ID L5JPZ2_PTEAL Unreviewed; 772 AA.
AC L5JPZ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Bifunctional coenzyme A synthase {ECO:0000313|EMBL:ELK01479.1};
GN ORFNames=PAL_GLEAN10019519 {ECO:0000313|EMBL:ELK01479.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01479.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KB031150; ELK01479.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JPZ2; -.
DR STRING; 9402.L5JPZ2; -.
DR eggNOG; KOG3220; Eukaryota.
DR eggNOG; KOG3351; Eukaryota.
DR InParanoid; L5JPZ2; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:InterPro.
DR CDD; cd19687; bHLHzip_Mlx; 1.
DR CDD; cd02022; DPCK; 1.
DR CDD; cd02164; PPAT_CoAS; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR PANTHER; PTHR15741; BASIC HELIX-LOOP-HELIX ZIP TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR15741:SF25; MAX-LIKE PROTEIN X; 1.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..772
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003968367"
FT DOMAIN 603..661
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 568..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 658..685
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 568..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 86041 MW; 91E002B2EB6427EF CRC64;
MAVFRSGLLV LTTPLGSLAP RLAPILTLAA RLVNHTLYVH LQPGMSLEGA AQPQASPVQA
TFEVLDFIST LYSGAKVHTH LDVRILLTNI RTKSAFLPLL PSPVQNLAHP PEVVLTDFQT
LDGSQYNPVK QQLERYATSC YSCCPQLSSV LLNPDYGELP VGSLDVPLPS TIRPSSPVAR
SPKQPVRGYL RGAVGGTFDR LHNAHKVLLS VACILAQEQL VVGVADKDLL KSKLLPELLQ
PYTERVEHLS EFLVDIKPSL TYDIVPLLDP YGPAGSDPSL EFLVVSEETC RGGMAVNRFR
LENDLEELAL YQIQLLKDLN HKENEEDKVS SSSFRQRMLG NLLRPPYKRP ELPSCLYVIG
LTGISGSGKS SVAQRLKGLG AFVIDSDQLG HRAYAPGGPA YQPVVEAFGT DILHKDGIIN
RKVLGSRVFG NKKQLKILTD IMWPVIAKLT REELDQAVAE GKHVCVIDAA MLLEAGWQNM
VHEVWTVVIP ETEAVRRIVE RDGLSEAAAQ SRLQSQMNGQ QLVDQSHVVL STLWEPHITQ
RQVEYAYSDN SLDPGLFVES TRKGSVVSRA NSIGSTSASS VPNTDDEDSD YHQESYKESY
KDRRRRAHTQ AEQKRRDAIK RGYDDLQTIV PTCQQQDFSI GSQKLSKAIV LQKTIDYIQF
LHKEKKKQEE EVSTLRKDVM ALKIMKVNYE QIVKAHQDNP HEGEDQVSDQ VKFNVFQGIM
DSLFQSFNAS ISMASFQELS ACVFSWIEEH CKPQTLREIV IGVLHQLKNQ LY
//
