ID E1Z690_CHLVA Unreviewed; 1718 AA.
AC E1Z690;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHLNCDRAFT_50422 {ECO:0000313|EMBL:EFN58609.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN58609.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN58609.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; GL433837; EFN58609.1; -; Genomic_DNA.
DR RefSeq; XP_005850711.1; XM_005850649.1.
DR STRING; 554065.E1Z690; -.
DR GeneID; 17358367; -.
DR KEGG; cvr:CHLNCDRAFT_50422; -.
DR eggNOG; KOG0298; Eukaryota.
DR InParanoid; E1Z690; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000008141; 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; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd15517; PHD_TCF19_like; 1.
DR CDD; cd16449; RING-HC; 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); 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR048686; SHPRH_helical_1st.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 481..531
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 523..565
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 1538..1587
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1119..1150
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1718 AA; 183150 MW; E351EA2D4D7A244E CRC64;
MKRKRAPKRD VPRPEERNFL APPEHDEGGG GDGGGGEGVD WAAGEAGLED SDDSEGYAWR
PVKRGHRHRR RRRVLGGEED GPLTVAVQAA PPAEQRWRFA ELAVEWREAG SSSSQQRLEL
EDGQLRLCLP PDGGDVRVHY QASGGALWLG ATAAPPAEGE ALLLLLKSGH LSCSVPALPS
GASGSASGRL HLSLTDKAAA DAAEHAEEQQ QRQWHRQLLA VLRWLLPQLD PEQELELQSP
QKQAELLASP LCSPRAAAGA AAAGFGNPAA AAGTAAAGLA SPRSPGAAAG GVPGAAAGFD
VSELYAAVKP TGREPELPAC ATAAYLLPTL RRYQARAAQW MVLREQGLVA APGEAAAAAA
AAGGSQAADI KAEEGHQARD GAEPPLHPLW RRVPCSAGGG DGSSSDAGAC FFVNAYNGRI
SLERFPATPE VRGGILSDEM GLGKTVELLA CIAAHPYTGP PPTFQKPQQG GQRGSKRRAA
RVACLCGATS EEGYEGLWLQ CDSCDTWLHA ACCGLRRAPP GDFVCGGCQR AAAAARVAQD
CGATLVVCPT PILHQWRDEI LRHIKPGALR LLIYEGQPQP GAGAASKVVT AAELAAADIV
LTSYDVLRRD VNHCPDEAEQ AGAGRSLRWR KKYEASGAGG WAYVGLRAAG CEVMPTPLTR
LRWWRVCLDE AQMVESSTAK AAEMALKLHT VHRWCVTGTP VSRSLEDIYG LLAFLQASPY
SNRHWWQRAV QQPYEAGSRA GRARLLSLLR PALGGLLWRS SKADVAHELG LPPQHHHLKS
LQMSAIERHF YSRQHQECVA KARAALSSQL LAAATAAAAA HDGVAISDSR EAGAGAAAAA
EAGAAPASPP AVRLPPAATA AAGFEDRALT RREEASLLHP LLRLRQACCH PQVGGAGIRA
VGPAGHNRSP MTMGEVLEVM LAKARVEAED AQRLLLASLN GLAGLLLLQE QPVEAVRAYR
EALATIEQNK SLIRADKLQQ LHTLTNLAAV LGPEGRSVEG AAPTLRDAWL ETEAQEIREE
YLAESLSRLT DAAQEVEEVQ RHVQRCKAPL LQHVSAAEAE ELLAGWYMRG VALIVAHGRD
HHTQRAVAER IKEQVKEETM YLRSVSQNAA SIASRFRDLH GLELAVKQEV RELGRAQAEA
TQELQRLQAA CRAPPPALVE LAATCSRCRA ETAVAGRVCR HCRLEELFWS WEGWEGWEGG
AWACLLSVHN ARGPAHQLQT TICAGLSPPA AQAGRAFALY SKAREGGGRV TADDAIRQAQ
QATLFNRVGR GGLGEAAAEQ LGGSIGDAGG EDEEGGHHLL LGAGRRDDAV AKTEIVRRPG
DAENVLRLLL HQLRLVKKDL VMTAGKAHLE LMEQYRRLYL KARALSLAQR QRLYAVDELE
QCTMRIKLLS DNELRLKEGE EIYRVYEHEV PVRSTELSND KASAELELHR KLGTLRYLTG
IKAREAARAA AAAAAEAQVA AAAEEDAAAG PMGDGVEEAG TGAAGKHSVA PAAGAGRGEP
GVDAGLPCQP AASEAGTTAA ARGLVAAAAG EEDREDICPI CHDRLGQEMV MLACAHRLCC
RCSVALQERL PAGQPKASRR IECPVCRTRV PVSDLVYIDA RLASPGGKVR RRSGRGCCRA
CGCCRGSMGH RQGMRLARAC NWLMGGRLLT ACATCELQRA RGEEAEGEGD IEVKGSYGTK
CGVFEHRTSL QQGKADWGIS MATFCWKGMQ RESRGEVS
//
