ID A0A2B7XMP5_9EURO Unreviewed; 894 AA.
AC A0A2B7XMP5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=AJ79_05595 {ECO:0000313|EMBL:PGH09868.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH09868.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH09868.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH09868.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH09868.1}.
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; PDNB01000090; PGH09868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XMP5; -.
DR STRING; 1447875.A0A2B7XMP5; -.
DR OrthoDB; 206729at2759; -.
DR Proteomes; UP000223968; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd04813; PA_1; 1.
DR CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22765; RING FINGER AND PROTEASE ASSOCIATED DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22765:SF483; RING FINGER PROTEIN MUG145; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000223968};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..894
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012202870"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 744..787
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 119..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 95839 MW; 7D57FB7150125EF5 CRC64;
MRPPRLILLL ACFIFLPILL TTLSLLSAHP QHGQTSQASS VSGGVGRFKT LFSFHAPSSL
FPPSAMISLT DDNSTFFLAR PAAFGPALPS TGLSGQLWIG SGFGDDALRK GGLTTGAEGE
LGCSDVPGWE DSGKSQNKEA GSSHTSERLS AGMKAKNGPD NNVEALHKRG DERSLDLPRP
GGKENHPTKD DGTDDHLHHP LPESGSPATP NADKNKQLAH ADIQSLQESA EIRGKIVLLS
RGGCGFLEKV KWTQRRGGIA LIVGDHTRGG GLVTMYARGD TSNVTIPALF TSHTTAHLLS
SLIPPEVPSE PSSPEDLSKS ASGDKADKNP KNGKPAAATK AASKPTSTAA SPAAPPRKGF
LHSLFSAIGL WRENAYPWHL QEDSHRPPSS GNIDWVMLNE FDEEETPSPK KPAQSNKAKE
GGKSPSSQDS ESRQGSNDDF VIGVQDWRDP DLVVAGNNDN SPKPTSKPET STSKQKGDDA
KGRAGDNNPN PSGNGLKGGS ITPGSGEYAP QDKSTNGKGT GRDSNRPSAA SDSRSGNSRE
NSHWWFGLGG TDDDESSRSV EDKSKGQSDK KAKEATAPVH KSSKEGSKHP DHEGLWVTLT
PTSMSTSPFF DTLLVLVVSP LITLTVVYAL LLLRSRIRRR RWRAPKAVVD RLPVRTYHTI
TSMSSSSGSP QAGPSPEASS PSSPLLSHPR ARSPRPRQRS QTTSGIVAAS SHDASNESPS
NGAEKSNAGS SLWRRRYTGR QVECVVCLEE YIDGQSRVMS LPCGHEFHAE CITPWLTTRR
RTCPICKGDV VRSMGHRSSS SHRSERPERM SDDIQARIAE TRNDSPSAAI PLSQVPDDID
SDLERGDSTT SLVNNSQNSN TQSNWRNLAS LSISALSGDA MWHQPRSPRS DRNR
//
