ID A0A0D2BP70_9EURO Unreviewed; 867 AA.
AC A0A0D2BP70;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_06725 {ECO:0000313|EMBL:KIW54361.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54361.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW54361.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54361.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847320; KIW54361.1; -; Genomic_DNA.
DR RefSeq; XP_013314945.1; XM_013459491.1.
DR AlphaFoldDB; A0A0D2BP70; -.
DR STRING; 348802.A0A0D2BP70; -.
DR GeneID; 25328633; -.
DR HOGENOM; CLU_330652_0_0_1; -.
DR OrthoDB; 1404660at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24096:SF265; ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G14270)-RELATED; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 582..671
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 771..796
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 802..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 96093 MW; EDFB1AC983183EEE CRC64;
MSLSTDSSTG HFWTSSKSLS GAAEEILTTD VLTFTFANLS RYDNDKPIFI DAKNPSHFVS
ASQASEIVAR LVKGFERIGI KEGDCVCLHA YNNIWYPLIW LAIIGSKAIA SPINPAYTST
ELDRHLNLTN PKFIFTQPTC IEPIIQAASK CSIPTSRIFF IGGLHDAPLC GCRNWQTLLV
EGGKDTLGPS FEHGRSLQDR VAVYAMTSGT TGLPKAAMIP HRYIVAQAAA LEDQFKARSY
QPSQLICLPV FHAFASPLAL VLPLRLGVPT YFLPKFNLPD FLQAVHKFNI TDSPVVPPIV
GTLAHLSGGE GQQLRSLRYV ICAGATLNSR AQTRLSERLH PEANVAQCWG TTEAGWHTLF
DWNEKDTSGS VGRLLPNVDI KLLDDKQNNI KSEDEVGEAL IRSAGMFHRY VGDHQASSEA
FDRDGFYRTG DFAFVRDGKV FYTGRRKEIM KVNGWQVSPI EVETVLLEDP RIADAAVYGV
SCDNGQGIWQ TTLCAYVVRN FLESVNANDR LSDEPNEEAV HKLSEEDVKK FVASKLISYK
HLKRVSFKES VSSNRVTLAS FVDRCKSTRS QEMAGTQPDI AVQIIVPNDT NPSAAPLLSA
ERRITPSWTI SQLKSKLEPV TGIPASAQSL RTRSLNGTFV HLSDESSLVG DAHYGLHRGS
EIEIIDTRPA GARQTFNFAD LSSVEKYQMP ESQYEKLDDS VLAWKKRAKL GRFDPSSQKS
KPVSEMAEER RRADKEVIER RGIEVGMRCR VGRDDMRRGV VRFVGEIDGL GGARESGCVW
VGVELDEPVG RNDGSVLVEI AADDADDDDD EKEEGKGERV GKKEKMVRVF ECRDKFGVFV
RPEKVEVGEQ WTMLGLDDLG DEDMEEV
//
