ID A0A0W4ZTU2_PNEJ7 Unreviewed; 785 AA.
AC A0A0W4ZTU2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=T551_01024 {ECO:0000313|EMBL:KTW31763.1};
OS Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW31763.1, ECO:0000313|Proteomes:UP000053447};
RN [1] {ECO:0000313|Proteomes:UP000053447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTW31763.1}.
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DR EMBL; LFWA01000004; KTW31763.1; -; Genomic_DNA.
DR RefSeq; XP_018230455.1; XM_018373287.1.
DR AlphaFoldDB; A0A0W4ZTU2; -.
DR STRING; 1408657.A0A0W4ZTU2; -.
DR GeneID; 28939542; -.
DR VEuPathDB; FungiDB:T551_01024; -.
DR eggNOG; KOG1102; Eukaryota.
DR eggNOG; KOG1873; Eukaryota.
DR OrthoDB; 1385257at2759; -.
DR Proteomes; UP000053447; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053447};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 26..143
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 171..781
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 785 AA; 88967 MW; 53A06EA11CEF7992 CRC64;
MGKSNKYNTR IHSKCSLATT LHQNTLHQKP INSCIHQEVS IDFDKICRSL RFERKEKICS
MCRKDRSKKN VNNISLCLHC GGVFCISFGR SHAFEHTLQE SMHCLFISIE NAVIWCLSCK
NILSPQESMI LGMKEVQKLV QRKFCIYQKV KNEKKITKDN RCSLEYKSLV PGLQNLGNTC
YFNSVMQVLA ASLPLHDIVS PTPLFNRFCI QIKGTGSLIT AFVEYLNAVY SCTSENTIFK
PQKLFSQIQK KHKQFTPSKQ QDAHELLRYF LDSLNMEETS NTSNRNTFEK LSKSKQKTFE
KNDVSLISDI KVENLNGNNN DTQNKNITFI DKLFGGRLAS IVICNTCKSV STSYEKFQDI
SLSIKTHNAT DIACDTKVNS KRIGSKKTRK KKGSSDNLLF NCSKTSCSHL NGCSESVSDD
ESSTPTTGSE NMSKTCLHFK ELSVDSFEKD GLSSCKNASI ASEITTKTES EYIDLLLFER
NNIDEEKKDS WNLEDSLRQF TSVEILENEN GYACEECAKR LRSTAKKCIY KPSQALRRSF
RLSNTKSSKS HIDSFLTNGS SELFLSSSSF SDLCSQPSES HLPVLHISSH EHQHSFCMSP
GVCSTNTPSY LDYEYSSSDS SKPRSVLSSA FRRFLIDLPL PPILILHLKR FQQLIGRLRS
SFKKIDTFVD FPETLDLTDY VTPRLRSGPG LLYMLTGVIV HIGTLTHGHY ASYILTHKIR
PLNEPLSTTL IDSNLSDSLS SIKTSQTPLR QWVFANDTLT RPATWDEVRR SVGYLFVYEQ
IYDVS
//
