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
//