|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
20-248 |
7.35e-70 |
|
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: 233.79 E-value: 7.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 20 ACSRGACYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136 77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136 156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234
|
....
gi 568911959 245 RLQG 248
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
26-248 |
1.16e-56 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 195.88 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 26 CYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ-YGQWQMKCCKCDSRLPrnYNSHRVENVASSSG--PMRWWQSQNDVS 102
Cdd:pfam00055 1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILsGLEGGKKCFICDSRDP--HNSHPPSNLTDSNNgtNETWWQSETGVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 103 P---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNW-QDVRCrplSQ 178
Cdd:pfam00055 77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVIC---TS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 179 RPNG--HLTGGKVQLNLMDLASAIP-ASQSKKIQELGDITNLRVNFTKLA-PVPQRGSYP---PSAYFAVSQLRLQG 248
Cdd:pfam00055 154 EYSDisPLTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtLGDELLDDPsvlRKYYYAISDISVGG 230
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1098-1168 |
1.14e-23 |
|
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: 95.59 E-value: 1.14e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911959 1098 GNRILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303 1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
376-425 |
1.24e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.22 E-value: 1.24e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568911959 376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGC 425
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
530-579 |
5.80e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 5.80e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568911959 530 ACDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
531-568 |
8.43e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 8.43e-12
10 20 30
....*....|....*....|....*....|....*...
gi 568911959 531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
531-568 |
1.71e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 1.71e-11
10 20 30
....*....|....*....|....*....|....*...
gi 568911959 531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
375-426 |
3.61e-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: 59.29 E-value: 3.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568911959 375 PCECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGLTfANPKGCH 426
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
376-425 |
9.06e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.09 E-value: 9.06e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568911959 376 CECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGltfANPKGC 425
Cdd:smart00180 1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
830-1161 |
4.79e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVStsrlLMEEDVQRTRLLIQQVRGFLTDPDtDAATIQQVS 909
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS----ALRKDLARLEAEVEQLEERIAQLS-KELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 910 EAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDI----ARARRLQAEAEQARSRAHAVEGQVDDvvgnlrq 985
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLERRIAA------- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 986 gtvalqeaqdtmqgTGRSLRLIQERVGEVQQVLVPAErlvkgmkEQMSGFWARMKELRRQ---AQEEQAQAMQARQLAEG 1062
Cdd:TIGR02168 836 --------------TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESEleaLLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1063 ASQQAM----NAQEGFKRLKQKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgetmemmdkmkdmesELLRGSQAIML 1138
Cdd:TIGR02168 895 ELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ---------------ERLSEEYSLTL 953
|
330 340 350
....*....|....*....|....*....|....
gi 568911959 1139 ---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168 954 eeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
428-475 |
1.08e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 1.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568911959 428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
427-476 |
1.10e-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: 55.05 E-value: 1.10e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568911959 427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
834-1088 |
2.70e-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: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 834 QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLlmeeDVQRTRLLIQQVRgfltdpdtdaATIQQVSEAVL 913
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQ----------AEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 914 ALwlptdSATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEA 993
Cdd:COG1196 299 RL-----EQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 994 QDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG 1073
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250
....*....|....*
gi 568911959 1074 FKRLKQKYTELKDRL 1088
Cdd:COG1196 451 EAELEEEEEALLELL 465
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
478-531 |
4.25e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 4.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568911959 478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGCRAC 531
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
478-528 |
4.32e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 4.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568911959 478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGC 528
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
428-475 |
4.95e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 4.95e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568911959 428 CDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKlASGLGC 475
Cdd:smart00180 1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
249-301 |
1.45e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 1.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568911959 249 SCFCHGHADRcapnpggSTTAVQVNNVCVCQHNTAGPNCDRCAPFYNNRPWRP 301
Cdd:cd00055 1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
477-529 |
4.14e-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: 4.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568911959 477 PCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGH--VATGCR 529
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
250-304 |
2.17e-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: 45.81 E-value: 2.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 250 CFCHGHA---DRCAPNPGgsttavqvnnVCVCQHNTAGPNCDRCAPFYNNRPWRPAEG 304
Cdd:pfam00053 1 CDCNPHGslsDTCDPETG----------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1111 |
1.16e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSR---LLMEEDVQRTRLLIQQVRGFLTDPDTDaatIQQVSEAVLALWLP 918
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 919 TDSATVLRKM--KEIQAIAARLPNVDSVLSQTKQDIARARRLQA-----EAEQARSRAHAVEGQVDD--VVGNLRQGTVA 989
Cdd:PRK02224 407 LGNAEDFLEElrEERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEEDreRVEELEAELED 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 990 LQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWA---RMKELRRQAQEEQAQAMQARQLAEGASQQ 1066
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEE 566
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568911959 1067 AMNAQEGFKRLKQKYTELKDRLgqspvlgEQGNRILSIKMEAEEL 1111
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERI-------ESLERIRTLLAAIADA 604
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
313-367 |
1.99e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.73 E-value: 1.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 313 CDCNGH---SETCHFdpavfaasqgtNGGVCDnCRDHTEGKNCERCQLHYFRNRRPSA 367
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
829-1088 |
2.13e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTD----------- 897
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----LESRVAELKEELRQSREKHEEleekykelsas 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 898 -----PDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARRLQAEAEQARSRAHA 971
Cdd:pfam07888 110 seelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 972 VEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGE----------VQQVLVPAERLVKGMKEQMSGfwarMKE 1041
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSS----MAA 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568911959 1042 LRRQAQEEQAQA-MQARQLAEGASQQAMNAQEGFKRLKQKYTEL-------KDRL 1088
Cdd:pfam07888 266 QRDRTQAELHQArLQAAQLTLQLADASLALREGRARWAQERETLqqsaeadKDRI 320
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
259-299 |
3.37e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 3.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568911959 259 CAPNPGGSTTAV--QVNNVCVCQHNTAGPNCDRCAPFYNNRPW 299
Cdd:smart00180 1 CDCDPGGSASGTcdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
312-362 |
5.96e-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: 41.57 E-value: 5.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568911959 312 RCDCNGH---SETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRN 362
Cdd:cd00055 1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
844-1114 |
1.10e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 844 QTRQMIRAAEEAASRVQADAQR--LETQVSTSRLLME--------------EDVQRTRLLIQQVrgfltdpDTDAATIQ- 906
Cdd:NF041483 73 QAEQLLRNAQIQADQLRADAERelRDARAQTQRILQEhaehqarlqaelhtEAVQRRQQLDQEL-------AERRQTVEs 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 907 QVSEAVLalWlptdsATVLRKMKEIQAiaARLpnVDSVLSQTKQDIARAR------------RLQAEAEQARSRAHAVEG 974
Cdd:NF041483 146 HVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEAEAILR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 975 QV-DDVVGNLRQGTVALQEAqdtmqgTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE--EQA 1051
Cdd:NF041483 215 RArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEA 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 1052 QAMQARQL--AEGASQQAM-NAQEGFKRLKQKYTElkdrlgQSPVLGEQGNRILS-IKMEAEELFGE 1114
Cdd:NF041483 289 KEAAAKQLasAESANEQRTrTAKEEIARLVGEATK------EAEALKAEAEQALAdARAEAEKLVAE 349
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
828-1078 |
2.33e-04 |
|
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: 44.20 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRtrllIQQVRGfltdpdtdaaTIQQ 907
Cdd:smart00283 13 AEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITA----MDQIRE----------VVEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 908 VSEAVLALwlptdsatvLRKMKEIQAIAArlpNVDSVLSQTkqDI---------ARA--------------RRL----QA 960
Cdd:smart00283 79 AVSAVEEL---------EESSDEIGEIVS---VIDDIADQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 961 EAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaERLVKGMKEQMSG---FWA 1037
Cdd:smart00283 145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQAAGseeVNA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568911959 1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:smart00283 222 AIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
313-366 |
8.92e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 8.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 313 CDCNG---HSETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRNRRPS 366
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
832-1065 |
1.44e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 832 AEQLRNFNT-QLQQTR-----------QMIRAAEEAASRVQADAQRLETQVSTS---RLLMEEDV--QRTRLLIQQVRGF 894
Cdd:NF041483 238 AEQLRSSTAaESDQARrqaaelsraaeQRMQEAEEALREARAEAEKVVAEAKEAaakQLASAESAneQRTRTAKEEIARL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 895 LTDPDTDAATIQQVSEAVLA------------------LWLPTDSATVLRKmkeiqaiAARlpNVDSVLSQTKQDiARAR 956
Cdd:NF041483 318 VGEATKEAEALKAEAEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKAT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 957 -----------RLQAEAEQARSRAHAVE------GQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliQERVGE------ 1013
Cdd:NF041483 388 traaaeeaeriRREAEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirg 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 1014 ------VQQV---LVPAERLVKGMK----EQMSGFWA-----------RMKELRRQAQE--EQAQAMQARQLAEGASQ 1065
Cdd:NF041483 466 earreaVQQIeeaARTAEELLTKAKadadELRSTATAeservrteaieRATTLRRQAEEtlERTRAEAERLRAEAEEQ 543
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
828-1088 |
4.48e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 828 AGRVAEQLRNFNTQLQ-QTRQMI----RAAEEAASRVQADAQ----RLETQVSTSRLLMEEDVQRTRLLIQQvrgfltdp 898
Cdd:NF041483 773 AEQTAQQVRDSVAGLQeQAEEEIaglrSAAEHAAERTRTEAQeeadRVRSDAYAERERASEDANRLRREAQE-------- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 899 DTDAATI---QQVSEAVlalwlptDSATVLRKMKEIQAIAARLPNVDSvLSQTKQDIARARrlqAEA-EQARSRAHAVEG 974
Cdd:NF041483 845 ETEAAKAlaeRTVSEAI-------AEAERLRSDASEYAQRVRTEASDT-LASAEQDAARTR---ADArEDANRIRSDAAA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 975 QVDDVVGNLRQGTVALQEAqdtmqGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARmkeLRRQAQEEQAQAM 1054
Cdd:NF041483 914 QADRLIGEATSEAERLTAE-----ARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER---LRAEAAETVGSAQ 985
|
250 260 270
....*....|....*....|....*....|....*.
gi 568911959 1055 QA--RQLAEGASQQAMNAQEGfKRLKQKYTELKDRL 1088
Cdd:NF041483 986 QHaeRIRTEAERVKAEAAAEA-ERLRTEAREEADRT 1020
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
827-1110 |
6.07e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRL--ETQVSTSRLLMEEdVQRTRLLIQQVRG----FLTDPDT 900
Cdd:NF041483 566 IAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIrrEAAEETERLRTEA-AERIRTLQAQAEQeaerLRTEAAA 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 901 DAATIQQVSEAVlALWLPTDSATVLRKMK------------EIQAIAARLPN-VDSVLSQTKQDIARARR--------LQ 959
Cdd:NF041483 645 DASAARAEGENV-AVRLRSEAAAEAERLKseaqesadrvraEAAAAAERVGTeAAEALAAAQEEAARRRReaeetlgsAR 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 960 AEAEQARSRAHAvegQVDDVVGNLRQgtvALQEAQDTMQgtgrslRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwarm 1039
Cdd:NF041483 724 AEADQERERARE---QSEELLASARK---RVEEAQAEAQ------RLVEEADRRATELVSAAEQTAQQVRDSVAG----- 786
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911959 1040 keLRRQAQEEQAqamQARQLAEGASQQA-MNAQEGFKRLKQKYTELKDRlgqspvLGEQGNRILSIKMEAEE 1110
Cdd:NF041483 787 --LQEQAEEEIA---GLRSAAEHAAERTrTEAQEEADRVRSDAYAERER------ASEDANRLRREAQEETE 847
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
20-248 |
7.35e-70 |
|
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: 233.79 E-value: 7.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 20 ACSRGACYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136 77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136 156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234
|
....
gi 568911959 245 RLQG 248
Cdd:smart00136 235 AVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
26-248 |
1.16e-56 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 195.88 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 26 CYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ-YGQWQMKCCKCDSRLPrnYNSHRVENVASSSG--PMRWWQSQNDVS 102
Cdd:pfam00055 1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILsGLEGGKKCFICDSRDP--HNSHPPSNLTDSNNgtNETWWQSETGVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 103 P---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNW-QDVRCrplSQ 178
Cdd:pfam00055 77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVIC---TS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 179 RPNG--HLTGGKVQLNLMDLASAIP-ASQSKKIQELGDITNLRVNFTKLA-PVPQRGSYP---PSAYFAVSQLRLQG 248
Cdd:pfam00055 154 EYSDisPLTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtLGDELLDDPsvlRKYYYAISDISVGG 230
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1098-1168 |
1.14e-23 |
|
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: 95.59 E-value: 1.14e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911959 1098 GNRILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303 1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
376-425 |
1.24e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.22 E-value: 1.24e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568911959 376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGC 425
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1100-1167 |
2.59e-12 |
|
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: 63.07 E-value: 2.59e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 1100 RILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATC 1167
Cdd:cd22295 3 RAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
530-579 |
5.80e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 5.80e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568911959 530 ACDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
531-568 |
8.43e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 8.43e-12
10 20 30
....*....|....*....|....*....|....*...
gi 568911959 531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
531-568 |
1.71e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 1.71e-11
10 20 30
....*....|....*....|....*....|....*...
gi 568911959 531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
375-426 |
3.61e-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: 59.29 E-value: 3.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568911959 375 PCECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGLTfANPKGCH 426
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
376-425 |
9.06e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.09 E-value: 9.06e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568911959 376 CECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGltfANPKGC 425
Cdd:smart00180 1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
830-1161 |
4.79e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVStsrlLMEEDVQRTRLLIQQVRGFLTDPDtDAATIQQVS 909
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS----ALRKDLARLEAEVEQLEERIAQLS-KELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 910 EAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDI----ARARRLQAEAEQARSRAHAVEGQVDDvvgnlrq 985
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLERRIAA------- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 986 gtvalqeaqdtmqgTGRSLRLIQERVGEVQQVLVPAErlvkgmkEQMSGFWARMKELRRQ---AQEEQAQAMQARQLAEG 1062
Cdd:TIGR02168 836 --------------TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESEleaLLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1063 ASQQAM----NAQEGFKRLKQKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgetmemmdkmkdmesELLRGSQAIML 1138
Cdd:TIGR02168 895 ELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ---------------ERLSEEYSLTL 953
|
330 340 350
....*....|....*....|....*....|....
gi 568911959 1139 ---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168 954 eeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
428-475 |
1.08e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 1.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568911959 428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
427-476 |
1.10e-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: 55.05 E-value: 1.10e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568911959 427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
834-1088 |
2.70e-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: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 834 QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLlmeeDVQRTRLLIQQVRgfltdpdtdaATIQQVSEAVL 913
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQ----------AEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 914 ALwlptdSATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEA 993
Cdd:COG1196 299 RL-----EQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 994 QDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG 1073
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250
....*....|....*
gi 568911959 1074 FKRLKQKYTELKDRL 1088
Cdd:COG1196 451 EAELEEEEEALLELL 465
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
478-531 |
4.25e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 4.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568911959 478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGCRAC 531
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
478-528 |
4.32e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 4.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568911959 478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGC 528
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
428-475 |
4.95e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 4.95e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568911959 428 CDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKlASGLGC 475
Cdd:smart00180 1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
249-301 |
1.45e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 1.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568911959 249 SCFCHGHADRcapnpggSTTAVQVNNVCVCQHNTAGPNCDRCAPFYNNRPWRP 301
Cdd:cd00055 1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
477-529 |
4.14e-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: 4.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568911959 477 PCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGH--VATGCR 529
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
830-1090 |
4.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVS 909
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----LEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 910 EAvlalwlptDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVA 989
Cdd:COG1196 333 EE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 990 LQEAQDTMQgtGRSLRLIQERvGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMN 1069
Cdd:COG1196 405 LEEAEEALL--ERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|.
gi 568911959 1070 AQEGFKRLKQKYTELKDRLGQ 1090
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEAD 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
828-1081 |
3.45e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrlLMEEDVQRTRLLIQQVRgfltdpdtdAATIQQ 907
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELAELLR---------ALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 908 VSEAVLALWLPTDSATVLRKMKEIQAIAarlPNVDSVLSQTKQDIARARRLQAEAEQARSRahavegqvddvvgnLRQGT 987
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLQYLKYLA---PARREQAEELRADLAELAALRAELEAERAE--------------LEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 988 VALQEAQDTMQgtgrslRLIQERvgevqqvlvpaERLVKGMKEQMSGFWARMKELRRQAQEEQAQAmqARQLAEGASQQA 1067
Cdd:COG4942 181 AELEEERAALE------ALKAER-----------QKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAE 241
|
250
....*....|....
gi 568911959 1068 MNAQEGFKRLKQKY 1081
Cdd:COG4942 242 RTPAAGFAALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1087 |
9.66e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 846 RQMI---RAAEEAASRVQADAQRLETqvstsrllMEEDVQRTRlliQQVRgFLTDpdtdaatIQQVSEAVLALWlptDSA 922
Cdd:COG4913 214 REYMleePDTFEAADALVEHFDDLER--------AHEALEDAR---EQIE-LLEP-------IRELAERYAAAR---ERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 923 TVLRKMKE---IQAIAARLPNVDSVLSQTKQDIARarrLQAEAEQARSRAHAVEGQVDDVVGNLRQ-GTVALQEAQDTMQ 998
Cdd:COG4913 272 AELEYLRAalrLWFAQRRLELLEAELEELRAELAR---LEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 999 GTGRSLRLIQERVGEVQQVL------VPAERlvkgmkeqmSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQE 1072
Cdd:COG4913 349 RLERELEERERRRARLEALLaalglpLPASA---------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
250
....*....|....*
gi 568911959 1073 GFKRLKQKYTELKDR 1087
Cdd:COG4913 420 ELRELEAEIASLERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
831-1071 |
9.67e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 831 VAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRllmEEDVQRTRLLIQQVRGfltdpdtdaatiQQVSE 910
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERARA------------LYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 911 AVLALWlptdsaTVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSrahavegQVDDVVGNLRQGTVAL 990
Cdd:COG3883 100 GSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 991 QEAQDTMQgtgrslRLIQErvgevqqvlvpAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNA 1070
Cdd:COG3883 167 EAAKAELE------AQQAE-----------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
.
gi 568911959 1071 Q 1071
Cdd:COG3883 230 A 230
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
250-304 |
2.17e-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: 45.81 E-value: 2.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 250 CFCHGHA---DRCAPNPGgsttavqvnnVCVCQHNTAGPNCDRCAPFYNNRPWRPAEG 304
Cdd:pfam00053 1 CDCNPHGslsDTCDPETG----------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
827-1104 |
3.69e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 51.17 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATIQ 906
Cdd:COG0840 80 VLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 907 QVSEAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQ--TKQDIARARRLQAEAEQARSR--AHAVEGQVDDVVGN 982
Cdd:COG0840 160 AAALAALLEAAALALAAAALALALLAAALLALVALAIILALllSRSITRPLRELLEVLERIAEGdlTVRIDVDSKDEIGQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 983 LRQgtvALQEAQDTMQGTGRSLRLIQERVGE-VQQVLVPAERLVKGMKEQMSGF---WARMKELRRQAQEEQAQAMQARQ 1058
Cdd:COG0840 240 LAD---AFNRMIENLRELVGQVRESAEQVASaSEELAASAEELAAGAEEQAASLeetAAAMEELSATVQEVAENAQQAAE 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568911959 1059 LAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPV----LGEQGNRILSI 1104
Cdd:COG0840 317 LAEEASELAEEGGEVVEEAVEGIEEIRESVEETAEtieeLGESSQEIGEI 366
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
829-1078 |
3.76e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 51.17 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 829 GRVAEQLRNFNTQLQQTRQMIR---------------AAEEAASRVQADAQRLEtQVSTSrllMEE---DVQRTRLLIQQ 890
Cdd:COG0840 238 GQLADAFNRMIENLRELVGQVResaeqvasaseelaaSAEELAAGAEEQAASLE-ETAAA---MEElsaTVQEVAENAQQ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 891 VRGFLTDPDTDAATIQQVSEAVLALW--LPTDSATVLRKMKEIQAIAArlpNVDSVLSqTKQDI---------------A 953
Cdd:COG0840 314 AAELAEEASELAEEGGEVVEEAVEGIeeIRESVEETAETIEELGESSQ---EIGEIVD-VIDDIaeqtnllalnaaieaA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 954 RA--------------RRLqAE-----AEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEV 1014
Cdd:COG0840 390 RAgeagrgfavvadevRKL-AErsaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEV 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 1015 ----QQVLVPAERLVKGMkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:COG0840 469 sdliQEIAAASEEQSAGT-EEVN---QAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFK 532
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
929-1111 |
4.79e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 929 KEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQ 1008
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1009 ERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE-EQAQAMQARQLAEgASQQAMNAQEGFKRLKQKYTELKDR 1087
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAElQSEIAEREEELKE-LEEQLESLQEELAALEQELQALSEA 179
|
170 180
....*....|....*....|....*.
gi 568911959 1088 LGQSPV--LGEQGNRILSIKMEAEEL 1111
Cdd:COG4372 180 EAEQALdeLLKEANRNAEKEEELAEA 205
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
834-1066 |
7.37e-06 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 49.65 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 834 QLRNFNTQLQQTRQMIRAAEEAASRVQadaQRLETQVSTsrllmEEDVQRTRLLIQQVRGFLTDpdtdAATIQQVSEAVL 913
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELAR---ARYEAGLAS-----RLDVLQAEAQLAQARAQLAQ----AEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 914 ALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQ---DIARARrlqAEAEQARSRAHAVEGQ----VDDVVGNLRQG 986
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALErrpDLRAAE---AQLEAAEAEIGVARAAflpsLSLSASYGYSS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 987 TVALQEAQDTMQGTGRSLRL-----------IQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQ 1055
Cdd:COG1538 229 SDDLFSGGSDTWSVGLSLSLplfdggrnrarVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEA 308
|
250
....*....|.
gi 568911959 1056 ARQLAEGASQQ 1066
Cdd:COG1538 309 AEEALELARAR 319
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
936-1104 |
9.90e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.89 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 936 ARLpnvDSVLSQTKQDIARARRLQAEAEQARSRA-HAVEGQVDDVVGNLRQGTVALQEAQDTMQgtgRSLRLIQERVgev 1014
Cdd:COG1566 74 ARL---DPTDLQAALAQAEAQLAAAEAQLARLEAeLGAEAEIAAAEAQLAAAQAQLDLAQRELE---RYQALYKKGA--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1015 qqvlVPAERLvkgmkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAmNAQEGFKRLKQKYTELKDRLGQ---- 1090
Cdd:COG1566 145 ----VSQQEL-----DEAR---AALDAAQAQLEAAQAQLAQAQAGLREEEELA-AAQAQVAQAEAALAQAELNLARttir 211
|
170
....*....|....
gi 568911959 1091 SPVLGEQGNRILSI 1104
Cdd:COG1566 212 APVDGVVTNLNVEP 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1111 |
1.16e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSR---LLMEEDVQRTRLLIQQVRGFLTDPDTDaatIQQVSEAVLALWLP 918
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 919 TDSATVLRKM--KEIQAIAARLPNVDSVLSQTKQDIARARRLQA-----EAEQARSRAHAVEGQVDD--VVGNLRQGTVA 989
Cdd:PRK02224 407 LGNAEDFLEElrEERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEEDreRVEELEAELED 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 990 LQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWA---RMKELRRQAQEEQAQAMQARQLAEGASQQ 1066
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEE 566
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568911959 1067 AMNAQEGFKRLKQKYTELKDRLgqspvlgEQGNRILSIKMEAEEL 1111
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERI-------ESLERIRTLLAAIADA 604
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
830-1161 |
1.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLEtqvstSRLLMEEDVQRTRLLIQQ--VRGFLTDPDTDAATIQQ 907
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA-----DYEGFLEGVKAALLLAGLrgLAGAVAVLIGVEAAYEA 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 908 VSEAVLALWLPTDSATVLRKMKE-IQAIAARLPNVDSVLSQTKqdiARARRLQAEAEQARSRAHAVEGQVDD-------- 978
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATFLPLDK---IRARAALAAALARGAIGAAVDLVASDlreadary 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 979 -VVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQmsgfwARMKELRRQAQEEQAQAMQAR 1057
Cdd:COG1196 616 yVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE-----LLAALLEAEAELEELAERLAE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1058 QLAEGASQQAMNAQEGfKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAEELFGEtmemmdkmkdmesELLRGSQAIM 1137
Cdd:COG1196 691 EELELEEALLAEEEEE-RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE-------------LLEEEALEEL 756
|
330 340
....*....|....*....|....*.
gi 568911959 1138 LRSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:COG1196 757 PEPPDLEELERELERLEREIEalGPV 782
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
827-1097 |
1.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQAdaqrletqvstsrllmeEDVQRTRLLIQQVRGflTDPDTDAATIQ 906
Cdd:COG3206 95 VLERVVDKLNLDEDPLGEEASREAAIERLRKNLTV-----------------EPVKGSNVIEISYTS--PDPELAAAVAN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 907 QVSEAVLAlwlptdsATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRlQAEAEQARSRAHAVEGQVDDVVGNLRQG 986
Cdd:COG3206 156 ALAEAYLE-------QNLELRREEARKALEFL---EEQLPELRKELEEAEA-ALEEFRQKNGLVDLSEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 987 TVALQEAQDTMQGTGRSLRLIQERVGEVQQVL--VPAERLVKGMKEQMSGFWARMKELR----------RQAQEEQAQAM 1054
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALR 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568911959 1055 Q-----ARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQ 1097
Cdd:COG3206 305 AqlqqeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
313-367 |
1.99e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.73 E-value: 1.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 313 CDCNGH---SETCHFdpavfaasqgtNGGVCDnCRDHTEGKNCERCQLHYFRNRRPSA 367
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
929-1091 |
2.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 929 KEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDdvvgNLRQgtvALQEAQDTMQGTGRSLRLIQ 1008
Cdd:COG1196 225 LEAELLLLKL---RELEAELEELEAELEELEAELEELEAELAELEAELE----ELRL---ELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1009 ERVGEVQQVLVPAErlvkgmkeqmsgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRL 1088
Cdd:COG1196 295 AELARLEQDIARLE--------------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
...
gi 568911959 1089 GQS 1091
Cdd:COG1196 361 AEA 363
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
829-1088 |
2.13e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTD----------- 897
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----LESRVAELKEELRQSREKHEEleekykelsas 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 898 -----PDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARRLQAEAEQARSRAHA 971
Cdd:pfam07888 110 seelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 972 VEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGE----------VQQVLVPAERLVKGMKEQMSGfwarMKE 1041
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSS----MAA 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568911959 1042 LRRQAQEEQAQA-MQARQLAEGASQQAMNAQEGFKRLKQKYTEL-------KDRL 1088
Cdd:pfam07888 266 QRDRTQAELHQArLQAAQLTLQLADASLALREGRARWAQERETLqqsaeadKDRI 320
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
259-299 |
3.37e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 3.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568911959 259 CAPNPGGSTTAV--QVNNVCVCQHNTAGPNCDRCAPFYNNRPW 299
Cdd:smart00180 1 CDCDPGGSASGTcdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
312-362 |
5.96e-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: 41.57 E-value: 5.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568911959 312 RCDCNGH---SETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRN 362
Cdd:cd00055 1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
830-1090 |
9.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVS--TSRLLMEEDVQRTR------------LLIQQVRGFL 895
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKearlllliaaalLALLGLGGSL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 896 TDPDTDAATIQQVSEAVLAL---WLPTDSATVLRKMKEIQAIAAR-------------------------LPNVDSVLSQ 947
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALlflLLAREKASLGKEAEELQALPALeeleeeeleellaalglppdlspeeLLELLDRIEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 948 TKQDIARARRLQAEAEQARSRAHAVE----GQVDDvVGNLRQGTVALQEAQDTMQgtgrSLRLIQERVGEvqQVLVPAER 1023
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAAllaeAGVED-EEELRAALEQAEEYQELKE----ELEELEEQLEE--LLGELEEL 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 1024 LVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEgFKRLKQKYTELKDRLGQ 1090
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-LAELLQELEELKAELRE 487
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
844-1114 |
1.10e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 844 QTRQMIRAAEEAASRVQADAQR--LETQVSTSRLLME--------------EDVQRTRLLIQQVrgfltdpDTDAATIQ- 906
Cdd:NF041483 73 QAEQLLRNAQIQADQLRADAERelRDARAQTQRILQEhaehqarlqaelhtEAVQRRQQLDQEL-------AERRQTVEs 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 907 QVSEAVLalWlptdsATVLRKMKEIQAiaARLpnVDSVLSQTKQDIARAR------------RLQAEAEQARSRAHAVEG 974
Cdd:NF041483 146 HVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEAEAILR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 975 QV-DDVVGNLRQGTVALQEAqdtmqgTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE--EQA 1051
Cdd:NF041483 215 RArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEA 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 1052 QAMQARQL--AEGASQQAM-NAQEGFKRLKQKYTElkdrlgQSPVLGEQGNRILS-IKMEAEELFGE 1114
Cdd:NF041483 289 KEAAAKQLasAESANEQRTrTAKEEIARLVGEATK------EAEALKAEAEQALAdARAEAEKLVAE 349
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
942-1095 |
1.15e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.49 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 942 DSVLSQTKQDIARARRLQAEAEQAR-----SRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERV----- 1011
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARlqaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1012 -----GEVQQVLVPAERLVKGMKEQMSGFWARMKELrrQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKD 1086
Cdd:pfam00529 132 lapigGISRESLVTAGALVAQAQANLLATVAQLDQI--YVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
....*....
gi 568911959 1087 RLGQSPVLG 1095
Cdd:pfam00529 210 TEIRAPVDG 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
832-1076 |
1.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 832 AEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQvstsrllmeedvqrtRLLIQQVRGFLtdpdtdaatiqqvsea 911
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER---------------REALQRLAEYS---------------- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 912 vlalWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQ 991
Cdd:COG4913 658 ----WDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 992 EAQDTMQGTGRSLR--LIQERVGEVQQvlvpaerlvkgmkeqmsgfWARMKELRRQAQEEQAqamQARQLAEGASQQAMN 1069
Cdd:COG4913 734 DRLEAAEDLARLELraLLEERFAAALG-------------------DAVERELRENLEERID---ALRARLNRAEEELER 791
|
....*..
gi 568911959 1070 AQEGFKR 1076
Cdd:COG4913 792 AMRAFNR 798
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
843-1072 |
1.95e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 843 QQTR-----QMIRAAEEAASRVQAD---AQRLETQVSTSRllMEEDVQRTRLLIQQVRgfLTDPDTDAATIQQVSEAVLA 914
Cdd:COG3096 408 QQTRaiqyqQAVQALEKARALCGLPdltPENAEDYLAAFR--AKEQQATEEVLELEQK--LSVADAARRQFEKAYELVCK 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 915 LWLPTDSAT-------VLRKMKEIQAIAARLPNVDSVLSQTKQDIAR---ARRLQAEAEQARSRAHAVEGQVDDVvgnlr 984
Cdd:COG3096 484 IAGEVERSQawqtareLLRRYRSQQALAQRLQQLRAQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEEL----- 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 985 qgtvaLQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaerlvkgmkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGAS 1064
Cdd:COG3096 559 -----LAELEAQLEELEEQAAEAVEQRSELRQQL-----------EQLR---ARIKELAARAPAWLAAQDALERLREQSG 619
|
....*...
gi 568911959 1065 QQAMNAQE 1072
Cdd:COG3096 620 EALADSQE 627
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
828-1078 |
2.33e-04 |
|
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: 44.20 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRtrllIQQVRGfltdpdtdaaTIQQ 907
Cdd:smart00283 13 AEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITA----MDQIRE----------VVEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 908 VSEAVLALwlptdsatvLRKMKEIQAIAArlpNVDSVLSQTkqDI---------ARA--------------RRL----QA 960
Cdd:smart00283 79 AVSAVEEL---------EESSDEIGEIVS---VIDDIADQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 961 EAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaERLVKGMKEQMSG---FWA 1037
Cdd:smart00283 145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQAAGseeVNA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568911959 1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:smart00283 222 AIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
929-1111 |
3.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 929 KEIQAIAARLPNVDSVLSQTKQDIaraRRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGR----SL 1004
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRI---RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1005 RLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQamnaQEGFKRLKQKYTEL 1084
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE----RAALEALKAERQKL 200
|
170 180
....*....|....*....|....*..
gi 568911959 1085 KDRLGQSpvLGEQGNRILSIKMEAEEL 1111
Cdd:COG4942 201 LARLEKE--LAELAAELAELQQEAEEL 225
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
830-1090 |
3.93e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAE-QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVstSRLLMEEDVQ---RTRLLIQQVRGFLTDPDTDAati 905
Cdd:pfam01576 688 RALEqQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF--ERDLQARDEQgeeKRRQLVKQVRELEAELEDER--- 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 906 QQVSEAVLA----------LWLPTDSAT--------VLRK----MKEIQ-----AIAARlpnvDSVLSQTKQDIARARRL 958
Cdd:pfam01576 763 KQRAQAVAAkkkleldlkeLEAQIDAANkgreeavkQLKKlqaqMKDLQreleeARASR----DEILAQSKESEKKLKNL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 959 QAE----------AEQARSRAHAVEGQVDDVVGNLRQGTVALQ------------------EAQDTMQGTGRSLRLIQER 1010
Cdd:pfam01576 839 EAEllqlqedlaaSERARRQAQQERDELADEIASGASGKSALQdekrrleariaqleeeleEEQSNTELLNDRLRKSTLQ 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1011 VGEVQQVLVpAERL----VKGMKEQMSgfwARMKELRRQAQEEQAQ----------AMQAR--QLAEGASQQAMNAQEGF 1074
Cdd:pfam01576 919 VEQLTTELA-AERStsqkSESARQQLE---RQNKELKAKLQEMEGTvkskfkssiaALEAKiaQLEEQLEQESRERQAAN 994
|
330
....*....|....*.
gi 568911959 1075 KRLKQKYTELKDRLGQ 1090
Cdd:pfam01576 995 KLVRRTEKKLKEVLLQ 1010
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
952-1155 |
7.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 952 IARARRLQAEAEQARSRAHAVEGQVDdvvgnlrqgtvALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERL--VKGMK 1029
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLE-----------ALEAELDALQERREALQRLAEYSWDEIDVASAEREIaeLEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1030 EQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRIlsikmEAE 1109
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-----LLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568911959 1110 ELFGEtmemmDKMKDMESELLRG-SQAIMLRSADLSGLEKRVEQIRS 1155
Cdd:COG4913 753 ERFAA-----ALGDAVERELRENlEERIDALRARLNRAEEELERAMR 794
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
313-366 |
8.92e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 8.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 313 CDCNG---HSETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRNRRPS 366
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1090 |
9.67e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFltdpdtdaatIQQVSEAVLAlwlptds 921
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----------LSSLEQEIEN------- 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 922 atvlrKMKEIQAIAARLPNVDSVLSQTKQDIA---------RARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQE 992
Cdd:TIGR02169 756 -----VKSELKELEARIEELEEDLHKLEEALNdlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 993 AQDTMQGTGRSLRLIQERVGEVQQvlvpAERLVKGMKEQMSG-----------FWARMKELRRQAQEEQAQAMQARQLAE 1061
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEK----EIENLNGKKEELEEeleeleaalrdLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|....*....
gi 568911959 1062 GASQQAMNAQEGFKRLKQKYTELKDRLGQ 1090
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
830-1112 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSrllmEEDVQRTRLLIQQVRgfltdpdtdaATIQQVS 909
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL----NEQLQAAQAELAQAQ----------EELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 910 EAvlalwlptdsATVLRkmKEIQAIAARLPNVDSVLSQTKQDIArarRLQAEAEQARSRAHAVEGQVDdvvgNLRQGTVA 989
Cdd:COG4372 108 EE----------AEELQ--EELEELQKERQDLEQQRKQLEAQIA---ELQSEIAEREEELKELEEQLE----SLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 990 LQEAQDTMqgtgrslrLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAM-------QARQLAEG 1062
Cdd:COG4372 169 LEQELQAL--------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsleaklgLALSALLD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568911959 1063 ASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAEELF 1112
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
817-1112 |
1.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 817 ALPRAKGAFHMAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllmEEDVQRTRLLIQQVRGFLT 896
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 897 DPDTDAATIQQVSEAVLAlwLPTDSATVLRKMKEIQAIAARLPNVDSV-LSQTKQDI----ARARRLQAEAEQARSRAHA 971
Cdd:COG4717 147 RLEELEERLEELRELEEE--LEELEAELAELQEELEELLEQLSLATEEeLQDLAEELeelqQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 972 VEGQVDDVVGNLRQGTVA--LQEAQDT---------MQGTGRSLRLIQERVGEVQQVLVPA----------ERLVKGMKE 1030
Cdd:COG4717 225 LEEELEQLENELEAAALEerLKEARLLlliaaallaLLGLGGSLLSLILTIAGVLFLVLGLlallflllarEKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1031 QMSGFWARMKELRRQAQEEQAQAMQARQLAEGAS-QQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAE 1109
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
...
gi 568911959 1110 ELF 1112
Cdd:COG4717 385 EEL 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
840-1063 |
1.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 840 TQLQQTRQMIRAAEEAASRVQADAQRLETqvstsrllMEEDVQRTRLLIQQVRgfltdpdTDAATIQQVSEAvLALWlpt 919
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELR-------EELEKLEKLLQL-LPLY--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 920 dsatvlrkmKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDdvvgnlRQGTVALQEAQDTMQG 999
Cdd:COG4717 132 ---------QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911959 1000 TGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWarmKELRRQAQEEQAQAMQARQLAEGA 1063
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLE---NELEAAALEERLKEARLLLLIAAA 257
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
832-1065 |
1.44e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 832 AEQLRNFNT-QLQQTR-----------QMIRAAEEAASRVQADAQRLETQVSTS---RLLMEEDV--QRTRLLIQQVRGF 894
Cdd:NF041483 238 AEQLRSSTAaESDQARrqaaelsraaeQRMQEAEEALREARAEAEKVVAEAKEAaakQLASAESAneQRTRTAKEEIARL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 895 LTDPDTDAATIQQVSEAVLA------------------LWLPTDSATVLRKmkeiqaiAARlpNVDSVLSQTKQDiARAR 956
Cdd:NF041483 318 VGEATKEAEALKAEAEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKAT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 957 -----------RLQAEAEQARSRAHAVE------GQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliQERVGE------ 1013
Cdd:NF041483 388 traaaeeaeriRREAEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirg 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911959 1014 ------VQQV---LVPAERLVKGMK----EQMSGFWA-----------RMKELRRQAQE--EQAQAMQARQLAEGASQ 1065
Cdd:NF041483 466 earreaVQQIeeaARTAEELLTKAKadadELRSTATAeservrteaieRATTLRRQAEEtlERTRAEAERLRAEAEEQ 543
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
831-1069 |
1.52e-03 |
|
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: 42.85 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 831 VAEQLRNfntQLQQTRQMIraAEEAA------SRVQADAQRLETQVSTsrllMEEDVQ-----------RTRLLIQQVRG 893
Cdd:pfam01576 851 ASERARR---QAQQERDEL--ADEIAsgasgkSALQDEKRRLEARIAQ----LEEELEeeqsntellndRLRKSTLQVEQ 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 894 FLTDPDTDAATIQQVSEAvlalwlptdSATVLRKMKEIQAiaaRLPNVDS-VLSQTKQDIARarrLQAEAEQArsrahav 972
Cdd:pfam01576 922 LTTELAAERSTSQKSESA---------RQQLERQNKELKA---KLQEMEGtVKSKFKSSIAA---LEAKIAQL------- 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 973 EGQVDdvvgnlrqgtvalQEAQDTmQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQ--EEQ 1050
Cdd:pfam01576 980 EEQLE-------------QESRER-QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEeaEEE 1045
|
250 260
....*....|....*....|....*.
gi 568911959 1051 AQAMQA------RQLAEGA-SQQAMN 1069
Cdd:pfam01576 1046 ASRANAarrklqRELDDATeSNESMN 1071
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
929-1111 |
1.59e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 929 KEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQ 1008
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1009 ERVGEVQQVLVPAERLVKgMKEQMSGFWARMKELRRQAQ--EEQAQAMQaRQLAEGASQqamnaQEGFKRLKQKYTELKD 1086
Cdd:PRK03918 280 EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSrlEEEINGIE-ERIKELEEK-----EERLEELKKKLKELEK 352
|
170 180
....*....|....*....|....*
gi 568911959 1087 RLGQSPVLGEQGNRILSIKMEAEEL 1111
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKEELERL 377
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
852-1090 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 852 AEEAASRVQADAQRLETQVStsrllmeeDVQRTrLLIQQVRgfltdpdtdAATIQQVSEAvlalwlptdsatvLRKMKEI 931
Cdd:COG3096 380 AEARLEAAEEEVDSLKSQLA--------DYQQA-LDVQQTR---------AIQYQQAVQA-------------LEKARAL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 932 QAIAARLP-NVDSVL--SQTKQDIARARRLQAE-----AEQARSRAHAVEGQVDDVVGNLRQGTvALQEAQDTMQgTGRS 1003
Cdd:COG3096 429 CGLPDLTPeNAEDYLaaFRAKEQQATEEVLELEqklsvADAARRQFEKAYELVCKIAGEVERSQ-AWQTARELLR-RYRS 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 1004 LRLIQERVGEVQQVLVPAERLV---KGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQK 1080
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
250
....*....|
gi 568911959 1081 YTELKDRLGQ 1090
Cdd:COG3096 587 LEQLRARIKE 596
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
966-1086 |
2.48e-03 |
|
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: 40.82 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 966 RSRAHAVEGQVDDVVGNLRQgtvALQEAQDTMQGTGRSL-------RLIQERVGEVQQVlvpAERLVKGMKEQMSG---- 1034
Cdd:pfam04012 10 RANIHEGLDKAEDPEKMLEQ---AIRDMQSELVKARQALaqtiarqKQLERRLEQQTEQ---AKKLEEKAQAALTKgnee 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568911959 1035 ----FWARMKELRRQAQEEQAQAMQARQLAEgasqqamNAQEGFKRLKQKYTELKD 1086
Cdd:pfam04012 84 lareALAEKKSLEKQAEALETQLAQQRSAVE-------QLRKQLAALETKIQQLKA 132
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
842-1084 |
2.96e-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: 41.86 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRllmeEDVQRTRLLIQQVRgfLTDPDTDAATIQQVSEAVLALwlptDS 921
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLK----EQLQLLNKLLPQAN--LLADETLADRLEELREELDAA----QE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 922 AtvlrkMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQV---DDVVGNLRQgtVALQEAQDtMQ 998
Cdd:COG3096 908 A-----QAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPH--FSYEDAVG-LL 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 999 GTGRSLrliqerVGEVQQVLVPAERLVKGMKEQMsgfwarmkelrRQAQEEQAQAMQARQLAEGASQqamNAQEGFKRLK 1078
Cdd:COG3096 980 GENSDL------NEKLRARLEQAEEARREAREQL-----------RQAQAQYSQYNQVLASLKSSRD---AKQQTLQELE 1039
|
....*.
gi 568911959 1079 QKYTEL 1084
Cdd:COG3096 1040 QELEEL 1045
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
830-1105 |
2.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVS 909
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 910 EAVLALWlptDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQ-AEAEQARSRAHAVEGQVDDVVGNLRQGTV 988
Cdd:COG4372 157 EQLESLQ---EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAeAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 989 ALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAM 1068
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
250 260 270
....*....|....*....|....*....|....*..
gi 568911959 1069 NAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIK 1105
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
828-1088 |
4.48e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 828 AGRVAEQLRNFNTQLQ-QTRQMI----RAAEEAASRVQADAQ----RLETQVSTSRLLMEEDVQRTRLLIQQvrgfltdp 898
Cdd:NF041483 773 AEQTAQQVRDSVAGLQeQAEEEIaglrSAAEHAAERTRTEAQeeadRVRSDAYAERERASEDANRLRREAQE-------- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 899 DTDAATI---QQVSEAVlalwlptDSATVLRKMKEIQAIAARLPNVDSvLSQTKQDIARARrlqAEA-EQARSRAHAVEG 974
Cdd:NF041483 845 ETEAAKAlaeRTVSEAI-------AEAERLRSDASEYAQRVRTEASDT-LASAEQDAARTR---ADArEDANRIRSDAAA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 975 QVDDVVGNLRQGTVALQEAqdtmqGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARmkeLRRQAQEEQAQAM 1054
Cdd:NF041483 914 QADRLIGEATSEAERLTAE-----ARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER---LRAEAAETVGSAQ 985
|
250 260 270
....*....|....*....|....*....|....*.
gi 568911959 1055 QA--RQLAEGASQQAMNAQEGfKRLKQKYTELKDRL 1088
Cdd:NF041483 986 QHaeRIRTEAERVKAEAAAEA-ERLRTEAREEADRT 1020
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
827-1110 |
6.07e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRL--ETQVSTSRLLMEEdVQRTRLLIQQVRG----FLTDPDT 900
Cdd:NF041483 566 IAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIrrEAAEETERLRTEA-AERIRTLQAQAEQeaerLRTEAAA 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 901 DAATIQQVSEAVlALWLPTDSATVLRKMK------------EIQAIAARLPN-VDSVLSQTKQDIARARR--------LQ 959
Cdd:NF041483 645 DASAARAEGENV-AVRLRSEAAAEAERLKseaqesadrvraEAAAAAERVGTeAAEALAAAQEEAARRRReaeetlgsAR 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 960 AEAEQARSRAHAvegQVDDVVGNLRQgtvALQEAQDTMQgtgrslRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwarm 1039
Cdd:NF041483 724 AEADQERERARE---QSEELLASARK---RVEEAQAEAQ------RLVEEADRRATELVSAAEQTAQQVRDSVAG----- 786
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911959 1040 keLRRQAQEEQAqamQARQLAEGASQQA-MNAQEGFKRLKQKYTELKDRlgqspvLGEQGNRILSIKMEAEE 1110
Cdd:NF041483 787 --LQEQAEEEIA---GLRSAAEHAAERTrTEAQEEADRVRSDAYAERER------ASEDANRLRREAQEETE 847
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
945-1090 |
7.09e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 945 LSQTKQDIARAR-----------RLQAEAEQARsRAHAVEGQVDdvvgnLRQGTVALQEaqdtmqgtgrsLRLIQERVGE 1013
Cdd:COG1196 181 LEATEENLERLEdilgelerqlePLERQAEKAE-RYRELKEELK-----ELEAELLLLK-----------LRELEAELEE 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911959 1014 VQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQ 1090
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
842-998 |
8.80e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQ-----VRGFLTDpdtdAATIQQVSEAVLALW 916
Cdd:COG1842 32 IRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALER----KAELEAQAEALEAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 917 lpTDSATVLRKMKE-IQAIAARLPNVdsvlsQTKQDIARARRLQAEAEQARSRAHAvEGQVDDVVGNLRQgtvaLQEAQD 995
Cdd:COG1842 108 --AQLEEQVEKLKEaLRQLESKLEEL-----KAKKDTLKARAKAAKAQEKVNEALS-GIDSDDATSALER----MEEKIE 175
|
...
gi 568911959 996 TMQ 998
Cdd:COG1842 176 EME 178
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
829-1100 |
9.14e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 829 GRVAEQLRNFNTQLQQT----RQMIRAAEEAASRVQADAQRLetqvstSRLLMEEDvqRTRLLIQQV---RGFLTDPDTD 901
Cdd:PRK10246 307 AHTRQQIEEVNTRLQSTmalrARIRHHAAKQSAELQAQQQSL------NTWLAEHD--RFRQWNNELagwRAQFSQQTSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 902 AATIQQVSEAVLALwlptdsatvlrkmkeIQAIAArLPnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVG 981
Cdd:PRK10246 379 REQLRQWQQQLTHA---------------EQKLNA-LP--AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQK 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911959 982 NLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPaerlVKGMKEQMsgfwARMKELRRQ-AQEEQAQ-------- 1052
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD----VKTICEQE----ARIKDLEAQrAQLQAGQpcplcgst 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568911959 1053 ---AMQARQ-LAEGASQQAMNAQEgfKRLKQKYTELKDRLGQSPVLGEQGNR 1100
Cdd:PRK10246 513 shpAVEAYQaLEPGVNQSRLDALE--KEVKKLGEEGAALRGQLDALTKQLQR 562
|
|
| |
