ID H2ZXU7_LATCH Unreviewed; 714 AA.
AC H2ZXU7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP44 {ECO:0000313|Ensembl:ENSLACP00000002218.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002218.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000002218.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. USP44 subfamily.
CC {ECO:0000256|ARBA:ARBA00038113}.
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DR EMBL; AFYH01171650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01171651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01171652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2ZXU7; -.
DR STRING; 7897.ENSLACP00000002218; -.
DR Ensembl; ENSLACT00000002236.1; ENSLACP00000002218.1; ENSLACG00000001981.1.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000160526; -.
DR HOGENOM; CLU_008279_13_1_1; -.
DR InParanoid; H2ZXU7; -.
DR OMA; RYQCNGK; -.
DR TreeFam; TF315281; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000001981; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 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; 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:UP000008672};
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 3..100
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 277..689
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 202..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 81089 MW; A8C394804FC91DED CRC64;
NMDKCKHVGR VRLAQDHSIL NPQKWHCVDC NTTDSMWACL SCSHVACGRY IEEHALKHFQ
ESKHPLALEV NELYVFCYLC DDYVLNDNAT GDLKLLRSTL SAIKSQNYEC TTRSGRTLRS
VGSGDDSYLS QGCTQAILRN EDRMFTALWH RRRSLMNKVF RSWFELTPAG KRAIAEERLK
EEAEMKREMA KKRREELKRQ LKEELKAMPP RKSSRVQEQR KTTTKPATPA LQRTTQPAAT
AVARRSKKNT STSSEVKLKK IGDSPVKRRP TVTPGVTGLR NLGNTCYMNS ILQVLSHLQM
FRECFLQLDL SQAQEILACA ANGKARSLGK PSSLADLVSN SKGKNEKKKE PALFRRPSLS
AGLSGGASQS RNMELIQPKE PSSTHISLCH ELHTLFQVMW SGKWALVSPF AMLHSVWRLI
PAFRGYAQQD AQEFLCELLD KVQQELKTAG TKYPAFVPIS QIKLIKQVLN VVNTIFHGQL
LSQVTCLVCD NKSNTVEPFW DLSLEFPERY HCNGKESASQ NSCLLTEMLA KFTETEALEG
KIYACDQCNN LIKKKKKKKN QNLLLVPAAR RLLLIASPRV FVMPCKIFRW SGRNHREKIG
VHVSFDQIIN MEPYCCREST RSLKPECFIY DLSAVVMHHG KGFGSGHYTA YCYNTEGGFW
VHCNDSKLSM CTAEEVCKAQ AYILFYTQRI TWEHGHFITK KFPPVLPSNN AMPA
//
