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Database: UniProt
Entry: A0A2J5HQV6_9EURO
LinkDB: A0A2J5HQV6_9EURO
Original site: A0A2J5HQV6_9EURO 
ID   A0A2J5HQV6_9EURO        Unreviewed;       740 AA.
AC   A0A2J5HQV6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alpha-1,6 mannosyltransferase subunit {ECO:0000313|EMBL:PLN79526.1};
GN   ORFNames=BDW42DRAFT_186677 {ECO:0000313|EMBL:PLN79526.1};
OS   Aspergillus taichungensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN79526.1, ECO:0000313|Proteomes:UP000235023};
RN   [1] {ECO:0000313|Proteomes:UP000235023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA   Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA   Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA   LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA   Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA   Cantor M.N., Hua S.X.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family.
CC       {ECO:0000256|ARBA:ARBA00037964}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375}.
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DR   EMBL; KZ559559; PLN79526.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J5HQV6; -.
DR   OrthoDB; 2965755at2759; -.
DR   Proteomes; UP000235023; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43083:SF6; MANNAN POLYMERASE COMPLEXES SUBUNIT MNN9; 1.
DR   PANTHER; PTHR43083; MANNAN POLYMERASE II; 1.
DR   Pfam; PF03452; Anp1; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:PLN79526.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Transferase {ECO:0000313|EMBL:PLN79526.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        256..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          43..128
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          155..244
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          252..345
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  81995 MW;  EB904FFFBE94332F CRC64;
     MSSPPYTPSR LEGAASMESS KVVDTTERKG AAPPPTPDTK KNYKGFVAGV FSGIAKLSGM
     SPRCVFDTVK VRLQTSKDGH FRGPLDCVLQ TVRKEGVAGF YKGATPPLVG WMVMDSVMLG
     SLTLYRRLLL ENVFSRPEIR RITPFAASQK DPSTLPSFGH GIAGIMAGTT VSFIAAPVEH
     VKARLQIQYA ADKSQRLYSG PIDCTKKLLG THGISGLYRG LFATILFRSF FFFWWGSYDV
     LTRMMREHTN MSAPAINFWA GGVSAQIFWI TSYPSDVVKQ RLMTDPMGGG LNDGQRQFRG
     WKDAAIAVYK ERGWKGYWRG FVPCFLRAFP ANAMALVAFE GLSFRHRTAA MAVARSMRRT
     SPITLLLAAL LAFGFLIFLI SPSASSPPLA DSVHAQPLTD NSGSSSQRRV QDAAQNPLSP
     PTKPFHKAQP IRDDGQSAPP PVVHYDLNTL TTTSDSAGQR ERVLILTPLA RFYQAFWDNL
     VRLDYPHELI SLGFIAPHTF EGNAAVASLE AAISKTQSGP IKNRFASISI LRQDFDPPLQ
     SQDEKERHKM SAQKARRESM SRARNSLLFT TLGPSTSWVL WLDADIVETP PTLIQDLSSH
     SLPVIVPNCF QRYYNTEKKA MDVRPYDFNS WIDSPTAQEL AETMDPDEIL LEGYAEIPTY
     RALMAYMADL SAPNPGRVVD LDGVGGTALM VKADVHRDGA MFPPFPFYHL VETEGFARMA
     QRLGYTVHGL PDYLVYHYNE
//
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