ID   CAF16_YEAST             Reviewed;         289 AA.
AC   P43569; D6VTK2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=CCR4-associated factor 16;
GN   Name=CAF16; OrderedLocusNames=YFL028C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   INTERACTION WITH CCR4 AND SSN2.
RX   PubMed=11113136; DOI=10.1074/jbc.m009112200;
RA   Liu H.-Y., Chiang Y.-C., Pan J., Chen J., Salvadore C., Audino D.C.,
RA   Badarinarayana V., Palaniswamy V., Anderson B., Denis C.L.;
RT   "Characterization of CAF4 and CAF16 reveals a functional connection between
RT   the CCR4-NOT complex and a subset of SRB proteins of the RNA polymerase II
RT   holoenzyme.";
RL   J. Biol. Chem. 276:7541-7548(2001).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- SUBUNIT: Interacts with CCR4 and SSN2. {ECO:0000269|PubMed:11113136}.
CC   -!- INTERACTION:
CC       P43569; P39954: SAH1; NbExp=3; IntAct=EBI-22808, EBI-16451;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; D50617; BAA09210.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12412.1; -; Genomic_DNA.
DR   PIR; S56226; S56226.
DR   RefSeq; NP_116625.1; NM_001179938.1.
DR   AlphaFoldDB; P43569; -.
DR   SMR; P43569; -.
DR   BioGRID; 31118; 58.
DR   DIP; DIP-5946N; -.
DR   IntAct; P43569; 3.
DR   STRING; 4932.YFL028C; -.
DR   CarbonylDB; P43569; -.
DR   MaxQB; P43569; -.
DR   PaxDb; 4932-YFL028C; -.
DR   PeptideAtlas; P43569; -.
DR   EnsemblFungi; YFL028C_mRNA; YFL028C; YFL028C.
DR   GeneID; 850516; -.
DR   KEGG; sce:YFL028C; -.
DR   AGR; SGD:S000001866; -.
DR   SGD; S000001866; CAF16.
DR   VEuPathDB; FungiDB:YFL028C; -.
DR   eggNOG; KOG2355; Eukaryota.
DR   GeneTree; ENSGT00390000009359; -.
DR   HOGENOM; CLU_057592_3_0_1; -.
DR   InParanoid; P43569; -.
DR   OMA; YLGTEWV; -.
DR   OrthoDB; 3092537at2759; -.
DR   BioCyc; YEAST:G3O-30432-MONOMER; -.
DR   BioGRID-ORCS; 850516; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P43569; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43569; Protein.
DR   GO; GO:0030014; C:CCR4-NOT complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   CDD; cd00267; ABC_ATPase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43158; SKFA PEPTIDE EXPORT ATP-BINDING PROTEIN SKFE; 1.
DR   PANTHER; PTHR43158:SF2; SKFA PEPTIDE EXPORT ATP-BINDING PROTEIN SKFE; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..289
FT                   /note="CCR4-associated factor 16"
FT                   /id="PRO_0000093464"
FT   DOMAIN          7..249
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   289 AA;  33090 MW;  2250CC15F9CE1354 CRC64;
     MVSQFAIEVR NLTYKFKESS DPSVVDINLQ IPWNTRSLVV GANGAGKSTL LKLLSGKHLC
     LDGKILVNGL DPFSPLSMNQ VDDDESVEDS TNYQTTTYLG TEWCHMSIIN RDIGVLELLK
     SIGFDHFRER GERLVRILDI DVRWRMHRLS DGQKRRVQLA MGLLKPWRVL LLDEVTVDLD
     VIARARLLEF LKWETETRRC SVVYATHIFD GLAKWPNQVY HMKSGKIVDN LDYQKDVEFS
     EVVNAKVNGQ VAFENDNNKV VISKVNSLHP LALEWLKRDN QIPDKEIGI
//