ID A0A151NTG9_ALLMI Unreviewed; 824 AA.
AC A0A151NTG9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP45 {ECO:0000313|EMBL:KYO40043.1};
GN ORFNames=Y1Q_0006576 {ECO:0000313|EMBL:KYO40043.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO40043.1};
RN [1] {ECO:0000313|EMBL:KYO40043.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO40043.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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|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:KYO40043.1}.
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DR EMBL; AKHW03002098; KYO40043.1; -; Genomic_DNA.
DR RefSeq; XP_019341927.1; XM_019486382.1.
DR RefSeq; XP_019341928.1; XM_019486383.1.
DR AlphaFoldDB; A0A151NTG9; -.
DR STRING; 8496.A0A151NTG9; -.
DR GeneID; 102560115; -.
DR KEGG; amj:102560115; -.
DR CTD; 85015; -.
DR eggNOG; KOG1873; Eukaryota.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000050525; 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 CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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:SF34; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 45; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
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 35..152
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 192..823
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 91424 MW; 1DBDB2F68DCDE256 CRC64;
MRVKDPSRAN PEKTKRNKRP NKPQDEDSSD DIAGLTCQHV SQAVDVHLVK RAVAQNVWSI
CSECLKERRI SDRELVMPSD IWLCLKCGSQ GCSQNSEGQH SLKHFQTSHT EPHCIVVNLS
TWIIWCYECD EELSTHCNKK VLAQIVDFLQ KHVSRTEPSS SSKIIRLREE KSDTSEILKG
KGSANGALIP VKGINNLGNT CFFNAVMQNL AQTHILNELM CEMKEKGTKL KISQVTDSQL
DPLVVNLSSP GPLTSAMFLF LHSMREAGKG PLSPKILFSQ LCQKAPRFKG FQQQDSQELL
HYLLDAMRTE ETKRIQTGIL KAFNNPTTKT ADEETKRKVK AYGREGVKMN FIDRIFVGEL
TSTVMCEECE NISTVKEPFI DLSLPIIEER VSKPVPLGRT SKGKTTQEVD FGHYNCPSVT
ALNNQQAKIT KKRSLTKDKN QLNYERRLSR KSSSGGEDRS PVIMHEKDDK LEAECGSGVL
YSEDTIPESA VNGSQTEGSE KDISCSESSV DADSEASEGE SASTQSLFGT SSNTSGLHVD
RLNHLSGNVK PPNSKPSDSH NEVAVITAIS KLSLSDTVKE CEETITGDSP LSLSSNSMFS
MEKSPVSKNP QNAFQTLSQT YSTSSKECSV QSCLYQFTSV ELLMGNNKLL CESCTERKQK
YQKKTNSTEK KMEGVYTNAR KQLLISAVPA ILVLHLKRFH QAGLSLRKVN RHVDFPLVLD
LAPFCSASCK NVTDGAKVLY SLYGIVEHSG SMRGGHYAAY VKVRSPSKKL LEHISINKNG
LGLKEAVGAS TGQWVYVSDV HVQMVPESRV LNAQAYLLFY ERIL
//
