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Database: UniProt
Entry: M2X511_GALSU
LinkDB: M2X511_GALSU
Original site: M2X511_GALSU 
ID   M2X511_GALSU            Unreviewed;      1531 AA.
AC   M2X511;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=SNF2 domain-containing protein {ECO:0000313|EMBL:EME31570.1};
GN   ORFNames=Gasu_12420 {ECO:0000313|EMBL:EME31570.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME31570.1, 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; KB454491; EME31570.1; -; Genomic_DNA.
DR   RefSeq; XP_005708090.1; XM_005708033.1.
DR   STRING; 130081.M2X511; -.
DR   EnsemblPlants; EME31570; EME31570; Gasu_12420.
DR   GeneID; 17090206; -.
DR   Gramene; EME31570; EME31570; Gasu_12420.
DR   KEGG; gsl:Gasu_12420; -.
DR   eggNOG; KOG0298; Eukaryota.
DR   OMA; QLFEQMC; -.
DR   OrthoDB; 8175at2759; -.
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   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR048686; SHPRH_helical_1st.
DR   InterPro; IPR048695; SHPRH_helical_2nd.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR   PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21325; SHPRH_helical-1st; 1.
DR   Pfam; PF21324; SHPRH_helical-2nd; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000030680};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1223..1278
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1351..1497
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1531 AA;  177740 MW;  4BBE7C80EA405CF4 CRC64;
     MILGMTTPSN RKRKRVTRKA GPVFTSFCEI SEDQIDVGEG PWCLLWPFMR EVQGTDDQLQ
     TMSLANLYYC GEQTLEGRFW RVSIDSNESR ERTEDFAIKI WEGVSTQESE KSLISVNCSF
     FVKSSHRTNF YTYSGEVILC DRLAKAIRYL ADNHFLAARV VTYSLYDEDL TFPERSCFRV
     EFYFTEKLFL NAPKSATEYR KLSVFTHVRI LMSWLHSDIS TFTLFSEAFC CQDAHLILDS
     LWFNRVCETI QLERQKSSSN LWELERSQMT LLEQQLSIIL RPYQRKAISW MLYREEMSTM
     NMNGEESNPL WFPMFSKNSD SNISFFYNPC TGQVSKKSFE PFMDIRGGIL ADEMGLGKTV
     EVLSLIILTL TKRKEVTSLE KPERVFWGGN LDSFSDKDKV EAFSFVTSTQ NVEKCSCCQE
     LTVNDHVPEE FHSLFVRCDE CGKVEHAWCA NYRFERAIRV LQASPHLCYQ CEADYKSQKV
     LQSHATLIVC PSAILGQWEE EIERNTKTVI YHYTYRGMKE SGYVPARTLA EMDIVLTTYE
     ALRNDLNRVD LGSGPSLRYA KVFRAVPTPL CRIEWFRICL DEAQIVEGGS SGAADMAQYL
     SGTRRWCVTG TPIHKDMSDF YGLLKFLQVV PFQDHFWWNR FVWKPALFGN DQNLRRLVDR
     LVWRNTKNIV YNELNLPPQS TLKVILSFGP IERHFYDRQY ELCVEEASRL LFSQGKFQNG
     VSSLEDFSKD SVMGEKLFFR LLRLRQACCH PQVGSDGIRV LQKSTMTMQE VLEALVQRRT
     VEVSEAQRSY IASMNGLAAL HILQENLIKA VDIYRNVLRF AKENEEHVTM DSLQKLHVLH
     NLSQVLEMIE SKIDDKSQSS KDNNLNSYKA VGRTLEESEY KTEMQELEAR YTSEKLAKLS
     KAKASYEASK MSSEELIAKR ATIPWWMEVL AEMVANNKSL EEQIMEQIRS QLLYSSQGVF
     TETSIVSRFH SLEGLRYVLM NELEKRDRCR LELLETLENL PGARTPTTSE IMASGNCRYC
     RVEGDGPACC HCIAKEKFLA YERSLFLVRM INIGRKCNTS HGRYGVISEG DEGARLQSEI
     EKILKIIKSC IRRHYRKRFS WLKDMERHFQ EVEALKEEFR ECHVYFEAQH DFLSALDELE
     MSKMRISLKI SDQDQKRKNV DSYQISPSQV GSLFMQFEHD RSLAEVDFQH KRSQLLFLKR
     LRAEQESCNQ EGKEDDTVRM QPCPVCWREL EAQIVILPCG HRFCAECVSH MVQQRISEQV
     EIQKKSESEQ YISCPSCRVS VIVNELCYIE RKSEDESCIR KIERICSIDG NRMEEGAENW
     TTQQFYSLWK SLQGDSVRDS FGTKISAFAI YLKMIIERDT DAKCIVFSEW NDVLEIVSRA
     LERMNVVFTR TEQRRGKSFE TVLRKFRTNF EIRVLLLPVR SGSNGLNLTE ATHVFLIEPL
     LTDSLEAQAI GRVHRIGQKK PTFVHRFLIE NTIEEKVDEL RRKKRASSIQ NNSKALNVRG
     SRTMAAEEVL TVQDLYLLFP SEQQQYTVDS R
//
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