DBP5_SCHPO
ID DBP5_SCHPO Reviewed; 503 AA.
AC Q09747;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP-dependent RNA helicase dbp5;
DE EC=3.6.4.13;
GN Name=dbp5; ORFNames=SPBC12C2.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: ATP-dependent RNA helicase associated with the nuclear pore
CC complex and essential for mRNA export from the nucleus. May participate
CC in a terminal step of mRNA export through the removal of proteins that
CC accompany mRNA through the nucleopore complex. May also be involved in
CC early transcription (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: Associates with the nuclear pore complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore
CC complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore
CC complex cytoplasmic fibrils. {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. DDX19/DBP5
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA90819.1; -; Genomic_DNA.
DR PIR; T39375; T39375.
DR RefSeq; NP_596016.1; NM_001021924.2.
DR PDB; 3FHO; X-ray; 2.80 A; A/B=139-503.
DR PDBsum; 3FHO; -.
DR AlphaFoldDB; Q09747; -.
DR SMR; Q09747; -.
DR BioGRID; 276519; 9.
DR STRING; 4896.SPBC12C2.06.1; -.
DR iPTMnet; Q09747; -.
DR MaxQB; Q09747; -.
DR PaxDb; Q09747; -.
DR PRIDE; Q09747; -.
DR EnsemblFungi; SPBC12C2.06.1; SPBC12C2.06.1:pep; SPBC12C2.06.
DR GeneID; 2539975; -.
DR KEGG; spo:SPBC12C2.06; -.
DR PomBase; SPBC12C2.06; dbp5.
DR VEuPathDB; FungiDB:SPBC12C2.06; -.
DR eggNOG; KOG0332; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q09747; -.
DR OMA; EYCTPIQ; -.
DR PhylomeDB; Q09747; -.
DR EvolutionaryTrace; Q09747; -.
DR PRO; PR:Q09747; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0002184; P:cytoplasmic translational termination; ISO:PomBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Helicase; Hydrolase; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleotide-binding; Nucleus;
KW Protein transport; Reference proteome; RNA-binding; Translocation;
KW Transport.
FT CHAIN 1..503
FT /note="ATP-dependent RNA helicase dbp5"
FT /id="PRO_0000055020"
FT DOMAIN 147..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 325..493
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..142
FT /note="Q motif"
FT MOTIF 261..264
FT /note="DEAD box"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3FHO"
FT TURN 362..366
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:3FHO"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 440..444
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:3FHO"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:3FHO"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:3FHO"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:3FHO"
SQ SEQUENCE 503 AA; 56305 MW; 68C7C8BD6AED252F CRC64;
MSTTLGQESK TDWASLDSDE EVQRISDKVN QLNTSENKNE DQKATNLSDR LGPKITENVD
AKSEQDKATN TIAEDANTKQ SENDESNLIP NKNEVRVKLA DLQADPNSPL FSVKSFEELE
LKPELLKGIY SMKFQKPSKI QEKALPLLLS NPPRNMIGQS QSGTGKTAAF ALTMLSRVDA
SVPKPQAICL APSRELARQI MDVVTEMGKY TEVKTAFGIK DSVPKGAKID AQIVIGTPGT
VMDLMKRRQL DARDIKVFVL DEADNMLDQQ GLGDQSMRIK HLLPRNTQIV LFSATFSERV
EKYAERFAPN ANEIRLKTEE LSVEGIKQLY MDCQSEEHKY NVLVELYGLL TIGQSIIFCK
KKDTAEEIAR RMTADGHTVA CLTGNLEGAQ RDAIMDSFRV GTSKVLVTTN VIARGIDVSQ
VNLVVNYDMP LDQAGRPDPQ TYLHRIGRTG RFGRVGVSIN FVHDKKSWEE MNAIQEYFQR
PITRVPTDDY EELEKVVKNA LKM
