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Conserved domains on  [gi|366064016|gb|EHN28226|]
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flagellar basal body P-ring biosynthesis protein FlgA [Salmonella enterica subsp. enterica serovar Montevideo str. 80959-06]

Protein Classification

flagella basal body P-ring formation protein FlgA( domain architecture ID 11482531)

flagella basal body P-ring formation protein FlgA is a periplasmic protein essential for flagellar P-ring assembly

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
flgA PRK07018
flagellar basal body P-ring formation protein FlgA;
1-219 9.79e-82

flagellar basal body P-ring formation protein FlgA;


:

Pssm-ID: 180794 [Multi-domain]  Cd Length: 235  Bit Score: 243.29  E-value: 9.79e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   1 MQTLKRGFAVAALLFSPLTMAQ--------DINAQLTTWFSQRL-AGFSDEVVVTLRS-SPNL-LPSCEQPAFSMTGSAK 69
Cdd:PRK07018   2 MLTLKRLLAIIALLFSALSAAAaatqqspeAISEQAEQFLEQQLeAGLPGKVSVTVATlDPRLrLPACDQLEASLPSNAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  70 LWGNVNVVARCANE---KRYLQVNVQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLA 146
Cdd:PRK07018  82 LWGNVTVGVRCGGPypwTVYVPVRVQVTGPYVVAARPLARGEKLSASDVTLREGDLDTLPPGVFTDPDQLVGAVSKRRIA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366064016 147 PGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEGQAMNNAAVAQNARVR-MTSGQIVSGTVDSDGNILINL 219
Cdd:PRK07018 162 PGQPIRLNMLRQAWVVCKGQTVSIIARGDGFSVKTEGEALNDGAVGQQIRVRnMASGQVVSGIVTGDGEVEVNL 235
 
Name Accession Description Interval E-value
flgA PRK07018
flagellar basal body P-ring formation protein FlgA;
1-219 9.79e-82

flagellar basal body P-ring formation protein FlgA;


Pssm-ID: 180794 [Multi-domain]  Cd Length: 235  Bit Score: 243.29  E-value: 9.79e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   1 MQTLKRGFAVAALLFSPLTMAQ--------DINAQLTTWFSQRL-AGFSDEVVVTLRS-SPNL-LPSCEQPAFSMTGSAK 69
Cdd:PRK07018   2 MLTLKRLLAIIALLFSALSAAAaatqqspeAISEQAEQFLEQQLeAGLPGKVSVTVATlDPRLrLPACDQLEASLPSNAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  70 LWGNVNVVARCANE---KRYLQVNVQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLA 146
Cdd:PRK07018  82 LWGNVTVGVRCGGPypwTVYVPVRVQVTGPYVVAARPLARGEKLSASDVTLREGDLDTLPPGVFTDPDQLVGAVSKRRIA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366064016 147 PGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEGQAMNNAAVAQNARVR-MTSGQIVSGTVDSDGNILINL 219
Cdd:PRK07018 162 PGQPIRLNMLRQAWVVCKGQTVSIIARGDGFSVKTEGEALNDGAVGQQIRVRnMASGQVVSGIVTGDGEVEVNL 235
FlgA COG1261
Flagellar basal body P-ring formation protein FlgA [Cell motility];
68-219 4.98e-46

Flagellar basal body P-ring formation protein FlgA [Cell motility];


Pssm-ID: 440873 [Multi-domain]  Cd Length: 158  Bit Score: 149.66  E-value: 4.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  68 AKLWGNVNVVARCANE--KRYLQVNVQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDL 145
Cdd:COG1261    4 ARLWGRLSVGVRCDGKgwTVYVPARVAVYGEVVVAARPLARGEVITADDLRLEEGDLARLPGGALTDPDELVGKVARRSL 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 366064016 146 APGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEGQAMNNAAVAQNARVRMT-SGQIVSGTVDSDGNILINL 219
Cdd:COG1261   84 RAGQPLRASDLRAPPLVKRGQTVTIVARGGGFSVSAEGRALENGALGDRIRVRNLsSGKVVSGRVVGDGTVEVGL 158
flgA_cterm TIGR03170
flagella basal body P-ring formation protein FlgA; This model describes a conserved C-terminal ...
97-217 3.03e-35

flagella basal body P-ring formation protein FlgA; This model describes a conserved C-terminal region of the flagellar basal body P-ring formation protein FlgA. This sequence region contains a SAF domain, now described by pfam08666. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274466 [Multi-domain]  Cd Length: 122  Bit Score: 121.10  E-value: 3.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   97 YVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEG 176
Cdd:TIGR03170   1 VVVAKRPLKRGEVITPEDLKLERGDLARLPGGVLTDPDEVVGKVAKRPLRAGQPLTANMLRPPWLVKRGDTVTVIARGGG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 366064016  177 FSVNAEGQAMNNAAVAQNARVR-MTSGQIVSGTVDSDGNILI 217
Cdd:TIGR03170  81 LSITTEGKALEDGAVGDQIRVRnLSSGKIISGIVTAPGTVEV 122
ChapFlgA pfam13144
Chaperone for flagella basal body P-ring formation; ChapFlgA is a family similar to the SAF ...
98-217 1.26e-24

Chaperone for flagella basal body P-ring formation; ChapFlgA is a family similar to the SAF family, and includes chaperones for flagellar basal-body proteins and pilus-assembly proteins, FlgA, RcpB and CpaB. ChapFlgA is necessary for the formation of the P-ring of the flagellum, FlgI, which sits in the peptidoglycan layer of the outer membrane of the bacterium. FlgA plays an auxiliary role in P-ring assembly.


Pssm-ID: 432991 [Multi-domain]  Cd Length: 122  Bit Score: 93.76  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   98 VAVAA-PVARGGKLTPANVTLKRGRLDQLPPRTVLDirQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEG 176
Cdd:pfam13144   3 VVVAArPLARGEVITASDLALKKRDLARLPGGYLTD--QAIGKRVKRSIRAGQPIRQNMLEAPPLVKKGQKVTIIARGGG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 366064016  177 FSVNAEGQAMNNAAVAQNARVRMT-SGQIVSGTVDSDGNILI 217
Cdd:pfam13144  81 FRITTEGKALENGAEGDQIRVKNLqSGRIVTGRVTGPGTVEV 122
SAF_CpaB_FlgA_like cd11614
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus ...
96-156 7.93e-10

SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB; FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure.


Pssm-ID: 212159 [Multi-domain]  Cd Length: 61  Bit Score: 52.86  E-value: 7.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 366064016  96 NYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMI 156
Cdd:cd11614    1 PVVVAARDLPAGTVITADDLTLVEVPLSLLPPGALTDPDDVVGRVARRPLRAGEPITASML 61
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
96-157 3.35e-08

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins;


Pssm-ID: 214862 [Multi-domain]  Cd Length: 63  Bit Score: 48.72  E-value: 3.35e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 366064016    96 NYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIR 157
Cdd:smart00858   2 NVVVAARDLPAGEVITAEDLRLGHVALRDLPGGGLTPYGQVIGRVARRDIAAGEPITASNLE 63
 
Name Accession Description Interval E-value
flgA PRK07018
flagellar basal body P-ring formation protein FlgA;
1-219 9.79e-82

flagellar basal body P-ring formation protein FlgA;


Pssm-ID: 180794 [Multi-domain]  Cd Length: 235  Bit Score: 243.29  E-value: 9.79e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   1 MQTLKRGFAVAALLFSPLTMAQ--------DINAQLTTWFSQRL-AGFSDEVVVTLRS-SPNL-LPSCEQPAFSMTGSAK 69
Cdd:PRK07018   2 MLTLKRLLAIIALLFSALSAAAaatqqspeAISEQAEQFLEQQLeAGLPGKVSVTVATlDPRLrLPACDQLEASLPSNAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  70 LWGNVNVVARCANE---KRYLQVNVQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLA 146
Cdd:PRK07018  82 LWGNVTVGVRCGGPypwTVYVPVRVQVTGPYVVAARPLARGEKLSASDVTLREGDLDTLPPGVFTDPDQLVGAVSKRRIA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366064016 147 PGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEGQAMNNAAVAQNARVR-MTSGQIVSGTVDSDGNILINL 219
Cdd:PRK07018 162 PGQPIRLNMLRQAWVVCKGQTVSIIARGDGFSVKTEGEALNDGAVGQQIRVRnMASGQVVSGIVTGDGEVEVNL 235
FlgA COG1261
Flagellar basal body P-ring formation protein FlgA [Cell motility];
68-219 4.98e-46

Flagellar basal body P-ring formation protein FlgA [Cell motility];


Pssm-ID: 440873 [Multi-domain]  Cd Length: 158  Bit Score: 149.66  E-value: 4.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  68 AKLWGNVNVVARCANE--KRYLQVNVQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDL 145
Cdd:COG1261    4 ARLWGRLSVGVRCDGKgwTVYVPARVAVYGEVVVAARPLARGEVITADDLRLEEGDLARLPGGALTDPDELVGKVARRSL 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 366064016 146 APGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEGQAMNNAAVAQNARVRMT-SGQIVSGTVDSDGNILINL 219
Cdd:COG1261   84 RAGQPLRASDLRAPPLVKRGQTVTIVARGGGFSVSAEGRALENGALGDRIRVRNLsSGKVVSGRVVGDGTVEVGL 158
flgA_cterm TIGR03170
flagella basal body P-ring formation protein FlgA; This model describes a conserved C-terminal ...
97-217 3.03e-35

flagella basal body P-ring formation protein FlgA; This model describes a conserved C-terminal region of the flagellar basal body P-ring formation protein FlgA. This sequence region contains a SAF domain, now described by pfam08666. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274466 [Multi-domain]  Cd Length: 122  Bit Score: 121.10  E-value: 3.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   97 YVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEG 176
Cdd:TIGR03170   1 VVVAKRPLKRGEVITPEDLKLERGDLARLPGGVLTDPDEVVGKVAKRPLRAGQPLTANMLRPPWLVKRGDTVTVIARGGG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 366064016  177 FSVNAEGQAMNNAAVAQNARVR-MTSGQIVSGTVDSDGNILI 217
Cdd:TIGR03170  81 LSITTEGKALEDGAVGDQIRVRnLSSGKIISGIVTAPGTVEV 122
ChapFlgA pfam13144
Chaperone for flagella basal body P-ring formation; ChapFlgA is a family similar to the SAF ...
98-217 1.26e-24

Chaperone for flagella basal body P-ring formation; ChapFlgA is a family similar to the SAF family, and includes chaperones for flagellar basal-body proteins and pilus-assembly proteins, FlgA, RcpB and CpaB. ChapFlgA is necessary for the formation of the P-ring of the flagellum, FlgI, which sits in the peptidoglycan layer of the outer membrane of the bacterium. FlgA plays an auxiliary role in P-ring assembly.


Pssm-ID: 432991 [Multi-domain]  Cd Length: 122  Bit Score: 93.76  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016   98 VAVAA-PVARGGKLTPANVTLKRGRLDQLPPRTVLDirQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEG 176
Cdd:pfam13144   3 VVVAArPLARGEVITASDLALKKRDLARLPGGYLTD--QAIGKRVKRSIRAGQPIRQNMLEAPPLVKKGQKVTIIARGGG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 366064016  177 FSVNAEGQAMNNAAVAQNARVRMT-SGQIVSGTVDSDGNILI 217
Cdd:pfam13144  81 FRITTEGKALENGAEGDQIRVKNLqSGRIVTGRVTGPGTVEV 122
flgA PRK06005
flagellar basal body P-ring formation protein FlgA;
130-215 1.15e-11

flagellar basal body P-ring formation protein FlgA;


Pssm-ID: 180347 [Multi-domain]  Cd Length: 160  Bit Score: 60.47  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016 130 VLDIRQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEGQAMNNAAVAQNARVR-MTSGQIVSGT 208
Cdd:PRK06005  69 VLSIDQVVGKVAKRTLLPGRPIPVSALREPSLVTRGSPVKLVFSAGGLTITAAGTPLQSGAAGDLIRVRnVDSGVIVSGT 148

                 ....*..
gi 366064016 209 VDSDGNI 215
Cdd:PRK06005 149 VLADGTI 155
SAF_CpaB_FlgA_like cd11614
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus ...
96-156 7.93e-10

SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB; FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure.


Pssm-ID: 212159 [Multi-domain]  Cd Length: 61  Bit Score: 52.86  E-value: 7.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 366064016  96 NYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMI 156
Cdd:cd11614    1 PVVVAARDLPAGTVITADDLTLVEVPLSLLPPGALTDPDDVVGRVARRPLRAGEPITASML 61
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
96-157 3.35e-08

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins;


Pssm-ID: 214862 [Multi-domain]  Cd Length: 63  Bit Score: 48.72  E-value: 3.35e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 366064016    96 NYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIR 157
Cdd:smart00858   2 NVVVAARDLPAGEVITAEDLRLGHVALRDLPGGGLTPYGQVIGRVARRDIAAGEPITASNLE 63
SAF pfam08666
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
96-157 1.09e-07

SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.


Pssm-ID: 430140 [Multi-domain]  Cd Length: 63  Bit Score: 47.17  E-value: 1.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 366064016   96 NYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIR 157
Cdd:pfam08666   2 NVVVAARDLPAGEVITADDLTLVRPPLALPPGLFPIAYGEVIGKVARRDIAAGEPLTASDLE 63
flgA PRK06804
flagellar basal body P-ring formation protein FlgA;
104-215 4.45e-07

flagellar basal body P-ring formation protein FlgA;


Pssm-ID: 235863 [Multi-domain]  Cd Length: 261  Bit Score: 49.11  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016 104 VARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEGFSVNAEG 183
Cdd:PRK06804 145 LERGRKVQADDIELKKKNISGVQGGYITDPDEAIGLTIKRRIRQLQAVIPSQLEQPVLVERGQHVLMIAAQDGIEAQTLG 224
                         90       100       110
                 ....*....|....*....|....*....|...
gi 366064016 184 QAMNNAAVAQNARVR-MTSGQIVSGTVDSDGNI 215
Cdd:PRK06804 225 IAQKNGRKGELIKVKnLSSGRVVTATVDGSGRV 257
flgA PRK12786
flagellar basal body P-ring formation protein FlgA;
91-218 5.56e-06

flagellar basal body P-ring formation protein FlgA;


Pssm-ID: 237201 [Multi-domain]  Cd Length: 338  Bit Score: 46.19  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  91 VQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQV 170
Cdd:PRK12786 188 AYETVEAPVLARAVGRGEVIKSSDVVWERRPKARVSGDDIASREDLVGMQARRALRAGQPLRGADLAKPDLVQRGQLVTL 267
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 366064016 171 IANGEGFSVNAEGQAMNNAAVAQNARV-RMTSGQIVSGTVDSDGNILIN 218
Cdd:PRK12786 268 IYQTPGIYLTARGKALEDGAEGDVVRVlNLQSKRTVTGTVTGRGQVSVD 316
flgA PRK12618
flagellar basal body P-ring formation protein FlgA;
98-218 1.95e-03

flagellar basal body P-ring formation protein FlgA;


Pssm-ID: 183626 [Multi-domain]  Cd Length: 141  Bit Score: 37.37  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366064016  98 VAVAAPVARGGK-LTPANVTLKrgrlDQLPPRTVLDIRQIQDAVSLRDLAPGQPVQLTMIRQAWRVKAGQRVQVIANGEG 176
Cdd:PRK12618  21 TVVAARTIRALTvIGAEDLALK----PGDTPGALTDPAQAIGQEARVTLYAGRPIRAADLGPPAIVDRNQLVPLAYRLGG 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 366064016 177 FSVNAEGQAMNNAAVAQNARV-RMTSGQIVSGTVDSDGNILIN 218
Cdd:PRK12618  97 LEIRTEGRALSRGGVGDEIRVmNLSSRTTVSGRIAADGSVIVG 139
CpaB COG3745
Flp pilus assembly protein CpaB [Intracellular trafficking, secretion, and vesicular transport, ...
88-151 4.25e-03

Flp pilus assembly protein CpaB [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442959 [Multi-domain]  Cd Length: 259  Bit Score: 37.27  E-value: 4.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 366064016  88 QVNVQATGNYVAVAAPVARGGKLTPANVTLKRGRLDQLPPRTVLDIRQIQDAVSLRDLAPGQPV 151
Cdd:COG3745   34 AAAAVPTVPVVVAARDIPAGTPLTADDLAVVEWPADAVPEGAFTDPEELVGRVARVPIEAGEPI 97
 
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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