ID A0A5A7RHF2_STRAF Unreviewed; 793 AA.
AC A0A5A7RHF2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN ORFNames=STAS_34263 {ECO:0000313|EMBL:GER56538.1};
OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER56538.1, ECO:0000313|Proteomes:UP000325081};
RN [1] {ECO:0000313|Proteomes:UP000325081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081};
RX PubMed=31522940; DOI=10.1016/j.cub.2019.07.086;
RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L.,
RA Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P.,
RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S.,
RA Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C.,
RA Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T.,
RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I.,
RA Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D.,
RA Shirasu K.;
RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of
RT Plant Parasitism.";
RL Curr. Biol. 29:3041-3052.e4(2019).
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 ECO:0000256|PIRNR:PIRNR016308};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308}.
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:GER56538.1}.
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DR EMBL; BKCP01012736; GER56538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A7RHF2; -.
DR Proteomes; UP000325081; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02658; Peptidase_C19B; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
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|PIRNR:PIRNR016308, ECO:0000313|EMBL:GER56538.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308}; Protease {ECO:0000256|PIRNR:PIRNR016308};
KW Reference proteome {ECO:0000313|Proteomes:UP000325081};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 156..266
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 308..791
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 607..648
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 667..707
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 753
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 793 AA; 88983 MW; 021E3855BDC79D5C CRC64;
MELLRSNLFR VRIPEPSNRI YKEECCISFD TPKSEGGLYV DMNSFLAFGK EFVGWNYEKT
GNTVYLHIKE TRKPVSEDRP SKKPTLLAIG VEGGFDNNEP EYEKNYEVVI LPDYVTLPFP
SVELPEKVRL AVDAVIMNVA AEKKEQVAAW TADTKIISKH AMELKQLDNG VIVPRSGWKC
EKCDKTDNLW LNLTDGSILC GRRNWDGSGG NDHAVNHYNV TKFPLAVKLG TITADIEAAD
VYSYDEDASV VDPLLAQHLQ HFGIDFSSLQ KTEMTTAERE LDHNTNFDWN RIQESGEDIE
PLFGPGYTGL VNLGNRLCSL HVDFVLGRYY LDQNLKSAFD AAPADPTVDL NAQLTKLAHG
LLSGKYSVPA MKLDNTGDAP QATLIAKQEG IPPRMFKSVI AAKHPEFSTM RQQDALEFFL
HLIDHVERVN TGNPMLDPSR SFKFGIEERL QCPSGKVAYN RRYDYILSLN IPLHKATNKR
ELEDFRKLKA ERDARGEELT SKEIVRPRVP LMDCLELFST PEELHDFYSS ALNSKTTAIK
TAGLTSFPDY LVLHMRKFVL EEGWVPKKLD VYIDVPDTID ISHMRSKGLQ PWEELLPESA
PEDSGISANE DIVQQLVAMG FQYNHCRKAA VSTSNSGLEE AMNWLLSHMN DPDIDEPITK
AQNSAPYVDP SKVETLVSFG FEEDVARKAL QASDGDIEKA TEWIFNPPSG ISSMDATPSN
SGNVAEAPLP DGEGRYRLIG LVSHIGTSTH CGHYVAHIYK DGRWVIFNDE KVALSKNPPL
DMGYLYFFER IDG
//