PRP16_YEAST
ID PRP16_YEAST Reviewed; 1071 AA.
AC P15938; D6VXE6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16;
DE EC=3.6.4.13;
GN Name=PRP16; OrderedLocusNames=YKR086W; ORFNames=YKR406;
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 [GENOMIC DNA].
RX PubMed=2138057; DOI=10.1016/0092-8674(90)90086-t;
RA Burgess S., Couto J.R., Guthrie C.;
RT "A putative ATP binding protein influences the fidelity of branchpoint
RT recognition in yeast splicing.";
RL Cell 60:705-717(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8203164; DOI=10.1002/yea.320100210;
RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G.,
RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae
RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open
RT reading frames.";
RL Yeast 10:231-245(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=1825134; DOI=10.1038/349494a0;
RA Schwer B., Guthrie C.;
RT "PRP16 is an RNA-dependent ATPase that interacts transiently with the
RT spliceosome.";
RL Nature 349:494-499(1991).
RN [6]
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).
CC -!- FUNCTION: Influences the fidelity of branchpoint recognition in yeast
CC splicing. This is RNA-dependent ATPase which is essential for
CC viability. It may mediate one of the many ATP-requiring steps of
CC spliceosome assembly and that accuracy of branchpoint recognition may
CC be coupled to ATP binding and/or hydrolysis.
CC {ECO:0000269|PubMed:1825134}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Binds to the spliceosome.
CC -!- MISCELLANEOUS: Present with 1250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000305}.
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DR EMBL; M31524; AAA34911.1; -; Genomic_DNA.
DR EMBL; Z27116; CAA81637.1; -; Genomic_DNA.
DR EMBL; Z28311; CAA82165.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09236.1; -; Genomic_DNA.
DR PIR; S38164; S38164.
DR RefSeq; NP_013012.3; NM_001179876.3.
DR PDB; 5LJ5; EM; 3.80 A; Q=1-1071.
DR PDB; 5WSG; EM; 4.00 A; e=1-1071.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5WSG; -.
DR AlphaFoldDB; P15938; -.
DR SMR; P15938; -.
DR BioGRID; 34217; 331.
DR DIP; DIP-2824N; -.
DR IntAct; P15938; 22.
DR MINT; P15938; -.
DR STRING; 4932.YKR086W; -.
DR iPTMnet; P15938; -.
DR MaxQB; P15938; -.
DR PaxDb; P15938; -.
DR PRIDE; P15938; -.
DR EnsemblFungi; YKR086W_mRNA; YKR086W; YKR086W.
DR GeneID; 853961; -.
DR KEGG; sce:YKR086W; -.
DR SGD; S000001794; PRP16.
DR VEuPathDB; FungiDB:YKR086W; -.
DR eggNOG; KOG0924; Eukaryota.
DR GeneTree; ENSGT00940000156898; -.
DR HOGENOM; CLU_001832_6_3_1; -.
DR InParanoid; P15938; -.
DR OMA; PYVVYHE; -.
DR BioCyc; YEAST:G3O-32049-MON; -.
DR PRO; PR:P15938; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P15938; protein.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000378; P:RNA exon ligation; IDA:SGD.
DR GO; GO:0016073; P:snRNA metabolic process; IMP:SGD.
DR GO; GO:0040031; P:snRNA modification; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1071
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT PRP16"
FT /id="PRO_0000055150"
FT DOMAIN 360..526
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 540..735
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 132..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 473..476
FT /note="DEAH box"
FT COMPBIAS 136..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 373..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 386
FT /note="Y->D: Suppressor phenotype."
FT CONFLICT 698
FT /note="A -> R (in Ref. 1; AAA34911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1071 AA; 121653 MW; EB7D4C4A18F5D4E1 CRC64;
MGHSGREERI KDIFKELTSK ELTPGLLLTL QKLAQKPNTN LEQFIASCKA LTKLSSNNPI
IFNELLELLK NKSEEDSTGP KKIAPSINKR KKFKIQLDLD DNEDELDSPV QKKPAPTRTL
FKRIDKLKAK QLRQYSPTVK DPSPNSEQQT QNGHAETKDY EPTRSEVVEE DREWYDNDDD
YGNLVPEPLS ELPEEAKLLP VIRNIDNDDA LRNTVQLYPI PLKQRMEWIP PFLSKFALEN
KVPTSIIIGS ISETSSQVSA LSMVNPFRNP DSEFSANAKR GSKLVALRRI NMEHIQQSRD
NTTVLNTAMG EVLGLENNNK AKDKSNQKIC DDTALFTPSK DDIKHTKEQL PVFRCRSQLL
SLIRENQVVV IIGETGSGKT TQLAQYLYEE GYANDRGKSI VVTQPRRVAA ISVAKRVAME
MQVPLGKEVG YSIRFEDVTD SECTKLKFVT DGILLRETLL DDTLDKYSCV IIDEAHERSL
NTDILLGFFK ILLARRRDLK LIITSATMNA KKFSAFFGNA PQFTIPGRTF PVQTIYTSNP
VQDYVEAAVS QAVKIHLAND CSSGDILIFM TGQEDIETTF DTLQEKFLQV YSKKFGTANF
EEINDIEILP IYSALPADLQ FKIFQDLHGT KRKIIIATNI AETSLTIKGI RYVIDCGYSK
LKVYNPKIGL DSLVITPISK ANADQRSGRA GRTAPGTAYR LYTEDTFKED MYLQTIPEIQ
RTNLSNTLLL LKSLDVTDEL SKFPFIDKPP LQTFLSSLYE LWFIGAIDTS GQLTPLGLQM
AKFPLQPSLS KILLIAVRNG CSDEMLTIVS MLSVPQVFYR PKERQKEADI ARNKFFIAKS
DHLTLLNVFE QWRANNFSSH WCNKHFVQYK SLVRARDIRD QLLTILKSQK IPVISSGKDW
DIIKKCICSG FAHQAAKITG LRNYVHLKTG VSVQLHPTSA LHGLGDLPPY VVYHELLMTS
KEYICCVTSV DPFWLMEYGG LLYDIKRIKN DQEATTTGLF GEHYEHTLDK VEDDIDINIR
RCKDMRDSVI QELKMTDNSN KEDKKQKTKK QNILNGKENS MKPFKRRKPF F
