ID A0A319A7J7_ASPLB Unreviewed; 1203 AA.
AC A0A319A7J7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:PYH56029.1};
GN ORFNames=BO96DRAFT_367604 {ECO:0000313|EMBL:PYH56029.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH56029.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH56029.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH56029.1,
RC ECO:0000313|Proteomes:UP000247441};
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 (DEC-2016) 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 CSC1 (TC 1.A.17) family.
CC {ECO:0000256|ARBA:ARBA00007779}.
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DR EMBL; KZ821351; PYH56029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319A7J7; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR InterPro; IPR032880; Csc1/OSCA1-like_N.
DR InterPro; IPR022257; PHM7_ext.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR PANTHER; PTHR13018:SF20; SPORULATION-SPECIFIC PROTEIN 75; 1.
DR Pfam; PF14703; PHM7_cyt; 2.
DR Pfam; PF12621; PHM7_ext; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 20..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..188
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 212..284
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 562..648
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 659..931
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1123..1194
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 287..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 135848 MW; 224292D9A1ED5609 CRC64;
MTDLGSALEH AGGSGKNKEG ISIGTFVASL TTAIVVFAVE FLLFILLKGK LTRIYQPRTY
LVSDRERTQP SPPGFFRWIG PVFRTSSTEF IQKCGLDAYF FLRYLRMLLK IFIPLGCLIL
PVLLPLNKVD GKDTSYKNGT AADGQWNVTG LDQLAWGNVK PENTSRYWGH LVMAVIAIFY
VCAVFFDELR GYIRLRQAYL TSPQHRLRAS ATTVLVTAIP ESWLSVEALE SLFDVFPGGI
RNIWINRNFD DLNEKVKQRD ELALKLEAAE TDLIIKCKKA QLKQARAEAK KAGKNPNTAE
TKEKKDADRR ASALALDGGV SSGNPHQART LDQILHRTKS RKKPEQPGPK KRLNPLDPAV
EAAEAVGQGM GKLGKTMIGG FKKVEHGLDG TLARSGGFVP GDAIVIPAHH SEPETDEANN
ADDMEPQVWS TDPRDHAEPV PESSASEARP ASRPKRPFWK SQLSKDSKTS SEPDELPLTA
PESPVENEEV EASGSESGNS IKEKIPSDNA RGFKEGDRVQ GEEYPIAYNE GFDNEDFGEP
LWQKYIRPKD RDTMRLPIFG LSWMPSLWLI GKKVDTIDYC RKELARLNLE IEIDQQNPEK
FPHMNSAFIQ FNHQVAAHMA CQAVSHHVPK QMAPRLVEIS PDDVIWDNMS IKWWERYLRT
FGIIAVVCGM VIGWAIPVAF TGLLSQLSYL EAAFTWLSWL STLPGWFISA IQGVLPALFL
AILMAILPLI LRFLSRTQGL STGMAVELTV QNYYFAFLFV QLFLVVTISS SFSTIISNVT
DVTSWPELLA QNIPSSSNYF FSYMILQAMS VSAGALVQIV NLVSWFILAP ILDKTARKKW
GRTTNLNQMQ WGTFFPVYTT LASIGLIYCV IAPLILIFNV ITFSLFWFVY RYNTLYVTKF
RFDTGGLLFP RAINQLFTGL YVMELSLIGL FFLVRDTQGE VACEGQAIIM IIVLILTAGY
QILLNDAFGP LFRYLPITLE DDAVRRDEEF ARAQRTRLGL PNEEEEDPND TIEHQLAERE
HRQHQIDRMS HDIELKTLES SSPDRENHHI MHRPHLGPQR KSWAERSPNR RSPYYKAHSN
TQVPSVQRLR DRIAQDAEAQ GPPSRNVGTT LFAGIHDELE DLTPDERDQL VQRAFQHDAL
RAKRPVIWIP RDDLGVSDDE VYRTQRFSKH IWISNEYQAL DGKCHTIFSR SPPDFSEVDL
IQL
//
