ID A0A139I6A6_9PEZI Unreviewed; 911 AA.
AC A0A139I6A6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_1304 {ECO:0000313|EMBL:KXT10293.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT10293.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT10293.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT10293.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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:KXT10293.1}.
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DR EMBL; LFZO01000270; KXT10293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I6A6; -.
DR STRING; 113226.A0A139I6A6; -.
DR Proteomes; UP000073492; 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; cd18583; ABC_6TM_HMT1; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221:SF668; ABC TRANSPORTER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
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:UP000073492};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..597
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 631..865
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 200..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100718 MW; AD4A275F25C1C1C8 CRC64;
MATTGGRHGS AIAALHYIGP IVAGTYFVAA KTTAGCLLQH ASAHAGSRSR RYAAISLQAA
VAVTAAAEAL SAIIQYLQQP GWYASQDYIV YLILLFAVHG SLVLGLLENK KPLWHPYLGA
WLLALGFEIP LFTLQITSDL PESISGLPEN DYSRARMVLC VARAALLVVV FLIISALALH
DRPKSVKLDA ESDALLQAGV NGSSANGSAN GKKPKRKSSS PSSRDSILCN RASGSASNTD
AGYSDTLKGD DDDDDVDVDS DSEEPERDKE LKKQQQKRLE ESGSWLGYIK EFRIFVPMLL
PWKDRLVQAC FAVIALIIVA ERALNILVPR QLGIIVTELS QTGMTGQVPW KAIGLWVLYA
SLDSPACLPL IKQLAQIPIE QYGYKQISTT AFSHIMGLSM DFHNEKDCGE LIRAVDQGTT
LQNLVDFFLF EVAPMFFDLV VAFVYVSLLF DVYMAMILIG VGIAYVWIGT KVTAWSMRHR
RNFNTAWRNE SKVQTEAIVN WSTVSHFNRG QYETQRYVNT VDSFNLAEWK YYLTYHLGAA
AQSFIMLVGR LTAVMLAATR VAQGRAPVGS FVTLVTYWRS IEYPLANVSY SVRRVSQMLI
DSERLLQLLT TKATVTNSPT AKDIEISEGE VVFDHVNFSY DPRRATLKDV NFRVKPGQTV
ALVGETGGGK STILKLLYRY YDVADGAIRI DGQDIREVTL DSMRNSFGMV PQDPSLFNVS
IMENIRYARL DATDQEVHEA CRAAAIHDKI MSFPDGYKAT VGERGVKLSG GELQRVAIAR
AILRRPKIVL LDEATSQIDA ETEALIQEAF KGLTADRTTF IVAHRLSTIQ HADLILVIND
GQIVERGTHD ELFRKKGKYV ALWSKQLSKE VRDMGNTLDV TKKDEDLIAL DELQPASEGA
SSGTRRDEES R
//
