ID A0A1E3PNR9_9ASCO Unreviewed; 399 AA.
AC A0A1E3PNR9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=JAB1/MPN domain-containing protein {ECO:0000313|EMBL:ODQ67061.1};
GN ORFNames=NADFUDRAFT_81676 {ECO:0000313|EMBL:ODQ67061.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ67061.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ67061.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ67061.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M67C family.
CC {ECO:0000256|ARBA:ARBA00010981}.
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DR EMBL; KV454407; ODQ67061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PNR9; -.
DR STRING; 857566.A0A1E3PNR9; -.
DR OrthoDB; 5490729at2759; -.
DR Proteomes; UP000095009; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR InterPro; IPR015063; USP8_dimer.
DR PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR PANTHER; PTHR12947:SF13; FI19924P1; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000095009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 223..351
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
SQ SEQUENCE 399 AA; 44424 MW; F00911F6E7576D8E CRC64;
MLQPRQIKTL VKAATDYDFS TEVSFRSWIH VAATIRQQAE IYRAEGAYEE AYILFYRYAD
LLLNNLPQHP AAKGTKNSEA VRQLVNKNLD DVLGRLEQLK AILLEWIEAD KRAEAERIKS
ERIKTERVSR PTVTPRRPVD DQTREAEYAQ ALASLASLKQ GPVSTSSSQF TIPDVSYPSV
PHVLTPLSPK STGTPTAPIV PTTAKNTEHK ITQYTENGTP LRTTFLPRSL QARFLDLAAS
NTVLNLETCG ILCGKLNRNA FFITHLVIPA QTSTANTCTT QDEEVMFGYI DSLDLFILGW
IHTHPTQSCF MSSVDLHTHS AYQIMLPEAI AVVCAPQHEP SVGVFRLTDP PGMDIIKECK
EGAGGKFHLH EETGLYASAY NPGHVKLLDH IDVVTKDLR
//
