ID A0A3E2HE39_SCYLI Unreviewed; 1090 AA.
AC A0A3E2HE39;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RFU31678.1};
DE Flags: Fragment;
GN ORFNames=B7463_g4705 {ECO:0000313|EMBL:RFU31678.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU31678.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU31678.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU31678.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU31678.1}.
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DR EMBL; NCSJ02000071; RFU31678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HE39; -.
DR STRING; 5539.A0A3E2HE39; -.
DR OMA; EHINTSM; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd16457; RING-H2_BRAP2; 1.
DR CDD; cd12717; RRM_ETP1; 1.
DR CDD; cd01803; Ubl_ubiquitin; 4.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR011422; BRAP2/ETP1_RRM.
DR InterPro; IPR034931; ETP1_RRM.
DR InterPro; IPR047243; RING-H2_BRAP2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF00240; ubiquitin; 4.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00213; UBQ; 4.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 4.
DR PROSITE; PS00299; UBIQUITIN_1; 4.
DR PROSITE; PS50053; UBIQUITIN_2; 4.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 77..152
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 153..228
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 229..304
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 738..777
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 774..882
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT REGION 404..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 942..1040
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 404..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU31678.1"
FT NON_TER 1090
FT /evidence="ECO:0000313|EMBL:RFU31678.1"
SQ SEQUENCE 1090 AA; 120991 MW; 1257A9DF73BCC9DD CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKSKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKS
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVESSDT IDNVKSKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGEEGRYQR RMPSYFYHLK FELYPYDYAN LPGLIIKSDD LRTSIAQGRS TRPTNGQHQQ
GEALDLPSAW LPEPGTDIFD TSSWPSHTTS ISELEGFNWA TAQKSGRVRT NTASSRKSYS
ESPTATGSAG PRTKEAVIDC GPSRGSDILP NDEVTGIGSR RAESLFVPAP SSSAETDFPP
PNPTHLIGDP KTAIKDWRFA KVRVESFDMA ETNKPGPAGM DNEANKGINA GLAAAAGMGN
VTKARFEPLE TKSTELGWGI VHLYRDGEET PGLNNPDIDL YSAEDTPSRG GLGQQESTNS
TDNKNDCTTL CIPAVPSYLT ANDFLGFVGE KTRMQVSHFR MVMTGRMNRY LVLMKFRDPK
VAKRWRAEWD GKVFNSMEPE TCHVTFIKSI TFHTPASSRP STSFPELSHD PFSPSSNSST
FLKPFPPPTP NLVELPTCPV CLERMDDTTG LLTILCQHVF HCDCLQKWRG TGCPVCRHTN
PSLALPASST YDPANPPFGS GEASLCSICD STEDLWICLI CGNVGCGRYK GGHAKEHWKE
SAHNFALEIE TQHVWDYAGD MWVHRLIRDK GDSKVIELPS ASRSRLGSRG DRDMDMVPRE
KIESIGMEYT HLLSSQLESQ RVYYEELVSK AVAKVSAASS AAAQAASRAE EAISKLNELT
VENKRLREEI ITGLEKDLER EKKKAEKSSE VARGFGKSLM EEKKVSEGLM GRIEHINTSM
MAMSKELTQL KEENLDLKEQ NRDLLFSITA QEKLKTMEEA GDGIEAGEVE GGTVSLPPEK
KRGKGKGRGR
//
