ID A0A093XUV1_9PEZI Unreviewed; 1148 AA.
AC A0A093XUV1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=O988_08158 {ECO:0000313|EMBL:KFX90534.1};
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:KFX90534.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX90534.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX90534.1,
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 -!- 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:KFX90534.1}.
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DR EMBL; JPJR01002040; KFX90534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XUV1; -.
DR STRING; 1391699.A0A093XUV1; -.
DR HOGENOM; CLU_000315_3_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; cd18008; DEXDc_SHPRH-like; 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; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 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; PF13445; zf-RING_UBOX; 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:UP000029329};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 384..578
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 775..821
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 893..1054
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 129833 MW; F55BE97470C34A6D CRC64;
MDPSGTGRHT PPITQPTQSL TSVENAQDES PRGGLFGTPA LDGGNFQEKR PRESLFVTPE
PDDDISTHDY VEEPISHQAP TPHFNSQDET QRIRLGQEAM RREILTKRKS GADSIFDSGR
AKVQRPNPGT GSPFNEESNE EDHSWMGADN GENGTDEQDV LLKNMDALKK AMKDNGELTS
SQHLEYLQAS QRLQTASRRQ NKATGKRAIN KTARDVQNSL REREAEKMAN RAAKSGSAGN
KGRAAKKSKG KKQGTGSVPT GNPPAYKRRM KNKLPEVDDT VQKLLESLVY SDTVKERMEQ
GDVEKGPDIV ANVKAKQLKQ LLGSIPLDYD TYKAKNERKQ LHDASKAFGH GKVKAINGQW
LLAGMKTELY HHQLLNANWM VQRELSVDRP NGGILADGMG LGKTVSTLAT MVGNQPAEKD
IAEMRKATLI VVPASLLSQW KAEIKRHVDE KIFPVVVPYK ASSDSPAKLL ELCDVVLTSF
TEVMNSWPFP NSAEEKADAR KIGEDEWANR HDSRKGELHK VNWYRVVLDE AQAIKNHKSR
TSIACHKLQS TYRWALSGTP MQNSLNEMYP YFRFLRMHWA DSFSTFKRNF GDPDAIDSTK
RLTVMLSIIM QRRTIGSKIL GRPLVHLPPI HPHLKVVTLS GEERAIYRTL EDRFRIMMNI
NFKAKTAEKN YGTYLHQLLR LRQAASHPFL LERCVKDLFE VEDILALRRR LKRLKKDKRP
MYEQIDQWAS QPTTSEQNQG SGKVAFGRSD FGKDFDFEGF LTEADHKKMY DRLMCSLCSD
IAVDPVQTEC GHIFCTSCLE GNMHAQTATL EFDYNTCPTC EKIIEGYEKL KFPHLKGTDD
GAGSERSTSS QPKEQPPPKK DPNFKPHIKD SEWLKMVLEG SKKLLPSSKA IALKSQIIHW
LHEAPDDKIL IFTQFRMMTR IIGLLCEKEG WGHVFFTGDM NMKQRNYSVE RFHTDKNIKI
MIAVLKCGGV GLNLNCANRC ITIDPWWNHS VEQQAFGRVY RIGQVKETHV ARFVVKNTVD
MRILDMQKEK MSEIDGAMLS AGKPLPPLTI EEMASLFGDL VKDEDGDTQV VADYESEVES
EGDYEDEDEV VEESAEDEIV GEEEGVSVAL IYLFTVQTTP VLHLNYSYSR ERYLSRNYNS
RADSWLST
//
