ID U1GEC7_ENDPU Unreviewed; 1081 AA.
AC U1GEC7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUS_00258 {ECO:0000313|EMBL:ERF70071.1};
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:ERF70071.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
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DR EMBL; KE721353; ERF70071.1; -; Genomic_DNA.
DR RefSeq; XP_007804106.1; XM_007805915.1.
DR AlphaFoldDB; U1GEC7; -.
DR GeneID; 19235321; -.
DR eggNOG; KOG0011; Eukaryota.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_286052_0_0_1; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd14280; UBA1_Rad23_like; 1.
DR CDD; cd14281; UBA2_Rad23_like; 1.
DR CDD; cd01805; Ubl_Rad23; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 1.10.10.540; XPC-binding domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR NCBIfam; TIGR00601; rad23; 1.
DR PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR PANTHER; PTHR10621:SF0; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF101238; XPC-binding domain; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1081
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004611287"
FT DOMAIN 673..744
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 819..859
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1034..1075
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 631..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..781
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 115821 MW; DEE50F52F266B6F9 CRC64;
MKHVGMNLST SVIFHVLLCA FAVAQFPPTP ENVTTIKSRF DEGITISYKE VCAMTLFPWH
SRRVPSNRLS VQPRICETTP GVRSYAGYVT LPPGTVNEIN QNFSISTFFW FFESRKDPSN
APLTIWMNGG PGSSSMIGLL QENGPCFINA DSNSTMLNPW SWNTEVNMLY VDQPVQTGFS
YDTLNNGTYD ATTQQITLSD FTDGIPEQNN TFYTGTFPSI DKYSTTNSTQ NSARAIWYFA
QEWFQEFPAY RPNDSRISIW TESYGGRYGP SFTAYFQQQN EKIANKTITT EGEMYYIRLD
TLGIINGCID LLTQAPSYPE MAYNNTYGIQ VINETVYRQA LDAWSRPQGC RDLILTCRAL
ARDGDPMMYG NNETVNLACR EADEFCSNQV EGPFFYGDRG YYDITHVDPD PFPPPYYEGF
LQQPQVQSAL GTPLNWSQSI DSVYYAFSST GDYPRSDVLG YLEDIAYILE SGIKVALVYG
DSDYACNLIG GEEVSLAINY TDSEHFRAAG YTPIQTNSSY VGGQVRQYDA GHEAPSYQPE
TSYEIFMRAL TNRDIATGTI STADNETYST TGTSSTWQIK NEAPEPPAPT CYVRALLASC
TEDQIAAVVN GTALVQNWIV IDDNTAALSA NTASNGSSSG DLPGSPGGSS TGISSGGAAQ
PTSATSTGDG FELEDLKQQK FTIEAEPSET IAQVKEKISA EKGWDVAQQR LIYSGKVLLD
TNTVESYNIE EKGFLVCMVS KPKPAPAASK TATPSTPSAS TSTPAPPAAP QPNPASTATS
NPPATPSPAG AGAAAATAPP SASPASASFT DPSALLVGQQ GTEVIAQMEA MGFARADIDR
AMRAAYFNPD RAVDYLLNGI PDNVQAEQRQ AAAARANPEG GAGGEGQGAG TSAQTTSSPV
ATGGTAGTTT TDEPVNLFEA AAQAGGRGGA TGGAGAGAGA GARAAAGAGL AGAPANLDFL
RNSPQFQQLR QLVQQQPAML EPVLQQVADG NPQLAQMIGQ NQAQFLQLLS EDIGGEGITG
MGDTGPNTVP ISVTEEERDA IDRLCRLGFP QDQVVQAYFA CDKNEELAAN YLFEQPEEDD
A
//
