ID A0A397TJV4_9GLOM Unreviewed; 577 AA.
AC A0A397TJV4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE SubName: Full=Concanavalin A-like lectin/glucanase domain-containing protein {ECO:0000313|EMBL:RIA95291.1};
GN ORFNames=C1645_757897 {ECO:0000313|EMBL:RIA95291.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA95291.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA95291.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA95291.1,
RC ECO:0000313|Proteomes:UP000265703};
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 -!- 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:RIA95291.1}.
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DR EMBL; QKYT01000064; RIA95291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397TJV4; -.
DR STRING; 658196.A0A397TJV4; -.
DR Proteomes; UP000265703; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363:SF6; RING FINGER AND SPRY DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Lectin {ECO:0000313|EMBL:RIA95291.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 225..414
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 476..511
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 520..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 64127 MW; 2E7449098687EED1 CRC64;
MQKLALRILG RFSRKTFIRS AWKNLNSLSE HDELTEALDT LISMSHEENE FIELITVIVD
VLSEAPMASA FLCHIIDSAA LPSKETSHKI TTRLLQKLKP GGIYRSKPKK RTRVNAAIIW
SVLAEKLAGE ISLSLFSDNV CTTLLDYLQY DHDASVRLFA LIALEKFGMT GQNKEKILNS
GRDIHKILQC IAKELHSGEG SSEDINRRRQ LKFCLEWALK NTFDSGKEDM CDSDEGSVNS
NNINVMLNPL DATAHWKISR NGLEIRNDNS TFESIRATMG VSSGKWFYEV VLLTNGIMQI
GYATKRCLFG PEEGTGVGDD QYGFAFDGCR NVLWANGVSV PYGGSESWKP GDVVGVYMDV
SSGCVRFYLN GKDLGVVYPL NLAQFRKLAE SSLHPALSFT SYQQAIVNFG AEKFRYPPPP
SLFAYQTLNS QGQISSELRN SIQKRVWRAS RYRSMSVNPY WKQQFESTEE DLDTQCSICF
ATPPAIVLGP CNHDGFCTDC AKMMHSCPLC RTPISYRKPM NNNTTSLPST PTKLSIASTS
ASSSLSAPST AIVLPPTPPH SRPASSITSW EPRCLEP
//
