GenomeNet

Database: UniProt
Entry: M9LRJ5_PSEA3
LinkDB: M9LRJ5_PSEA3
Original site: M9LRJ5_PSEA3 
ID   M9LRJ5_PSEA3            Unreviewed;      1097 AA.
AC   M9LRJ5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Protein containing adaptin N-terminal region {ECO:0000313|EMBL:GAC75711.1};
GN   ORFNames=PANT_18d00026 {ECO:0000313|EMBL:GAC75711.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC75711.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
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}.
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DR   EMBL; DF196784; GAC75711.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LRJ5; -.
DR   STRING; 1151754.M9LRJ5; -.
DR   OrthoDB; 49929at2759; -.
DR   Proteomes; UP000011976; 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   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; 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; IPR021133; HEAT_type_2.
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   SMART; SM00298; CHROMO; 1.
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.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   REPEAT          93..131
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          451..665
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          691..1007
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          820..881
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1004..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1090
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  120014 MW;  0CAC3E32EAA9DAD5 CRC64;
     MSSASQALEG LYKAPSAEEC YVAAEQLAEY VNSTSLRVLQ SEGVLDSLVK ASKNKKSGYE
     REAAAIGLDA IFVKVAGKNA PSPLGAEPWL LDTLPAILEL YADKGDVVRQ AAETAASSLL
     ALVPPEAAPE FLTVLYEVLG SGSAKWQAKV GALKLIGRLS ATASEQIGDE LVELIPYLTR
     AMHETKAEIS KQARKTAIKV CEACLDNKDI RPFIPDLVGC MAQPDAVPEC IKKLSGTTFV
     AEVTGPALAV MVPLLARALN ERSQNVQRQA VVVVDNLCKL VRDPHEAAKF LPELTPGVER
     IEKGASFPEV REHAKSALDT LTAATAAVDA SAATEDPKKV FAQQCAAALD AILAAVQAYV
     PEEHANLKSD AFAMTGLNYL SKSVARLANK RILHTSAWEE VYVLPYLRRV CKDDDAAKTA
     TADLRKTYIE LDKARFGNSE EEDDDEAGEC LCRTEFSLAY GGLLLLNHTT LKLYRGHRYG
     IVAANGSGKS TLLKAMRDGK VEGYPSQDEV RTLMVEHSLQ GEDGSTPIID FIANDKKLVG
     KTREQVAEKL REVGFDDEKQ KNPVSSLSGG WKMKLELARA MLSDAVVYLL DEPTNHLDVQ
     SIAWLENFLV TNKQITVVTV SHDSGFLDNI CTDIIHYEKK KLRYYKGNLS DFVATKPEAK
     AYYSLAATTV KFSFPPPGSL MGVRSNTRTI LKMSNCTYTY PGMTKPSLHD TSCAISLSSR
     VGVLGPNGAG KSTLIKVLTG ETVPQQGKVE KHPNLRIAMM AQHAFHHLEQ HLEKSAVEYI
     AWRYQDGHDR EMTEKASRKM TDEEKAQMET PIKSTTGESR KVEYIVGRQK LKKSYQYEIK
     WVGYEHRNNS WIPRERLLEL GFSKLVQQFD DFEASREGAG SREISVKLIR QHLEAVGLQG
     EIAQHHAVGG YSGGQKVKVV LAAAMWNNPQ VLVLDEPTNY LDRDALGGLA TAIRDWAGAV
     VIISHNMEFV GALCPEIWNV DNGRIMSRTK TALAEGAFLD EMENASTPGA SVPGTPLPGS
     TAASRLTSKA GTPVSSVAPT PAGSGDEGEQ DMSKFKAKKG KKKLTRNEKK AQEERRRLRL
     SRWLTYGGER EPDTDDE
//
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