ID A0A2N3MYV5_9PEZI Unreviewed; 950 AA.
AC A0A2N3MYV5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=jhhlp_008732 {ECO:0000313|EMBL:PKS05358.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS05358.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS05358.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS05358.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:PKS05358.1}.
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DR EMBL; NLAX01001623; PKS05358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3MYV5; -.
DR STRING; 41688.A0A2N3MYV5; -.
DR VEuPathDB; FungiDB:jhhlp_008732; -.
DR InParanoid; A0A2N3MYV5; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000233524; 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; cd18008; DEXDc_SHPRH-like; 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; 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; PTHR45626:SF12; DNA REPAIR PROTEIN RAD16; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 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; 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 3: Inferred from homology;
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:UP000233524};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 353..538
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 701..741
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 782..936
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKS05358.1"
FT NON_TER 950
FT /evidence="ECO:0000313|EMBL:PKS05358.1"
SQ SEQUENCE 950 AA; 106554 MW; D6156E3DCD283C35 CRC64;
SGRVINTPGS SRSATPGGRP PVPKTRSQVT TIEVRLPGRS LPGGSVELAT DHSGALPSRP
ILALSSDDEG PPRRSSRRSL ANSPRLTASQ RPKYLQRTDL SLNPTKMEIE DDDDDAEMST
DYIVAKRLQE EEYTQAAIET QLETAGLEPP SKRIKSNKLS PGPTAVSSRQ STRSRTSING
RASGVSNGSL PVLASDGQRP TRASATRLSR ASRAAQPSGF ISASQLLQQD GAEDSLPSDF
STGSSSGPDT EFNSEESEAE GDEEGEEGEA ETDEVTRRVA RAVQDRRAFG QRATARAVRT
VRQKLEGFHP ELKELWSDLE SEPPFVPVQV EQPASIHRRM KGFQLEGLSW MKQMEASKYK
GGILGDEMGL GKTIQAVSLI MSDFPAGKPS LVLVPPVALL QWVSEIDSYT DKTLKTFVYH
ATNSETKTLK LNELKKFDVI IMSYNSLESM YRRETKGHRR KRKGDDCTEE IHTQPSIIHK
IDFHRLILDE AHEIKTRTTS TARACFALKG TYRWCLTGTP LQNVIGEFFS LVQFLDVRPF
STYMCRSCPC TLPNWNFGES RYCHACKHGA LGHFSVFNQE ILIPIQRHGQ RGPGQIAFNR
LLLLTDRIML RRLKKNHTES MELPTKELRV SRQFFSEPEN DVVKKIMGDA RQAFEAFALD
GTILNNYANI FSLIMHLRQS ADHYDLVLKR NADGGQNILE CCICESPAED AISSKCRHHF
CRSCARSYLD NVENPDCPRC HIPLSIDLVQ PEIEQDQMLF KKSSIVNRIQ MENWTSSSKI
ELLVHELFRL RSEDSTHKSI IFSQFTSMLQ LIEWRLRHAG LTTVMLDGSM TPAQRNASIN
HFMKNVDVEC FLVSLKAGGV ALNLTEASRV FLVEPWWNPA VEWQSADRCH RIGQARPCII
TNLVIEDSVE SRIVMLQEKK TRMIHSTMNK DTEAAQSLTP EDMQFLFRGI
//
