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Database: UniProt
Entry: A0A0V0RY17_9BILA
LinkDB: A0A0V0RY17_9BILA
Original site: A0A0V0RY17_9BILA 
ID   A0A0V0RY17_9BILA        Unreviewed;       964 AA.
AC   A0A0V0RY17;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Carnosine N-methyltransferase {ECO:0000256|ARBA:ARBA00015448};
DE            EC=2.1.1.22 {ECO:0000256|ARBA:ARBA00012003};
GN   Name=Ap2s1 {ECO:0000313|EMBL:KRX19350.1};
GN   ORFNames=T07_2626 {ECO:0000313|EMBL:KRX19350.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX19350.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX19350.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX19350.1};
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   -!- SIMILARITY: Belongs to the carnosine N-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010086}.
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:KRX19350.1}.
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DR   EMBL; JYDL01000060; KRX19350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0RY17; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0030735; F:carnosine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.450.60; -; 1.
DR   Gene3D; 3.90.79.20; -; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR012901; CARME.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12303:SF6; CARNOSINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12303; UNCHARACTERIZED; 1.
DR   Pfam; PF07942; CARME; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM01296; N2227; 1.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF55811; Nudix; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 2.
DR   PROSITE; PS50089; ZF_RING_2; 2.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022927};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          458..502
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          711..935
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   DOMAIN          794..841
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   964 AA;  110461 MW;  97ACC36D7F90FF54 CRC64;
     MARMDLHRSS LSDYSFMTAK KCFEHYYSSS LTILQEKYSA YKALPEKHKA LIPTFFEHIA
     RIRESITINM QFFTQIYTTG MHMVEEESRK NTLLAGNVTR MTCEFVVGKT QQILHDVIRE
     WSAVGISERK SVYGPILAYM EDLKKSTTPE SIKILIPNAG LGRLVWELAK LGYHCDACES
     SAAHVLTTNF MINHSDANSP VTIYPWINKW TNHRNCAEQI QSVTVPDVRP DLIRNGKQCN
     LVAGDFLNLY VDEHETYDII CTVRYINHPK KIRDYVEKVY DLLKPGAVWI NMGPMLFHGR
     NEDSNVRVPP YELVRLHIQE LGFHFEKEQL GIPINITYYN QSMLSCTEKE ASAEFAEKSE
     MIRFILIQNR AGKTRLAKWY MHFDDNEKQK LIEEVHAVVT VRDAKHTNFV EMRDFIDLTH
     CDTEEKRRSK RSQKRKASAD ISFVDLTDDK TEKSKLACCK CEMSIQMLLK NGAVISSILC
     GHVFCNKCLL SIPTKRKSGC CPKLVLKTVI NQLLRKTTLL HNSKRLTSYL VNKIRMHEWM
     KSNDSVLLAE FKRGNFAVCV EKQPLIHSLN NNQTDQYKLL QINYKCLKKV LLEYKLNFDV
     KDTALLDVVP MQSTTNDIEE EWTPVFALNI KNASSVGTKK DLAQALGGEF HDFRKVFLAT
     DTSNAKLLTK MRNIFRWHNS FQNCPRCTAR LNFKVSKASA KCPECDAVYY PPVAPVAITL
     VSTADMKYLL LVRQKHHPKR LYTAISGFSE LESKDSVRIR PSRKENQQAM EVIDLTLDSS
     STSSSCSIVN DLQCPACFSS FEEILKEGNA VMTTPCGHVF CARCIYTVFS GKRSLKCPIC
     RRNITESSES LEDAVLREIA EEVGILVENF QYMGISQSWP FPNNSLMCAY LAYADRSQTI
     SIDRKELVDA RWFSREMVAS AFENTQNLEE SKEEEEEEDG PLLISSKGTI VHEMIKFWLS
     QKAD
//
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