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
//