GenomeNet

Database: UniProt
Entry: C1MR96_MICPC
LinkDB: C1MR96_MICPC
Original site: C1MR96_MICPC 
ID   C1MR96_MICPC            Unreviewed;      1823 AA.
AC   C1MR96;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Dead-box like helicase with PHD domain {ECO:0000313|EMBL:EEH57845.1};
GN   ORFNames=MICPUCDRAFT_57576 {ECO:0000313|EMBL:EEH57845.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH57845.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH57845.1,
RC   ECO:0000313|Proteomes:UP000001876};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889}.
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; GG663738; EEH57845.1; -; Genomic_DNA.
DR   RefSeq; XP_003057894.1; XM_003057848.1.
DR   STRING; 564608.C1MR96; -.
DR   GeneID; 9683702; -.
DR   KEGG; mpp:MICPUCDRAFT_57576; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   eggNOG; KOG0383; Eukaryota.
DR   OMA; GWGATQD; -.
DR   OrthoDB; 12149at2759; -.
DR   Proteomes; UP000001876; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd18033; DEXDc_FANCM; 1.
DR   CDD; cd12091; FANCM_ID; 1.
DR   CDD; cd15568; PHD5_NSD; 1.
DR   Gene3D; 1.20.1320.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039686; FANCM/Mph1-like_ID.
DR   InterPro; IPR044749; FANCM_DEXDc.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEH57845.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001876};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          343..514
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          689..913
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1778..1823
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          24..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          937..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1220..1668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1713..1746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..57
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..956
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1248..1271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1311..1343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1458..1475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1544..1558
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1584..1601
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1605..1628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1648..1663
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1823 AA;  191649 MW;  177AE9F0599D5C0C CRC64;
     MPFEIADDWD DDALMGVDVD AIAAARTSAP PAGPSDRDPA PGHRPAPRQP PPATHHHRPQ
     QQPNRATAAA PPRQRHPPPQ QHFDGGGGPP HPANEGFSGH TGYKGGFSGH GGGAQQGGRQ
     GWQRQRGGGG GGARWNASDA NHRTGHDAVD RALASNAPRF TANNQPPVNQ RTVTTMFAAK
     GGPKQTLFRP GVEEKQRTLD SMFGGSGGRG GGGGGGGGGD GDGDGGSADV LPHQRPIEID
     GDGDAWWSAP PPVAAAAAAA PRRQAPAAVH HHTHPSKWQP SQHVASTPEG QYAGRLTPSA
     MGTPNSQGLI RCSDANGMLL DPHAAQSYVY PGQLVRRDYQ YNITRDALTT NSLVCLPTGL
     GKTLIAAVVM YNFYRWFPKG KVVFLAPTRP LVDQQKAACR DICGIPENDI CVLMGSTKKD
     ESGTRRAFWD QKRVFFCTPQ TMENDIASSV LPAKDVVCLV IDEAHRAKGK HAYCGVVRML
     WDRNVSFRLL ALTATPGHDI ADVQQVVRNL NIGRIDFRSD KDVDVKRHTH NRSIQLESVK
     ATRAISEVQD MLRDVLRPML KTLTSMGALP TEGVKMARFV EGTSKDIPQP FTIQLAQRDL
     QNGNTAVPPA KKNYAFSLCL QSYFIARLNA LLSGYSAQQA VDYVEDQNTK GYIGALFGAS
     PVMREVLDML RSMAGHGAHH SPKLARLTQI IRRHFATNNP ATRAIVFTSY RDSVRDIVRA
     LREVTVTTGG GNNLGPGDPL VDPEKGQKTV TGMFSAASGS GGGSGDTAGV PPEVPDGAEC
     RIKVAEFIGQ GDSSKGGGGG GAKGAGAARG TKGQSQKEQK AVLDAFRHGS LNTIVATSIG
     EEGLDIPAVD LIVFFDVVDT IRTIQRMGRT GRARDGKVVV LALEGREAEK FSKEQGKYEH
     LLRSLSDPGR CFQLCNDCPR MLPAGLDPRC ELKELGPTPE ALKAKREMEA RGSSGKKRKG
     ARGGAGRGNA SAFSIRPWDA PLTTVEHSLL QAYDCAPRAM GRIDMQNAAP LQRRPTPVFS
     VPHGRMCVAL MRAMSAAQGL PPPLDVRGES IEGGAIAREE KAKADAEAAR DRAHAEANAD
     APTTAFYAPP VEWDDDEWGD GGFVPAAFDD DVGGGGIDDD DEPLRANWDS QRSHGYEAPI
     LDASAVKDDG PRASVSQAPT ELDERAACEY DDDDVTRSID ASGSHGGFNG VGGGGAHTGA
     TQRLDFTATL VDPSPRRVVA NEAEPCENPE CAVIGCDDPK HGASRNDRTP LAQLTPPSQR
     PGSNAMNTQG ASVHGDPLCG EENDDVFATA PAPVARPSPS AAESARQRLR ERLSQQSQQQ
     RAHSQSQSQS QLRRQNTTQP EAQADVPDDD DETIADIAFH IKQKKLAAAA KKRATASAEK
     AAKASASKSK SKSVSASQMP PPPPRATVRE ASTPGFDVAP TVDDAVTPGA ADGWWGTGDA
     QDDAVGGWGG TQSGGGGGGG WGVSQNTQTS GGGWGAPATQ DDAGVGWGAS QGTQDSAGGG
     WGGVSDAGGD AGWGGGSPSQ NDDDAEGGWG DPPDENDARG GAPGTDPPPA PPASTPVQPT
     PDSDDLMVLK RRKRVAAPAP SPAVEPVRRR PPPPPPPSFA PAGDDDDDDG WRRGGATKRA
     DVLAAKRTKR ANAAKQAAVH RFMDDVASGD DDDDDDDDGW NTEDEAFVAA TQGDALDASG
     DEPALMHQQL ALLADAHTPL DVAGVVGRRF GPRVRRDVAD TPPGTTPGTG RSGGGGGDAA
     SQYGGSWIDD DEEATVLETQ FGDDDDASGE LLGSDGNMER CARCERGGVL VCCDACPGAY
     HLACVGLAET PPGAWLCPAC ERR
//
DBGET integrated database retrieval system