ID A0A367JYH1_RHIAZ Unreviewed; 2266 AA.
AC A0A367JYH1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Acetyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CU097_008447 {ECO:0000313|EMBL:RCH95042.1};
OS Rhizopus azygosporus (Rhizopus microsporus var. azygosporus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=86630 {ECO:0000313|EMBL:RCH95042.1, ECO:0000313|Proteomes:UP000252139};
RN [1] {ECO:0000313|EMBL:RCH95042.1, ECO:0000313|Proteomes:UP000252139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 357.93 {ECO:0000313|EMBL:RCH95042.1,
RC ECO:0000313|Proteomes:UP000252139};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:RCH95042.1}.
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DR EMBL; PJQL01000509; RCH95042.1; -; Genomic_DNA.
DR STRING; 86630.A0A367JYH1; -.
DR Proteomes; UP000252139; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06606; STKc_MAPKKK; 1.
DR CDD; cd00200; WD40; 1.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00619; GATAZNFINGER.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 7.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000252139};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT DOMAIN 1..254
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 258..490
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT DOMAIN 585..633
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT DOMAIN 1112..1377
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 1460..1501
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1600..1646
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1691..1721
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1730..1769
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2266 AA; 253730 MW; 57E31162E1B32982 CRC64;
MTTTINEKRR QAEEGGGPTR IEAQHKKGKL TARERLGLLL DRGSFREYDT FVEHECTDFD
MSQHKIPGDG VVTGHGTIHG RKVFVYSQDF TVLGGSLSRT NANKILKVMD QAMLVGAPVI
GLQDSGGARI QEGVNSLAGY ADIFQKNVLA SGVIPQISVV MGPCAGGAVY SPALTDFTFM
VRDSSYMFVT GPDVVKAVLN EQVSQEELGG ARTHTEKSGV AHNAFDNDAE ALQGVRDLLT
YLPQSNREPA PTVECDDPVD REDEAIDRII PSDSAIAYDM KEIVARVTDA HSFYEISADY
ASNILVGFAR LSGQPVGVIA NQPLVSSGAL DIDASLKAAR FIRFCDAFNI PLVTFVDVPG
FMPGTSQEHG GIIKHGAKLL YAYCEATVPK LTVITRKAYG GAYIVMSSKH LRGDYNVAWP
SAEIAVMGAG GAVEIIFRNH PDKATMKKEY KERFATPLFA AKKGYLDDIV EPRHTRARLI
EQLNLLKLKN LVNPAKKHGS FFDEDVILSD KELMDDTYHQ VTEDEEEQEE QEEEEEYIFE
EEEEYEEIEE EDDDPDWGSS HKKKSTPSIT QAKKQIKKEV DCDIKCSNCE TTNTPLWRRN
PEGEVLCNAC GLFLKLHGVV RPLSLKTDVI KKRNRSGNMK RRKWLITNGW SPLVPVFYEH
KIQHDQFLNL TMEKLDDVLN HVHISHSEKQ RLLSAIKQVK ADQAQHQHLH RQSLPRIIIP
TSNNHTKITT SPNNQHFDIS QYIPKRTSST ESNVSKILEA FQPSILHMKT KSPTSPRINP
SDPEILSKLL GKRVPLQHAL TQDRRIQVTL DADTFIKLWI KESSDALTIK HAVLQKLSID
ADPSYFYFYH ENGVQSTIPL TDEELVRVCQ SSDDSRTNRV LVVPVEGYEL MCQQRSTYHD
PHYVRYVLAP AGYHFANPPS IPSSELWATP PSKHLLNTQP SSWPAEQQLN VEGISLYDPP
TPRNDDLDFT AVKSFTSSSA TPTEPPSPIG SQKSDGDAFA EDDVLGERPS VEKLYRNIDQ
YLPGHDLDKE ITVENNAIPP SISRRLHGHR PSVRVVAKEA HRRWRQETRN VGNTVLRRKS
TKMWGSKVER VKPGEEGCIV ASDKPVPTRM QWMRGELIGR GSFGRVYHAL NVATGEWIAV
KQVDVAVTQA DKRNQDLKEA ADALYHEISL LKDLDHINIV QYMGYDFNPD EGLIFIFLEY
VPGGSIASLL KQYSVFEEPL ISFFTRQILQ GLEYLHERGI LHRDIKAGNV LIDQNGICKI
TDFGLSKNQN ESAYDSASNN STMKGTVFWM APEALTNNYS AKVDIWSLGC TVLEMLTGTH
PWMHLTSLAA LYAIGNHKSP EIPSNISSEA KDFLEQCFRI NPEDRPTAKQ LLEHPFVQPN
DSFNFKPSLY GKEGLGVLGN LSQLSNSRPI HPARCIHTIS QEDNNSVLSL VSSRRYLFSG
SQSSKIHVWC LQTFRLVTIL RGHTGSVLGL TLSADEQYLF SCSGDGTVRV WNTETLTCAY
LIQSCHDVGD IFSVVYSDKH NMLFFGSQNT SIQWYDFADP QTHGHKIDIP SVPPSPRRRK
GKPINFFELS GHLGEEEERI QELLDKNVIK CVIREKNVYS NAHDGYVYCL LHAKDVPNME
GEVLISGSGD GNVKIWSINQ GVIQHMRTLK GNSDKGILSL ALSEDGYLFC GVQGGDIQIW
DLETYQMIRS VIAHTDDVLA IAVRRGGFIS ASADGSIRLW DEVFQLKEVL IEHHGIVLSL
TEREDCLISG SSDQSIKFWD ISSNAHAPAD IMRRYSSGTL QGTPSTDMML YVLEKWVAIR
TVSGMPRYME ECRRGARFLK NVLQQLGAVS RMIPGASGRN PLVYGRFSGK GNDQKRVPTV
LIYGHYDVIA VEHEKNMWGS DPFELTGKNG YLYGRGTSDN KGPMLACIFA VNELLKEGQL
DVNVVFLIEG EEESGSIGLY EAVEQNKDLF KDVDMILLSN SYWLGEDVPC ITYGLRGVVH
ATVSICNQRA DLHSGVEGGA VSEPLVDLIH VLGKLVDTDK KVLVPDFYKD VRPVTETEER
LYDPIIEWMK TSKTAQSSTR THHSTIALPS PVKESEADKE TQCKMKIADE ELDAETQKKQ
LMARWRYPTL TIHKIDVSIN NPTIIPRTAK ASVSMRVVPD QSISEICSQF TEYVHEVFAS
CKSDNKISVN IESVAEYWLG DLNNKYFRAV ETAVEKEWKV KPLYIREGGS IPAVRWLEKF
CNAPAVHIPF GQSSDQAHLH NERIRLLNLI AGKRIIKSLL TALPEL
//
