ID E2B4N5_HARSA Unreviewed; 509 AA.
AC E2B4N5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=EAI_07634 {ECO:0000313|EMBL:EFN89316.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN89316.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN89316.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL445584; EFN89316.1; -; Genomic_DNA.
DR RefSeq; XP_011143109.1; XM_011144807.2.
DR AlphaFoldDB; E2B4N5; -.
DR STRING; 610380.E2B4N5; -.
DR MEROPS; C19.972; -.
DR EnsemblMetazoa; XM_011144807.3; XP_011143109.1; LOC105185371.
DR GeneID; 105185371; -.
DR KEGG; hst:105185371; -.
DR InParanoid; E2B4N5; -.
DR OMA; NKFVAER; -.
DR OrthoDB; 719409at2759; -.
DR PhylomeDB; E2B4N5; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
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; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 41..138
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 163..493
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 509 AA; 59137 MW; 654275BACEF0BE90 CRC64;
MASDKQSILR KRKLVNVGSD SDNEAEKNGK HVTRTKSEAP RLCPYLDTIN RQFLDFDFEK
LCSVSLSRIN VYACLVCGKY FQGRGSNTHA YTHSVADTHH VFLNLHTLKF YCLPDNYEIV
DSSLDDIKYV LNPTFDKTQI AQLDKSDKQS RAIDGSMYSP GIVGMNNIKA NDYCNVILQA
LSHVTPLRDF FLRESNYSHV KRPPGDSSYL LVQRFGELMR KLWNPRNFKA HVSPHEMLQA
VVLWSKKRFQ FTEQGDPVDF LSWFLNALHL ALNGTKKRDS SIIYKTFLGH MRIYTRKIPP
LELEESQRSE LLHTVEYGET VTESPFLYLT CDLPPPPLFK DQFTENIIPQ VNLYTLLNKF
NAVTEKEYKT YKENFMKRFE ITELPPYLIL YIKRFTKNTF FVEKNPTIVN FPVKNVDFGD
ILTPEVKAKH PYTTYDLVAN IVHDGEPGQG TYRVHILHRA TGQWYELQDL HVTQILPQMI
TLTEAYIQIY ELRKDTHMEN GDNKNKKTT
//
