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Conserved domains on  [gi|17505853|ref|NP_491709|]
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ShKT domain-containing protein [Caenorhabditis elegans]

Protein Classification

tyrosinase family protein( domain architecture ID 10447028)

tyrosinase family protein such as tyrosinase, a metal-containing oxidase that catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine

Gene Ontology:  GO:0046872|GO:0016491
PubMed:  29473882|11412044

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Tyrosinase pfam00264
Common central domain of tyrosinase; This family also contains polyphenol oxidases and some ...
 137-320 5.48e-41

Common central domain of tyrosinase; This family also contains polyphenol oxidases and some hemocyanins. Binds two copper ions via two sets of three histidines. This family is related to pfam00372.


:

Pssm-ID: 425566  Cd Length: 209  Bit Score: 149.16  E-value: 5.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505853   137 YERIGRIHSQMSAAGGAHSGPAFLPWHREFVKRVEFALRQV----DPTVNLPYWDSTLDsrlprPADTIMFSDYLMGSTG 212
Cdd:pfam00264   4 YDDFAAIHGIPFTPWPIHGNGLFLPWHRYYLLLFEQALREEcgyaDPTGTLPYWDWTDD-----PTSPGISSPTSLGGNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505853   213 ----------LVNDGPFTNWRT-----LAGRAQILRAVGAQGAPLSQNDIDFVMRQTQIDQVLSFTAPQQGCpyrTDF-N 276
Cdd:pfam00264  79 tfippnggvgEVTNGPFANYTVpnlgpHTIRRPPDNALAYNPRCLTRDNPLLKQQLNTLDVVDDLLTYQPDY---TSFsN 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17505853   277 CLEYT--------HGNVHIFVGGDMFDTATSSNDPSFFLHHAFIDFVWEEWR 320
Cdd:pfam00264 156 TLEGDggneeglpHNGVHVWVGGDMGDVFTAPNDPIFFLHHANIDRLWAIWQ 207
PLN00052 super family cl28127
prolyl 4-hydroxylase; Provisional
 502-536 1.62e-05

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 47.74  E-value: 1.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17505853  502 CTDRHTQCSSWSRSGECTKNQLWMT------ENCRKSCNKC 536
Cdd:PLN00052 268 CADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
PLN00052 super family cl28127
prolyl 4-hydroxylase; Provisional
 456-492 1.31e-04

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 44.66  E-value: 1.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 17505853  456 ESCFNENQCCASWAASGECSRNTAYM------NEWCKASCGVC 492
Cdd:PLN00052 266 EGCADKSAHCAEWAAAGECEKNPVYMvgaegaPGNCRKSCGVC 308
PLN00052 super family cl28127
prolyl 4-hydroxylase; Provisional
 612-645 1.37e-04

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 44.66  E-value: 1.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17505853  612 CVDYHRSCAGWARVGECQKNP-WM--AE----NCRSSCNSC 645
Cdd:PLN00052 268 CADKSAHCAEWAAAGECEKNPvYMvgAEgapgNCRKSCGVC 308
PLN00052 super family cl28127
prolyl 4-hydroxylase; Provisional
 558-602 1.35e-03

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 41.58  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17505853  558 PAQQCDNSDGCFNENVCCAVWGLMGECRKNTRYMA------CNCRVSCGHC 602
Cdd:PLN00052 258 PPVVPKDTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
 
Name Accession Description Interval E-value
Tyrosinase pfam00264
Common central domain of tyrosinase; This family also contains polyphenol oxidases and some ...
 137-320 5.48e-41

Common central domain of tyrosinase; This family also contains polyphenol oxidases and some hemocyanins. Binds two copper ions via two sets of three histidines. This family is related to pfam00372.


Pssm-ID: 425566  Cd Length: 209  Bit Score: 149.16  E-value: 5.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505853   137 YERIGRIHSQMSAAGGAHSGPAFLPWHREFVKRVEFALRQV----DPTVNLPYWDSTLDsrlprPADTIMFSDYLMGSTG 212
Cdd:pfam00264   4 YDDFAAIHGIPFTPWPIHGNGLFLPWHRYYLLLFEQALREEcgyaDPTGTLPYWDWTDD-----PTSPGISSPTSLGGNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505853   213 ----------LVNDGPFTNWRT-----LAGRAQILRAVGAQGAPLSQNDIDFVMRQTQIDQVLSFTAPQQGCpyrTDF-N 276
Cdd:pfam00264  79 tfippnggvgEVTNGPFANYTVpnlgpHTIRRPPDNALAYNPRCLTRDNPLLKQQLNTLDVVDDLLTYQPDY---TSFsN 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17505853   277 CLEYT--------HGNVHIFVGGDMFDTATSSNDPSFFLHHAFIDFVWEEWR 320
Cdd:pfam00264 156 TLEGDggneeglpHNGVHVWVGGDMGDVFTAPNDPIFFLHHANIDRLWAIWQ 207
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 502-536 1.62e-05

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 47.74  E-value: 1.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17505853  502 CTDRHTQCSSWSRSGECTKNQLWMT------ENCRKSCNKC 536
Cdd:PLN00052 268 CADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 456-492 1.31e-04

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 44.66  E-value: 1.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 17505853  456 ESCFNENQCCASWAASGECSRNTAYM------NEWCKASCGVC 492
Cdd:PLN00052 266 EGCADKSAHCAEWAAAGECEKNPVYMvgaegaPGNCRKSCGVC 308
ShKT smart00254
ShK toxin domain; ShK toxin domain
 502-536 1.37e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 39.67  E-value: 1.37e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17505853    502 CTDRHTQCSSWSRsGECTkNQLWMTENCRKSCNKC 536
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 612-645 1.37e-04

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 44.66  E-value: 1.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17505853  612 CVDYHRSCAGWARVGECQKNP-WM--AE----NCRSSCNSC 645
Cdd:PLN00052 268 CADKSAHCAEWAAAGECEKNPvYMvgAEgapgNCRKSCGVC 308
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 501-536 1.41e-04

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 39.69  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17505853   501 DCTDRHTQCSSWSRSGeCTKNQL--WMTENCRKSCNKC 536
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPFYqdFMKENCPKTCGFC 37
ShKT smart00254
ShK toxin domain; ShK toxin domain
 458-492 3.27e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 38.51  E-value: 3.27e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17505853    458 CFNENQCCASWAAsGECSrNTAYMNEWCKASCGVC 492
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 611-645 1.21e-03

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 36.99  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17505853   611 SCVDYHRSCAGWARVGeCQKNPW---MAENCRSSCNSC 645
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPFYqdfMKENCPKTCGFC 37
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 558-602 1.35e-03

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 41.58  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17505853  558 PAQQCDNSDGCFNENVCCAVWGLMGECRKNTRYMA------CNCRVSCGHC 602
Cdd:PLN00052 258 PPVVPKDTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
ShKT smart00254
ShK toxin domain; ShK toxin domain
 612-645 1.52e-03

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 36.59  E-value: 1.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 17505853    612 CVDYHRSCAGWARvGECQKNPWMAENCRSSCNSC 645
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCTNPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 457-492 3.31e-03

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 35.83  E-value: 3.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17505853   457 SCFNENQCCASWAASGeCSRNT--AYMNEWCKASCGVC 492
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
ShKT smart00254
ShK toxin domain; ShK toxin domain
 568-602 4.27e-03

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 35.43  E-value: 4.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17505853    568 CFNENVCCAVWGlMGECrKNTRYMACNCRVSCGHC 602
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
 
Name Accession Description Interval E-value
Tyrosinase pfam00264
Common central domain of tyrosinase; This family also contains polyphenol oxidases and some ...
 137-320 5.48e-41

Common central domain of tyrosinase; This family also contains polyphenol oxidases and some hemocyanins. Binds two copper ions via two sets of three histidines. This family is related to pfam00372.


Pssm-ID: 425566  Cd Length: 209  Bit Score: 149.16  E-value: 5.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505853   137 YERIGRIHSQMSAAGGAHSGPAFLPWHREFVKRVEFALRQV----DPTVNLPYWDSTLDsrlprPADTIMFSDYLMGSTG 212
Cdd:pfam00264   4 YDDFAAIHGIPFTPWPIHGNGLFLPWHRYYLLLFEQALREEcgyaDPTGTLPYWDWTDD-----PTSPGISSPTSLGGNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505853   213 ----------LVNDGPFTNWRT-----LAGRAQILRAVGAQGAPLSQNDIDFVMRQTQIDQVLSFTAPQQGCpyrTDF-N 276
Cdd:pfam00264  79 tfippnggvgEVTNGPFANYTVpnlgpHTIRRPPDNALAYNPRCLTRDNPLLKQQLNTLDVVDDLLTYQPDY---TSFsN 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17505853   277 CLEYT--------HGNVHIFVGGDMFDTATSSNDPSFFLHHAFIDFVWEEWR 320
Cdd:pfam00264 156 TLEGDggneeglpHNGVHVWVGGDMGDVFTAPNDPIFFLHHANIDRLWAIWQ 207
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 502-536 1.62e-05

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 47.74  E-value: 1.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17505853  502 CTDRHTQCSSWSRSGECTKNQLWMT------ENCRKSCNKC 536
Cdd:PLN00052 268 CADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 456-492 1.31e-04

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 44.66  E-value: 1.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 17505853  456 ESCFNENQCCASWAASGECSRNTAYM------NEWCKASCGVC 492
Cdd:PLN00052 266 EGCADKSAHCAEWAAAGECEKNPVYMvgaegaPGNCRKSCGVC 308
ShKT smart00254
ShK toxin domain; ShK toxin domain
 502-536 1.37e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 39.67  E-value: 1.37e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17505853    502 CTDRHTQCSSWSRsGECTkNQLWMTENCRKSCNKC 536
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 612-645 1.37e-04

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 44.66  E-value: 1.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 17505853  612 CVDYHRSCAGWARVGECQKNP-WM--AE----NCRSSCNSC 645
Cdd:PLN00052 268 CADKSAHCAEWAAAGECEKNPvYMvgAEgapgNCRKSCGVC 308
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 501-536 1.41e-04

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 39.69  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17505853   501 DCTDRHTQCSSWSRSGeCTKNQL--WMTENCRKSCNKC 536
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPFYqdFMKENCPKTCGFC 37
ShKT smart00254
ShK toxin domain; ShK toxin domain
 458-492 3.27e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 38.51  E-value: 3.27e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17505853    458 CFNENQCCASWAAsGECSrNTAYMNEWCKASCGVC 492
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 611-645 1.21e-03

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 36.99  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17505853   611 SCVDYHRSCAGWARVGeCQKNPW---MAENCRSSCNSC 645
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPFYqdfMKENCPKTCGFC 37
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 558-602 1.35e-03

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 41.58  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17505853  558 PAQQCDNSDGCFNENVCCAVWGLMGECRKNTRYMA------CNCRVSCGHC 602
Cdd:PLN00052 258 PPVVPKDTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
ShKT smart00254
ShK toxin domain; ShK toxin domain
 612-645 1.52e-03

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 36.59  E-value: 1.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 17505853    612 CVDYHRSCAGWARvGECQKNPWMAENCRSSCNSC 645
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCTNPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 457-492 3.31e-03

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 35.83  E-value: 3.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17505853   457 SCFNENQCCASWAASGeCSRNT--AYMNEWCKASCGVC 492
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
ShKT smart00254
ShK toxin domain; ShK toxin domain
 568-602 4.27e-03

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 35.43  E-value: 4.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 17505853    568 CFNENVCCAVWGlMGECrKNTRYMACNCRVSCGHC 602
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
 
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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