRQMIRAAEESA 860
Cdd:COG3206 205 ----NGL-----------VDLSEE---------------------------AKLLLQQLSELESQLAEARAELAEAEARL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 861 SQIQS----------------SAQRLETQVSASRSQMEE----------DVRRTRLLIQQVRDFLtdpDTDAATIQEVSE 914
Cdd:COG3206 243 AALRAqlgsgpdalpellqspVIQQLRAQLAELEAELAElsarytpnhpDVIALRAQIAALRAQL---QQEAQRILASLE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 915 AVLALwLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARR----LQAEAEEARSRAHAVEGQV 980
Cdd:COG3206 320 AELEA-LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyesLLQRLEEARLAEALTVGNV 388
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
837-1127 |
4.82e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 837 EQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQvsasRSQMEEDVRRTRL----LIQQVRDFLtdpdtdaATIQEV 912
Cdd:COG1340 29 EKRDELNEELKELAEKRDELNAQVKELREEAQELREK----RDELNEKVKELKEerdeLNEKLNELR-------EELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 913 SEAVLALWLPTDSATVLQKmnEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARsRAHAVEGQVEDVVGNLRQgtv 992
Cdd:COG1340 98 RKELAELNKAGGSIDKLRK--EIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAK-KALEKNEKLKELRAELKE--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 993 aLQEAQDTmqgtsrslrlIQDRVAE-VQQvlrpAEKLVTSMTKQLGdfwtRMEELRHQARQQGAEAVQAQQLAEGASEQa 1071
Cdd:COG1340 172 -LRKEAEE----------IHKKIKElAEE----AQELHEEMIELYK----EADELRKEADELHKEIVEAQEKADELHEE- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 189083719 1072 lsaqegFERIKQKYAELKDRLgqsSMLGEQGARIQSVKTEaEELFGETMEMMDRMK 1127
Cdd:COG1340 232 ------IIELQKELRELRKEL---KKLRKKQRALKREKEK-EELEEKAEEIFEKLK 277
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
954-1092 |
6.10e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 954 QDIARAR-RLQAEAEEARSR----AHAVEGQVEDVVGNLRQGTVALqeAQDTMQGTSRSLRLIQDRVAEVQQVLRpaEKL 1028
Cdd:pfam01442 33 KETEALReRLQKDLEEVRAKlepyLEELQAKLGQNVEELRQRLEPY--TEELRKRLNADAEELQEKLAPYGEELR--ERL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083719 1029 VTSMTKQLGDFWTRMEELRHQARQQgaeavqAQQLAEGASEQALSAQEgfeRIKQKYAELKDRL 1092
Cdd:pfam01442 109 EQNVDALRARLAPYAEELRQKLAER------LEELKESLAPYAEEVQA---QLSQRLQELREKL 163
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
940-1095 |
6.90e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 940 ARLPNVDLvlsQTKQDIARARRLQAEAEEARSRA-HAVEGQVEDVVGNLRQGTVALQEAQDTMQgtsRSLRLIQDRVAEV 1018
Cdd:COG1566 74 ARLDPTDL---QAALAQAEAQLAAAEAQLARLEAeLGAEAEIAAAEAQLAAAQAQLDLAQRELE---RYQALYKKGAVSQ 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083719 1019 QQVLRpAEklvtsmtkqlgdfwTRMEELRHQARQQGAEAVQAQQLAEGASEQAlSAQEGFERIKQKYAELKDRLGQS 1095
Cdd:COG1566 148 QELDE-AR--------------AALDAAQAQLEAAQAQLAQAQAGLREEEELA-AAQAQVAQAEAALAQAELNLART 208
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
834-1139 |
1.12e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 834 QVAEQLRGFNAQLQRTRQMIRAAEESASQ--IQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDfLTDPDTDAATIQE 911
Cdd:COG3064 13 AAQERLEQAEAEKRAAAEAEQKAKEEAEEerLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKK-LAEAEKAAAEAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 912 VSEAvlalwlptDSATVLQKmNEIQAIAARLPNVdlvlsQTKQDIARARR-----LQAEAEEARSRAHA---VEGQVEDV 983
Cdd:COG3064 92 KAAA--------EKAKAAKE-AEAAAAAEKAAAA-----AEKEKAEEAKRkaeeeAKRKAEEERKAAEAeaaAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 984 VGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWtRMEELRHQARQQGAEAVQAQQL 1063
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA-ALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083719 1064 AEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQA 1139
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVA 312
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
825-1069 |
1.16e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.09 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 825 AGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDT 904
Cdd:COG0840 107 AALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 905 DAATIQEVSeAVLALWLptdSATVLQKMNEIQAIAARLPNVDL--VLSQTKQD----IARA------------RRLQAEA 966
Cdd:COG0840 187 ALLALVALA-IILALLL---SRSITRPLRELLEVLERIAEGDLtvRIDVDSKDeigqLADAfnrmienlrelvGQVRESA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 967 EEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEEL 1046
Cdd:COG0840 263 EQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEI 342
|
250 260
....*....|....*....|...
gi 189083719 1047 RHQArQQGAEAVqaQQLAEGASE 1069
Cdd:COG0840 343 RESV-EETAETI--EELGESSQE 362
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
827-1155 |
1.39e-03 |
|
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: 42.90 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 827 GAFLMAG-----QVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLtd 901
Cdd:pfam12128 332 GAFLDADietaaADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQ-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 902 pdtdAATIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQ---TKQDIARARRLQAEAEEARSRAHAVEG 978
Cdd:pfam12128 410 ----LAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 979 QVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRP-AEKLVTSMTKQLGDF------------------ 1039
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqAGTLLHFLRKEAPDWeqsigkvispellhrtdl 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1040 -----------------------------WTRMEELRHQARQQGAEAVQAQQLAEGASEQALS--------AQEGFERIK 1082
Cdd:pfam12128 566 dpevwdgsvggelnlygvkldlkridvpeWAASEEELRERLDKAEEALQSAREKQAAAEEQLVqangelekASREETFAR 645
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083719 1083 QKYAELKDRLGQSSMLGEQGAR-IQSVKTEAEELFGETMEMMDRmkdmELELLRGSQAIMLRSADLTGLEKRVE 1155
Cdd:pfam12128 646 TALKNARLDLRRLFDEKQSEKDkKNKALAERKDSANERLNSLEA----QLKQLDKKHQAWLEEQKEQKREARTE 715
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
832-1092 |
1.79e-03 |
|
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: 42.63 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 832 AGQVAEQLRGFNAQLQRT---RQMIRAAEESASQIQS---SAQRLETQVSASRSQMEEDVRRTRLLIQQVRDfltdpdTD 905
Cdd:COG3096 395 KSQLADYQQALDVQQTRAiqyQQAVQALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSV------AD 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 906 AATIQ--EVSEAVLALWLPTDSATVLQKMNEI-------QAIAARLPNVDLVLSQTKQDIAR---ARRLQAEAEEARSRA 973
Cdd:COG3096 469 AARRQfeKAYELVCKIAGEVERSQAWQTARELlrryrsqQALAQRLQQLRAQLAELEQRLRQqqnAERLLEEFCQRIGQQ 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 974 HAVEGQVEDVvgnlrqgtvaLQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQ 1053
Cdd:COG3096 549 LDAAEELEEL----------LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS 618
|
250 260 270
....*....|....*....|....*....|....*....
gi 189083719 1054 GAEAVQAQQLAEgASEQALSAQEGFERIKQKYAELKDRL 1092
Cdd:COG3096 619 GEALADSQEVTA-AMQQLLEREREATVERDELAARKQAL 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
936-1162 |
2.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 936 QAIAAR-LPNVD-----LVL--SQTKQDIARA-------RRLQAEAEEARSRAHAVEgQVEDVVGNLRQGTVALQEAQDT 1000
Cdd:COG4913 199 KTQSFKpIGDLDdfvreYMLeePDTFEAADALvehfddlERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1001 MQGT-----SRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAqqlAEGASEQALSAQ 1075
Cdd:COG4913 278 RAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1076 EGFERIKQKYAELKDRLGQSSMLGEQG-----ARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAImlrSADLTGL 1150
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEfaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL---EAEIASL 431
|
250
....*....|....*....
gi 189083719 1151 EKR-------VEQIRDHIN 1162
Cdd:COG4913 432 ERRksniparLLALRDALA 450
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1102-1172 |
2.90e-03 |
|
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: 37.42 E-value: 2.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083719 1102 GARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK 1172
Cdd:cd22299 2 KGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
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|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
825-964 |
3.28e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.63 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 825 AGGAFL------MAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSqmeedvrRTRLLIQQVRDF 898
Cdd:PRK06975 339 VGGYALnrkvdrLDQELVQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADAQS-------AQQALEQQYQDL 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083719 899 LTdpDTDAATIQEV----SEAVLALWLPTDSATVLQKMneiQAIAARL-----PNVDLVLSQTKQDIARARRLQA 964
Cdd:PRK06975 412 SR--NRDDWMIAEVeqmlSSASQQLQLTGNVQLALIAL---QNADARLatsdsPQAVAVRKAIAQDIERLKAAPS 481
|
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| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
828-1020 |
5.03e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 828 AFLMAGQVAEQLRGF-------NAQLQRTRQMIraaEESASQIQSS-AQRLETQVSASRSQMEEDVRRTRLliqqvRDFL 899
Cdd:PRK10246 281 AALSLAQPARQLRPHweriqeqSAALAHTRQQI---EEVNTRLQSTmALRARIRHHAAKQSAELQAQQQSL-----NTWL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 900 TDPDTDAATIQEVS--EAVLAlWLPTDSATVLQKMNEIQAIAARLPNV-DLVLSQTKQDIARARRLQAEAEEARSRAHAV 976
Cdd:PRK10246 353 AEHDRFRQWNNELAgwRAQFS-QQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHAEQRPLRQRLVAL 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 189083719 977 EGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQ 1020
Cdd:PRK10246 432 HGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQ 475
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| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
833-1126 |
5.46e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 833 GQVAEQ-LRgfNAQLQrTRQMIRAAEESASQIQSSAQRL--ETQVSASRSQME---EDVRRTRLLIQQVRDfltdpdtDA 906
Cdd:NF041483 71 GYQAEQlLR--NAQIQ-ADQLRADAERELRDARAQTQRIlqEHAEHQARLQAElhtEAVQRRQQLDQELAE-------RR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 907 ATIQ-EVSEAVLalWlptdsATVLQKMNEIQAiaARLpnVDLVLSQTKQDIARAR------------RLQAEAEEARSRA 973
Cdd:NF041483 141 QTVEsHVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 974 HAVEGQV-EDVVGNLRQGTVALQEAqdtmqgTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQ 1052
Cdd:NF041483 210 EAILRRArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEK 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 1053 QGAEAVQ--AQQL--AEGASEQalsaqegfeRIKQKYAELkdrlgqSSMLGEQGARIQSVKTEAEELFGETMEMMDRM 1126
Cdd:NF041483 284 VVAEAKEaaAKQLasAESANEQ---------RTRTAKEEI------ARLVGEATKEAEALKAEAEQALADARAEAEKL 346
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| mukB |
PRK04863 |
chromosome partition protein MukB; |
843-1155 |
7.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 843 NAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMeedvrrtrLLIQQVRDF--LTDPDTDAATIQEVSEAVLALw 920
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL--------SALNRLLPRlnLLADETLADRVEEIREQLDEA- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 921 lptdsatvLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQV---EDVVGnlRQGTVALQEA 997
Cdd:PRK04863 907 --------EEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfalTEVVQ--RRAHFSYEDA 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 998 QDTMQGTSRSLRLIQDRVAEVQQVLRpaeklvtsmtkqlgdfwtrmeELRHQARQQGAEAVQAQQLAegaseqaLSAQEG 1077
Cdd:PRK04863 977 AEMLAKNSDLNEKLRQRLEQAEQERT---------------------RAREQLRQAQAQLAQYNQVL-------ASLKSS 1028
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083719 1078 FERIKQKYAELKDRLGQSSMLGEQGARIQSvKTEAEELFGETMEmmDRMKDMELELLRGSQaimlrSADLTGLEKRVE 1155
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLGVPADSGAEERA-RARRDELHARLSA--NRSRRNQLEKQLTFC-----EAEMDNLTKKLR 1098
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
936-1074 |
8.07e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 40.02 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 936 QAIAARLPNVDLVLSQtkqdiARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQdtmqgtsRSLRLIQDRV 1015
Cdd:COG1538 32 QARAGLLPSQELDLGG-----KRRARIEAAKAQAEAAEADLRAARLDLAAEVAQAYFDLLAAQ-------EQLALAEENL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083719 1016 AEVQQVLRPAEKLVtsmtkQLGDfWTRMEELRHQARQQGAEA-VQAQQLAEGASEQALSA 1074
Cdd:COG1538 100 ALAEELLELARARY-----EAGL-ASRLDVLQAEAQLAQARAqLAQAEAQLAQARNALAL 153
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