ID A0A2H3IGG5_9EURO Unreviewed; 1064 AA.
AC A0A2H3IGG5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ubiquitin supergroup {ECO:0000313|EMBL:PCH01645.1};
GN ORFNames=PENO1_042160 {ECO:0000313|EMBL:PCH01645.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH01645.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH01645.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH01645.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the LIMR family.
CC {ECO:0000256|ARBA:ARBA00010487}.
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:PCH01645.1}.
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DR EMBL; NPFK01000097; PCH01645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IGG5; -.
DR STRING; 290292.A0A2H3IGG5; -.
DR OrthoDB; 2731916at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 1.20.58.120; BAG domain; 1.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR21355:SF0; G-PROTEIN COUPLED RECEPTOR-ASSOCIATED PROTEIN LMBRD2; 1.
DR PANTHER; PTHR21355; UNCHARACTERIZED; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF04791; LMBR1; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF63491; BAG domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 823..879
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 1004..1060
FT /note="BAG"
FT /evidence="ECO:0000259|PROSITE:PS51035"
FT REGION 463..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..118
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 878..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 116380 MW; 2B7B57383D4D910B CRC64;
MYSLRSNARY QLTVLCCGIV GLIYISIQNG FDFTSIKSLV MALAYVWGLI LAIYLMGHGL
VSIPRSFFRK ASTADALRRI QAHAPKIHDR LTDAITELEE VEAQVAQLQK RKTGTARMFE
DWIEELADYT NIPDSRPAAL HSLAEPTAVP AVITERYLAG LSRRLQRARH QKARFVDEWD
RIVRSAADYQ TILNSTASKK LDFGPVGGSE AGSSTRRAGL ITPYMRYVIY VHVLPGLRLV
MGAVFAAASL CVVWSEVVKA LAPKLCLISL SLVPNPDKAQ IGLGGQLIAS MWLLYMCTAA
LKGVNDAQVW GNRALVRRNT YGESACWYAG QVAKLTVPLA YNFLTFLPSE LRHDTIFYQF
LGKYINLTPL GKGFDYFPVF VLLPVCATMF NLYGRIKKVF GFGFVDDEDP EADPGGFGTG
GWREGRALIE RELVGLGSLG LTSRSVDAGR TAGLASSSSS TSLNISRAAS PQPGWSSSST
VPRTSSRAPL IGTSSSANAI TATTIIDDGV AEEENFFQSF AHRVRNTIDT ASTPRWLQGG
FSNISTPRWL NSDREDSGAN NGSTQGGNKI FGGLFGQRSS DGHTPPGQNF CHVIRFLNWR
LLQLKIPLPA SSSLLILLFL TQLRFPFFLF HFLLTLYDNG AEASMTLLPD WPVTLSSLGE
ASISYPQQVI RRLSSLTLGS SSFLGTTSKG KDNLSLFIHN LLANATSPLS IAALSLTAIL
GILTIVAMSW RDTFGFFRRA SSYGHNAPAA PPQVSDSDYS YLTNDDIVEP RSYQQSHHDG
RRVVRRDVNH LEDESPDILL LKHRGVTYPL HFTPYAIDDG DLTIGEVRRL AAEKTGTADV
KRIRILYKGK LLRDDAKPCK DEGLRQNSEV MCVVSEVRPG ESTSSLSGSE GGSRSEALSL
DSRSNQSPPA GGGGGKKKGN KKKKKKQQYL SPEPTIAEAR PTPSKDNLAP PSDVRPTSAG
RSSAAPSPAP SLQQFATPIE RVDALLRYLR TELTPLCEKH FSHPPTDPKA RSYEHKLLNE
TILSQVILKA DSIDSEDARP ARRALIKEAQ GLLNKLDALP PQSP
//
