ID   LMBD1_AJECN             Reviewed;         590 AA.
AC   A6QTW5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Probable lysosomal cobalamin transporter;
GN   ORFNames=HCAG_00821;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Probable lysosomal cobalamin transporter. Required to export
CC       cobalamin from lysosomes allowing its conversion to cofactors (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH476655; EDN02957.1; -; Genomic_DNA.
DR   RefSeq; XP_001543775.1; XM_001543725.1.
DR   AlphaFoldDB; A6QTW5; -.
DR   SMR; A6QTW5; -.
DR   STRING; 339724.A6QTW5; -.
DR   TCDB; 9.A.54.1.3; the lysosomal cobalamin (b12) transporter (l-b12t) family.
DR   EnsemblFungi; EDN02957; EDN02957; HCAG_00821.
DR   GeneID; 5450939; -.
DR   KEGG; aje:HCAG_00821; -.
DR   VEuPathDB; FungiDB:HCAG_00821; -.
DR   HOGENOM; CLU_028341_1_0_1; -.
DR   OMA; IITTFTW; -.
DR   OrthoDB; 744771at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006876; LMBR1-like_membr_prot.
DR   Pfam; PF04791; LMBR1; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Lysosome; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..590
FT                   /note="Probable lysosomal cobalamin transporter"
FT                   /id="PRO_0000365821"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          567..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  66363 MW;  75393DA1C398C437 CRC64;
     MALLQSSLIW VVYAIVFFLL VAVSSIFIYI YQTPSERSTY VTTVCIFTLT ALLATVLLLP
     VDVALVSSTT SSREGRRKSW ATQDEVDKIT FSLAVAYYFL YSLDAVLCLL VVPFTYFWYE
     EYDEVASEDG SQTFRKRFWG AFKYTVAFIL LTVILFLVGF FVPIGRRKDK PNLDLDYFRR
     LLTENHGERA LTFALGLLIT IGILVYVLYT STGLALLPVT IIKSAPAISS PTLSANTASR
     LEENIERQRQ LEGRCGGNPD RLPSKQRREL DSLVRQARTL RRRQRLAEEA RRPSGSWLLN
     AWFKLSAVFR PLKLLSGLLL LAIAMLVWVS MLLTSIDKAM NSICKQNCGY ILGKTNILNP
     INWVFVHSSK VFPVDYILFV FLVLVFFCSS VVGIATTGIR FLWVRIFQLR KGHTSPQALL
     ITTVMLTLIT LALNYSISMV VAPQYATYGP QTFCDHPPKH PGEQPDCTGL EPLIKPCSEL
     SENPTAKEIC TPTVVSTFLN RITLNFPFFG IVDFWAQFFF LGLSLLVFLV TIFRTPKLDE
     QQFDEDAEAA EEEGLLASTG RRFGATWEDI TGRASRSPQV SGSAGRGTRE