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Database: UniProt
Entry: U1HRX0_ENDPU
LinkDB: U1HRX0_ENDPU
Original site: U1HRX0_ENDPU 
ID   U1HRX0_ENDPU            Unreviewed;      1219 AA.
AC   U1HRX0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
GN   ORFNames=EPUS_03097 {ECO:0000313|EMBL:ERF73265.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73265.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
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; KE720961; ERF73265.1; -; Genomic_DNA.
DR   RefSeq; XP_007801038.1; XM_007802847.1.
DR   AlphaFoldDB; U1HRX0; -.
DR   MEROPS; M67.A14; -.
DR   GeneID; 19238145; -.
DR   eggNOG; KOG2880; Eukaryota.
DR   eggNOG; KOG3822; Eukaryota.
DR   HOGENOM; CLU_268845_0_0_1; -.
DR   OrthoDB; 177109at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0008410; F:CoA-transferase activity; IEA:InterPro.
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; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR   InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR004164; CoA_transf_AS.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR   InterPro; IPR015063; USP8_dimer.
DR   NCBIfam; TIGR02429; pcaI_scoA_fam; 1.
DR   NCBIfam; TIGR02428; pcaJ_scoB_fam; 1.
DR   PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR   PANTHER; PTHR13707:SF23; SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE; 1.
DR   Pfam; PF01144; CoA_trans; 2.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   SMART; SM00882; CoA_trans; 2.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
DR   SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR   PROSITE; PS01274; COA_TRANSF_2; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          1008..1137
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          837..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1122..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1153
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1219 AA;  134541 MW;  BC73EE647026E335 CRC64;
     MVLRTQTCQR LARNLSRKPS DVRQEPPSTA RNENKWLTLL TSIQAQNFRV RNFSSTLGRN
     EINKILPTAA EAIRDMKSNA TLLAGGFGLC GVPDTLINQV HSTPSITGLT AVSNNAGVEG
     AGLGLLLASK QIKRMIASYV GENKTLERMY LSGELEMELT PQGTLAERCR AGGAGIPAFY
     TPAAFGTVVQ TGDLPLRHNP DGTVAQYSQP RDVKVFDGKS YVMEESIKGD YAFVKAWKAD
     KLGNCQFRFA AANFNGAMGR NAKMTIVEAE NIVEVGEIDP AAVHLPGIYV KRVIQSTAKK
     NIEKYTFAKE EGADMSALGK GDTASKRERI VKRAAKEFQN GMYANLGIGM PMLAPSFVDP
     LVEVQLQSEN GILGLGPYPK KGEEDADLIN AGKETVTLLP GASCFGSDES FGMIRAGRIE
     LTMLGAMQVS ARGDLANWML PGKIKGFGGA MDLVSNPSKT RVVVTMEHTD KKGRPKILKQ
     CEFPLTGRAC VSRIITELCV FDVDFTNGLT LIELADGVTV DEVKAKTEAP FNVADDQRSM
     AFAFGSIDGE AQRLGVGLGE KHSTTILIVD ISSPKTFELL RNFDESGSAS YSSPTEFNKI
     GAWMTRSGPN KPHTFLDLFQ APLITTSRIL IMTFTTINSD SLGVVADRKR KASERHAQFD
     LRRPTLGGSS RLAARPHNVE QITKAAQTYE YSGLVPLRYW LRTAATMLKE AEIYEREGDD
     EQAYLLLFRH AHLVLTNLAV HPDAPASELL KEAKKDVQHN LEKLDKLNPR IKKRYERFQE
     MLSEREARRL ALLEAEQSEV EGDAISFQGA LESDNVHHLE GGENRELAVQ LARHEMSRRA
     TERKATRQAG ISQGEERVAR AGRAGRVWEI ADNREPDDLS RRLQEVRAQV ERPGREVGQP
     SQRKDTDKTY AYPHIPLNHA MPKPEPVIPF KTVQAPDLPP KSSLRSNISA PPLPEKLSAA
     ITDHSPPYEP SPIVPAKHQN QQQTHPLKAT YTFKPSAYLE NGNPLRTLFL PPTLRYSFLA
     LARANTERNL ETCAFLAGTL LSNALFVSKL IFPRQTATSD TCEMTHESDL FDYIDSFEDL
     MILGWIHTHP RQTCFMSSRD LHTHAGYQMM LPESVAVVCA PSQRPSRPSA SGAIGGFGHH
     HHPHHHHHHH HHHHDDDGDR AGDWGVFRLT DPPGKGVILA CEKPGVFHPH DCANIYTDAL
     RPGHVVEASG LEFEVVDLR
//
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