ID A0A225AF40_9EURO Unreviewed; 1070 AA.
AC A0A225AF40;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OKL59922.1};
GN ORFNames=UA08_04651 {ECO:0000313|EMBL:OKL59922.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL59922.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL59922.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL59922.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKL59922.1}.
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DR EMBL; LFMY01000006; OKL59922.1; -; Genomic_DNA.
DR RefSeq; XP_020120043.1; XM_020266944.1.
DR AlphaFoldDB; A0A225AF40; -.
DR STRING; 1441469.A0A225AF40; -.
DR GeneID; 31004406; -.
DR OrthoDB; 2420228at2759; -.
DR Proteomes; UP000214365; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF428; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000214365};
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 134..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 628..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..202
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 234..468
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 520..773
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 810..1067
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1070 AA; 118888 MW; 9BC34A0FE905CD47 CRC64;
MNRLRLMTRS ALVGLIHDKT MRAPSVAYDN GEATTLMSTD ADSLDGVAEM VHEIWAQIIE
VLIGTSIHLL YLLDWVLKFV PLQKNWNNAT QSRIAATSSV LSAMKVIKML GIQRNLMSHI
QELRKRELWA ASRLRWIVVY YNASANALGI FTPAITLIVY ALISLARGGN LDTETAFTTI
AILSMVTHPA NMVMTIVPRA VAAFAGLERI QTFLLKQPLQ DNRGILPERF EHPSPVIQIH
ELSIEHKQLV LDNINFEIAA GSLNIISGHT GSGKSTLLRA ILGEVVPTHG SVSLSTREIA
YCAQRPWLPN GTIKEAVYGA TEFHDASDQY HEWWYNEVIE ACRLTHDFDY LPDGDQTQIG
SRGINLSGGQ RQRVTLARAL FARCDILLLD DIFSGLDGET EQTVFNNLLS SRGLLRRMNT
TVVLVSNSLQ HLQTADHIVV LNNHGILAQG NWHKIQTEAV YPAKFSSGHR VKDSAILSGN
FEKLNAQLRA KDETEVDLAR QTGDPAVYGY YFGFINSVNI LFLLVSTASY SFFVTLPQYW
LQLWTELGGR NSSYYIGGFL LLSFMSWSST SIQMWSILIR LAPQSGLRIH QRLLRIVMSA
PLSYFSKTDT GSILNRFSQD VQFVDKQLPS ALQTVVTLCV VLVYIIQKAY LRTSRQLRFL
ELESRAGVFS SFLESVEGLE TIRSFGWSRS VIQGNILSVD NSQRPEFLLL CLQRWLNIVL
DLLAAAIATC VVAIAVAFRG RVSGAQVGIA LNIMLVANTT LLKFVENWTT LETSLGAVAR
LKTLEEITPC EGAKTENLDP PENWPPKGHI EFTNITASYH SESVALRNLS LDIPAGQKLI
VCGRTGSTLL LTLLRLLELQ SGHIELDGID IKQVRLDLLR QRCFVVVSQD PLILPNETLR
WNLDPDTSVP NDILVASLAK AGLWAHFFDS DRGRDVEINI NASGFDAHPI LDRKVSLFQE
LSVGQCQLFA LCRALVKVNA LRRSGVKPVI ILDEVTSSLD TATESTIHQI IDDEFTEKGH
TVIIVTHRLG ALEEHAETGR DIVALIANGR VQEVIEDLGP ATFQRFGQAG
//
