ID E5R067_ARTGP Unreviewed; 867 AA.
AC E5R067;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=PA domain-containing protein {ECO:0000313|EMBL:EFQ97478.1};
GN ORFNames=MGYG_00518 {ECO:0000313|EMBL:EFQ97478.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; DS989822; EFQ97478.1; -; Genomic_DNA.
DR RefSeq; XP_003176430.1; XM_003176382.1.
DR AlphaFoldDB; E5R067; -.
DR STRING; 535722.E5R067; -.
DR GeneID; 10031747; -.
DR VEuPathDB; FungiDB:MGYG_00518; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_007230_0_0_1; -.
DR InParanoid; E5R067; -.
DR OMA; SGNIDWV; -.
DR OrthoDB; 206729at2759; -.
DR Proteomes; UP000002669; 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:UP000002669};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..867
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003197796"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 722..765
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 117..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 92809 MW; C0948FC5B45FC0C5 CRC64;
MRPPQLILLL VCLVFVPLFI TTVVRQTASP ENAATSEYRR SYSSKAGRLR DLFFHAPSSL
FPPSALISLT DDNSTFFLAR PAAFGPPLPS SGLDGQLWIG SGFGDDVSKK GGITTKAEGE
LGCSDVPGWQ EGDRTAQSGS GGRLGTDKTT TQVKPGIRVG EDPAINIQKG TNTVSPEDNL
KNSGSPTKND GTDDHLHRSL GDSLSPSFND AKGKNKQPTH ADIQSLQESA EISGKIVLLS
RGGCGFLEKT KWVQRRGGIA LIVGDNESGG GLVTMYAHGD TSNVTIPAVF TSHTTAHLLS
SLIPSDKGQG PNSPGNKLKA PNSGNQNKKT SSSVGKTSIV APPSKSTKPT QSKAKDTPSS
DGGFFSSIFS FWNDKSVHED SSRPPSSGNI DWISQNRKPD SQTPPKPGQG SNRQDKEKGT
APVQAKPDPH QNREDDFVIG VQDWRDPDLI VKPTTTTTSK PQPTSQNGNS NSKDGSGTDT
KGFKGGSITP GSGEYAHQDK FTQVKGGSNG SHKQSLNSQS GSGNTGKKGH WWTRIFGWGE
ASDDKNTAFS NGHIGIQNGR GSHNDHGHHG DKEPEKHEGL WVTLAPTSMS TSPFFDTLLV
LVVSPLITLT VVYALLLLRS RIRRRRWRAP KAIVDQLPVR TYHTITSSSN SSTPPRTAVP
DSASPSSPLL ARSESRAQFS TNAGAAASSS LPNMMGFSGS AEKSNAGSTL WRRKYTGRQV
ECVVCLEEYV DGQSKVMSLP CGHEFHAECI TPWLTTRRRT CPICKGDVVR SLGNQGPNDY
GSASLDPSPS FDQARAVEDH SGFPSSAIPI PEHENADSEL ERGALLGDAL NASHRSTWRG
LTSLSLSALS GDSMWHQVRH TRSQRNR
//
