ID F0U703_AJEC8 Unreviewed; 892 AA.
AC F0U703;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=PA domain-containing protein {ECO:0000313|EMBL:EGC42374.1};
GN ORFNames=HCEG_01736 {ECO:0000313|EMBL:EGC42374.1}, I7I53_06492
GN {ECO:0000313|EMBL:QSS51226.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|EMBL:EGC42374.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|EMBL:EGC42374.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QSS51226.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:QSS51226.1};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS990636; EGC42374.1; -; Genomic_DNA.
DR EMBL; CP069103; QSS51226.1; -; Genomic_DNA.
DR AlphaFoldDB; F0U703; -.
DR STRING; 544711.F0U703; -.
DR VEuPathDB; FungiDB:I7I53_06492; -.
DR HOGENOM; CLU_007230_0_0_1; -.
DR OMA; SGNIDWV; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR Proteomes; UP000663419; Chromosome 2.
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:UP000008142};
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 TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 741..784
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 118..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 95908 MW; 081FF33A8EB8EE05 CRC64;
MRPPRLILLL ACFIFLPIFL TILSLLFSHP QHGSASQSSV SGGAGRLRAL FSFHAPSSLF
PPSAMISLTD DNSTFFLARP AAFGPTLPSS GLSGQLWIGS GFGDDVLRKG GVSTGAEGEL
GCSDVPGWED NDKNQNHDVG SGQGTAKLTS GIKKKNTANK PVKALNERRD EHSSDLVGFS
DQTNRPSKED GTDDHLHHPL PASGPPGLPS AAKGKEPAHA DIQSLQESAE IRGKIVLLSR
GGCGFLEKAK WAQRRGGIAL VVGDDTRGGG LVTMYARGDT SNITIPAIFT SHTTAHLLSS
LIPSEAQSEP SSVQDQSKAT FVGKPANIEN SRKSATATRV ATQPTKMADS TSYPPSKGFF
QSLFSAIGLG HDKASPWQLQ EDSRRPPSSG NIDWVMQNEF DDEETSPKSR KPTPNNMRKE
NGDDISLESH QGGSDDFVIG VQDWRDPDLV THPKTNNPPQ TTLKPKSSSV KQKDDQAGVL
GGDNTNGPGG SGLKGGSITP GSGEYSSQDK SAVDKGTGRD PSTPPGAADS RYGNSKQDSH
WWSGWGKTSD DDQISTSSND RDKGQQNMNV KETSTPLQRS SKERGKHPEH EGLWVTLTPT
SMSTSPFFDT LLVLVVSPLI TLTVVYALLL LRSRIRRRRW RAPKAVVDRL PVRTYHSIPS
GSPSSTSSQT ATSPEASSAS SPLLSHSRAR SPRPRPRSQT TAGIVASSSH DATNSSSTNA
EKSNSDSSLW RRRYTGRQVE CVVCLEEYID GQSRVMSLPC GHEFHAECIT PWLTTRRRTC
PICKGDVVRS MGGPSSSDQT LEGPERMSED IQARIAETRN DSPSAAVPIS NVSGFINSDL
ERGDDSRVSL LSRSEAPNPQ SSWRNLASLS ISALNGDSVW HQSRSPRSDR NR
//
