ID A0A178B0M1_9PLEO Unreviewed; 1398 AA.
AC A0A178B0M1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=MATH and UCH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ06DRAFT_345641 {ECO:0000313|EMBL:OAL02640.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL02640.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL02640.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL02640.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KV441709; OAL02640.1; -; Genomic_DNA.
DR STRING; 765868.A0A178B0M1; -.
DR InParanoid; A0A178B0M1; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43215:SF4; MORN REPEAT FAMILY PROTEIN; 1.
DR PANTHER; PTHR43215; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR Pfam; PF02493; MORN; 4.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00698; MORN; 4.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 260..456
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 1350..1385
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 155318 MW; 24ADF3845335C19F CRC64;
MSVSIEQPLH FSQQPSSPTF SSPPRSPNQL LHAQTPASPP PLPSVDVDMS SSVTTLAPAG
QQHDRDDANM DEDVNLANDN ARHTSRDQSS HDPPNNNVAV EVAAVDEDAM DITPDTDAQV
VLEPEQTDAL HPAASSPQPP ANGGSVAEDN GDQAAPNPPP DNVTQTENAP PSQPPPPVDP
SLQPPPPPPP IEAVRSDSDS SDDDDGLQPW HPVQEDTSSP DEDELKVIEA STEHSALDHE
YWESRAFLPL EEPEYSVGET GRIDWTIDAY NGTRENPNRE LVMTSDVVTV GGHQWQIKFY
PRGNDSDYLS VYLECLSVMD PKKKSGKDQA DVSKSDDLPT EKEKYQNTME TVGQGADDAS
STPQAPVDPQ HAPLPLLGSK TVAKRKSVAA QVSVVLYNPT EPRVHYSRTA LHRFCSGSPD
WGWTRFHGPY YDIAQRMHGQ RSALLRDDKL AFTGYIRVVD DETKCLWEHP NRENPWDSFA
MTGLQSLALG EDASAPGGNM ISAIASWLLF KPFRNLLYAL DVPDPEEEQL CPPKPLLTAL
QKVLYMLRTR VEPGAGPVAL DDVLDALDWY GIHDRLDKLD VIEVWEVLRA KLEEELQGTS
REGILESMFG PKRDYSNGVP CYRVPVLGVE TMQEAVAHAA NFAVAGQSLP EFLAIELDRQ
TFDVKTRSYA KVLNKVTLDD RLSIDGTSYT LYGFVVHKQT LQSYVYQPIV RPEGPGSRWY
SYSDSKDENQ VRCLTKRQAI DEHEGKAGKE QVMGNDAVAY IVMYIRDDVA QAAFISDTAT
ESWTVPKWLR EEVERDKEPE SAPLMPSTSV DAGAMNEAAK DDQTATDNSE QVEVTDFVVI
ESRVFNDHEG PGNFNAYDRK WSPDGCEYVH SVQLASSFGC AEIVEKLAPL FPSVQDKRQI
LFWFLEPSRG AEGRPQFRGT GKTIYSRGTY DRYTENKDWT LADQAFTSSR IWVHILDFAN
LPELPKEVDN AKQERVEPEQ SQSETDIAEE MPAPTSNTEN EEPLPLPELA MPPEDTPMSE
PEERIIEPVE TQAPREEHVH VPTENAEGGD TAMVELLSAD IPDPPAVEVL IPEQTNSGDT
EMGGTQENLA LPPPPPAQTE MEPAQPPPPE RPRTPDPPPD EIYFFLKIWN AENQTLTSRG
SHLCLTSARV DETVVKLLGL PIEDKKKLEL WEEDEPTNAR PIKHRRSFAQ LDLRNTAIII
AAMPMTSEQR SALSDRAAFA DPSAYLTYRA FARNFPGSLN GHFTYNYFSS QYYKGEVKNG
HRHGHGTLIY HSGATYSGSF RLGQCHGHGL YTFQNGDTYD GDWVDNQQHG SGTFVEAATG
NTYVGGWKND KKFGEGVTHW KNAQEAERMC RICWDEPAEA AFYDCGHVVA CLTCAREVQN
CPVCRKRVLS AMKLYYVA
//
