ID A0A093YA13_9PEZI Unreviewed; 1470 AA.
AC A0A093YA13;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=O988_03764 {ECO:0000313|EMBL:KFX99592.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX99592.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX99592.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX99592.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX99592.1}.
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DR EMBL; JPJR01000642; KFX99592.1; -; Genomic_DNA.
DR STRING; 1391699.A0A093YA13; -.
DR HOGENOM; CLU_001592_1_0_1; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
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; 1.
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; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
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; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 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; PS51192; HELICASE_ATP_BIND_1; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 324..525
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1128..1166
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1470 AA; 165255 MW; 0CC96E17A58C0D48 CRC64;
MASPIINPIS GENGVDQRMA DVDISSEGHC PSSVVEYLER MTTLPEPSIK EPPNKRQRLN
SDSDLEYMVV KRSSLTLKFR QSPHNPARSP LTYQAETIRT QVEESKRSVV LRIRDNNCRD
WNILDGSFEA DNVPIRDINV AGLLPSYTNN KHNPKAHGRL WTETGFSLSV EEGFDVLLLT
WTIKWNLSPS LAYISATRPE RRDLNSVIEA YFPDPAQGNN KGTRILPQDF YNSVYVPANN
DATAASIEIP GLKTQLYPFQ KRAVRWLLER EHVQWSVDYL CLEDATVKSE RVPCSFYKVT
DGDGRACWVS SLLQAATRDI SAYKAAEDNL LGGLLVEEMG LGKTLEITAL ITLHRSHPDK
LGSFADPYTS KEAVPIKATL IITPPSILQQ WQSELERHAP GLKVMHYQGK TKHKNLTEKQ
LLDMIAEQDV VLTTYRVLAG EIHHAKSSER FSRHTGGLKH SMSIFTHFLW WRCVLDEAQM
IEGSITNAAT MARMVPRVNS WGVTGTPVKK DVEDLFGLLK FIRYEPFGIL PWTWAAILRD
PPAFRTLFQR IALRHTKSIV RDELQLPPQK RYVITMPFTP VEEQHYQSLF QQMCDECGVD
LQGGPLADDW DPTRARTIER MRSWLSRLRQ SALHPEIGVK NRRALGRKDG PLRTVEEVLE
TMLEQTELSV RGDQRTLHLT RLKRGQTLEN SPRVKEALEI WKSVLADASA AVLVCREQLQ
HEIDSPPKNR ALGDGPLLND EEVLSGDDSD TDDMEYAAES TARVGALRNR LNAALEIQHI
AEFFCANAYF QIKSNEEMTK PDSEEFKELE KLEAKGYEQA KMIRQEILKE IFGRNIRPME
RLAKRASSED FLSIPEFKLK VQKGGIESKK LFEQLDKLAA ALDAQANQLD EWRETTIQSL
LQPLVDEEEA IEMTGEEYLH STELQQEIVI YVLALRAVIE DRHDALSGQE NQLVKHEVKT
AIAQAKADDG PLPELTLELL KARAEIKPSI TLGSIRGILS DLKTLSSELK LEVTKGSSRA
AYELEIVEQN MTIARKHLDA QNKAVAALRQ EIDEFTTLMN LRVEYYRQLQ QISDMVLPLE
EDAPANLSQT LLDTEKKLAA KVATSSSKLR YLVHLKEEST AGMEARECLI CVAPFENGLL
TVCGHLFCKE CMGLWLRAHK NCPACKRGVT LNDLHDVTYK PQELKMAEET PITPHNQDRA
LVSPKQSGIY SQISRDTLAQ IKNIDLVGPS FTTKVDTLCR HLLWLRDADP FAKSIIFSQF
SDFLVILGRA FAHHRIGYSS IDKADGIEKF KNDPATECFL LHAKSQSSGL NLVNASHVFL
CEPLINTAIE LQAIARVDRI GQQQSTTVWL YLIDGTVEEA IYDISVRRRI EHMGGASKAA
SKESTPELAD RKIEVANSLE LQQAPLAKLL TKGKECGELV GNDDLWECLF GNRKGAGGGA
AAAAAEERLD REVARHFGAE AAEARIAEGA
//
