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Database: UniProt
Entry: Q4WIB1_ASPFU
LinkDB: Q4WIB1_ASPFU
Original site: Q4WIB1_ASPFU 
ID   Q4WIB1_ASPFU            Unreviewed;       857 AA.
AC   Q4WIB1;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=PA and RING finger domain protein {ECO:0000313|EMBL:EAL87344.1};
GN   ORFNames=AFUA_2G02470 {ECO:0000313|EMBL:EAL87344.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL87344.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL87344.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:EAL87344.1}.
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DR   EMBL; AAHF01000008; EAL87344.1; -; Genomic_DNA.
DR   RefSeq; XP_749382.1; XM_744289.1.
DR   AlphaFoldDB; Q4WIB1; -.
DR   STRING; 330879.Q4WIB1; -.
DR   EnsemblFungi; EAL87344; EAL87344; AFUA_2G02470.
DR   GeneID; 3506732; -.
DR   KEGG; afm:AFUA_2G02470; -.
DR   VEuPathDB; FungiDB:Afu2g02470; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_007230_0_0_1; -.
DR   InParanoid; Q4WIB1; -.
DR   OMA; SGNIDWV; -.
DR   OrthoDB; 206729at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..857
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004246242"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          709..752
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          106..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  91708 MW;  DC3812B29D3ECC3F CRC64;
     MRPPRLVSIV FCILFFPIFL TLFSALSSSP RVADPSSLAG QTTGFHAFFS FNIPSSLFPP
     SAIISLTDDN STFFLARPAA FGPLLSDKGL SGPLWVGSGF GEKTSGGAEG ELGCSDIPGW
     GDGDSRRSPD KSTIAADKTS SSGIRDGLAA SLGQHRADPQ QESDSEHLAA GVASPPSTND
     GTDDHLHHPL PDSDVVDAGA PEKPRERQNK PAAHADIQSL QESAEIDGKV VLLSRGGCGF
     LEKVKWAQRR GAIAVIVGDD TRGGSLVTMY ARGDTSNVTI PAVFTSYTTA HLLSSLMPPQ
     AGAESSLDEK AASSRTVVSS GPDKQRLSPT TTTSVTPSST PTTQAAVDEQ LQTAPRPKTG
     FFHSLLSLLG LGRSNNGHAL QKFEDSRRPP NSGNIDWVRL GDKQQSNKPH NSAAHDRKES
     ESVSSLADGD GFIIGVQDWR DPDLVPARTI SLPSPSSVAS SAKTESGNSA KSQKKTSNSP
     KGGSITPGSG EYRSVDRSSD NKEVPSRDGS PVNSAGNAGS DKGWFFKRFF APRRTEGANL
     YKPANNKMRR NTDQNAKVTE HEGLWVTLTP TSMSTSPFFD TLLVLVVSPL LTLTVVYALL
     LIRSRIRRRR WRAPKSIVER LPVRTYHTIP TPSSAASSSR SSSPGPVSPT SPLLGSRSRP
     ELAPSRSSFL RSGTAEAKKT RNMDSAKGEK SGSASSVWRR KYTGRQVECV VCLEEYIDGQ
     SRVMSLPCGH EFHAECITPW LTTRRRTCPI CKGDVVRSMA QNTTAESRDS SQRMVDGDDH
     HGFESHRSVS SAPMLIANPG EEETSAPEHY GASDLGPLQG HASSAPPSSS WRNMASLSLS
     ALSGDTIWHQ TQPDNDR
//
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