ID A0A0F0I122_ASPPU Unreviewed; 875 AA.
AC A0A0F0I122;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=PA1 like protein {ECO:0000313|EMBL:KJK60342.1};
GN ORFNames=P875_00053456 {ECO:0000313|EMBL:KJK60342.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK60342.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK60342.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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:KJK60342.1}.
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; JZEE01000744; KJK60342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I122; -.
DR STRING; 1403190.A0A0F0I122; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
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 604..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 729..772
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 135..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 94241 MW; A23B82C7D4F714F1 CRC64;
MRPPRLIFLV FCFIFFPIFL TLFSVLTSSS RVTTPSSFAG RATGLHALLS FNIPSSLFPP
SAIISLTDDN STFFLARPAA FGPLLPDKGL SGQLWIGSGF GDRTTAGAEG ELGCSDIPGW
GEGDSHRQDI PAASDALLGK PVPGGADPAT SNIHRTDSKP DIDSQASPND GVVTPSTNDG
TDDHLHHPLP ESKVAESGVS EQRGDNHQNR QTEHADIQSL QETAEISGKV VLLSRGGCGF
LEKVKWVQRR GGIALIVGDD TRGGSLITMY ARGDTSNVTI PALFTSYTTA HLLSSLVPPQ
AGGDSGVDDA SGPRHTKLSG QSTTGNQEIV PSTTSAAAVS PTSTRYAASP GGKSTTATRK
AGFIQSLVSL LGIERNSGRL PEDSQRPPSS GNIDWVLKDP WDDMEVSEDG TDRVHNRAKA
DSGAGDRKKP DVSSQEADGD GFVIGVQDWR DPDLLVPISS SIPVPSSVPE SDARKTQTTG
KGSRPTGASL KGGSITPGSG EYRTLDKSKT SKAELHSSNH KSVASDTQGY PKQSKGWFAR
HFSWTKRGEK DSSRPVRRDH VEDRKLHGAS TFQGLQNTGQ LEHEGLWVTL TPTSMSTSPF
FDTLLILVVS PLLTLTAVYA LLLLRSRIRR RRWRAPKSLV DRLPVRTYHT INTSSSSTSS
SSRSSSPGPV SPTSPLLGSR NRSGYRRAQE TPEATVDLKS PKMKSSKKEK AGSSSALWRR
KYTGRQVECV VCLEEYVDGQ SRVMSLPCGH EFHAECITPW LTTRRRTCPI CKGDVVRSMS
QNKAAETRES AESIDHTYPH ELDSHPNASS APVPITNNGE DEVSDLERRG GSDVGLLERH
SSSAPPPNWR NFAALSFSAL SGDTIWHQGR TDRER
//
