ID A0A2P6VGA6_9CHLO Unreviewed; 2637 AA.
AC A0A2P6VGA6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=C2E20_3710 {ECO:0000313|EMBL:PSC73107.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC73107.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC73107.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC73107.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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:PSC73107.1}.
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DR EMBL; LHPF02000008; PSC73107.1; -; Genomic_DNA.
DR STRING; 554055.A0A2P6VGA6; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd00590; RRM_SF; 3.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 670..712
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1107..1184
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 381..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1854..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2419..2447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2637 AA; 275113 MW; 9F2A318BDFDDED25 CRC64;
MLQEGKVCLN KPDSVRAADE LASNAGTPQL AEALLAEDIH ADELVVTVLQ ECLRRADVKP
QEVGDVCLGS VFPPSSKRAN EVRAALLLAG FPNKVPAYTV NRQCAAGLQA IANVAAGIKA
GYYDIAIAGG IEHLTKDPLD WQGSDNPRVL ESPDAKDVGL ALGLTAENVA EKYGVPREEQ
DRLAAASHAK AAAAQASGKF VDEIATVHAR VTDPKTGDVT EVSVDHDDSI RADTSYDKLH
AMKPYFKKDG TVTAGNACQN TDCAAAMLLM RRAEAEKRGL PILGVLRSFA TVGVPPGVMG
TAPTLAIPKA LERAGLRKED VEVFELNEAF ASQTAYCLRE LGLPEEKVNV NGGAIALGHP
AGATGARITV SLLHELARRS ADEATSSGSA DHEGGSVNGN EQKPRYGVVA LCTGAGMGAA
AVFEGTRSTA GSASFSRMGS TSSAADLGST SSAADMGITA STADVPSRQG DDDAVLGTVL
VNQRALRNGP APEEDPDLAL AKMLQAQEQA WLAMAGGSGA LENLPLGGGG GAPGGAAEPA
AAAEGGDGEE LTDEEMARRL QEDEEREFQA RLLALAGVGP AGVAAGGGDG AADDGGGDAE
GGDAGNEGYL TEDDADPDEL TYEELTALGE AVGTVSRGLP QAAIDALPTA QYYEVAGTAG
AEGAEAEEQC PICRVEYEPE DKLRVLPLCR HYYHLECIAE WLCRNKACCI CNKEVVEEKG
GSGGNSSGAP AAQAPAEGAS SEGGVDGVLG DRRRQEGLAL LCATKHEAGR LAHVEELLAE
HHRRAAAAGS AASGTEPPSV VRGLLVRYRL EGGYHLRQAQ RAEVAPDGSG KPLFLVQDPR
PDARSPLRKI PIHSLSGTNT LVKDDQWDKA GRGEVAALIA FWRHRGEAPT VAEAAAAAWR
KQVALGWEAQ YGGLPTEEVI RHLPMLLAVT RDAPSIVQAQ KLFTAEPSPV LPPVGSTRLR
LAVRTRPEEP PLPTSAYAPA DPYGGVGAAR NAPTAGGAYA GAPPDAGPGW YASPPAAGAR
WDASPRANAA AAAGVPRRSA RDRQPSPPPR SPTPSPSPRR AALAAPAGVA GVAGAAPAEE
APLAPVLLRH FRRAVFKPTE EWELIGREVQ ATGLAPTVSE RMLEAAFREA GATVRDVRVT
RQGDPRGELG FVLVASASQA AALVERLQGA KLEGRRMFLR GVRNEIEFIE RTMPEAAAVA
KRVMAVAAAG HARSPAHAGG PFWDPVWQLE WDCAQRLRAA EGPLPLQQLL KSVEWPRQVF
AASPGCLPGF LARRPFLFDL QQGGGGELSV SLLPGAKDWL MYKHALLQYL ADHPPRVPLR
QLEEALPPPA SLPACMRGMW LSKLMEHYLS CEVWSAAGRT AYRDPRTVTV ELQPFSAGAG
GPRFPRICGH FRGLAALDCP DQERCELPHA PQRVFKRLTM THRPPAGPLG GGDAPLLPPH
PGLLASAVPP AAALAPTRKV LSMLLATKSE LGRLAQVEAL AEYHHGLRSG AQPPPSVLHG
VLARVKLMGR CRLRLVAGAE AAAEAGGAPS ALLLQAPEAG IAGGAPPLRR LPIEGISSTN
PLDDQHWEAA GSGEVAELAA AWQACGYALP LAEALGAAWR KQAALQWHAQ QWQQAPDERL
RQVPSLLAAL ADAGGLALMQ QQLAALQADS LNYDLPAAAA ALSAALYRAV PASEPGAAAK
RAALSALLHL GLACVDGVEG SYCQLPVPAV HVQEALREAA ARDRQVAGQL AMLALQPSAS
ALPLAARLLT DCHDRRLVSL SGGAADTCQL LLHVDHLAEA YLGGGGGTRL PAAPGGAPTG
GPAGLGLAIS TALDTLSADS GSTPDASAAA AAAAPSRLDG PACLGAPAAA MPPSPWELLT
PGGGPPVSPT RSGTRSAGSI RSAGSTRSVG GTDDVTSGGP TRWHGVGGGG APPAGPPLVP
LLLPETEDWP AEWVLTGSML YCTRIPKAAA PHELHALLES AGVTVLSSRL LNGDRRGNIA
FVQLGSARQV ALAVQRLHGA KLCGSTLEMR ESAKELEWDC CQLLQTAGRP LDSWELLAGV
AAHVPPQLGR PISGVLSIFL SRRPHLFSLS HTPGSLLVSL VPGAEPFMKY KRALLQYLAD
HPPRVELHVL EAALPPPRDL HPSIGRKRLA DILAGFLKDE GAPAGDRGAA SPPLLLGPAA
LDTGRREGVS QLVASKKELG QLAQVEHFLA GAHHSTQPPG TQPPPSVLSG VLARFKSAGQ
YHLRPVVGVE AAAAGSGPEA VLFQAPEAAA AGAPPALRRI PLAAVSSANP CDEKNWEAAG
HGEVAALAAA WQACGYALPL AEAAGAVWRK QAALQWHAQH GKQAAEERQQ HIPALLAALA
DTEGLARVPA GDLPAAQAAL ADAISRVVPA SERDAAAKRA ALSALLRLGL LPYGVQASSY
RQLRVSASDV QEAMREVAAR RTGGRAAGDA GAAAQRKRSR SCSPVRGHGG ALHLPLEPLL
LRHSDARPSE WVLCSQELYI SGIHARTTPE ELRAALEGAG ATLKGLRMKP GDVRGSLAYA
MLPSAQDAVA LVLRLQGVQV GPNRIFLREQ QRRPPAQLSA QTPRSVALNK EDRVQLAPGA
VPFLTYKRAL LQYLADHRPR VRQRQLEAAM PRPAELPASM HGQAFYLFLY RKLGREQ
//
