ID A0A094FSC4_9PEZI Unreviewed; 1615 AA.
AC A0A094FSC4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V500_04576 {ECO:0000313|EMBL:KFY91613.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY91613.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY91613.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
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:KFY91613.1}.
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DR EMBL; JPKC01001513; KFY91613.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094FSC4; -.
DR HOGENOM; CLU_001592_1_0_1; -.
DR Proteomes; UP000029284; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000029284};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 432..634
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1272..1310
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1382..1534
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1064..1112
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1615 AA; 181277 MW; ABAA183E954FE9FB CRC64;
MRQTKFKVLG HGLWKLIGKP LFYLNANLPT RGHGGVWVDK AAGWWGRLEP GGVPRPRYRT
RTCLRLWPNT GLIPSVDFAS SLDLAFVAMA PITKPGSGEN GVDQRMASVN ISSKGNSGKT
FSHNLDLVVL TIGFAGYCPS SVVEYLERMT TLPEPSPQEP PSKRQRLNSD SDLDYMVVKR
SSLTLKFRQS PSKNARLPLT YQSETAGTQV EESGSQVVLR ISDNGGRDWD ILDGTFDADN
VPIRDINIAG SIPFRAKHKH NPTAHGRLWA ETGFSLSVEE GFEVLLLTWT VKWNISPSLA
YISATLPKRR DLELVIETYF PDPAQSNNKG TRMLPQDFYN SVHVPAKNDA AAALIETPDL
KCQLYPFQKR AVRWLLEREG VEWSVEGNCV EDTAVKSGKV PCSFYEVVDE DGRTCWVSSL
LQAATRDLSA YKTAEEELIG GLLVEEMGLG KTIEITALMT LHRGNPDSLQ TVVDRYTSQE
AIPIKATLII TPPSILKQWE SELARHAPSL KVMHYQGKTK HKKLSDEQLL DMIAEHDVVL
TTYRVLAGEI YHAVPVPGRV SRHLGDLQQN MTIFTHFLWW RCVLDEAQMI EGSITNAAKM
AQMIPRVNSW GVTGTPVKKD VEDLFGLLKF IRYEPFGVLP WTWAAILRNP SAFQTLFQRI
ALRHTKSIVR DELQLPPQKR YVITMPFTPV EEQHYQSLFQ KMCDECGVDL QGGPLTDDWD
PTRGRTIERM RDWLSRLRHS ALHPEIGVKN RRALGRKEGP LRTVEEVLET MLEQTELSIR
GDQRTLHLTR LKRGQTLENS PRVKEALEIW KSVLVDANAA VLVCREQLQH EIDFPKVNKA
LGGGPLLVDE EISSGDNSDT DDEGPGSEST MRIGALRNRL NAALEIQHIA VFFCANAYFQ
IKSNEEMTKP ESEEFKELEK LEAEGYQQAK MIRQEILKEI FRKNTKPMER LAKKASSADF
LSIPEFHTNV QKGGIESRRF LEQLDELAAA LDAQANQLDE WREATIQNLL QPLVDEEGAI
EMTGEEYTQS TRLQQELVIY VLALRAVIED RHDALSGQEN QLVKHEVKTA IAQAKADVEQ
AEADAEQAEA DAENADVDVE QAEADIEQAD SDKWSLPLKT LELLEARAEL KPPKAMGSVR
GILSDLRKLS SQLRNDAMKG NSRSANELVI VEKNMTIIRK HLEKQLKAAT ALRQEIDEFT
SLMNLRVEYY RQLQQISDMV LPLGEGSPPD LSITLLETEQ KLAAKIATAS AKLRYLVHLK
EESTADAEER DCLICQSPFE NGSLTVCGHI FCKECMQLWW RGHKNCPACK RVLTMNDLHD
ITYKPQELKM AEEAPITPHN QDRAQVSPSK QKGIYSQISR DTLTQIKNID LVGPSFTTKV
DTLCRHLLWL READPYAKSI IFSQFSDFLD ILGRAFAHHR IGYSTIDKPR GIEKFKNDPA
IECFLLHAKS QSSGLNLVNA SHVFLCEPLI NTALELQAIA RVDRIGQEQA TTVWLYLIDG
SVEEAIYDIS VRRRMEHIGG TSTAASKEST PELVDRKIED ANSLELQQAP LANLLAKGKE
AGEFVDNDDL WECLFGNRKG AGEAAAAADA EERLDREVAR HFGAEAAEAR IAEGV
//