ID   UCP12_SCHPO             Reviewed;        1327 AA.
AC   O94536;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Putative ATP-dependent RNA helicase ucp12;
DE            EC=3.6.4.13;
GN   Name=ucp12; ORFNames=SPCC895.09c;
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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329672; CAA22845.1; -; Genomic_DNA.
DR   PIR; T41647; T41647.
DR   RefSeq; NP_588050.1; NM_001023042.2.
DR   AlphaFoldDB; O94536; -.
DR   SMR; O94536; -.
DR   BioGRID; 275833; 16.
DR   STRING; 4896.SPCC895.09c.1; -.
DR   iPTMnet; O94536; -.
DR   MaxQB; O94536; -.
DR   PaxDb; O94536; -.
DR   PRIDE; O94536; -.
DR   EnsemblFungi; SPCC895.09c.1; SPCC895.09c.1:pep; SPCC895.09c.
DR   GeneID; 2539263; -.
DR   KEGG; spo:SPCC895.09c; -.
DR   PomBase; SPCC895.09c; ucp12.
DR   VEuPathDB; FungiDB:SPCC895.09c; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   HOGENOM; CLU_001832_4_0_1; -.
DR   InParanoid; O94536; -.
DR   OMA; YEADPFL; -.
DR   PhylomeDB; O94536; -.
DR   PRO; PR:O94536; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:PomBase.
DR   Gene3D; 3.10.110.10; -; 1.
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   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1327
FT                   /note="Putative ATP-dependent RNA helicase ucp12"
FT                   /id="PRO_0000314097"
FT   DOMAIN          276..315
FT                   /note="UBA"
FT   DOMAIN          405..504
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   DOMAIN          587..756
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          797..968
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           703..706
FT                   /note="DEAH box"
FT   COMPBIAS        9..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         600..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1327 AA;  149881 MW;  1707E67AADFB0157 CRC64;
     MGSKGKKGKS SEVNLETSKN KEKNIKGKKK NSLDPIEKNK QETAGLQTTS RPTAKQLVGG
     SSWTGKIPVV LLNEHCQRSK WEKSDVKVRQ TKSKNYIFTS VVLAKKDPKN PSILDHVSLI
     PPKSYYENGY FPEKETLVEA RNVGAVYALH RIMSHKSLQH ALPPEHRNIW FDMEKQKKEE
     LKNKHSWLYN EDPFKAAKEL QAARASSAAK PPPKASQKNE KVSLTSIKNT SLSHFSKFNF
     KYALPIHMSL ENRRSLENLF RNMNTWDILE DTKNLEPDTS IVNDLISLGF RDIHAKEACQ
     YCVSLEDALE WLIIHVPEDD LPTRFLPSDY TTGISVQNLN SANLAIHYNA KRISETGYSF
     DLCFSTLQTF ENNIQISSEY LQQHLIGESF DGNISLEPNS TEWDDDVSAL QSILDNKVSK
     IENGCRVRID YPTSEFGELF VDFRRPARSY PAHIPLMSLS STKRMASYIK LSILKKMVVY
     AMDLRGECML SWLYNHLQEN IEDFLQNIGS LLNISAATIG VSLSSQNKSA PTAKKNNSFK
     PKLFRRSREL SEKLCNNWSE RVKSPSYQLK VREREKLPAW ESRRKIMDAI QHSQVVVISG
     ETGSGKSTQV VQFILDHYLS SGEKDLQTVV CTQPRRISAI SLAERVAFER DTTVGKEVGY
     SVHGEKSISK ETLLEFCTTG LLLRRIQQHG LGFLSTLSCV VVDEVHERSI ENDILLTLLK
     LVISRIPNLK VILMSATVNS DTFKYYFGNA GHLHIHGRTF PIKDYYIEDF APKLNEDDDE
     EDVPRRKKKE YEIDYHLISR LVSSIDAELG SSSGSILVFL PGVSNIARCI REIKSKDGSK
     FEVLPLHASL NTSEQRRCFK TYTKRKIICA TNIAETSITI DDVVAVIDSG RVKQIDYDVE
     RDLVTFKETW ASRAACQQRR GRAGRVKKGI CYKLYTRGFE EKGMLGQTPP EVLRTALSQV
     CLNVVPLVKR FSSAGNSVNQ GSIKKFMNSL IDPPNDATVD LALKKLIQVG ALTVSEDLTG
     LGEYLVSLPI DLKLGKLLVF GSIFGYLEPA LTITAILSTK SPFLGDDEAR EIRSKQSQGW
     GDVLADARVY HNWLEILETR GVKKTVQWCE EMHLHYTTLQ QIRQNRNELS EAAQLLELTT
     KKLTGNFDWY STENLTVLST LIAAALSPNV VKCVYPDKKF VASFSGSLEM EQEARLTKFY
     DQNNQRLFIH PSSTMFVNSP NASRCTFVAY EQKVETTKPF LRNCTPINTY GMILLGANDI
     LIDPLGKGLI LDQAYCIKAW PKVVILLKML KRCLDASLHE RLESSSGLNY ESEIHQCIRT
     LIAGNGV