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Database: UniProt
Entry: A0A0V0TUT7_9BILA
LinkDB: A0A0V0TUT7_9BILA
Original site: A0A0V0TUT7_9BILA 
ID   A0A0V0TUT7_9BILA        Unreviewed;      1184 AA.
AC   A0A0V0TUT7;
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:KRX42783.1};
GN   Name=Znrf2 {ECO:0000313|EMBL:KRX42783.1};
GN   ORFNames=T05_5583 {ECO:0000313|EMBL:KRX42783.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42783.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX42783.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX42783.1};
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:KRX42783.1}.
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DR   EMBL; JYDJ01000135; KRX42783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TUT7; -.
DR   STRING; 144512.A0A0V0TUT7; -.
DR   Proteomes; UP000055048; 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:UP000055048};
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        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          167..207
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1184 AA;  134383 MW;  DF3B70911735458A CRC64;
     MGSRQSVANP PRQRGTNSLP ANGSAPGTGY TSAGRGGAAA SGSYGGVNEI GSDIIGRMLS
     QSLQSRTNRS YSMPGPSSSM LDHSSDSSDP DSSSMGLFSL DRWLNLSTES DGRGIVDIAH
     IPSAHVRYFV CHKMIPSDDV ECHLVMCLTR PRLTYNEDVL TEEKGECVIC LEEMKEGDTI
     ARLPCLCIYH KGCIDNWFKV KNTCPEHPVT AFEQSFEEKN NIDQSFVAHK SFTKLVIFRS
     EIALLSVAIC ELSSFIAVWW LIFHFNACFD CSFIKTEKAS IQQRANQPAQ PILFSNLTLN
     ITVLIYIVIF TLFTMLMRFT MRRICIIVIF WFAMQFNTIT FEKSILPRPV FSRKSNSEPD
     YSVHIFYYMW YGNVAFDQFF LHWNHRILPH YNPLIASKYL VGRREAPEDI GSNFYPKLGC
     YSSRDPKILA QHMQWIRDAG IGVVVVGWYP PDASDDEGHP WDDAIPSLLD EANRWQLKVC
     FLIEPYKGRN GETIRTDIEY ILQSYGRHDA FYKILTNGIS KPVFYVYDSY LVSNSDWQAL
     LLTDGKNTIR NTDLDSIILA LLVKRTDTDA ILTTGFDGFF TYFASTDFTD GSKPSNWPDL
     VLFATRNGLL TSLSVGPGYV DERIRPWNGE NTRSRCNGSY YEKMWKAAVN CKPTFVSITS
     FNEWHEGTQI EPAVPYKNEN YEYLNYLPME EDFYLKLTKR FIDDKSDLHI AKKYRDFVYP
     PSEDSYLLLE AVQLDWEKIK TLKPVICLEI GCGSGVIACS VAKSLQSGAV VFTTDISQIA
     VELTKVNVEQ NNIDKIFCPI VADLISPLYD RLLNSVDLLL FNPPYIPRLS DFDDTDELSS
     TWCGGGPEGT DILRRIFFQI HNLLSDNGLF YLVAIEENNI EKLLQLNSHL VGKGKNKMAS
     RLAKIHFVEL NIVRRLDESE KHVVSAVKYA VEELGYTSVA VNVELSATND NGQRNSGLVV
     PEPLLVDWAN VVERSKPWRL YTRLTLKVDS VDLLSSLMNN ETVLKYDIIA VCPLSEAIFN
     FVFNNVEVDL LTTDMMNRDV WFEDESCYRK AVQCGKFIEI SYSPAILSAE KRIEIFSHGN
     ELFRMVGRRG VILTSRAFGA FEMRGPYDVI NIGYLFGMNP NEARDAITVN PRKLLNAVGI
     KKRTLSHTLF TRHFSQLQMN EVENILQVPE FKIEIETNSS NEKQ
//
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