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
//