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Conserved domains on  [gi|501336683|ref|WP_012368318|]
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MULTISPECIES: prepilin-type N-terminal cleavage/methylation domain-containing protein [Proteus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10506 super family cl26825
prepilin peptidase-dependent protein;
4-159 5.28e-24

prepilin peptidase-dependent protein;


The actual alignment was detected with superfamily member PRK10506:

Pssm-ID: 236704 [Multi-domain]  Cd Length: 162  Bit Score: 91.21  E-value: 5.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501336683   4 NHYSHSKHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQLVQSVREVMAFLAYQQQRSLLFNckVQIVLWLSPINKL 83
Cdd:PRK10506   1 MKRSMKKQRGYTLIELLVVMTIVSILSAWGLYGWQRWQQRQRLWQTAQQLLDFLLRLQEDANWHN--RDHILWLIREGQG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501336683  84 ---------------EAKSLTTPTTKESIqlglnnqLIRSTATRFTFCGLRQTLRPMHFVLSNGDEEVKIIISSLGRIRA 148
Cdd:PRK10506  79 wclvssvagantctgSSPFVFTPPWPDVA-------LASDTTPSLAFYGLRNTAWAGHIRLKNSAGEWRLVISSRGRIRL 151
                        170
                 ....*....|.
gi 501336683 149 CSQTIKAFSVC 159
Cdd:PRK10506 152 CSEGESEGPLC 162
 
Name Accession Description Interval E-value
PRK10506 PRK10506
prepilin peptidase-dependent protein;
4-159 5.28e-24

prepilin peptidase-dependent protein;


Pssm-ID: 236704 [Multi-domain]  Cd Length: 162  Bit Score: 91.21  E-value: 5.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501336683   4 NHYSHSKHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQLVQSVREVMAFLAYQQQRSLLFNckVQIVLWLSPINKL 83
Cdd:PRK10506   1 MKRSMKKQRGYTLIELLVVMTIVSILSAWGLYGWQRWQQRQRLWQTAQQLLDFLLRLQEDANWHN--RDHILWLIREGQG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501336683  84 ---------------EAKSLTTPTTKESIqlglnnqLIRSTATRFTFCGLRQTLRPMHFVLSNGDEEVKIIISSLGRIRA 148
Cdd:PRK10506  79 wclvssvagantctgSSPFVFTPPWPDVA-------LASDTTPSLAFYGLRNTAWAGHIRLKNSAGEWRLVISSRGRIRL 151
                        170
                 ....*....|.
gi 501336683 149 CSQTIKAFSVC 159
Cdd:PRK10506 152 CSEGESEGPLC 162
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
7-73 5.57e-11

Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 55.24  E-value: 5.57e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501336683   7 SHSKHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQLVQSVREVMAFLAYQQQRSLLFNCKVQI 73
Cdd:COG4970    4 LRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALRLARSEAIRRGQPVTL 70
 
Name Accession Description Interval E-value
PRK10506 PRK10506
prepilin peptidase-dependent protein;
4-159 5.28e-24

prepilin peptidase-dependent protein;


Pssm-ID: 236704 [Multi-domain]  Cd Length: 162  Bit Score: 91.21  E-value: 5.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501336683   4 NHYSHSKHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQLVQSVREVMAFLAYQQQRSLLFNckVQIVLWLSPINKL 83
Cdd:PRK10506   1 MKRSMKKQRGYTLIELLVVMTIVSILSAWGLYGWQRWQQRQRLWQTAQQLLDFLLRLQEDANWHN--RDHILWLIREGQG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501336683  84 ---------------EAKSLTTPTTKESIqlglnnqLIRSTATRFTFCGLRQTLRPMHFVLSNGDEEVKIIISSLGRIRA 148
Cdd:PRK10506  79 wclvssvagantctgSSPFVFTPPWPDVA-------LASDTTPSLAFYGLRNTAWAGHIRLKNSAGEWRLVISSRGRIRL 151
                        170
                 ....*....|.
gi 501336683 149 CSQTIKAFSVC 159
Cdd:PRK10506 152 CSEGESEGPLC 162
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
7-73 5.57e-11

Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 55.24  E-value: 5.57e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501336683   7 SHSKHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQLVQSVREVMAFLAYQQQRSLLFNCKVQI 73
Cdd:COG4970    4 LRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALRLARSEAIRRGQPVTL 70
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
1-64 9.48e-06

Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 42.75  E-value: 9.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501336683   1 MTGNHYSHSKhlGSSLFEVLIVMAIVAILSALSLSSY-HQLLRQR--QLVQSVREVMAFLA--YQQQRS 64
Cdd:COG4968    1 MKKRMRRRQR--GFTLIELMIVVAIIGILAAIAIPSYqDYVERARraEAKAALLELAQAQEryYADNGS 67
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
7-58 2.53e-05

Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 41.15  E-value: 2.53e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501336683   7 SHSKHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQR-------QLVQSVREVMAFLA 58
Cdd:COG4795    4 ARRRQRGFTLLELLVALAIFALLLLAAYRGLDSVLRSRerleqqaERLQELQRALALLE 62
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
1-53 3.30e-05

Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 441768 [Multi-domain]  Cd Length: 99  Bit Score: 40.67  E-value: 3.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501336683   1 MTGNHYSHSKHlGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQLVQSVREV 53
Cdd:COG2165    1 MKLRRRRRRQR-GFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNL 52
PRK10574 PRK10574
putative major pilin subunit; Provisional
10-46 3.18e-04

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 38.86  E-value: 3.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 501336683  10 KHLGSSLFEVLIVMAIVAILSALSLSSYHQLLRQRQL 46
Cdd:PRK10574   3 KQRGFTLIELMVVIAIIAILSAIGIPAYQNYLQKAAL 39
PilA COG4969
Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];
13-37 8.06e-04

Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];


Pssm-ID: 443995 [Multi-domain]  Cd Length: 134  Bit Score: 37.38  E-value: 8.06e-04
                         10        20
                 ....*....|....*....|....*
gi 501336683  13 GSSLFEVLIVMAIVAILSALSLSSY 37
Cdd:COG4969    7 GFTLIELMIVVAIIGILAAIAIPAY 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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