ID A0A135S3L8_9PEZI Unreviewed; 985 AA.
AC A0A135S3L8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=CSAL01_00716 {ECO:0000313|EMBL:KXH30488.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH30488.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH30488.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH30488.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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:KXH30488.1}.
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DR EMBL; JFFI01002554; KXH30488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135S3L8; -.
DR STRING; 1209931.A0A135S3L8; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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 InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF50044; SH3-domain; 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:UP000070121};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
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 REGION 117..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 110421 MW; 4A6C8E59F8991DFF CRC64;
MDSSRPALDL EGELTCSICT ELLYQPLTLL DCLHTYCGAC LKDWFSFQAQ QAENSPTPPA
PGTNIFTCPS CRAPVRDTRH NATVATLLDM FVAANPDRRR SESDVAEMVK KYKPGDQVLP
EVKIPERTPE ERRAEEEERR LLEDVREMSL RDAGVDSSSG HRHRRRREDS SSADGRTRRS
RDHSRDSRHT HRHEGSRRPR DDEGRSSGDQ LQPDSRSGEQ RRHRRSESRQ RAQESSDMRR
RQIEHQSSLR SLISSSDLSE RDVQKEIEDF ARQIQEEGLL DGLDLDNIDL SRNDELSRKI
TEAYRRRQRE RERTRAEGTR RRDASGQSRH SPDRVQEIRS SASDTSRPSS RQRPHSRSTS
ATGFLEDRSR PPLSQSALHL EVRPEERRRR RRTSSGGRSA TTPLPATQSE TRVATRSQTD
LSSRTHFGEA VAPRTVFTEA RSSSTPSVPT TTQSPTTTTS PAPRELTFAN RMTNSSGLVS
SNFAASPPIE PLSPRLQRPN RPADLSIISQ ATSGPVGLGL GLGIGSPTTP GHQRTRSQLY
PEPSITCSRC AKQHIEYELH YNCGICASGN WNICIDCYRS GKGCLHWFGF GYGAWAKWEK
ARHTAHEDIP RPHMLTANRY LQPKIIPGGA EGRRTLTTDD PMKRLESGNF CARCQTWANE
CFWRCDVCNF GDWGFCNNCV NQGRSCTHPL LPLTYQPQSS HTPPASPRSP RPPHSAAVLT
GPNIHNIGPF KPLTFTTRCD VCQDPISPSH SRYHCFTCTS SIEPDTLPGD YDICTNCYAN
LEARDQVSPE NGHAGWRRCL NGHRMIVVGF RDGPGGQLRH ILSDLVGGRN LRITQSEGTD
DQAPQKWWWH EGGQTRERFV TRDVAADAPT TGEGLAQGFP ADGGVGMRAT ATWAWYPKAE
DELLFPKGAE IREIEDVNGD WFFGVYMGAK GLFPSPPIRY SRDNQQLEKS VDRMNQFGSA
VAEVHRLPAA TTPGPVTRAP HLHGR
//
