ID A0A1Y2VDN0_9PEZI Unreviewed; 954 AA. AC A0A1Y2VDN0; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 25-MAY-2022, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTA95709.1}; DE Flags: Fragment; GN ORFNames=M434DRAFT_393565 {ECO:0000313|EMBL:OTA95709.1}; OS Hypoxylon sp. CO27-5. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon. OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA95709.1, ECO:0000313|Proteomes:UP000194361}; RN [1] {ECO:0000313|EMBL:OTA95709.1, ECO:0000313|Proteomes:UP000194361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA95709.1, RC ECO:0000313|Proteomes:UP000194361}; RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1; RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S., RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V., RA Henrissat B., Gladden J.M.; RT "Characterization of four endophytic fungi as potential consolidated RT bioprocessing hosts for conversion of lignocellulose into advanced RT biofuels."; RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017). CC -!- SIMILARITY: Belongs to the SH3RF family. CC {ECO:0000256|ARBA:ARBA00008649}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KZ112440; OTA95709.1; -; Genomic_DNA. DR STRING; 1001938.A0A1Y2VDN0; -. DR EnsemblFungi; OTA95709; OTA95709; M434DRAFT_393565. DR Proteomes; UP000194361; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000194361}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 16..72 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 895..954 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 93..256 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 290..529 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..116 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..150 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 158..208 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..246 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 291..316 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 344..373 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 404..495 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 509..529 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 954 FT /evidence="ECO:0000313|EMBL:OTA95709.1" SQ SEQUENCE 954 AA; 107148 MW; 19DFDB44E879E704 CRC64; MASSKPSVDL EKELTCAICT DILYQPLTLL DCLHTFCGSC LKDWFGWQQT VAETSPNPPA PGSQRFTCPS CRAPVRDTRH NATVNTLLEM FLTANPSKDK PEDEKDEMRK KYKPGDNVLP AVRIPDKSPE ERRLEEMERQ MLERARHMSL QDAGVETGES SRARRYRDYS RSDDRRGRSD RDSSRDTRYR DGHDRARRDD ENRRRVDSNG MLQPDLPLDE RQRHSSESHH RSRDSSRTRR RQVEHQASIR SLISSSDVDF RDIEREIEEF ARQIQEEGLL DGLDLDNIDL AQNDELSKKI TEAYRRRQRE RTRPLRPVQQ PRSSDPGIST HRSEHVRSAS RPPLTDVSRP SSRPRSSSAQ SRPGTSQSQV DDRSRPPRPP VTSTHLEVRT DPERRHRRRT SSGGRSATDP VQPRTAETTP PAARSQTDLS SRQQGSDPSS RRPSISESRS ASMPTTNSAT QLSLGDNSRP RDLSFSGRAS AAQIPSAPSP EPNSDDSSKA RPKRTRRPSS LVAPQSPLPS LGLIQSSSHG IHHQRARSQF YYEPSITCSR CKRSHIEYEL HYNCSKCHNG SWNICLSCYR AGKGCEHWFG FGYAAFKNWE RVVAAGNEGL EPPHMLTTCR YRQPKYAPGG AEGRRTITTD DPANRLESGM FCMRCFSWAN ECFWRCESCN EGDWGFCNNC VNMSKCCTHP LLPLAYVSPS PSSIVPPDSP RLARRPRGAT LSAGPNAVSL GNFKSLTFTT ACEICHDAIP PKHRRYHCPE CTSKNAPDAQ QGDYEICVDC YASLVHNKRV SDENGHAGWR RCLEGHRMAI TGFTEGSLGL RRCIFNDVVG GRALHTEPYE GNGMSTEEQR AEGGPRLQKW SWKAANGSRL ERLVAVDVAA TAPDLGTELF PPDGGAGLKA VAKWSWYPQP GTTDELLFPK GAEIREVEDV NGEWLFGSYM GTEGLFPAPY VRVI //