ID A0A250XJ57_9CHLO Unreviewed; 1022 AA.
AC A0A250XJ57;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=CEUSTIGMA_g10533.t1 {ECO:0000313|EMBL:GAX83107.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX83107.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX83107.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX83107.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000256|ARBA:ARBA00004815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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:GAX83107.1}.
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DR EMBL; BEGY01000092; GAX83107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250XJ57; -.
DR STRING; 1157962.A0A250XJ57; -.
DR OrthoDB; 49929at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03221; ABCF_EF-3; 1.
DR CDD; cd18626; CD_eEF3; 1.
DR Gene3D; 1.20.1390.20; -; 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; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR040533; EF3_4HB.
DR InterPro; IPR047036; EF3_4HB_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR PANTHER; PTHR19211:SF5; ELONGATION FACTOR 3A-RELATED; 1.
DR Pfam; PF17947; 4HB; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; ARM repeat; 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.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REPEAT 83..120
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 419..633
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 659..974
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 951..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..419
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 994..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1022 AA; 111800 MW; B00260F76AC7E739 CRC64;
MSAEKVIELF KKLSVSATPE ARDAASADVV KAVKADGISS LATVAEQLKA ALEEASSREA
ALVTFKLLIT EFGAKAEPYL FPLLPALLER ASDKVPAVKT GAEAAATALF AVLNSYSTEN
ALPALFEGMQ QQKNWQTKVL ALNLLAGLAK TAPTQIAYCL HEIVPRLTDS MADAKEQVKA
ATTVALTETF AVNGNRDITQ FLPALIGCIA RPAETTDCIH KLAATTFVQQ VEGAPLSIIV
PLLVRGLRER ATAIKRKSAV IIDNMAKLVE NPHDAAPFLP KLLPELEKVS NEVADPECRK
VAANAHATLL RVGGEGKLSA PKKADVEVMK ERLSSALGAK ASSVENTTLT YAASLVCQLC
NFKNWMASEW SNVVTPYLAA FVSQEEAQAA VSSLLTQSKE DAEKEAAAAQ EEEEAGEDLC
NCEFSLAYGA KILLSMAKLR LKKGKRYGLC GPNGAGKSTL MRAIANGQVE GFPTQDQLKT
IYVEHDIDSE EADTPSLDFV ANDSRLGGAP REEVEKMLVS VGFSEEYLKK PVGSLSGGWK
MKLALARAIL MKAQILLLDE PTNHLDVKNV AWLENYLNSL TDVTSIMVSH DSGFLDRVCT
HILNYEGRKL KCYRGNLSEF VKQYPAAKSY YELTNANVAF KFPEPGYLEG VKTKDKAILK
MIKMGYRYPG SEKNTVTDIS LYCTLSSRVV VHGANGAGKS TMIKVLCGEA EPTEGTCWKH
PNLRIAYVAQ HAFHHLEQHL EKTPNQYIQW RYAIGEDREA LTKVDRKLTE EEEKKMKQVL
VIDGVKRVVE KILGRRKLKS SYEYEVQWVG CHPDQNAYLP RDELVQMGFE KLVNEVDAKE
AAAQGLYAKP LTALNISKHL EDFGLDTEFS THSLMRGLSG GQKVKVVLGA AMWNNPHMIV
LDEPTNYLDR DSLGALAESI KAFGGGVIMI THNQEFSSAI CSETWNVADG RMTPSGQTPG
GGSKEKVEFK QEEETTDAFG NVIKVKAAKK LKMSNKEKKA LQKLREARKA RGEEVTDSEE
DA
//