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Database: UniProt
Entry: A0A1Y1IL33_KLENI
LinkDB: A0A1Y1IL33_KLENI
Original site: A0A1Y1IL33_KLENI 
ID   A0A1Y1IL33_KLENI        Unreviewed;      1235 AA.
AC   A0A1Y1IL33;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=Minichromosome maintenance 9 {ECO:0000256|ARBA:ARBA00042301};
GN   ORFNames=KFL_005670050 {ECO:0000313|EMBL:GAQ89831.1};
OS   Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ89831.1, ECO:0000313|Proteomes:UP000054558};
RN   [1] {ECO:0000313|EMBL:GAQ89831.1, ECO:0000313|Proteomes:UP000054558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ89831.1,
RC   ECO:0000313|Proteomes:UP000054558};
RX   PubMed=24865297; DOI=10.1038/ncomms4978;
RA   Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA   Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA   Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA   Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA   Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA   Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA   Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA   Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA   Tabata S., Ida S., Kurokawa K., Ohta H.;
RT   "Klebsormidium flaccidum genome reveals primary factors for plant
RT   terrestrial adaptation.";
RL   Nat. Commun. 5:3978-3978(2014).
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};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; DF237516; GAQ89831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1IL33; -.
DR   STRING; 105231.A0A1Y1IL33; -.
DR   OrthoDB; 147095at2759; -.
DR   Proteomes; UP000054558; Unassembled WGS sequence.
DR   GO; GO:0042555; C:MCM complex; IBA:GO_Central.
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:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR041562; MCM_lid.
DR   InterPro; IPR033762; MCM_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11630:SF48; DNA HELICASE MCM9; 1.
DR   PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF17855; MCM_lid; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00350; MCM; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054558}.
FT   DOMAIN          312..511
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          658..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          956..1235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1062
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1235 AA;  132707 MW;  82B0E46FD2B73C53 CRC64;
     MARASQEAVV HDEEYVDALY KFAMEYHAQD LAEILLKPDD DLHYAVHVSF QELHGDERFE
     AMANLLCCKP RWLLPLFDEA LSKAQVDIAD VHELQEDMSF KAHVHARVTL MECPEMKPSI
     SRIRCEDIGR ILAVRGTIIR TGAVKMLEGE REYECAKCKL RFKVTPQLEQ DNKLTLPASC
     PSDRTKPCKS VTFNYVDESK VCHDYQEIKI QEEMHGLGVG SVPRSIVAVL QDDLVDYCKA
     GDDVEVTGVL CCKWKPVMKG VRCDLEMVIL ANSVRKASAD KAAVDLSPET VYKFQEYWRQ
     FLDCPLKGRN GILKGICPQV YGLFTVKLAV ALTLIGGVAR VDKSGTRVRG EPHLLIVGDP
     GTGKSQFMKY AAKLSARSVV TTGMGSTGAG LTVTAVRDNG EWMLEAGALV LADGGLCCID
     EFDGIREADR ATIHEAMEQQ TLSVAKAGLV TTLNTRCTVF AVCNPKGQYD PDNTLEVNTS
     LAAPLLSRFD IVLVLLDTKN PDWDRIVSSH ILTEHKNAHR ADEDTSISSP TPSALWTIDM
     LRSYIYYVKA AFQPTLTPEA ERVIVNYYQL QRRSNAGNRN QARTTIRMLE SLVRIAQAHA
     RLMFRHEVLR TDAVVAVVTI ESSMTTSAIL ENMTNALHSS FKDEPDAEYR DIEAQILTAL
     GIPPPSDEER AAEMTRGRHE EGPCGDQEGE KDAEVTRGGQ ESEPGTESAA KGAEGNERRE
     MGLLVDVGRS FESEDASGED GDLLLRPDSG GLQGRESEPP EALGSQLEMG ERSPSRENED
     GGNCENPDRR CGTSEEAQTV RNMGVEDQTV GNDPGVGEAA TWQAEARALE ARLRGFRQAG
     VDVSTTDDVG ERQKAERWTR ADGERSGGPS SKRADGCRTG GVSGVRREAD ALLGSDSEAK
     GVETGGLHGA PNAPSEGTGV SKNPVTKNAD AENRVAGNPG TELPVCLSPL ARRTSASLAG
     AGSGHVGAAG GGHVAAEDGA GPSGDVAVKG KKCAGRGSLS GGSSGEDVSQ AFGGFERRIS
     ERGAENAALE REPVSEATGE HAGKCDRPEG ASDRRTDGTG RGHDDFAGQG LETVRADRGV
     NVTGQHDANG LTIEPGREPP SSEEAQESSG PARPLSATSR FGSSETSALI RTLTQRLARP
     SQKASDPANG VRPPCPEPQL RAPSNQGGLE SNPVAPLADR AVNAASGPKA QAGGLGMLRK
     RLQGRRSAEE SEDANWLSDE QWGISSPGAK RARNT
//
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