ID A0A0D2CBA7_9EURO Unreviewed; 1119 AA.
AC A0A0D2CBA7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=PV08_01412 {ECO:0000313|EMBL:KIW20834.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW20834.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW20834.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW20834.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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DR EMBL; KN847492; KIW20834.1; -; Genomic_DNA.
DR RefSeq; XP_016241050.1; XM_016375774.1.
DR AlphaFoldDB; A0A0D2CBA7; -.
DR STRING; 91928.A0A0D2CBA7; -.
DR GeneID; 27328495; -.
DR VEuPathDB; FungiDB:PV08_01412; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03221; ABCF_EF-3; 1.
DR CDD; cd18626; CD_eEF3; 1.
DR Gene3D; 2.40.50.990; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 3; 1.
DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 488..706
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 732..1049
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1062..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 123347 MW; D05AFFABAB9702A2 CRC64;
MPHIESPPLA PAMASTVVPT KSSFSGHPPT PEEVSGILKT ILEADAAQTA LDASYALTNL
LIQSIGIRGL LGYDLIPAIK KAAADKKSGS KRESAMFILG AMFEKFPREQ PISEVVFLVR
DGGLLYLVLD GLADKGPSVR ESAQYAVDEL FKNLEPEAMV AGLLPALHRY LSKPTGKWQG
TVAAFALLGK MADKAQMGTG TKEEEQAKDV LRNAMGRTLK ELIPVVEGGM HDLKAEVAKA
ATKTMTSLTT LLQNDDVGPR VPLLIDTMKN PSAQTLQKAI HALSQTTFVA IVTSPVLALL
TPLLERSLNT PTTSQEVLRQ TVVVVENLTK LVHDPEEART FLPKLQPGVQ RVKNGASLPE
VRELATRAND VMKKAMGEDK DAANNGQIAK ATTDDVLKIL DSQLRAQGGL QKEDAAIWKD
GQIYVSEMVR EDVNSRAFAR IPSRVGPYLK YMLPDESCSA VADGVQKYFI EEDHKKFGAP
VVEDPNEVEI VNADFSLAYG GMLLLSHTNL RLLKGHRYGL CGRNGAGKST LMRSIADGKL
EGFPSKDVLR TCFVEHNQGE DADISILEYV AKDPEIAKEG RERISEVLSE VGFTAGPEGR
QSHKVGSLSG GWKMKLALAR AMLMRADVLL LDEPTNHLDV ANVKWLEEYL QKHSEITSLI
VSHDSGFLDA VCTDILHYEQ KKLVHYPGNL AAFVKVKPEG KSYYTLSATQ VQFKFPPPGI
LSGVKSNTRS IIRMTNVSYT YPGASKPSLQ DVSCQLSLSS RVAIIGANGA GKSTLIKMLT
GEAIPQTGKV EKHPNLRIGY IKQHALEHVE MHLEKTPNQY LQWRYANGDD REVLMKATRV
LTDEDKEQME KWVDLGDGKG PRQIENLMGR QKYKKTFQYE VKWRNMLPKF NSQVSRESLL
EWGFQKLIQE FDDHEASREG LGYRVLEPKV ISKHFEDVGL DPEIANHNEI SGLSGGQKVK
VVLAGAMWNN PHLLVLDEPT NFLDRDSLGG LAVAIRDYKG GVVMISHNEE FVGALCPEQW
HVADGKVMHK GHLAIDLNRF EDSRPGSSNV SSVVSSANVS ATNSGVEDNS EMKFKAKKKK
KLTRAQMKER EVRRRLRHIE WLNSPKGTPH PPDTDDEAE
//
