ID A0A0Q3LZZ0_AMAAE Unreviewed; 255 AA.
AC A0A0Q3LZZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN ORFNames=AAES_244113 {ECO:0000313|EMBL:KQK76077.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK76077.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK76077.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK76077.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC kinases and is essential for their biological function.
CC {ECO:0000256|ARBA:ARBA00002449, ECO:0000256|RuleBase:RU311113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001332};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004726}.
CC -!- SUBUNIT: Forms a homohexamer that can probably bind six kinase
CC subunits. {ECO:0000256|ARBA:ARBA00011253}.
CC -!- SIMILARITY: Belongs to the CKS family. {ECO:0000256|RuleBase:RU311113}.
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:KQK76077.1}.
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DR EMBL; LMAW01002883; KQK76077.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3LZZ0; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23293:SF9; FAD SYNTHASE; 1.
DR PANTHER; PTHR23293; FAD SYNTHETASE-RELATED FMN ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01111; CKS; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR SMART; SM01084; CKS; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|RuleBase:RU311113};
KW Cell division {ECO:0000256|RuleBase:RU311113};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 67..222
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 255 AA; 29483 MW; B9E93D9E020A70D9 CRC64;
MLPKDIAKLV PKTHLLSESE WRNLGVQQSQ GWVHYMIHEP GSALGQKVAA ALRTIEEALE
RYSLAQICVG FNGGKDCTAL LHLVHAAVER RXPARQEKLQ VLYIRIVSPF PEMEQFIQAT
VQRYKVQLCT VEGSIREALV HLKEQQPQIE AVLMGTRRTD PYSCTLTPMC LTDPGWPXYM
RVNPLLDWTY RDIWEFLRQL FVPYCXLYDK GYTSLGSMAN TLKNPALRYT DSQGRDRYRP
AYELENEEEE RTSRQ
//
