ID A0A397UNB1_9GLOM Unreviewed; 669 AA.
AC A0A397UNB1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=BTB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C2G38_2042511 {ECO:0000313|EMBL:RIB11624.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB11624.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB11624.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB11624.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) 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}.
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:RIB11624.1}.
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DR EMBL; QKWP01001112; RIB11624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397UNB1; -.
DR STRING; 44941.A0A397UNB1; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.420; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR PANTHER; PTHR46236:SF35; TRAF-LIKE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR46236; TRAF-LIKE SUPERFAMILY PROTEIN; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 22..94
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT DOMAIN 323..451
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
SQ SEQUENCE 669 AA; 78223 MW; 8A7741188AD3801A CRC64;
MGKFFDLLSN NLNELLKNSD EYNVIIEVGQ EPNIKAFKAH SIILSSRCLY FKDKLAAITY
NDNNKKIIKQ TNVSIEVFEI IIKYIYDGTI PFETIKASVI FELLIAFNEF GLEEMIKHTQ
LFLIKNNASW LRHNFSRVFQ TCFKDSLEDL QQFYVNIISK HPNIIFDSDG FLTLSENIII
FILNLDNLQI DEVKIWDYVI KWGIAQNPSL PSDLDQWIDE HFLALKNSLQ NCLPLIRYFQ
ISGCDVYDKI RPYRKILEPT LWDDIMLKLV APNKAITITS HVLPPRTKLS TTLPSRDIIT
DNNASEIIDN KVMPDLGYEI EDFQYYTWRI TGWSGLEKRT TSPEFEVGGW KWRILLFPFG
SNNSYTEIYL NFADLKGAPA GWHSCVQFAL LLWNPDDPIS YVSHNTHHRF TAKEPDWGFT
RFCTLHKLFT PLENRTRPLI ENNACNITVF VRIIKDPTGV LWHDFKNEEI KAEESHLYLS
IKIVTPQIFA QNQGLDLANF DDLLFAIPQF KVLKSETYRN FKCIAAKRFG YSVEQIRFWI
LVNRQNKTVR PDTPINDNFY DMSMEEIRTK EVARQKELKL FLEVAKPING KAYINRALCH
LYIQKFDKVG DIVPILCEKK GFPQHTRLKI YEEIKPDRID EMKPYLTFKK SEIQDGDIIC
FQKALTEEE
//
