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Conserved domains on  [gi|1981299054|ref|WP_203212406|]
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prepilin-type N-terminal cleavage/methylation domain-containing protein [Sulfitobacter mediterraneus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
1-70 1.03e-13

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


:

Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 64.27  E-value: 1.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054   1 MTPRPARAgdAGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERTDGRLERLSDIDRGFLLLRRDLMQM 70
Cdd:COG4795     1 MKRARRRQ--RGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQELQRALALLERDLRQA 68
T2SSJ super family cl42010
Type II secretion system (T2SS), protein J; The T2SJ proteins are pseudopilins, which are ...
11-161 3.57e-12

Type II secretion system (T2SS), protein J; The T2SJ proteins are pseudopilins, which are targeted to the membrane in E. Coli. T2SJ forms a complex with T2SI (pfam02501) and T2SK (pfam03934) which is part of the Type II secretion apparatus involved in the translocation of proteins across the outer membrane in E.coli. The T2SK-I-J complex has quasihelical characteriztics.


The actual alignment was detected with superfamily member TIGR01711:

Pssm-ID: 455355 [Multi-domain]  Cd Length: 192  Bit Score: 61.85  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054  11 AGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERTDGRLERLSDIDRGFLLLRRDLMQMDGLSARLNRGA----LQFRR 86
Cdd:TIGR01711   1 RGFTLLELLVAIAIFASLSLGAYQVLDSVMQSDEATRVQEARLRELQRAMGAMERDLTQMVERPVRDDGEAseqdLRGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054  87 PSEER------FVFLTYLADDDAFQR-------------RIE---------VATNEPIGQRLIEKTLSADWQLMDgTGRW 138
Cdd:TIGR01711  81 LSEGSddqgveFTRGGWRNPLGQQPRsrlqrvgwrlsgeTLErrywlypdrAQGSKPRIQPVLDGVTALSWRFYD-KGNW 159
                         170       180
                  ....*....|....*....|...
gi 1981299054 139 HSAWPPRGApqRPHAAELSLSLR 161
Cdd:TIGR01711 160 QGEWPTDNS--LPLAVEVTLELR 180
 
Name Accession Description Interval E-value
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
1-70 1.03e-13

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 64.27  E-value: 1.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054   1 MTPRPARAgdAGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERTDGRLERLSDIDRGFLLLRRDLMQM 70
Cdd:COG4795     1 MKRARRRQ--RGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQELQRALALLERDLRQA 68
gspJ TIGR01711
type II secretion system protein J; This model represents GspJ, one of two proteins highly ...
11-161 3.57e-12

type II secretion system protein J; This model represents GspJ, one of two proteins highly conserved at their N-termini and described by pfam02501 but easily separable phylogenetically. The other is GspI. Both GspI and GspJ are proteins of the type II secretion pathway, or main terminal branch of the general secretion pathway. This pathway carries proteins across the outer membrane. Note that proteins of type II secretion are cryptic in E. coli K-12 - present but not yet demonstrated to act on any target.


Pssm-ID: 130772 [Multi-domain]  Cd Length: 192  Bit Score: 61.85  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054  11 AGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERTDGRLERLSDIDRGFLLLRRDLMQMDGLSARLNRGA----LQFRR 86
Cdd:TIGR01711   1 RGFTLLELLVAIAIFASLSLGAYQVLDSVMQSDEATRVQEARLRELQRAMGAMERDLTQMVERPVRDDGEAseqdLRGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054  87 PSEER------FVFLTYLADDDAFQR-------------RIE---------VATNEPIGQRLIEKTLSADWQLMDgTGRW 138
Cdd:TIGR01711  81 LSEGSddqgveFTRGGWRNPLGQQPRsrlqrvgwrlsgeTLErrywlypdrAQGSKPRIQPVLDGVTALSWRFYD-KGNW 159
                         170       180
                  ....*....|....*....|...
gi 1981299054 139 HSAWPPRGApqRPHAAELSLSLR 161
Cdd:TIGR01711 160 QGEWPTDNS--LPLAVEVTLELR 180
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
7-33 1.21e-03

Prokaryotic N-terminal methylation motif; This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N-terminus of pilins and other proteins involved in secretion, see pfam00114, pfam05946, pfam02501 and pfam07596.


Pssm-ID: 429756 [Multi-domain]  Cd Length: 27  Bit Score: 35.04  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....*..
gi 1981299054   7 RAGDAGVSLIEVLVSLAIFAIIGVAGL 33
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
10-33 8.11e-03

prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all examples of the N-terminal region of bacterial proteins that resemble type IV pilins at their N-terminus, with a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue, usually Phe, is methylated. Separate domains of the prepilin peptidase appear responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this N-terminal domain. The N-terminal cleavage and methylation site is described by PROSITE motif PS00409 as [KRHEQSTAG]-G-[FYLIVM]-[ST]-[LT]-[LIVP]-E-[LIVMFWSTAG](14). [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274182 [Multi-domain]  Cd Length: 24  Bit Score: 32.66  E-value: 8.11e-03
                          10        20
                  ....*....|....*....|....
gi 1981299054  10 DAGVSLIEVLVSLAIFAIIGVAGL 33
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
 
Name Accession Description Interval E-value
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
1-70 1.03e-13

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 64.27  E-value: 1.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054   1 MTPRPARAgdAGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERTDGRLERLSDIDRGFLLLRRDLMQM 70
Cdd:COG4795     1 MKRARRRQ--RGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQELQRALALLERDLRQA 68
gspJ TIGR01711
type II secretion system protein J; This model represents GspJ, one of two proteins highly ...
11-161 3.57e-12

type II secretion system protein J; This model represents GspJ, one of two proteins highly conserved at their N-termini and described by pfam02501 but easily separable phylogenetically. The other is GspI. Both GspI and GspJ are proteins of the type II secretion pathway, or main terminal branch of the general secretion pathway. This pathway carries proteins across the outer membrane. Note that proteins of type II secretion are cryptic in E. coli K-12 - present but not yet demonstrated to act on any target.


Pssm-ID: 130772 [Multi-domain]  Cd Length: 192  Bit Score: 61.85  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054  11 AGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERTDGRLERLSDIDRGFLLLRRDLMQMDGLSARLNRGA----LQFRR 86
Cdd:TIGR01711   1 RGFTLLELLVAIAIFASLSLGAYQVLDSVMQSDEATRVQEARLRELQRAMGAMERDLTQMVERPVRDDGEAseqdLRGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981299054  87 PSEER------FVFLTYLADDDAFQR-------------RIE---------VATNEPIGQRLIEKTLSADWQLMDgTGRW 138
Cdd:TIGR01711  81 LSEGSddqgveFTRGGWRNPLGQQPRsrlqrvgwrlsgeTLErrywlypdrAQGSKPRIQPVLDGVTALSWRFYD-KGNW 159
                         170       180
                  ....*....|....*....|...
gi 1981299054 139 HSAWPPRGApqRPHAAELSLSLR 161
Cdd:TIGR01711 160 QGEWPTDNS--LPLAVEVTLELR 180
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
1-46 2.83e-06

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


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 43.43  E-value: 2.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1981299054   1 MTPRPARAGDAGVSLIEVLVSLAIFAiIGVAGLAVLDTVSRTGERT 46
Cdd:COG4967     1 MSRRRRRRRQRGFTLIEVLVALVILS-IGLLGLAGLQAASLRSSQD 45
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
1-46 4.01e-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: 4.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1981299054   1 MTPRPARAGDAGVSLIEVLVSLAIFAIIGVAGLAVLDTVSRTGERT 46
Cdd:COG2165     1 MKLRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRA 46
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
7-33 1.21e-03

Prokaryotic N-terminal methylation motif; This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N-terminus of pilins and other proteins involved in secretion, see pfam00114, pfam05946, pfam02501 and pfam07596.


Pssm-ID: 429756 [Multi-domain]  Cd Length: 27  Bit Score: 35.04  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....*..
gi 1981299054   7 RAGDAGVSLIEVLVSLAIFAIIGVAGL 33
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
10-33 8.11e-03

prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all examples of the N-terminal region of bacterial proteins that resemble type IV pilins at their N-terminus, with a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue, usually Phe, is methylated. Separate domains of the prepilin peptidase appear responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this N-terminal domain. The N-terminal cleavage and methylation site is described by PROSITE motif PS00409 as [KRHEQSTAG]-G-[FYLIVM]-[ST]-[LT]-[LIVP]-E-[LIVMFWSTAG](14). [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274182 [Multi-domain]  Cd Length: 24  Bit Score: 32.66  E-value: 8.11e-03
                          10        20
                  ....*....|....*....|....
gi 1981299054  10 DAGVSLIEVLVSLAIFAIIGVAGL 33
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
 
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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