ID ADCK1_CHICK Reviewed; 519 AA.
AC Q5ZMT7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=AarF domain-containing protein kinase 1 {ECO:0000305};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=ADCK1; ORFNames=RCJMB04_1d9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Appears to be essential for maintaining mitochondrial cristae
CC formation and mitochondrial function by acting via YME1L1 in a kinase-
CC independent manner to regulate essential mitochondrial structural
CC proteins OPA1 and IMMT (By similarity). The action of this enzyme is
CC not yet clear. It is not known if it has protein kinase activity and
CC what type of substrate it would phosphorylate (Ser, Thr or Tyr)
CC (Probable). {ECO:0000250|UniProtKB:Q86TW2, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q86TW2}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AJ719297; CAG30956.1; -; mRNA.
DR RefSeq; NP_001073199.1; NM_001079731.1.
DR AlphaFoldDB; Q5ZMT7; -.
DR SMR; Q5ZMT7; -.
DR STRING; 9031.ENSGALP00000051871; -.
DR PaxDb; 9031-ENSGALP00000017088; -.
DR GeneID; 423382; -.
DR KEGG; gga:423382; -.
DR CTD; 57143; -.
DR VEuPathDB; HostDB:geneid_423382; -.
DR eggNOG; KOG1235; Eukaryota.
DR InParanoid; Q5ZMT7; -.
DR PhylomeDB; Q5ZMT7; -.
DR PRO; PR:Q5ZMT7; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13969; ADCK1-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR045307; ADCK1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR43173:SF28; AARF DOMAIN-CONTAINING PROTEIN KINASE 1; 1.
DR PANTHER; PTHR43173; ABC1 FAMILY PROTEIN; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..519
FT /note="AarF domain-containing protein kinase 1"
FT /id="PRO_0000252251"
FT DOMAIN 145..481
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 151..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 519 AA; 59201 MW; B770875CB6592577 CRC64;
MARRALKLAS LAAAASGIYL YGNKFMDPND FGVVRVGRAI ATTAVITYDY LTSLRNVPYG
SEEYDFLKSQ VHLRSAERLR ELCCANRGTF IKVGQHLGAL DYLLPEEYTR TLKVLHSQAP
QSTRQEIEQV IREDLGKEIK ELFVSFEDTP LGAASLAQVH KAVLQDGRTV AVKIQHPKVQ
AQSSKDIFLM EVLLLVVKQI FPDFEFMWLV EEAKKNLPLE LDFLNEGRNA EKVAQMLKNF
EFLKVPRIYW ELSTRRVLLM EFMEGGQVND KAYMEKNGID VNEISRNLGK LYSEMIFVNG
FVHCDPHPGN VLVKKCPDSG KAYIILLDHG LYQVLSESFR MDYCRLWLAL IKADMKRVQK
YSRRLGAGDL YPLFACMLTA RSWESVNRGI DQSPVSASED VEIRSNAAAY LPQITQLLNN
VPRQMLLLLK TNDLLRGIES ALHTRASASS FLNMSRCCIR AVSTYQRSKS HSLYRRVHIS
LTEALSLWQI NLYELFLWLK GSRLGSWVIA FLSRMHHST
//
