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Database: UniProt
Entry: A0A0G4FHC1_VITBC
LinkDB: A0A0G4FHC1_VITBC
Original site: A0A0G4FHC1_VITBC 
ID   A0A0G4FHC1_VITBC        Unreviewed;       889 AA.
AC   A0A0G4FHC1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Vbra_15412 {ECO:0000313|EMBL:CEM12692.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM12692.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM12692.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC       Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC       {ECO:0000256|ARBA:ARBA00008575}.
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DR   EMBL; CDMY01000436; CEM12692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4FHC1; -.
DR   STRING; 1169540.A0A0G4FHC1; -.
DR   VEuPathDB; CryptoDB:Vbra_15412; -.
DR   InParanoid; A0A0G4FHC1; -.
DR   OMA; DIQAGHF; -.
DR   OrthoDB; 7698at2759; -.
DR   PhylomeDB; A0A0G4FHC1; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd03223; ABCD_peroxisomal_ALDP; 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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11384:SF59; ATP-BINDING CASSETTE SUB-FAMILY D MEMBER; 1.
DR   PANTHER; PTHR11384; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1.
DR   Pfam; PF06472; ABC_membrane_2; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
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:UP000041254};
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        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          140..374
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          508..735
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..769
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  98855 MW;  564F5CFC42FABD2D CRC64;
     MTSGPVKASA GGLLPPGASI SPSSRRRNSR LAAAFLARLF GSPSRKLGWV SAAVLAWAYY
     HYQQELKART EEPRIRSRPR RGSSREQGPE EAEEEDNRGS SGPFDIHGRG KVDALFVRRL
     LGLVKIVIPG IACREVRLLV LLCAFLVART FMSIWIAALN GKIVKAIVQR NLRLFIRRIG
     TLAAYAVPAS FINSYIDYLG KDVALCFRER MSEHFCSRYL DKMVFYRLSH LDVRLPNAEQ
     RLTGDIERWS LALSSLVSNV LKPLLDIVLF TRKLSELVGI QGPIAAMGWY VLSGLAIRAV
     SPPFGKYTAQ EQRLEGEYRA VHADIVNNAE QIAFYRGNVF EQHRVKSAFE RVVAHLQHLQ
     VRRLYMGCFD SLLVKYGAVL VGYTVVGLPV FGPNRQAYLD SVQSDPTQIT QDYVRNSSLL
     INLAKAIGKL VVAYKDLQLL AGYTALISEL QDVLADLEQG HYSAFVPKTT TSTTDTQPSI
     QYPESEARPP PSPSHAPLRG RIVPSDEIRF VDVPIVTPAG DLLINNISFS VRRGMNVFII
     GPNGCGKSSL FRILGELWPL LGGELHKPPP HEIFYIPQRP YFPEGSLRDQ IIYPDTEEEC
     YQKGCTDWEL EELFGMVRLK YLLNRCPYGW DTWNDWDERL SGGEKQRLAM ARLCYHQPEF
     AILDECTSAV SVDVEGHLYS QCKQRGITFI SISHRLNLLK YHDYLLKFDG QGGWSFEKID
     QPLRVDSYSS FLTFHQPPNP PPPLMAGTPP APSSTTYPPD PPPSSSPSEA PNQPDTADQP
     LPFYHPPAAA AAAAAAASFS SHPAEMHIHP SQSLTSLAAR LPLGALRQVP SVPGDMPSMR
     HPPLLDSLGD DDRHGHHGRG SSGSEYGFRV HPPDMLSPID SPLYRGMSD
//
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