ID A0A0V0XXK9_TRIPS Unreviewed; 1084 AA.
AC A0A0V0XXK9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE SubName: Full=Prenylcysteine oxidase {ECO:0000313|EMBL:KRX92782.1};
DE Flags: Fragment;
GN Name=Pcyox1 {ECO:0000313|EMBL:KRX92782.1};
GN ORFNames=T4E_6137 {ECO:0000313|EMBL:KRX92782.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX92782.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX92782.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX92782.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000256|ARBA:ARBA00004567}.
CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC {ECO:0000256|ARBA:ARBA00009967}.
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:KRX92782.1}.
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DR EMBL; JYDU01000103; KRX92782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XXK9; -.
DR STRING; 6337.A0A0V0XXK9; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd13170; RanBD_NUP50; 1.
DR Gene3D; 1.10.405.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR010795; Prenylcys_lyase.
DR InterPro; IPR017046; Prenylcysteine_Oxase.
DR InterPro; IPR000156; Ran_bind_dom.
DR PANTHER; PTHR15944; FARNESYLCYSTEINE LYASE; 1.
DR PANTHER; PTHR15944:SF0; PRENYLCYS_LYASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR Pfam; PF08911; NUP50; 1.
DR Pfam; PF07156; Prenylcys_lyase; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Nuclear pore complex {ECO:0000256|ARBA:ARBA00023132};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Protein transport {ECO:0000256|ARBA:ARBA00023132};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transport {ECO:0000256|ARBA:ARBA00022816}.
FT DOMAIN 943..1066
FT /note="RanBD1"
FT /evidence="ECO:0000259|SMART:SM00160"
FT REGION 473..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX92782.1"
FT NON_TER 1084
FT /evidence="ECO:0000313|EMBL:KRX92782.1"
SQ SEQUENCE 1084 AA; 120438 MW; 2061DC8C7A222636 CRC64;
LSMFKENGDA WNGAISNWLF MRKMELRCDS FIYHLRQLRG AGFIRCMATA SALKIAVIGA
GIGGTSCSYF LRQIFGDGIE IDIFDGGKVG GRLATVEIER KHYESGGSVI HPQNEYMLIF
TESNSKLVTL FRLLVQYKLD PVRLQFAIEQ CLKRFLKIYA MQKNNYCYTT VRKMFSALDA
DLAANMNCSL RLALTKYGIQ NAIIDELVQA AMLCNYGQSV DIHSFVGMVS LAGMQQNLWS
VAEGNCTVAE KLLKISKATF HSCRILEITR QVNGSFSLHL TNNETLNTRR DGYKSVVIAC
PLIAGQIKLN VANLPSLEPF CSPYHRTTTT FVSGILRKHH PWSNRPDFVK TILVSDVDFP
IASLAKVDPL RRDDGLERQI GNYDMYKLFS RDFLTPEQLN MVFEQFSYHT AVPWLAYPEY
AGQSKDCSFI LTDGLYYVNA IENAASAMEM SCIGAKNVAL LLASHWNGDL TKVDSSSKRT
ADSELIREEF DRDDEPRASE EQSSGPMAKA SAEVIRKRLI KKVSRRNAIN TEITGSNPFK
NFTGFTNPEG YLKSKEPPVM PTPVSDPSSL EPVIEEPNII ISNMHKELSC SAVTLVQNDS
ELQMKQKSAL ANVQALNSKW LMAMCEHFEK MPFLDFSKVA FDYIKEMRIL IDICVALGIQ
LREENQKLPK EQTTNVEGPS SFKHLSETLE TPKDTSSKVT IHEPKKIAST EEEKSDKQKC
MVKIYKVALP ERSEANQQVK ETGAVKLSQE TISDVGEKIV ARKEENLTTE KKIDENNLLK
LADCAKESES SSSAALSAKN FSFNMKSTTT TSSSFGTTFG GALCDQLSKE VSASASKLTF
AFPSVSTSSA LAKPNVYFSS PTIAAAFGDT TATATTTSTT TTTTTTATTT VGSSLSMNLP
QFSFLTGNAA ASTSKGHSIN RIRLWLQQLH LCLEDLLHPR LNRKPPKVES VQVEEEGSVY
SEKCKLYFKQ DKEFVLKGVG YVYLKPNDNG KVQLIVRDNT ALGNLYLNIF LDELTPCQKI
SKNKIMLAAV PNPPIEGKSE NEAVTYLINM KSEKEADTLF DLINEAKAGC LNGQCNAMQR
LCFI
//
