PRP28_ASPCL
ID PRP28_ASPCL Reviewed; 798 AA.
AC A1CHL3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE EC=3.6.4.13;
GN Name=prp28; ORFNames=ACLA_048380;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May
CC destabilize the U1/5'-splice site duplex to permit an effective
CC competition for the 5'-splice site by the U6 snRNA, resulting in the
CC switch between U1 and U6 at the 5'-splice site. May also act to unwind
CC the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC the first covalent step of splicing (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Component of the U5 snRNP complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000305}.
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DR EMBL; DS027054; EAW10368.1; -; Genomic_DNA.
DR RefSeq; XP_001271794.1; XM_001271793.1.
DR AlphaFoldDB; A1CHL3; -.
DR SMR; A1CHL3; -.
DR STRING; 5057.CADACLAP00004304; -.
DR PRIDE; A1CHL3; -.
DR EnsemblFungi; EAW10368; EAW10368; ACLA_048380.
DR GeneID; 4704103; -.
DR KEGG; act:ACLA_048380; -.
DR VEuPathDB; FungiDB:ACLA_048380; -.
DR eggNOG; KOG0333; Eukaryota.
DR HOGENOM; CLU_003041_11_3_1; -.
DR OMA; KKFNFEW; -.
DR OrthoDB; 820037at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..798
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp28"
FT /id="PRO_0000282478"
FT DOMAIN 397..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 608..771
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 366..394
FT /note="Q motif"
FT MOTIF 525..528
FT /note="DEAD box"
FT COMPBIAS 12..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 798 AA; 88854 MW; 9FAE6625F3FA798E CRC64;
MDGFISNGPA EAPATMPPPE PFERPPTPPP PPPEDSAAPP PPPDTSAPPP PPEDAIPAPP
LEKKKKAGWG AKRAAATPLS VEELVRKKRE ADAAAAKPKF LSRAERERLA LEKRAKEVDA
DRRLKTERTA NGADSSSAQS TPVYPERPNS DKRVIPTGPR AMRNTEAPAR SGPAATRNKN
YDMTPPAPPK PMSFSLTDSK GDSKRQAEED ETVAQVALIK QRYMGEEKTS NFSAKKKRKR
TTDRKFNFEW NAEEDTSGDY NPLYQHRHEA NFYGRGRLAG FGDDVADSLA KKYARALEDR
DQEAGSIRAR EMLEMEKRRR EESTRNQLDK HWSEKKLEHM RERDWRIFKE DFNISTKGGS
VPNPMRSWEE SGLPKRLLEL VDRVGYKEPT PIQRAAIPIA LQSRDLIGVA VTGSGKTASF
LLPLLVYIAE LPRIDEFEWR KNDGPYAIVL APTRELAQQI EIEAKKFTQP LGFNVVSIVG
GHSLEEQAYS LRNGAEIIIA TPGRLVDCIE RRILVLSQCC YIIMDEADRM IDLGFEEPVN
KILDALPVTN EKPDSDEAEN SAAMRSHRYR QTMMYTATMP SAVERIARKY LRRPAIVTIG
SAGEAVDTVE QRVELIAGED KRKKRLADIL SSGEFRPPII VFVNIKRNCD AIAREIKHMG
FSSVTLHGSK TQDQREAALA SVRNGSTDVL VATDLAGRGI DVPDVSLVVN FNMATSIESY
THRIGRTGRA GKSGVAITFL GNEDADVMYD LKQMLMKSPI SRVPEELRKH EAAQSKPTRG
YAKKSDESSG FRDKGAWQ
