ID A0A2K1KIC3_PHYPA Unreviewed; 1469 AA.
AC A0A2K1KIC3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PHYPA_007202 {ECO:0000313|EMBL:PNR53527.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR53527.1};
RN [1] {ECO:0000313|EMBL:PNR53527.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_3790V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR53527.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_3790V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c5_3790V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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DR EMBL; ABEU02000005; PNR53527.1; -; Genomic_DNA.
DR STRING; 3218.A0A2K1KIC3; -.
DR PaxDb; 3218-PP1S41_312V6-1; -.
DR EnsemblPlants; Pp3c5_3790V3.1; Pp3c5_3790V3.1; Pp3c5_3790.
DR EnsemblPlants; Pp3c5_3790V3.2; Pp3c5_3790V3.2; Pp3c5_3790.
DR EnsemblPlants; Pp3c5_3790V3.3; Pp3c5_3790V3.3; Pp3c5_3790.
DR Gramene; Pp3c5_3790V3.1; Pp3c5_3790V3.1; Pp3c5_3790.
DR Gramene; Pp3c5_3790V3.2; Pp3c5_3790V3.2; Pp3c5_3790.
DR Gramene; Pp3c5_3790V3.3; Pp3c5_3790V3.3; Pp3c5_3790.
DR Proteomes; UP000006727; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 38..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 267..464
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1169..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 163189 MW; 6F1A56DD50A0D9A7 CRC64;
MDPRLDPDYL KPVSLLPTAF QSVFPFRYFN AVQSESFAEV FLSDDNLVIS APTGSGKTVL
FELCILRLLE KFLTTEGHFK HVSGARKAVY IAPMKALVQD KLRDWTLRFS SLGVKCQELT
GDSGPTNVGE MIDTDIILTT PEKFDVITRR HRDRGGMSFF GDIALILIDE VHLLSETRGA
ALEAVVSRLK MLARFPEIKG SPLSTIRFVA VSATVPNIED LAEWLHVPKN GMKRFGEEYR
PVKLTTTVLG YQPAKNDFLF ERRLQQYLLD ILLHHSEGKP SLVFCSTRKG AQDTAVALSQ
SVSQHGNHNP FVKNLEHFKR LQLAAQRTND VHMQQCIRSG VGYHNGGLSM EDRGLIEGLF
LTGDLLVLCT TSTLAQGVNL PAHAVIIKST QYYNKLKGCY VEYERSAILQ MSGRAGRPQF
DDSGVVVIMT RKDSVHLYHN LLSGSEPVES QLLSSIVEHL NAEIVLMTVS DCSQAIDWLK
CSYLYVRIKK NPQYYCVKQG VPRDQLENKL KDICVQNVNE LAKYGMVKTD EFGYVLTPLE
PGRIMEKYYM QFETMKAITK AAERATIEEL LHVLANAAEL SWIKLRRDEK KRLNDINGDI
SGRIRYHVNN SNGKLKKRIQ SGAEKIFILV NDALSGEPSV TDFTMSQDIN GICTTGTRIC
RCMSEYFIFM KRFTEIRNAL LLSKCLKQRL WESTKYQLKQ LVGVGLVTAK ALITAGVDSF
EKLASADPRR LEAITGRKFP YGDQLKASLN DAPPKVEMNL FESERDDQCL LTLHRVSQSQ
SSGKNFHMAE LVVGSMADNM LIFRERIRMD QFTSPYAVTI TSSSPSDEPL VLVAALISEE
YVGVDVVCKL VINRDSRDDQ LGLNEDYRHQ GPQTSMTRFY ISSPFKASFS INDLAASSAR
SHATSVMSSP LIKNKTLDSP RAQQTAASNI PIMEALSRYP SRHSNPCPAT LATRNFLNKI
GTDIDASDPL KDTFLRTLPI PAKTESNTTP GSEVLATCVI KPSKSPSSKS GHADHFDILT
TLQSSDLVET SICNSVLVPT ETYEKSPRTS SFVTPKRKDP PSCAPRRLFR RLCTRFEENR
MTTSLPSANG KTPNPSQSEE VSIKSTMCNG GPCSMNDIGF TENYADQATT SIPRNDCGSE
KSTKVTTLLY NSKVRTHDNV ELQAGVVSDM THQDSGPSED VTASAPPSLT SLSTTPDLLS
SDMRRKIRRT GFSSISCFSS VKNNDQRNSM VTLNIAQPSS CQPRCPDRSD EPQNIKHRSR
ILQSFPSRAP RVTDAVAQNS PHSKVSDQLT PWRATAGLIP TGSRSEAEAE SDLTNTETIS
NSCQQKTLWR SLDNNHLTKT NCVGAAKERN SFSQGPNNIK ITSSTRRLEA ASCALIDRPL
KQIAPYKALK SFDFGSSRKP PPDVARGVNP ASEIPEPLDQ AASISNTRLK AEDLGFVTVE
VPSNHNSSTK KFSCLRFDQS HITARLRRL
//
