ID A0A085NHR2_9BILA Unreviewed; 1434 AA.
AC A0A085NHR2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=M513_06655 {ECO:0000313|EMBL:KFD52458.1}, M514_06655
GN {ECO:0000313|EMBL:KFD69008.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD69008.1};
RN [1] {ECO:0000313|EMBL:KFD69008.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD69008.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD52458.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
CC Evidence={ECO:0000256|ARBA:ARBA00034044};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363075}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
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DR EMBL; KL363227; KFD52458.1; -; Genomic_DNA.
DR EMBL; KL367499; KFD69008.1; -; Genomic_DNA.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR22760:SF1; DOL-P-MAN:MAN(7)GLCNAC(2)-PP-DOL ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF08264; Anticodon_1; 2.
DR Pfam; PF03901; Glyco_transf_22; 2.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT TRANSMEM 456..478
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 595..613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 625..647
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 659..680
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 737..754
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 761..778
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 790..811
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 957..977
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1010..1031
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1069..1088
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1094..1112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1119..1141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1208..1230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1237..1256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 1262..1281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT DOMAIN 1..83
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 133..178
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 199..300
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1434 AA; 165723 MW; 9B21C545A8695025 CRC64;
METGHDILGL WVTRMAMLSL QLTNRLPFSR ILFHGMVRDS EGQKMSKSRG NVVDPMELIE
GDQETRIGAD ALRISLLRSN PKGNTVSLDE AVRQHSRRFC NKLWQSFKYL TKLWNKKEIP
LPTAPASNGS PVDRWILSRL SSLVIDVHES LEAYNFHLSV EALVNFWWFD FCDIYLVRIV
ASNRCPLVIF PFSRRKEWSK HFFYPKDHLV AAEQMRSMLA MIASVYLRLL APYMPHLAEE
LYSLLPMADK AVSVHCSPYP TPSEVNFLDP HLEIQMRFVR DLIHQIRSLR RDVEVSMPIP
LIAVAWCKGI QRSAIENFAR LMQRLVEFRC TLDDNAEHVP PENCIMFVSQ EECRIYVHLK
NVKYEEVLKR FDRQLEMLER KRTKLTNWMQ AKTVQLPPEE AAKKVTQYMN DIRTVNEEMD
KLSRFRRDLQ RNHEHTKSFL LHYISPSPVI GSSNRMLLIL LRVLTFVIML YYAVLIPFTK
VEESFNMQAV HDLLFYGFNL SKYDHFEFPG VVPRTFIGPL YLAGIVSPLR MLEYPIKFSK
PYLQLFTRLA LGATVCFGHV RLSRSLKLAF DNNVACWYLA ITISQFHTMF YASRTLPNIF
ALALFLFVLA FYLDECYYKA AVVATFSATV FRLELGILYA IMFLPILMRW RRRGVKLACF
VLLAAICSVA LSTVIDSYFW NRLVWPEGTV WWYNIVLNKS SNWGTLPFLW YFYSAIPRNL
CCTVCFVPFS LFGPEKIRRL TLWALGYVLI YSFLPHKELR FIFYAIPLLN IAASWVSAEI
MLMRSSSVPT LIAIALSLLQ PMINILLALC FMRAAITNYP GGEAIVTLHT TLRAEGLSGK
PVRIHIDAYC AETGVTRFLQ VNPLWEYNKS ESLSLAEHKL DFDYLLIGDS DDVTQVNKNY
ITTHRTLFFF HGFAGIELER NATFPFLSVQ YKLKPRVALL KKEPLITTSA YPYKGKVVVV
ILLWVFFPTI YTLKLSFVEQ EEAQYVQALH DILYHGFNLE QYAHFGNADV APFSFLGPLY
FATLTYPALL LNRLAIIGKS EVIMFARLAF TCTTMAVTGR LAKCVANKFG VAFCIWYFLI
MLSQFQIIHS FTRLGPHSFS LLYAIIVICC MLERKYDKAM AAALFSAFVF RLESIVFHTL
LLGPCLLAKP SAERKELVKR SLKSLLTPVA FTLLIDSFFW QRTIWPEGCV WLNYPLFSTD
KSSSVHHFIW YFFSALPRCT QASFCFLLPF ASESRTIFAL HLAAISYVAY LSLIPIKSVW
TILYTLPTLN LVAAWNSSIW NHRLCRYNVA MRLHLLFNVL STVALFQTSL DGTSGGYAVK
EFHSLRQLQN ATDWSIRVLL DDHVRTHGYS QFLDSNPVWR YETTKQADLL LFQKQWYHYV
IVGDETNAIN KAQLYEESHD IIKVYRFPQT TVCDALPLLC TSERRPQLCV LKKK
//
