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Conserved domains on  [gi|654544817|ref|WP_028012525|]
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MULTISPECIES: type II secretion system major pseudopilin GspG [Enterobacter]

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 ...
 13-142 1.52e-62

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: 188.02  E-value: 1.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   13 GFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQALVTKPEIAPIPNG 92
Cdd:TIGR01710   2 GFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPKN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 654544817   93 YRAdGYIRRLPQDPWGGDYILVSPGEHGAVDVFSAGPDGE---ANTADDITNW 142
Cdd:TIGR01710  82 WHG-GYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQpggKGTDADIGNW 133
 
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 ...
 13-142 1.52e-62

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: 188.02  E-value: 1.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   13 GFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQALVTKPEIAPIPNG 92
Cdd:TIGR01710   2 GFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPKN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 654544817   93 YRAdGYIRRLPQDPWGGDYILVSPGEHGAVDVFSAGPDGE---ANTADDITNW 142
Cdd:TIGR01710  82 WHG-GYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQpggKGTDADIGNW 133
T2SSG pfam08334
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
 38-142 3.01e-50

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: 156.19  E-value: 3.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   38 MGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQALVTKPEIApiPNGYrADGYIR-RLPQDPWGGDYILVSP 116
Cdd:pfam08334   1 LGQLDKAKVKKAKAQIASLESALDLYRLDNGRYPTTEQGLAALVEKPSGA--PANW-NGPYLKkRLPKDPWGNPYQYRSP 77

                          90       100
                  ....*....|....*....|....*....
gi 654544817  117 GEHGAVDVFSAGPDGEANTAD---DITNW 142
Cdd:pfam08334  78 GEHGPFDLFSLGADGQPGGEGedaDIGNW 106
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-108 1.55e-27

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: 98.06  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   1 MALKRKNlARQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQAL 80
Cdd:COG2165    1 MKLRRRR-RRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYPSSLTGLLAD 79

                         90       100
                 ....*....|....*....|....*...
gi 654544817  81 VtkpeiapipngyRADGYIRRLPQDPWG 108
Cdd:COG2165   80 V------------RGGGYLGSNGLPPAG 95
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 11-75 8.05e-11

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: 54.83  E-value: 8.05e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654544817  11 QAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQ--KATSDIValEGSLDMYKLDNHRYPTTEQ 75
Cdd:NF040999   1 VKGFTLIEMLIVLLIISVLLLLFVPNLSKQKESVQEKgcEAVVKVV--ESQVELYELDHNKKPSLSE 65
PRK10574 PRK10574
putative major pilin subunit; Provisional
 10-44 4.27e-06

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 43.87  E-value: 4.27e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 654544817  10 RQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKA 44
Cdd:PRK10574   3 KQRGFTLIELMVVIAIIAILSAIGIPAYQNYLQKA 37
T4P_ComGE NF041013
competence type IV pilus minor pilin ComGE;
13-38 9.70e-04

competence type IV pilus minor pilin ComGE;


Pssm-ID: 468942 [Multi-domain]  Cd Length: 83  Bit Score: 36.02  E-value: 9.70e-04
                         10        20
                 ....*....|....*....|....*.
gi 654544817  13 GFTLLELMVVIVILGVLASMVVPNLM 38
Cdd:NF041013   5 GFILLESLVALALLALIVSLLLPSLT 30
 
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 ...
 13-142 1.52e-62

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: 188.02  E-value: 1.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   13 GFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQALVTKPEIAPIPNG 92
Cdd:TIGR01710   2 GFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPKN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 654544817   93 YRAdGYIRRLPQDPWGGDYILVSPGEHGAVDVFSAGPDGE---ANTADDITNW 142
Cdd:TIGR01710  82 WHG-GYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQpggKGTDADIGNW 133
T2SSG pfam08334
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
 38-142 3.01e-50

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: 156.19  E-value: 3.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   38 MGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQALVTKPEIApiPNGYrADGYIR-RLPQDPWGGDYILVSP 116
Cdd:pfam08334   1 LGQLDKAKVKKAKAQIASLESALDLYRLDNGRYPTTEQGLAALVEKPSGA--PANW-NGPYLKkRLPKDPWGNPYQYRSP 77

                          90       100
                  ....*....|....*....|....*....
gi 654544817  117 GEHGAVDVFSAGPDGEANTAD---DITNW 142
Cdd:pfam08334  78 GEHGPFDLFSLGADGQPGGEGedaDIGNW 106
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-108 1.55e-27

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: 98.06  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   1 MALKRKNlARQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQAL 80
Cdd:COG2165    1 MKLRRRR-RRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYPSSLTGLLAD 79

                         90       100
                 ....*....|....*....|....*...
gi 654544817  81 VtkpeiapipngyRADGYIRRLPQDPWG 108
Cdd:COG2165   80 V------------RGGGYLGSNGLPPAG 95
ComGC COG4537
Competence protein ComGC [Mobilome: prophages, transposons];
1-118 1.93e-23

Competence protein ComGC [Mobilome: prophages, transposons];


Pssm-ID: 443603 [Multi-domain]  Cd Length: 108  Bit Score: 88.06  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   1 MALKRKNLARQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTeqgLQAL 80
Cdd:COG4537    1 MKKKKRKLKKEKGFTLIEMLIVLLIISILLLIAVPNLTKQRETAQEKGCEANIKMVQSQVELYELDHGTYPAS---LEEL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 654544817  81 VtkpeiapipngyrADGYIR-RLPQDPWGGDYILVSPGE 118
Cdd:COG4537   78 V-------------DEGYLKeKQPTCPNGGEYTIDSNGE 103
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
4-73 2.35e-18

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


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 75.50  E-value: 2.35e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817   4 KRKNLARQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTT 73
Cdd:COG4968    2 KKRMRRRQRGFTLIELMIVVAIIGILAAIAIPSYQDYVERARRAEAKAALLELAQAQERYYADNGSYPSA 71
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
1-56 2.80e-13

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 61.02  E-value: 2.80e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 654544817   1 MALKRKnlaRQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVAL 56
Cdd:COG4970    1 MKRLRR---RQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAA 53
PilA COG4969
Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];
10-116 1.38e-11

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


Pssm-ID: 443995 [Multi-domain]  Cd Length: 134  Bit Score: 58.18  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544817  10 RQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVALEGSLDMYKLDNHRYPTTEQGLQALVTKPEIAPI 89
Cdd:COG4969    4 KQKGFTLIELMIVVAIIGILAAIAIPAYQDYVARARVSEALALASPLKTAVEECALENGSLPNCNAGDNGLPATIATKYV 83

                         90       100
                 ....*....|....*....|....*..
gi 654544817  90 PNGYRADGYIRRLPQDPWGGDYILVSP 116
Cdd:COG4969   84 SSVSVDNGVITVTGTAALAGLTLTLTP 110
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 11-75 8.05e-11

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: 54.83  E-value: 8.05e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654544817  11 QAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQ--KATSDIValEGSLDMYKLDNHRYPTTEQ 75
Cdd:NF040999   1 VKGFTLIEMLIVLLIISVLLLLFVPNLSKQKESVQEKgcEAVVKVV--ESQVELYELDHNKKPSLSE 65
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 10-34 3.86e-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: 46.60  E-value: 3.86e-08
                          10        20
                  ....*....|....*....|....*
gi 654544817   10 RQAGFTLLELMVVIVILGVLASMVV 34
Cdd:pfam07963   3 KQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 11-34 2.41e-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: 44.22  E-value: 2.41e-07
                          10        20
                  ....*....|....*....|....
gi 654544817   11 QAGFTLLELMVVIVILGVLASMVV 34
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 ...
 10-56 3.66e-07

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: 46.79  E-value: 3.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 654544817   10 RQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDIVAL 56
Cdd:TIGR01708   2 RQSGFTLIELLVVLAIMGLVAAAAALSLVSHYGTKSLDQVAGRLAAR 48
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 1-47 4.30e-07

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 45.78  E-value: 4.30e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 654544817   1 MALKRKnlaRQAGFTLLELMVVIVILGVLASM---VVPNLMGNKEKADTQ 47
Cdd:COG4795    1 MKRARR---RQRGFTLLELLVALAIFALLLLAayrGLDSVLRSRERLEQQ 47
PilW COG4966
Type IV pilus assembly protein PilW [Cell motility, Extracellular structures];
8-53 1.91e-06

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


Pssm-ID: 443992 [Multi-domain]  Cd Length: 158  Bit Score: 44.79  E-value: 1.91e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 654544817   8 LARQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKADTQKATSDI 53
Cdd:COG4966    1 RRRQRGFTLVELMVALAIGLIVLAAVLQLFLSSRRSYRTQEALARL 46
PRK10574 PRK10574
putative major pilin subunit; Provisional
 10-44 4.27e-06

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 43.87  E-value: 4.27e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 654544817  10 RQAGFTLLELMVVIVILGVLASMVVPNLMGNKEKA 44
Cdd:PRK10574   3 KQRGFTLIELMVVIAIIAILSAIGIPAYQNYLQKA 37
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
5-50 6.35e-06

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


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 41.89  E-value: 6.35e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 654544817   5 RKNLARQAGFTLLELMVVIVILGV----LASMVVPNLMGNKEKADTQKAT 50
Cdd:COG4967    4 RRRRRRQRGFTLIEVLVALVILSIgllgLAGLQAASLRSSQDARQRTQAA 53
PRK10506 PRK10506
prepilin peptidase-dependent protein;
6-31 2.25e-04

prepilin peptidase-dependent protein;


Pssm-ID: 236704 [Multi-domain]  Cd Length: 162  Bit Score: 39.21  E-value: 2.25e-04
                         10        20
                 ....*....|....*....|....*.
gi 654544817   6 KNLARQAGFTLLELMVVIVILGVLAS 31
Cdd:PRK10506   3 RSMKKQRGYTLIELLVVMTIVSILSA 28
T4P_ComGE NF041013
competence type IV pilus minor pilin ComGE;
13-38 9.70e-04

competence type IV pilus minor pilin ComGE;


Pssm-ID: 468942 [Multi-domain]  Cd Length: 83  Bit Score: 36.02  E-value: 9.70e-04
                         10        20
                 ....*....|....*....|....*.
gi 654544817  13 GFTLLELMVVIVILGVLASMVVPNLM 38
Cdd:NF041013   5 GFILLESLVALALLALIVSLLLPSLT 30
 
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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