ID A0A094D685_9PEZI Unreviewed; 1689 AA.
AC A0A094D685;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V493_01999 {ECO:0000313|EMBL:KFY30322.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY30322.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY30322.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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:KFY30322.1}.
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DR EMBL; JPJV01000762; KFY30322.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094D685; -.
DR HOGENOM; CLU_001592_1_0_1; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000029327; 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; cd16449; RING-HC; 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; PF13639; zf-RING_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:UP000029327};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 323..525
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1152..1190
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1689 AA; 190144 MW; 6D312E521225D4CA CRC64;
MAPITNPRSH EYGVEQRVAN VGISNEGYCP SSVVEYLERM TALPEPSLQE PPNKRQRLNS
DNDLDYMVVK RSSLTLKFRQ SPHKSARSPL TYQSETTRTQ VEETGNQVIL RIRDNEVRDW
NILSGTFDAD SVPIRDINIA GLIPYYAKHK SNPTAHGRLW AETGFSLSVE EGFELLLLTW
TVKWNFSPSL AYISATTPKR PDLESVLEAY FPDPAQIDCN GTRILPQDFY NSVHVPSKND
ATAETIEIPE LKSQLYPFQK RAVRWLLERE GAQWSAEENC VKDAVVKPEK LPCSFYEIVD
EDGRTCWVSS LLQAATRELS AYKAAEDEFI GGLLVEEMGL GKTLEITALI TLHKIRPDSL
RTIIDPYTSQ EAIPTKATLI ITPPSILQQW ESELARHAPS LKVMHYQGKT KHKKLTGKQL
LDMISEHDVV LTTYRVLAGE IYHAAQAPGR VSRHLGDSQQ NMSIFTHFLW WRCVLDEAQM
IEGSVTNAAK MAQMVPRVNS WGVTGTPVKK DVEDLFGLLK FVRYEPFGIL PWTWAAILRN
PPAFKTLFQR IALRHTKSIV RDELQLPPQK RYVITMPFTP VEEQHYQSLF QRMCDECGVD
IQGGPLTDDW DPTRTRTMEK MRVWLSRLRQ SALHPEIGVK NRRALGRKVG PLRTVEEVLE
TMLEQTELII RGDQRALYLS RLKRGQTLEN SPRVKEALEI WKSVLVDANA AVLVCREQLQ
REIDSPNGNM TLGGGPLLNN EEISSDDSSD TDDQGVESTA RVGALRNRLN AALEIQHMAV
FFCANAYFQI KSNEEMTKPD SEEFKGLENL EAEGYQEAKM IRQEILKEIY RKNTKPMERL
AKKASSEDFL SIPEFHTDVQ RGGIESRRLL EQLDGLAAAL DAQANQLDEW REVTIQNLLQ
PLVDEEEAIE MTGEEYLQST ELQQELVVYV LALRAVIEDR HDALTGQENQ LVKYEVKTAI
AQAKADIEQA VADLADADPD QAEADIEQAE ANKWLLPQKT LELLQARAEL KPPEAMGSVA
GILSELRTLS TQLKTDAKKG SSRAANELVI VERNMAIVRE HLGEQTKAVT ALRQEIDEFT
SLMNLRVEYY RQLQQISDMV LPLHEDSPPD LSITLLETEQ KLAAKIATSS SKLRYLVHLK
EESAADAEGR DCLICQSPFE NGSLTVCGHI FCKECMQLWW RVHKNCPACK RVLTIHDLHD
ITYKPQELKM AEETPITPHN QDRALVSPSK QSGIYSQISR DTLAQIKNID LVGPSFTTKV
DTLCRHLLWL READPFAKSI IFSQFSDFLI ILGRAFAHHR IGYSTIDKPG GIEKFKNDPA
TECFLLHAKS QSSGLNLVNA SHVFLCEPLI NTAIELQAIA RVDRIGQQQA TTVWLYLIDG
TVEEAIYDIS VRRRMEHMGG ASTAASKEST PELADRKIEV ANSLELQQAP LAKLLTKEKE
GGEFVGNEDL WECLFGNRRG AREGAAAAEE RLDREVARHF GAESAEARIA DGSQQRIRLI
RNILEEQKAS QLGTINDCLQ RVREFYGAQA DYITSASQTT SQSAKLQTNI TMKLTATLAS
LAVLSAAFVG NVSATSCYGK GELLQIKDAA YHFGRACRGY DGKKGSFQGP FKGGETKSTC
VNHNGDRFNF YLENREGHTR DLTDDGCVKE FTKIMNDCRY AWDRRLTQGG VNLANGNWWF
RADPNKGPC
//