ID M2R572_CERS8 Unreviewed; 516 AA.
AC M2R572;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cupin type-1 domain-containing protein {ECO:0000259|SMART:SM00835};
GN ORFNames=CERSUDRAFT_86806 {ECO:0000313|EMBL:EMD34051.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD34051.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD34051.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD34051.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR617774-2};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR617774-2};
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DR EMBL; KB445804; EMD34051.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R572; -.
DR STRING; 914234.M2R572; -.
DR HOGENOM; CLU_030515_2_0_1; -.
DR OrthoDB; 2358302at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033609; P:oxalate metabolic process; IEA:InterPro.
DR CDD; cd20305; cupin_OxDC_C; 1.
DR CDD; cd20304; cupin_OxDC_N; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR017774; Bicupin_oxalate_deCO2ase/Oxase.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR NCBIfam; TIGR03404; bicupin_oxalic; 1.
DR PANTHER; PTHR35848:SF6; CUPIN 2 CONSERVED BARREL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35848; OXALATE-BINDING PROTEIN; 1.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 4: Predicted;
KW Manganese {ECO:0000256|PIRSR:PIRSR617774-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617774-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..516
FT /note="Cupin type-1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004024112"
FT DOMAIN 184..327
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 362..503
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT REGION 79..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 409
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 414
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 453
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ SEQUENCE 516 AA; 54751 MW; 0E2DEB521651B042 CRC64;
MVAFRRSFIC TIFLATCVVA APASGSLPAS QVSSAPQVAS SISAIISSSA STPIVSSGSA
PAVSSSGIVS ASSIAPSASA SVPVPVTSSS APLAHNSEPA STVASAPTAS QNVPYAETVP
YASDDPNYPL WNTTGPDPDY EAVRGTLGAT VLGPQNDYIE MQNPDLLAPP TTDSGDVSNA
KWPFSLSHNR LLTGGWARQQ NVETMPIATS MAGVDMRLEA GAIRELHWHK TAEWAYMISG
SVQLTAVNSD GQNFLDTVSA GDLWYFPPGI PHSLQATDDN PAGAEFLLVF DDGSFSDDST
FLLTDWLAHV PKEVIAKNFQ ANISAFDHIP GEQLYIFPSA PPPDNAQAPQ DPQGQVPNPF
TFHLSQVQPT QLSGGSVKIV DSSTFTVATA IAAAEVTVEP GAMRELHWHP TQDEWSFFLE
GQGRITVFAS SGNARTFNYE PGDIGFVPAS FGHYVENTSN TTLRYLEIFN TDRFQDISLN
QWLALTPPAL VKAHLNLDDE TIDSLSKTKP VVIGPA
//
