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Conserved domains on  [gi|751632368|ref|WP_041100174|]
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ExeA family protein [Sulfuritalea hydrogenivorans]

Protein Classification

ExeA family protein( domain architecture ID 11461675)

type II secretory pathway component ExeA family protein is an ATPase that forms a complex with ExeB, and is involved in the function of the ExeAB complex in the assembly of the ExeD secretin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
1-262 1.22e-122

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 358.33  E-value: 1.22e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   1 MYLDHFGLSEAPFRITPHTDFFFDGANRGATLDALIYAVTHDEGIVKVSGEVGSGKTMLCRVLMERLPENVTIIYLANPS 80
Cdd:COG3267    1 MYLEFFGLKEKPFSLTPDPRFLFLSPSHREALARLEYALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  81 LSRDDILYAIADELRLNVPDNARSSVvLRALQDHLIKSFGEGRQVVVLIDEAHAMPAETLEEIRLLSNLEANRNKLLQLV 160
Cdd:COG3267   81 LSPAELLRAIADELGLEPKGASKADL-LRQLQEFLLELAAAGRRVVLIIDEAQNLPPETLEELRLLSNLETDSRKLLQIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 161 LFGQPELNDILARPDMRQLKERITHNFGLEPLVRDDIAHYLDFRMRAAGYKGPSVFSPPALKMIAQSSLGLTRRINILAD 240
Cdd:COG3267  160 LVGQPELRERLARPELRQLRQRITARYHLRPLDREETAAYIEHRLKVAGGEGDPLFTPEAIEAIYRASGGIPRLINNLCD 239
                        250       260
                 ....*....|....*....|..
gi 751632368 241 KSLLAAFSAGSHQIGTKEIQAA 262
Cdd:COG3267  240 RALLAAYAEGKKVVDAEIVREA 261
 
Name Accession Description Interval E-value
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
1-262 1.22e-122

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 358.33  E-value: 1.22e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   1 MYLDHFGLSEAPFRITPHTDFFFDGANRGATLDALIYAVTHDEGIVKVSGEVGSGKTMLCRVLMERLPENVTIIYLANPS 80
Cdd:COG3267    1 MYLEFFGLKEKPFSLTPDPRFLFLSPSHREALARLEYALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  81 LSRDDILYAIADELRLNVPDNARSSVvLRALQDHLIKSFGEGRQVVVLIDEAHAMPAETLEEIRLLSNLEANRNKLLQLV 160
Cdd:COG3267   81 LSPAELLRAIADELGLEPKGASKADL-LRQLQEFLLELAAAGRRVVLIIDEAQNLPPETLEELRLLSNLETDSRKLLQIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 161 LFGQPELNDILARPDMRQLKERITHNFGLEPLVRDDIAHYLDFRMRAAGYKGPSVFSPPALKMIAQSSLGLTRRINILAD 240
Cdd:COG3267  160 LVGQPELRERLARPELRQLRQRITARYHLRPLDREETAAYIEHRLKVAGGEGDPLFTPEAIEAIYRASGGIPRLINNLCD 239
                        250       260
                 ....*....|....*....|..
gi 751632368 241 KSLLAAFSAGSHQIGTKEIQAA 262
Cdd:COG3267  240 RALLAAYAEGKKVVDAEIVREA 261
AAA_22 pfam13401
AAA domain;
39-171 3.78e-29

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 111.28  E-value: 3.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   39 VTHDEGIVKVSGEVGSGKTMLCRVLMERLPE---NVTIIYLANPSlSRDDILYAIADELRLNVPDNARSSVVLRALQDHL 115
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSGT-SPKDLLRALLRALGLPLSGRLSKEELLAALQQLL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 751632368  116 IKSFgegRQVVVLIDEAHAMPAETLEEIRLLSNLeanRNKLLQLVLFGQPELNDIL 171
Cdd:pfam13401  80 LALA---VAVVLIIDEAQHLSLEALEELRDLLNL---SSKLLQLILVGTPELRELL 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
48-158 4.29e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368    48 VSGEVGSGKTMLCRVLMERLPENVTIIYLANPSLSRDDILYAIADELRLNVPDNARSSVVLRALQDHLIKSfgegRQVVV 127
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL----KPDVL 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 751632368   128 LIDEAHAM-PAETLEEIRLLSNLEANRNKLLQ 158
Cdd:smart00382  83 ILDEITSLlDAEQEALLLLLEELRLLLLLKSE 114
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
50-184 2.02e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 41.75  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  50 GEVGSGKTMLCRVLMERLPE-NVTIIYLaNPSLSRDDILYAIADELRLNVPDNARSSvvlralqdhliksfgEGRQVVVL 128
Cdd:cd00009   26 GPPGTGKTTLARAIANELFRpGAPFLYL-NASDLLEGLVVAELFGHFLVRLLFELAE---------------KAKPGVLF 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 751632368 129 IDEAHAMPAE---TLEEIRLLSNLEANRNKLLQLVLFGQPELNDILARPDMRQLKERIT 184
Cdd:cd00009   90 IDEIDSLSRGaqnALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
 
Name Accession Description Interval E-value
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
1-262 1.22e-122

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 358.33  E-value: 1.22e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   1 MYLDHFGLSEAPFRITPHTDFFFDGANRGATLDALIYAVTHDEGIVKVSGEVGSGKTMLCRVLMERLPENVTIIYLANPS 80
Cdd:COG3267    1 MYLEFFGLKEKPFSLTPDPRFLFLSPSHREALARLEYALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  81 LSRDDILYAIADELRLNVPDNARSSVvLRALQDHLIKSFGEGRQVVVLIDEAHAMPAETLEEIRLLSNLEANRNKLLQLV 160
Cdd:COG3267   81 LSPAELLRAIADELGLEPKGASKADL-LRQLQEFLLELAAAGRRVVLIIDEAQNLPPETLEELRLLSNLETDSRKLLQIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 161 LFGQPELNDILARPDMRQLKERITHNFGLEPLVRDDIAHYLDFRMRAAGYKGPSVFSPPALKMIAQSSLGLTRRINILAD 240
Cdd:COG3267  160 LVGQPELRERLARPELRQLRQRITARYHLRPLDREETAAYIEHRLKVAGGEGDPLFTPEAIEAIYRASGGIPRLINNLCD 239
                        250       260
                 ....*....|....*....|..
gi 751632368 241 KSLLAAFSAGSHQIGTKEIQAA 262
Cdd:COG3267  240 RALLAAYAEGKKVVDAEIVREA 261
AAA_22 pfam13401
AAA domain;
39-171 3.78e-29

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 111.28  E-value: 3.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   39 VTHDEGIVKVSGEVGSGKTMLCRVLMERLPE---NVTIIYLANPSlSRDDILYAIADELRLNVPDNARSSVVLRALQDHL 115
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSGT-SPKDLLRALLRALGLPLSGRLSKEELLAALQQLL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 751632368  116 IKSFgegRQVVVLIDEAHAMPAETLEEIRLLSNLeanRNKLLQLVLFGQPELNDIL 171
Cdd:pfam13401  80 LALA---VAVVLIIDEAQHLSLEALEELRDLLNL---SSKLLQLILVGTPELRELL 129
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
3-483 1.97e-19

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 90.68  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   3 LDHFGLSEAPFRITPHTDFFFDGANRGATLDALIYAVTHDEGIVKVSGEVGSGKTMLCRVLMERLPENVTIIYLANPSLS 82
Cdd:COG3266    5 ETLSTLALALLLLSLSLVLGDLGLLLLLLLRALLSALELLLATGLRLLLLAGLLLLLIRLLSEAVDLGALASAALLLALA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  83 RDDILYAIADELRLNVPDNARSSVVLRALQDHLIKSFGEGRQVVVLIDEAHAMPAETLEEIRLLSNLEANRNKLLQLVLF 162
Cdd:COG3266   85 SLALLGILLLALLALLLDLLLLADLLRAAALLLLKLLLLLLTLLLLVLLLLLALLLALLLDLPLLTLLIVLPLLEEQLLL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 163 GQPELNDILARPDMRQLKERITHNFGLEPLVRDDIAHYLDFRMRAAGYKGPSVFSPPALKMIAQSSLGLTRRINILADKS 242
Cdd:COG3266  165 LALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAAGAAEVLTARL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 243 LLAAFSAGSHqigtkeiqaairdcefSEATYGGRGTKKPRTLWLAALLGLAALAGIAWLLTASHN----DPAIPATSAIT 318
Cdd:COG3266  245 VLLLLIIGSA----------------LKAPSQASSASAPATTSLGEQQEVSLPPAVAAQPAAAAAaqpsAVALPAAPAAA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 319 PIAPAAPAAAVVASAAPVPPPAtipppapspapgatpppETKAEPADVTPPSPPSPPRAGPLTQARLEAGRAWLEQQPND 398
Cdd:COG3266  309 AAAAAPAEAAAPQPTAAKPVVT-----------------ETAAPAAPAPEAAAAAAAPAAPAVAKKLAADEQWLASQPAS 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 399 RWFIQVFAtdASRHGEIESMLRRLPPSkpemDNVRVYYSELSGKPRYGVMYGEYATRAAAVAAIGDLPKSLRVIKPYPRQ 478
Cdd:COG3266  372 HYTLQLLG--ASSEAALEAFAAKHSLK----GNLWVYPTTRNGKPWYVVVYGSYASRAEAKAAVAALPAELRASKPWVRS 445

                 ....*
gi 751632368 479 VVRLR 483
Cdd:COG3266  446 IAQVQ 450
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
32-270 8.07e-14

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 71.14  E-value: 8.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  32 LDALIYAVTHdEGIVKVSGEVGSGKTMLCRVLMERLPeNVtiIYL-ANPSLSRDDILYAIADELRLNVPdNARSSVVLRA 110
Cdd:COG2842   40 AEALDEARAL-PGIGVVYGESGVGKTTAAREYANRNP-NV--IYVtASPSWTSKELLEELAEELGIPAP-PGTIADLRDR 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 111 LQDHLiksfgEGRQVVVLIDEAHAMPAETLEEIRLLSNlEANrnklLQLVLFGQPELNDILARpdMRQLKERITHNFGLE 190
Cdd:COG2842  115 ILERL-----AGTGRLLIIDEADHLKPKALEELRDIHD-ETG----VGVVLIGMERLPAKLKR--YEQLYSRIGFWVEFK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368 191 PLVRDDIAHYLDFRMRaagykgpsVFSPPALKMIAQSSLGLTRRINILADKSLLAAFSAGSHQIGTKEIQAAIRDCEFSE 270
Cdd:COG2842  183 PLSLEDVRALAEAWGE--------LTDPDLLELLHRITRGNLRRLDRTLRLAARAAKRNGLTKITLDHVRAAALMLGEGP 254
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
30-157 1.80e-05

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 45.19  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   30 ATLDALIYAV-THDEGIVKVSGEVGSGKTMLCRVLMERLPENVTIIYLANP-----------SLSRDDILYAIADELRLN 97
Cdd:pfam13191  10 EQLLDALDRVrSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCdenlpysplleALTREGLLRQLLDELESS 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751632368   98 VPDNAR-----------------SSVVLRALQDHLIKSFGEGRQVVVLIDEAHAMPAETLEEIRLLSNLEANRNKLL 157
Cdd:pfam13191  90 LLEAWRaallealapvpelpgdlAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEASLQLLAALLRLLESLPLLV 166
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
48-158 4.29e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368    48 VSGEVGSGKTMLCRVLMERLPENVTIIYLANPSLSRDDILYAIADELRLNVPDNARSSVVLRALQDHLIKSfgegRQVVV 127
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL----KPDVL 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 751632368   128 LIDEAHAM-PAETLEEIRLLSNLEANRNKLLQ 158
Cdd:smart00382  83 ILDEITSLlDAEQEALLLLLEELRLLLLLKSE 114
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
50-184 2.02e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 41.75  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  50 GEVGSGKTMLCRVLMERLPE-NVTIIYLaNPSLSRDDILYAIADELRLNVPDNARSSvvlralqdhliksfgEGRQVVVL 128
Cdd:cd00009   26 GPPGTGKTTLARAIANELFRpGAPFLYL-NASDLLEGLVVAELFGHFLVRLLFELAE---------------KAKPGVLF 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 751632368 129 IDEAHAMPAE---TLEEIRLLSNLEANRNKLLQLVLFGQPELNDILARPDMRQLKERIT 184
Cdd:cd00009   90 IDEIDSLSRGaqnALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIV 148
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
50-153 3.63e-04

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 40.74  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368   50 GEVGSGKTMLCRVLMERLPENVTIIYLANPSLSRDDILYaiadelRLNVPDNARS---SVVLRALQdhliksfgEGRqvV 126
Cdd:pfam07728   6 GPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFG------RRNIDPGGASwvdGPLVRAAR--------EGE--I 69
                          90       100
                  ....*....|....*....|....*..
gi 751632368  127 VLIDEAHAMPAETLEEirLLSNLEANR 153
Cdd:pfam07728  70 AVLDEINRANPDVLNS--LLSLLDERR 94
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
33-122 2.20e-03

dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.


Pssm-ID: 410924 [Multi-domain]  Cd Length: 179  Bit Score: 38.90  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751632368  33 DALIYAVTHDEGIVKVSGEVGSGKTMLC----RVLMERLPENVTIIYLANPSlsrddilyaiadELRLNVPDNARSSVVL 108
Cdd:cd19516    1 PDLVEALFPREGLVYVAGATGSGKSTLLaaiyRYILENDPPDRKIITYEDPI------------EFVYDGIKSKHSIIVQ 68
                         90
                 ....*....|....
gi 751632368 109 RALQDHlIKSFGEG 122
Cdd:cd19516   69 SQIPRH-FKSFAKA 81
 
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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