ID A0A1V6TTS2_9EURO Unreviewed; 923 AA.
AC A0A1V6TTS2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c004G03897 {ECO:0000313|EMBL:OQE29290.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE29290.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE29290.1}.
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DR EMBL; MLQL01000004; OQE29290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TTS2; -.
DR STRING; 254877.A0A1V6TTS2; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR000433; Znf_ZZ.
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; SM00326; SH3; 1.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF50044; SH3-domain; 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:UP000191342};
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 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..63
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 859..920
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 100..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 103303 MW; 422FFFD98E8509EC CRC64;
MSHQSSGLAD LEKELICTEL LYQPLTLLDC LHTFCGSCVK EWFSAQGSRR SRTSPRFTCP
SCRTEVRDTR PNATVTTLLD MVLSAHPDRD RATDEKAEIA TRYTHGESVF PTLPSGGESA
EEDGEDDRRI IEEARELSLR ESRAQARREG RRMGQTSRTR ERSTHTERPE DGRSRRRRDD
DTTRQRTLRP DDSDHTRRVE HQSSLRSLLS LSSDAETMEE EILRQILEDG LLDNINLDNL
GPRQEEELSE RIAEAYRRRH MRRPQTRQRQ ELGREQRQEA DRATRTHTRS ESAHRTAEPT
AATREHNVRR PPVSRPHLLD SAPTRPSTAG HQRRNSEQVD GRRRTSPVRT NQASASDEAI
RPAARSSSDI TADRHLTQAG RVRSESSSAR PRRATESEQN ISRTWVAGGR ERSSSRQTAS
QSATNSPTSG SVPSSSSRRS TPTDHTLPSL SSPLVPVRSD RRTRPSSSRS NVPASPTVQF
PEPSISCDRC GKNNIQYDLH KKCTICKEGN FHLCLRCYRS GRGCLRWNGF GASAHTTFQR
IISSSSRRPI HINDPGHVLV WLKYQRPSET AHRTMSGERQ LTSDNPVRRL QSGLFCDTCQ
SSANDCFWEC SQCNEGDWGF CNSCVNRGRC CTHALLPIRR ITHSPHPSAP SITPPPAGSN
TLPTSSEVET FKILSFSTNC DICTYPIPAS NTRYHCLECN GGDYDVCTNC YLKLVATGKI
NKENGHNGWR RCLAGHRMIV VGFEDHEEGQ RRVIVRDLVG GRALKDEHVA QSHLQSPTSS
PTTGGPVASP ELGTGDWSWK DGPERRKKAS RLRGGPVPTI STTGSTVFAS DPSNPSHTSA
TTTPIQGIPP FRRFPPDGGV GLVVHALWSW YPEAEVEDEL VFPRGAHITE AENINDDWFW
GCYAGRTGLF PGSHVEFVRE VLR
//
