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Database: UniProt
Entry: M2XAC2_GALSU
LinkDB: M2XAC2_GALSU
Original site: M2XAC2_GALSU 
ID   M2XAC2_GALSU            Unreviewed;      1502 AA.
AC   M2XAC2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Chromatin remodeling complex SWI/SNF component, Snf2 {ECO:0000313|EMBL:EME26817.1};
GN   ORFNames=Gasu_56060 {ECO:0000313|EMBL:EME26817.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME26817.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
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DR   EMBL; KB454542; EME26817.1; -; Genomic_DNA.
DR   RefSeq; XP_005703337.1; XM_005703280.1.
DR   STRING; 130081.M2XAC2; -.
DR   EnsemblPlants; EME26817; EME26817; Gasu_56060.
DR   GeneID; 17085767; -.
DR   Gramene; EME26817; EME26817; Gasu_56060.
DR   KEGG; gsl:Gasu_56060; -.
DR   eggNOG; KOG0386; Eukaryota.
DR   OrthoDB; 1465at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT   DOMAIN          802..968
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1119..1278
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          171..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1502 AA;  174113 MW;  336327FB9D5817EB CRC64;
     MSGEKTKEKL SIQQVDGNIL LRKEDFLDED ILFDSRGNFE LPSFDALDEQ LETFFNSGTL
     NKTKKELNRQ NYEEKELSLE LEVDRNHSSA SHFENSSGEF YAWKTNSAVE NTNDKGDLTK
     PQKVFSNTKS TVSKSCVVEK NAPPLEAQSH VTLDSDTSRK KTIPLNHRNE MSDYGYYSKN
     SDPTGNSVFL ENRPKTDERN ELYYSDLYHP KRKREFIGEK LSSHSGISKE TSNLRTSQTM
     KLERNSSLSD GTTMHSNLNN LKRQKWILPQ DFETSSLQQP DRKLVEAQKD LFRQEFSSMP
     LKVSLQGSTS NVDVKAENSL PLQIVDSVMP VGHLSQTSKC NDVNKNDVKY LNESMQRQID
     DTKRHSVNRS SILTSRLHRF PLKPKILFGV IELLKCQRKR NLPSEETKYF ILMKLLKAHT
     VPYPNSILTF RHLFALRVQY RIFYEMKRGG RLPEDTLNAS RALTIGSGSI PQVEKMNNKS
     KPPERNFTRQ QVFVQSLPFP AEKLSSDLNI TPLDSSFLRK EADRLVTTLS RRFANKLATE
     ISSFKCNEDA SVEDSKRWGA QKRTLRIQYS KANLVVLQRK LRRRVLEERR MAEEQGKLGS
     KSRLRSFRAL MKEAEKMERF MLKEMEAQER EKRKNFVSFL SSLMSHINNF RQYHKEYVHR
     LRRSVARSVL RYHEDKARAV ERAEKEAERR RIIALKENDE EGYVNLLRQT KNERLLQVLN
     QTDEYLRHLG AVVKQQRDGT LNDGQHYLEK EETNKTDVLS RENCQTYYEI AHAIKEPITE
     LPTILQGGTL KQYQIQGLQW LVSLYVNHLN GILADEMGLG KTIQAIALLA YLVEKKNNSG
     PFLIVVPLST LSNWELEFEK WAPSLHVVVF KGDRKQRKSL YDTVIQPLNF NVCLTTFEFV
     SRGKNLLGKV EWNYLIVDEG HRMKNHESRI TAILSQQFKS RSRLLMTGTP LQNSLSELWS
     LLNFVLPNIF SSSETFESWF AAPFASIPGE KADLSEEETL LIIRRLHQVL RPFLLRRLKS
     DVLRMGDQLP TKQEHVILCE ISAWQKMVYR RILRGQKVVF TGLSGRRRHD FLSNPAMQLR
     KMANHPYLFY EDYSEELMLG NRDSEELFRA SGKFYMFDML LQKFLRTGHR VLVFNQMTRV
     IDLQERLLRF RGINFLRLDG STKSEMRRNI VEEFNRSDTI YHVLLLTTRA GGLGVNLQSA
     DTVIIFDSDW NPQMDLQAQD RAHRIGQDKE VLVLRIVAAN TIEERILERA SYKKDMEQKV
     IRAGMFNETS KDSDRQALLR ELLKDDEERS SEGHESRVPD LETINAMISR SDNEMEIFQQ
     VDEERQIELN SRSPLMEPNE IPSWVIGDVN EEDDEDLGEW SLSKSDYLPK ESESSYSFHS
     VSSDDEISYQ ASEWEVHSAH RSKRDSYEFH QVSSEWCESN AKLRNAQSDN VSGTTCLLEP
     DETCNENVVG RDDRESDYSD SYQKSISERA SISIEGLNGS LCFTDDETYS GWFEEAELGQ
     ET
//
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