ID A0A0V1CUA1_TRIBR Unreviewed; 1236 AA.
AC A0A0V1CUA1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glycoprotein endo-alpha-1,2-mannosidase {ECO:0000313|EMBL:KRY52864.1};
GN Name=MANEA {ECO:0000313|EMBL:KRY52864.1};
GN ORFNames=T03_7466 {ECO:0000313|EMBL:KRY52864.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52864.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52864.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52864.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family.
CC {ECO:0000256|ARBA:ARBA00009559}.
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:KRY52864.1}.
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DR EMBL; JYDI01000097; KRY52864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CUA1; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd11574; GH99; 1.
DR CDD; cd16695; mRING-CH-C4HC2H_ZNRF2; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR026071; Glyco_Hydrolase_99.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR002738; RNase_P_p30.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13572; ENDO-ALPHA-1,2-MANNOSIDASE; 1.
DR PANTHER; PTHR13572:SF4; RE57134P; 1.
DR Pfam; PF16317; Glyco_hydro_99; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF01876; RNase_P_p30; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..260
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 55..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 140521 MW; FEA212BA8126246E CRC64;
MKTPSNDRQL PFLFNLTFTL QLFWLLIYHA CMLMCCTFHV KINVSPRKVI STAMGSRQSV
ANPPRQRGTN SLPANGSAPG TGYTSAGRGG AAASGSYGGV NEIGSDIIGR MLSQSLQSRT
NRSYSMPGPS SSMLDHSSDS SDPDSSSMGL FSLDRWLNLS TESDGRGIVD IAHIPSAHVR
YFVCHKMIPS DDVECHLVMC LTRPRLTYNE DVLTEEKGEC VICLEEMKEG DTIARLPCLC
IYHKGCIDNW FKVKNTCPEH PVTAFEQSFE EKNNIDQSFV AHKSFTKLVI FRSEIALLSV
AICELSSFIA VWWLIFHFNA CFDCSFIKTE KASIQQRANQ PAQPILFSNL TLNITVLIYI
VIFTLFTMLM RFTMRRICII VIFWFAMQFN TITFEKSILP RPVFSRKSNS EPDYSVHIFY
YMWYGNVAFD QFFLHWNHRI LPHYNPLIAS KYLVGRREAP EDIGSNFYPK LGCYSSRDPK
ILAQHMQWIR DAGIGVVVVG WYPPDASDDE GHPWDDAIPS LLDEANRWQL KVCFLIEPYK
GRNGETIRTD IEYILQSYGR HDAFYKILTN GISKPVFYVY DSYLVSNSDW QALLLTDGKN
TIRNTDLDSI ILALLVKRTD TDAILTTGFD GFFTYFASTD FTDGSKPSNW PDLVLFATRN
GLLTSLSVGP GYVDERIRPW NGENTRSRCN GSYYEKMWKA AVNCKPTFVS ITSFNEWHEG
TQIEPAVPYK NENYEYLNYL PMEEDFYLKL TKRFIDDKNL HIPKKYRDFV YPPSEDSYLL
LEAVQLDWEK IKTLKPVICL EIGCGSGVIA CSVAKSLQSG AVIFATDISQ IAVELTKVNV
EQNNIDKIFC PIVADLISPL YDRLLNSVDL LLFNPPYIPR LSDFDDTDEL SSTWCGGGPE
GTDILRRIFF QIHNLLSDNG LFYLVAIEEN NIEKLLQLNS HLVGKGKNKM ASRLAKIHFV
ELNIVRRLDE SEKHVVSAVK YAVEELGYTS VAVNVELSAT NDNGQRNSGL VVPEPLLVDW
ANVVERSKPW RLYTRLTLKV DSVDLLSSLM NNETVLKYDI IAVCPLSEAI FNFVFNNVEV
DLLTTDMMNR DVWFEDESCY RKAVQCGKFI EISYSPAILS AEKRIEIFSH GNELFRMVGR
RGVILTSRAF GAFEMRGPYD VINIGYLFGM NPNEARDAIT VNPRKLLNAV GIKKRTLSHT
LFTRHFSQLQ MNEVENILQV PEFKIEIETN SSNEKQ
//
