ID   A0A319FEP2_ASPSB        Unreviewed;      1113 AA.
AC   A0A319FEP2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=DUF676 domain-containing protein {ECO:0000259|Pfam:PF05057};
GN   ORFNames=BO78DRAFT_371738 {ECO:0000313|EMBL:PYI05083.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI05083.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI05083.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI05083.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) 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 putative lipase ROG1 family.
CC       {ECO:0000256|ARBA:ARBA00007920}.
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DR   EMBL; KZ826361; PYI05083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319FEP2; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015693; P:magnesium ion transport; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR045863; CorA_TM1_TM2.
DR   InterPro; IPR007751; DUF676_lipase-like.
DR   InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR   PANTHER; PTHR47685; MAGNESIUM TRANSPORT PROTEIN CORA; 1.
DR   PANTHER; PTHR47685:SF1; MAGNESIUM TRANSPORT PROTEIN CORA; 1.
DR   Pfam; PF01544; CorA; 1.
DR   Pfam; PF05057; DUF676; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF144083; Magnesium transport protein CorA, transmembrane region; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        955..975
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        995..1016
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1028..1047
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..154
FT                   /note="DUF676"
FT                   /evidence="ECO:0000259|Pfam:PF05057"
FT   REGION          425..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          894..921
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        434..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1113 AA;  126932 MW;  D98F935280663363 CRC64;
     MWKMAADNEI NGGQPLRIET TVDVVAVPAI GADPRRTWLD ENSQTPWLLS DLTRCIPSAR
     VLLSDHGHLD SRDDLESLAH RLLKWLLEER QATSLRRPIF FICHSTGGLV AKAALIIASQ
     LTSKLGSILS SCYGIAFLAT PHHGSSYLSA PEFTRSTQRL MRLKHHVPPG LQELFRPRHP
     YLLRLSNQFR SISADIKIWT FLETVDSTLS ITDSETGDSV DMHVPITSIR SGILDLEHEK
     EVPLATDHVG TAYFKGQEFT TRMSFINELQ ASVSMAINLS KMADAPLDVD LEVMVQVNGF
     FEDTARGISD ETPLKLWSTK ASLKEYLTSG PSSCLSNRLK KTAGIPSSIY DDSSISSFDS
     RPTSAQVRSS MDGIVNPTAL HASESTRPKA IPQRPSIKES RSFLGQAFPR IHITEPTSQG
     YFDVQSDSAE EVQRSVPSQE DETEEDTKKR ETGTSNMIAS LPPRYRSFLP IPLPSRDNVD
     EQRAEMPRRV PRFDQPEPGS EKLLWIHVPY THTGWVPSIL SKACEDKERQ AFLEKFINEE
     SWYSNIIRAR HLEPHARYVR SSCIHFKQNK ASFPGGNERY KDPTLALYIP YLHWDTYWNL
     VQRRKVVEER LRQGRFRPVP SDISKSSLES KLIWKYLGNE PPIHIRRTLD QFGYPNLRST
     VARDDDQMLW KRTKKVVNLN DEIKISVQPE DGPEAKNTFM DGKVLMVDQL WLWIVDERTV
     VTFFPNQEAT TAEGKLYEQS NLYNSIYNEL NGDLARRFET AGDLASLIVL HAVTVLLDRT
     LHRDLQILRI FEESISILTE IVTKSFKRFR NRGFNTRPAD YNKNAEGRPM SAAERDERDN
     KVARRNREDL STLLELRDIV DELGTILKLL EQQTITVTAM TSYFEHKGCG KVFIDSALSR
     LEEYRNQVLD MRENATLAQK AVENLLDLKQ KQASVDESRL ARWEAEVTQD QSRSVMVFTI
     FTIIFLPLSF FTSLFGINAR EWSGTPENPT LGEMLYIAGP ASFAIIVIAL LIAFNERLRE
     TLWRAQKLIL DILADFLLAP ITLLFQWRKM AAASATKQDS GRTKGRLNRY RRNPQRQSQE
     DIWTEHEDKV AVAVPGDVEV ERYSEKGRER GRF
//