ID A0A016SX13_9BILA Unreviewed; 593 AA.
AC A0A016SX13;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Nuclear receptor domain-containing protein {ECO:0000259|PROSITE:PS51030};
GN Name=Acey_s0162.g3438 {ECO:0000313|EMBL:EYB95273.1};
GN ORFNames=Y032_0162g3438 {ECO:0000313|EMBL:EYB95273.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB95273.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB95273.1}.
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DR EMBL; JARK01001498; EYB95273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SX13; -.
DR STRING; 53326.A0A016SX13; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR11533:SF276; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..108
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT REGION 507..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 67002 MW; 5B21513BFF760D4F CRC64;
MFNTLASLDH SDVFGDVAST ALDELIRNSA AAIGGHTGLS GIQPMAGLNS SQFTQSGNLV
NSQETPSRGR KKNSTINLVC VVCGDQAFGK HYGVNACNGC KGFFRRRIGF RDTQLTLLLT
VAVQAVVAAV EKSGRACTKK LWFGNLVTLN WWDDTWLNEG FTTYFEKTKL VDNADGDLEL
HKDLFVHGND ASMRKDSLAA SRPLSSIVDI ATEIPEAFDK ISYGKGGSIL AMMRDVVGEQ
NFRKAIINYL KKFSFKTAST EDMWKAFDET IDHVKGPTGA KLNMLDFGNQ WSKQMGFPLV
TIESFNSSAV KLTQERYMLY PSALPLKKYR SPIYRYKWDI PLWYEKKGKL HQVWLTRDEP
LYLEVDQAVP INVNVDRRGY FRQNYDTAGW QKIIVQFKND HEVYSGWTRH GVISDAFAAA
LIDRLDYLTL FELLSYLPKE KENAVWNLVR SELMGLTRFF VGTDKEYADL YVLKLLEKPY
QKSLAQYISG EVTRNGVQMF RVVGNTEEHR DGHSKQMTEA PGSSDLSDPD FASSIIESYC
ELGSTNCSSI FQSLFEETVL NRCKGDEKSS RCVKYVHVYA PLRRCKITQI LGW
//