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Conserved domains on  [gi|2562027132|ref|WP_305562366|]
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type II secretion system major pseudopilin GspG [Limnobacter sp.]

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 ...
 18-151 1.77e-66

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: 198.42  E-value: 1.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERPTTEPQPR 97
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2562027132  98 NYKqGGYLGRVPVDPWGSNYQFLSPGINGEVDVMSFGADGKAGGEGVNADIGSW 151
Cdd:TIGR01710  81 NWH-GGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNW 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 ...
 18-151 1.77e-66

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: 198.42  E-value: 1.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERPTTEPQPR 97
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2562027132  98 NYKqGGYLGRVPVDPWGSNYQFLSPGINGEVDVMSFGADGKAGGEGVNADIGSW 151
Cdd:TIGR01710  81 NWH-GGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNW 133
T2SSG pfam08334
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
 44-151 1.20e-59

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: 180.08  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  44 MGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERPTTEpqPRNYkQGGYL-GRVPVDPWGSNYQFLSP 122
Cdd:pfam08334   1 LGQLDKAKVKKAKAQIASLESALDLYRLDNGRYPTTEQGLAALVEKPSGA--PANW-NGPYLkKRLPKDPWGNPYQYRSP 77

                          90       100
                  ....*....|....*....|....*....
gi 2562027132 123 GINGEVDVMSFGADGKAGGEGVNADIGSW 151
Cdd:pfam08334  78 GEHGPFDLFSLGADGQPGGEGEDADIGNW 106
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 14-116 1.85e-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: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERptte 93
Cdd:COG2165     7 RRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYPSSLTGLLADVRG---- 82

                          90       100
                  ....*....|....*....|...
gi 2562027132  94 pqprnykqGGYLGRVPVDPWGSN 116
Cdd:COG2165    83 --------GGYLGSNGLPPAGTP 97
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 18-101 1.14e-07

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: 46.74  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDearAVAAKQD--IASIMQA-LNLYRLDNSRYPTTDQgLQAlvERPTTEP 94
Cdd:NF040999    2 KGFTLIEMLIVLLIISVLLLLFVPNLSKQKE---SVQEKGCeaVVKVVESqVELYELDHNKKPSLSE-LVS--EGYITKK 75


                  ....*..
gi 2562027132  95 QPRNYKQ 101
Cdd:NF040999   76 QCPNYKD 82
PRK10574 PRK10574
putative major pilin subunit; Provisional
 18-84 1.72e-05

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 42.33  E-value: 1.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQ 84
Cdd:PRK10574    5 RGFTLIELMVVIAIIAILSAIGIPAYQNYLQKAALTDMLQTFVPYKTAVELCALEHGGLDTCDAGSN 71
T4P_ComGE NF041013
competence type IV pilus minor pilin ComGE;
18-76 3.00e-04

competence type IV pilus minor pilin ComGE;


Pssm-ID: 468942 [Multi-domain]  Cd Length: 83  Bit Score: 37.56  E-value: 3.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGrpDEARAVAAKQDIA--SIMQ-ALNLYRLDNSRY 76
Cdd:NF041013    4 KGFILLESLVALALLALIVSLLLPSLTQ--IQKEREEIKQKEEalQVLYeALQTYQLHLELN 63
 
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 ...
 18-151 1.77e-66

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: 198.42  E-value: 1.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERPTTEPQPR 97
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALVAPKLFSQADKAKAQVAKAQIKALKNALDMYRLDNGRYPTEEQGLAALVTKPSGEPLPK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2562027132  98 NYKqGGYLGRVPVDPWGSNYQFLSPGINGEVDVMSFGADGKAGGEGVNADIGSW 151
Cdd:TIGR01710  81 NWH-GGYLEKVPQDPWGNPYQYRDPGENGPYDLYSLGADGQPGGKGTDADIGNW 133
T2SSG pfam08334
Type II secretion system (T2SS), protein G; The Type II secretion system, also called ...
 44-151 1.20e-59

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: 180.08  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  44 MGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERPTTEpqPRNYkQGGYL-GRVPVDPWGSNYQFLSP 122
Cdd:pfam08334   1 LGQLDKAKVKKAKAQIASLESALDLYRLDNGRYPTTEQGLAALVEKPSGA--PANW-NGPYLkKRLPKDPWGNPYQYRSP 77

                          90       100
                  ....*....|....*....|....*....
gi 2562027132 123 GINGEVDVMSFGADGKAGGEGVNADIGSW 151
Cdd:pfam08334  78 GEHGPFDLFSLGADGQPGGEGEDADIGNW 106
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 14-116 1.85e-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: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERptte 93
Cdd:COG2165     7 RRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQIQQALERYRLDNGRYPSSLTGLLADVRG---- 82

                          90       100
                  ....*....|....*....|...
gi 2562027132  94 pqprnykqGGYLGRVPVDPWGSN 116
Cdd:COG2165    83 --------GGYLGSNGLPPAGTP 97
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
14-83 7.91e-20

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


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 79.35  E-value: 7.91e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGL 83
Cdd:COG4968     6 RRRQRGFTLIELMIVVAIIGILAAIAIPSYQDYVERARRAEAKAALLELAQAQERYYADNGSYPSALADL 75
ComGC COG4537
Competence protein ComGC [Mobilome: prophages, transposons];
1-104 1.71e-17

Competence protein ComGC [Mobilome: prophages, transposons];


Pssm-ID: 443603 [Multi-domain]  Cd Length: 108  Bit Score: 73.04  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132   1 MKKSNLYQKEVqekrlsKGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTd 80
Cdd:COG4537     1 MKKKKRKLKKE------KGFTLIEMLIVLLIISILLLIAVPNLTKQRETAQEKGCEANIKMVQSQVELYELDHGTYPAS- 73

                          90       100
                  ....*....|....*....|....*
gi 2562027132  81 qgLQALVERP-TTEPQPRNYKQGGY 104
Cdd:COG4537    74 --LEELVDEGyLKEKQPTCPNGGEY 96
PilA COG4969
Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];
14-92 1.77e-13

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


Pssm-ID: 443995 [Multi-domain]  Cd Length: 134  Bit Score: 63.19  E-value: 1.77e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQALVERPTT 92
Cdd:COG4969     2 KKKQKGFTLIELMIVVAIIGILAAIAIPAYQDYVARARVSEALALASPLKTAVEECALENGSLPNCNAGDNGLPATIAT 80
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
14-64 7.98e-12

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 57.16  E-value: 7.98e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQ 64
Cdd:COG4970     5 RRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALR 55
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 18-101 1.14e-07

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: 46.74  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDearAVAAKQD--IASIMQA-LNLYRLDNSRYPTTDQgLQAlvERPTTEP 94
Cdd:NF040999    2 KGFTLIEMLIVLLIISVLLLLFVPNLSKQKE---SVQEKGCeaVVKVVESqVELYELDHNKKPSLSE-LVS--EGYITKK 75


                  ....*..
gi 2562027132  95 QPRNYKQ 101
Cdd:NF040999   76 QCPNYKD 82
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 14-40 2.29e-07

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: 44.67  E-value: 2.29e-07
                          10        20
                  ....*....|....*....|....*..
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVV 40
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 18-40 7.91e-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: 43.06  E-value: 7.91e-07
                          10        20
                  ....*....|....*....|...
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVV 40
Cdd:TIGR02532   2 RGFTLIELLVVLAILGILALIAL 24
PRK10574 PRK10574
putative major pilin subunit; Provisional
 18-84 1.72e-05

putative major pilin subunit; Provisional


Pssm-ID: 236718 [Multi-domain]  Cd Length: 146  Bit Score: 42.33  E-value: 1.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGRPDEARAVAAKQDIASIMQALNLYRLDNSRYPTTDQGLQ 84
Cdd:PRK10574    5 RGFTLIELMVVIAIIAILSAIGIPAYQNYLQKAALTDMLQTFVPYKTAVELCALEHGGLDTCDAGSN 71
typeII_sec_gspH TIGR01708
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
 19-70 1.32e-04

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: 39.86  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2562027132  19 GFTLIEIMVVVVILGILATLVVPKiMGRPDEARAVaaKQDIASIMQALNLYR 70
Cdd:TIGR01708   5 GFTLIELLVVLAIMGLVAAAAALS-LVSHYGTKSL--DQVAGRLAARLRLAQ 53
T4P_ComGE NF041013
competence type IV pilus minor pilin ComGE;
18-76 3.00e-04

competence type IV pilus minor pilin ComGE;


Pssm-ID: 468942 [Multi-domain]  Cd Length: 83  Bit Score: 37.56  E-value: 3.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2562027132  18 KGFTLIEIMVVVVILGILATLVVPKIMGrpDEARAVAAKQDIA--SIMQ-ALNLYRLDNSRY 76
Cdd:NF041013    4 KGFILLESLVALALLALIVSLLLPSLTQ--IQKEREEIKQKEEalQVLYeALQTYQLHLELN 63
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 14-39 6.21e-04

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 37.30  E-value: 6.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLV 39
Cdd:COG4795     5 RRRQRGFTLLELLVALAIFALLLLAA 30
PilW COG4966
Type IV pilus assembly protein PilW [Cell motility, Extracellular structures];
14-40 1.02e-03

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


Pssm-ID: 443992 [Multi-domain]  Cd Length: 158  Bit Score: 37.47  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*..
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGILATLVV 40
Cdd:COG4966     1 RRRQRGFTLVELMVALAIGLIVLAAVL 27
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
14-65 3.20e-03

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


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 34.96  E-value: 3.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2562027132  14 KRLSKGFTLIEIMVVVVILGI----LATLVVpKIMGRPDEAR----AVAAKQDIASIMQA 65
Cdd:COG4967     7 RRRQRGFTLIEVLVALVILSIgllgLAGLQA-ASLRSSQDARqrtqAALLAQDLLERLRA 65
 
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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