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Database: UniProt
Entry: A0A1L9V085_ASPBC
LinkDB: A0A1L9V085_ASPBC
Original site: A0A1L9V085_ASPBC 
ID   A0A1L9V085_ASPBC        Unreviewed;      1291 AA.
AC   A0A1L9V085;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Enhancer of mRNA-decapping protein 3 {ECO:0000256|ARBA:ARBA00015797};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE   AltName: Full=Cyclophilin-60 {ECO:0000256|ARBA:ARBA00030661};
DE   AltName: Full=Cyclophilin-like protein Cyp-60 {ECO:0000256|ARBA:ARBA00030942};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000256|ARBA:ARBA00020592};
DE   AltName: Full=RING-type E3 ubiquitin transferase isomerase-like 2 {ECO:0000256|ARBA:ARBA00033051};
GN   ORFNames=ASPBRDRAFT_50142 {ECO:0000313|EMBL:OJJ77199.1};
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ77199.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC   {ECO:0000313|Proteomes:UP000184499};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- FUNCTION: May catalyze the cis-trans isomerization of proline imidic
CC       peptide bonds in oligopeptides thereby assisting the folding of
CC       proteins. May also function as a chaperone, playing a role in
CC       intracellular transport of proteins. May also have a protein ubiquitin
CC       ligase activity acting as an E3 ubiquitin protein ligase or as a
CC       ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on
CC       proteins. {ECO:0000256|ARBA:ARBA00003697}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
CC   -!- SIMILARITY: Belongs to the EDC3 family.
CC       {ECO:0000256|ARBA:ARBA00006610}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC       subfamily. {ECO:0000256|ARBA:ARBA00007930}.
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DR   EMBL; KV878679; OJJ77199.1; -; Genomic_DNA.
DR   STRING; 767769.A0A1L9V085; -.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_50142; -.
DR   OMA; RLCVNSK; -.
DR   OrthoDB; 1409462at2759; -.
DR   Proteomes; UP000184499; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd01923; cyclophilin_RING; 1.
DR   CDD; cd16663; RING-Ubox_PPIL2; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR025762; DFDF.
DR   InterPro; IPR019050; FDF_dom.
DR   InterPro; IPR026951; PPIL2_U-box_dom.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13612:SF0; ENHANCER OF MRNA-DECAPPING PROTEIN 3; 1.
DR   PANTHER; PTHR13612; UNCHARACTERIZED; 1.
DR   Pfam; PF09532; FDF; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM01199; FDF; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS51512; DFDF; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT   DOMAIN          266..302
FT                   /note="DFDF"
FT                   /evidence="ECO:0000259|PROSITE:PS51512"
FT   DOMAIN          442..667
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   DOMAIN          749..822
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   DOMAIN          1027..1179
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          62..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1151..1170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1196..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1267..1291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..94
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1291 AA;  140427 MW;  481FA277D157ED18 CRC64;
     MAAEFIGYDV LVTLRAPPNA TVQGEVANVI GQRLMLRNVK LSWIAHQLPT YSIEAPDIAD
     LSLGPATPRI TQRPPPPQGP QKTAPAPPPP SSSQNFVDPA ILSFSKPPSA PSGQGAESGP
     AQLPAPSISR STSQNFQFPQ VAHRDQAAVL NEPFSNLEVD VGNSASESRS AVPSGPVPVG
     RENLVSSQPT PQSATKASRR TGQPRTPKAV NEHDGATNTD PRSKGWRQTA FVEPSYPQLN
     KSLNKARRKK KNNRSNYAED PNGWATEDAT DIQEMGEFDF QSNLSKFDKR KVFEEIRNDD
     TTADEDRLVS FNRKVPKPGT NGGKNLHWTE NVLDSPEETE SDTDQVPSDA KLSSGTYSGR
     ERSRTSRAPS SRKGSAILGQ PLVPPQINSL GRSQLSTSRT TSPRPNKTSV SASPISAPGV
     PGGSLRLTTT NRSCPTVSPL QTLEVEQIAV AELGLTEDMI TENTGRGIAE AAVGLLTSDA
     AAPTMLVLTG NHRTGARAVS AARHLRNRGH RVTVCMLGIE HENELLESCR KQLDVFKKIG
     GRVHRWEDLS TRLSTSEFAP DLVVDALFGI HVAFDDLRTD DQATAFEMIS WANRSNLEIL
     SVDVPSGLSA MSGEVTTVEG GRLCVNSKSV VCLGAPKTGV VTALLSGEGL SWNLSVADIG
     IPQIVWRKYG SRRRHGIDFG NRWVVPLRYQ PPPEYPAINA WSIGGKGMIY CDDGAFITHS
     EWASEDAFSA SAGAGVGRSK RGGVDTTFKR LPFNFCSLSL QPFSHPVCTP SGTIFDLTNI
     LPWIKKHGTN PVNGAPLKSS DLIKLHLAKN ESDEYVDPVT YKVFTDNTHI VALRNTGNVF
     AWDTVERLNI KGKMWRDLVT DEEFTRKDII TLQDPQNVES RNLSSFNYLK EGESGLTDEQ
     IREREDPSNN VNVNALGSSA KILKAKEAVA KARAERSQRV GSTATSKELA KSGSAGNAAA
     QSQKTASFQS GKAVPYNAAK HTTGLAAASL TSTGMTPHTS AELALLSDEE YMLKRGRVKQ
     KGYARISTNV GDVNLELHTE YAPKAVWNFI KLAKKGYYRD VTFHRNIKGF MIQGGDPSGT
     GRGGESIWGK YFNDEFEGPL KHDSRGTLSM ANKGKNTNSS QFFIAYRALP HLNNKHTIFG
     HVIDDPTPSS TTLNNLEVHP TNPTTNRPTP DIRIIDVTVF VDPFEEFLKQ KQTEEAKAKG
     QIVNPEEEEQ NARRAEDDRI TWTGKRVRGT GPGAKDEGSG GVGKYLKAAL AERAGQEEDE
     IVEFVDDEPE PEPMRKKFKG GGGFGDFSSW D
//
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