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Conserved domains on  [gi|665842787|ref|WP_031210904|]
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MULTISPECIES: type II secretion system major pseudopilin GspG [Marinobacter]

Protein Classification

type II secretion system protein GspG( domain architecture ID 11493055)

type II secretion system protein GspG is involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins; required for the translocation of a variety of enzymes across the outer membrane

Gene Ontology:  GO:0015628

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
typeII_sec_gspG TIGR01710
type II secretion system protein G; This model represents GspG, protein G of the main terminal ...
 11-145 1.15e-70

type II secretion system protein G; This model represents GspG, protein G of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


:

Pssm-ID: 130771 [Multi-domain]  Cd Length: 134  Bit Score: 208.82  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   11 KGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALVNKPSGSPEPK 90
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665842787   91 NWnPDGYLKNVPEDPWGNNYQYVSPGVDGPYDLYSYGSDGQEGGDGDAADISVWD 145
Cdd:TIGR01710  81 NW-HGGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNWD 134
 
Name Accession Description Interval E-value
typeII_sec_gspG TIGR01710
type II secretion system protein G; This model represents GspG, protein G of the main terminal ...
 11-145 1.15e-70

type II secretion system protein G; This model represents GspG, protein G of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 130771 [Multi-domain]  Cd Length: 134  Bit Score: 208.82  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   11 KGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALVNKPSGSPEPK 90
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665842787   91 NWnPDGYLKNVPEDPWGNNYQYVSPGVDGPYDLYSYGSDGQEGGDGDAADISVWD 145
Cdd:TIGR01710  81 NW-HGGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNWD 134
T2SSG pfam08334
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
 37-144 6.93e-58

Type II secretion system (T2SS), protein G; The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria. The T2SG family includes proteins such as EpsG (P45773) in Vibrio cholera, XcpT also called PddA (Q00514) in Pseudomonas aeruginosa or PulG (P15746)in Klebsiella pneumoniae. The PulG is thought to be anchored in the inner membrane with its C-terminus directed towards the periplasme. Together with other members of the Type II secretion machinery, it is thought to assemble into a pilus-like structure that may function as a dynamic mechanism to push secreted proteins out of the cell. The polypeptide is organized into a long N-terminal alpha-helix followed by a loop region that separates it from a C-terminal anti-parallel beta-sheet.


Pssm-ID: 429925  Cd Length: 106  Bit Score: 175.45  E-value: 6.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   37 MGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALVNKPSGspEPKNWNpDGYL-KNVPEDPWGNNYQYVSP 115
Cdd:pfam08334   1 LGQLDKAKVKKAKAQIASLESALDLYRLDNGRYPTTEQGLAALVEKPSG--APANWN-GPYLkKRLPKDPWGNPYQYRSP 77

                          90       100
                  ....*....|....*....|....*....
gi 665842787  116 GVDGPYDLYSYGSDGQEGGDGDAADISVW 144
Cdd:pfam08334  78 GEHGPFDLFSLGADGQPGGEGEDADIGNW 106
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-107 2.04e-30

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: 105.38  E-value: 2.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   1 MNQPKALARTKGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALv 80
Cdd:COG2165    1 MKLRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYPSSLTGLLAD- 79

                         90       100
                 ....*....|....*....|....*..
gi 665842787  81 nkpsgspepknWNPDGYLKNVPEDPWG 107
Cdd:COG2165   80 -----------VRGGGYLGSNGLPPAG 95
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 11-74 2.01e-12

competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues.


Pssm-ID: 468929  Cd Length: 84  Bit Score: 59.06  E-value: 2.01e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665842787  11 KGFTLIEIMVVMVILGLLVAIVAPNIM-------GRSDQAKVTVAETQIsnianalDLYRLDNSHYPSTQQ 74
Cdd:NF040999   2 KGFTLIEMLIVLLIISVLLLLFVPNLSkqkesvqEKGCEAVVKVVESQV-------ELYELDHNKKPSLSE 65
PRK10574 PRK10574
putative major pilin subunit; Provisional
 9-34 4.67e-05

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 40.79  E-value: 4.67e-05
                         10        20
                 ....*....|....*....|....*.
gi 665842787   9 RTKGFTLIEIMVVMVILGLLVAIVAP 34
Cdd:PRK10574   3 KQRGFTLIELMVVIAIIAILSAIGIP 28
T4P_ComGE NF041013
competence type IV pilus minor pilin ComGE;
11-53 3.05e-04

competence type IV pilus minor pilin ComGE;


Pssm-ID: 468942 [Multi-domain]  Cd Length: 83  Bit Score: 37.56  E-value: 3.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665842787  11 KGFTLIEIMVVMVILGLLVAIVAPNIMG--------RSDQAKVTVAETQIS 53
Cdd:NF041013   4 KGFILLESLVALALLALIVSLLLPSLTQiqkereeiKQKEEALQVLYEALQ 54
 
Name Accession Description Interval E-value
typeII_sec_gspG TIGR01710
type II secretion system protein G; This model represents GspG, protein G of the main terminal ...
 11-145 1.15e-70

type II secretion system protein G; This model represents GspG, protein G of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 130771 [Multi-domain]  Cd Length: 134  Bit Score: 208.82  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   11 KGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALVNKPSGSPEPK 90
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665842787   91 NWnPDGYLKNVPEDPWGNNYQYVSPGVDGPYDLYSYGSDGQEGGDGDAADISVWD 145
Cdd:TIGR01710  81 NW-HGGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNWD 134
T2SSG pfam08334
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
 37-144 6.93e-58

Type II secretion system (T2SS), protein G; The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria. The T2SG family includes proteins such as EpsG (P45773) in Vibrio cholera, XcpT also called PddA (Q00514) in Pseudomonas aeruginosa or PulG (P15746)in Klebsiella pneumoniae. The PulG is thought to be anchored in the inner membrane with its C-terminus directed towards the periplasme. Together with other members of the Type II secretion machinery, it is thought to assemble into a pilus-like structure that may function as a dynamic mechanism to push secreted proteins out of the cell. The polypeptide is organized into a long N-terminal alpha-helix followed by a loop region that separates it from a C-terminal anti-parallel beta-sheet.


Pssm-ID: 429925  Cd Length: 106  Bit Score: 175.45  E-value: 6.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   37 MGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALVNKPSGspEPKNWNpDGYL-KNVPEDPWGNNYQYVSP 115
Cdd:pfam08334   1 LGQLDKAKVKKAKAQIASLESALDLYRLDNGRYPTTEQGLAALVEKPSG--APANWN-GPYLkKRLPKDPWGNPYQYRSP 77

                          90       100
                  ....*....|....*....|....*....
gi 665842787  116 GVDGPYDLYSYGSDGQEGGDGDAADISVW 144
Cdd:pfam08334  78 GEHGPFDLFSLGADGQPGGEGEDADIGNW 106
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-107 2.04e-30

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: 105.38  E-value: 2.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   1 MNQPKALARTKGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQGLEALv 80
Cdd:COG2165    1 MKLRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYPSSLTGLLAD- 79

                         90       100
                 ....*....|....*....|....*..
gi 665842787  81 nkpsgspepknWNPDGYLKNVPEDPWG 107
Cdd:COG2165   80 -----------VRGGGYLGSNGLPPAG 95
ComGC COG4537
Competence protein ComGC [Mobilome: prophages, transposons];
1-116 2.16e-22

Competence protein ComGC [Mobilome: prophages, transposons];


Pssm-ID: 443603 [Multi-domain]  Cd Length: 108  Bit Score: 85.36  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665842787   1 MNQPKALARTKGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTqqgLEALV 80
Cdd:COG4537    2 KKKKRKLKKEKGFTLIEMLIVLLIISILLLIAVPNLTKQRETAQEKGCEANIKMVQSQVELYELDHGTYPAS---LEELV 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665842787  81 NkpsgspepknwnpDGYLKNV-PEDPWGNNYQYVSPG 116
Cdd:COG4537   79 D-------------EGYLKEKqPTCPNGGEYTIDSNG 102
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
1-72 6.39e-19

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


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 77.04  E-value: 6.39e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665842787   1 MNQpKALARTKGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPST 72
Cdd:COG4968    1 MKK-RMRRRQRGFTLIELMIVVAIIGILAAIAIPSYQDYVERARRAEAKAALLELAQAQERYYADNGSYPSA 71
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 11-74 2.01e-12

competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues.


Pssm-ID: 468929  Cd Length: 84  Bit Score: 59.06  E-value: 2.01e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665842787  11 KGFTLIEIMVVMVILGLLVAIVAPNIM-------GRSDQAKVTVAETQIsnianalDLYRLDNSHYPSTQQ 74
Cdd:NF040999   2 KGFTLIEMLIVLLIISVLLLLFVPNLSkqkesvqEKGCEAVVKVVESQV-------ELYELDHNKKPSLSE 65
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
1-54 3.40e-12

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 57.93  E-value: 3.40e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665842787   1 MNQPKAlaRTKGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISN 54
Cdd:COG4970    1 MKRLRR--RQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAA 52
PilA COG4969
Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];
11-75 3.21e-09

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


Pssm-ID: 443995 [Multi-domain]  Cd Length: 134  Bit Score: 52.02  E-value: 3.21e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665842787  11 KGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISNIANALDLYRLDNSHYPSTQQG 75
Cdd:COG4969    6 KGFTLIELMIVVAIIGILAAIAIPAYQDYVARARVSEALALASPLKTAVEECALENGSLPNCNAG 70
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
1-71 2.37e-08

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


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 48.44  E-value: 2.37e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665842787   1 MNQPKALARTKGFTLIEIMVVMVILGL-LVAIVA--PNIMGRSDQAKV-TVAETQISNIANALDLYRLDNSHYPS 71
Cdd:COG4967    1 MSRRRRRRRQRGFTLIEVLVALVILSIgLLGLAGlqAASLRSSQDARQrTQAALLAQDLLERLRANPAAAGSYPG 75
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 9-33 4.16e-08

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: 46.21  E-value: 4.16e-08
                          10        20
                  ....*....|....*....|....*
gi 665842787    9 RTKGFTLIEIMVVMVILGLLVAIVA 33
Cdd:pfam07963   3 KQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 10-33 1.48e-07

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: 44.99  E-value: 1.48e-07
                          10        20
                  ....*....|....*....|....
gi 665842787   10 TKGFTLIEIMVVMVILGLLVAIVA 33
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
typeII_sec_gspH TIGR01708
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
 9-53 2.31e-06

type II secretion system protein H; This model represents GspH, protein H of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 130769 [Multi-domain]  Cd Length: 143  Bit Score: 44.48  E-value: 2.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665842787    9 RTKGFTLIEIMVVMVILGLLVAIVAPNIMGRS------DQAKVTVAETQIS 53
Cdd:TIGR01708   2 RQSGFTLIELLVVLAIMGLVAAAAALSLVSHYgtksldQVAGRLAARLRLA 52
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 5-33 1.58e-05

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 41.54  E-value: 1.58e-05
                         10        20
                 ....*....|....*....|....*....
gi 665842787   5 KALARTKGFTLIEIMVVMVILGLLVAIVA 33
Cdd:COG4795    3 RARRRQRGFTLLELLVALAIFALLLLAAY 31
PilW COG4966
Type IV pilus assembly protein PilW [Cell motility, Extracellular structures];
7-61 3.55e-05

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


Pssm-ID: 443992 [Multi-domain]  Cd Length: 158  Bit Score: 41.32  E-value: 3.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665842787   7 LARTKGFTLIEIMVVMVIlGLLVAIVAPNIMGRSDQAKVT---VAETQiSNIANALDL 61
Cdd:COG4966    1 RRRQRGFTLVELMVALAI-GLIVLAAVLQLFLSSRRSYRTqeaLARLQ-ENGRFALDL 56
PRK10574 PRK10574
putative major pilin subunit; Provisional
 9-34 4.67e-05

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 40.79  E-value: 4.67e-05
                         10        20
                 ....*....|....*....|....*.
gi 665842787   9 RTKGFTLIEIMVVMVILGLLVAIVAP 34
Cdd:PRK10574   3 KQRGFTLIELMVVIAIIAILSAIGIP 28
T4P_ComGE NF041013
competence type IV pilus minor pilin ComGE;
11-53 3.05e-04

competence type IV pilus minor pilin ComGE;


Pssm-ID: 468942 [Multi-domain]  Cd Length: 83  Bit Score: 37.56  E-value: 3.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665842787  11 KGFTLIEIMVVMVILGLLVAIVAPNIMG--------RSDQAKVTVAETQIS 53
Cdd:NF041013   4 KGFILLESLVALALLALIVSLLLPSLTQiqkereeiKQKEEALQVLYEALQ 54
TIGR02596 TIGR02596
Verru_Chthon cassette protein D; This model describes a nearly twenty member protein family in ...
 13-54 1.37e-03

Verru_Chthon cassette protein D; This model describes a nearly twenty member protein family in Verrucomicrobium spinosum and a somewhat smaller paralogous family in Chthoniobacter flavus. All members share a type IV pilin-like N-terminal leader sequence (TIGR02532). These proteins occur in the four-gene Verru_Chthon cassette, in which two other genes likewise encode a cleavage/methylation domain. Most of these cassettes occur next to an unusually large PEP-CTERM protein with an autotransporter domain. [Cell envelope, Surface structures]


Pssm-ID: 274219 [Multi-domain]  Cd Length: 195  Bit Score: 37.07  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 665842787   13 FTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQISN 54
Cdd:TIGR02596   1 FTLVELLVVIAIAALLMALSTPVVNQVLAAQQLGSSATRLAN 42
PRK10506 PRK10506
prepilin peptidase-dependent protein;
9-30 3.32e-03

prepilin peptidase-dependent protein;


Pssm-ID: 236704 [Multi-domain]  Cd Length: 162  Bit Score: 35.74  E-value: 3.32e-03
                         10        20
                 ....*....|....*....|..
gi 665842787   9 RTKGFTLIEIMVVMVILGLLVA 30
Cdd:PRK10506   7 KQRGYTLIELLVVMTIVSILSA 28
ComGF COG4940
Competence protein ComGF [Mobilome: prophages, transposons];
5-53 7.17e-03

Competence protein ComGF [Mobilome: prophages, transposons];


Pssm-ID: 443967 [Multi-domain]  Cd Length: 153  Bit Score: 34.99  E-value: 7.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 665842787   5 KALARTKGFTLIEIMVVMVILGLLVAIVAPNIMGRSDQAKVTVAETQIS 53
Cdd:COG4940   10 AASINRKGFTLLEKLAALMIIAYILAVLELLLKLLLKLNQSLDAGEQIE 58
 
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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