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Conserved domains on  [gi|487749552|ref|WP_001831502|]
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MULTISPECIES: HlyD family secretion protein [Staphylococcus]

Protein Classification

HlyD family secretion protein( domain architecture ID 11446287)

HlyD family secretion protein similar to Escherichia coli protein YhiI, Acinetobacter baumannii colistin resistance protein EmrA, and Burkholderia cepacia fusaric acid resistance protein FusE

Gene Ontology:  GO:0022857|GO:0016020|GO:0055085
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
51-213 1.75e-22

Multidrug resistance efflux pump EmrA [Defense mechanisms];


:

Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 92.80  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  51 ASGQIKSLNVKQGDKLDKGDKVAEV------LAQGQDgQSKDMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLY 124
Cdd:COG1566  167 AQAQLAQAQAGLREEEELAAAQAQVaqaeaaLAQAEL-NLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLW 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552 125 ITANVDEKDISDVEKGNDVDVDIDG-QKASIKGKVEEVGQATAASFslmPSSNSDGNytkVSQVVPVKISLDSNPSKNVV 203
Cdd:COG1566  246 VEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDPEPLR 319

                        170
                 ....*....|
gi 487749552 204 PGMNAEVKIH 213
Cdd:COG1566  320 PGMSATVEID 329
CusB_dom_1 super family cl46872
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 27-70 3.92e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


The actual alignment was detected with superfamily member PRK10476:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 346  Bit Score: 40.40  E-value: 3.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 487749552  27 HNTTSYVTTDNAKVDGDQIKISSPASGQIKSLNVKQGDKLDKGD 70
Cdd:PRK10476  31 WRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGD 74
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
51-213 1.75e-22

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 92.80  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  51 ASGQIKSLNVKQGDKLDKGDKVAEV------LAQGQDgQSKDMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLY 124
Cdd:COG1566  167 AQAQLAQAQAGLREEEELAAAQAQVaqaeaaLAQAEL-NLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLW 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552 125 ITANVDEKDISDVEKGNDVDVDIDG-QKASIKGKVEEVGQATAASFslmPSSNSDGNytkVSQVVPVKISLDSNPSKNVV 203
Cdd:COG1566  246 VEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDPEPLR 319

                        170
                 ....*....|
gi 487749552 204 PGMNAEVKIH 213
Cdd:COG1566  320 PGMSATVEID 329
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
105-195 6.90e-10

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 57.78  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552 105 GSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDV--DIDGQKASIKGKVEEVGQATAASFSLMPSSNSDGNYT 182
Cdd:PRK15136 234 GAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATItsDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWI 313

                         90
                 ....*....|...
gi 487749552 183 KVSQVVPVKISLD 195
Cdd:PRK15136 314 KVVQRLPVRIELD 326
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 89-198 7.16e-08

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 48.90  E-value: 7.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552   89 IKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDVDID-GQKASIKGKVEEVGQATAA 167
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDpGSDYTLEGKVVRISPTVDP 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 487749552  168 SfslmpssnsdgnytkvSQVVPVKISLDSNP 198
Cdd:pfam13437  82 D----------------TGVIPVRVSIENPK 96
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 86-213 2.33e-06

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 47.31  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552   86 DMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDVDIDGQ-KASIKGKVEEVgqa 164
Cdd:TIGR01730 134 YTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALpGEEFKGKLRFI--- 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 487749552  165 taasfslmpSSNSDGNytkvSQVVPVKISLDsNPSKNVVPGMNAEVKIH 213
Cdd:TIGR01730 211 ---------DPRVDSG----TGTVRVRATFP-NPDGRLLPGMFGRVTIS 245
PRK10476 PRK10476
multidrug transporter subunit MdtN;
27-70 3.92e-04

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 40.40  E-value: 3.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 487749552  27 HNTTSYVTTDNAKVDGDQIKISSPASGQIKSLNVKQGDKLDKGD 70
Cdd:PRK10476  31 WRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGD 74
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
51-213 1.75e-22

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 92.80  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  51 ASGQIKSLNVKQGDKLDKGDKVAEV------LAQGQDgQSKDMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLY 124
Cdd:COG1566  167 AQAQLAQAQAGLREEEELAAAQAQVaqaeaaLAQAEL-NLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLW 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552 125 ITANVDEKDISDVEKGNDVDVDIDG-QKASIKGKVEEVGQATAASFslmPSSNSDGNytkVSQVVPVKISLDSNPSKNVV 203
Cdd:COG1566  246 VEAYVPETDLGRVKPGQPVEVRVDAyPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDPEPLR 319

                        170
                 ....*....|
gi 487749552 204 PGMNAEVKIH 213
Cdd:COG1566  320 PGMSATVEID 329
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-213 1.69e-14

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 70.74  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  43 DQIKISSPASGQIKSLNVKQGDKLDKGDKVAEV--------LAQ--------------------------GQDGQSK--- 85
Cdd:COG0845   22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLdppdlqaaLAQaqaqlaaaqaqlelakaelerykallKKGAVSQqel 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  86 -----------------------------DMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISD 136
Cdd:COG0845  102 dqakaaldqaqaalaaaqaaleqaranlaYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLAR 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487749552 137 VEKGNDVDVDIDGQKA-SIKGKVEEVGqataasfslmPSSNSDgnytkvSQVVPVKISLDsNPSKNVVPGMNAEVKIH 213
Cdd:COG0845  182 LKVGQPVTVTLDAGPGkTFEGKVTFID----------PAVDPA------TRTVRVRAELP-NPDGLLRPGMFVRVRIV 242
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
105-195 6.90e-10

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 57.78  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552 105 GSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDV--DIDGQKASIKGKVEEVGQATAASFSLMPSSNSDGNYT 182
Cdd:PRK15136 234 GAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATItsDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWI 313

                         90
                 ....*....|...
gi 487749552 183 KVSQVVPVKISLD 195
Cdd:PRK15136 314 KVVQRLPVRIELD 326
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 89-198 7.16e-08

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 48.90  E-value: 7.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552   89 IKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDVDID-GQKASIKGKVEEVGQATAA 167
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDpGSDYTLEGKVVRISPTVDP 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 487749552  168 SfslmpssnsdgnytkvSQVVPVKISLDSNP 198
Cdd:pfam13437  82 D----------------TGVIPVRVSIENPK 96
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 86-213 2.33e-06

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 47.31  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552   86 DMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDVDIDGQ-KASIKGKVEEVgqa 164
Cdd:TIGR01730 134 YTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALpGEEFKGKLRFI--- 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 487749552  165 taasfslmpSSNSDGNytkvSQVVPVKISLDsNPSKNVVPGMNAEVKIH 213
Cdd:TIGR01730 211 ---------DPRVDSG----TGTVRVRATFP-NPDGRLLPGMFGRVTIS 245
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 72-208 8.34e-06

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 44.80  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552   72 VAEVLAQGQDGQSkdMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDVDID--- 148
Cdd:pfam16576  96 IAELERTGKVQPT--VTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPalp 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  149 GQkaSIKGKVEEVGqataasfslmPSSNSDgnytkvSQVVPVKISLDsNPSKNVVPGMNA 208
Cdd:pfam16576 174 GK--TFEGKVDYIY----------PTLDPK------TRTVRVRIELP-NPDGRLKPGMFA 214
PRK10476 PRK10476
multidrug transporter subunit MdtN;
86-213 2.98e-04

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 40.78  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749552  86 DMNIKMPQKGTIVKTDGIEGSMTQAGNPIAYAYNLDDLYITANVDEKDISDVEKGNDVDVD--IDGQKAsIKGKVEEVGQ 163
Cdd:PRK10476 208 DTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYsmIDRGRP-FEGKVDSIGW 286

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 487749552 164 ATAASFSLM-----PSSNSDGNYTKVSQVVPVKISLDSNPSKNVVPGMNAEVKIH 213
Cdd:PRK10476 287 GVLPDDGGNvprglPYVPRSINWVRVAQRFPVRIMLDKPDPELFRIGASAVVELR 341
PRK10476 PRK10476
multidrug transporter subunit MdtN;
27-70 3.92e-04

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 40.40  E-value: 3.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 487749552  27 HNTTSYVTTDNAKVDGDQIKISSPASGQIKSLNVKQGDKLDKGD 70
Cdd:PRK10476  31 WRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGD 74
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 29-78 1.22e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 38.94  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 487749552   29 TTSYVTTDNAKVDGDQIKISSPASGQIKSLNVKQGDKLDKGDkvaeVLAQ 78
Cdd:pfam00529   5 TKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGD----VLFQ 50
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
43-75 1.65e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 35.50  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 487749552   43 DQIKISSPASGQIKSLNVKQGDKLDKGDKVAEV 75
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATL 33
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 47-99 7.10e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 36.74  E-value: 7.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 487749552  47 ISSPASGQIKSLNVKQGDKLDKGDKVAEVLAQgqdgqsKDMN-IKMPQKGTIVK 99
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAM------KMENeIQAPVDGTVKE 572
 
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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