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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//