ID F7W2M9_SORMK Unreviewed; 503 AA.
AC F7W2M9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=WGS project CABT00000000 data, contig 2.22 {ECO:0000313|EMBL:CCC11880.1};
GN ORFNames=SMAC_05091 {ECO:0000313|EMBL:CCC11880.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC11880.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC11880.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC11880.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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};
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:CCC11880.1}.
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DR EMBL; CABT02000022; CCC11880.1; -; Genomic_DNA.
DR RefSeq; XP_003346833.1; XM_003346785.1.
DR AlphaFoldDB; F7W2M9; -.
DR GeneID; 10804232; -.
DR KEGG; smp:SMAC_05091; -.
DR VEuPathDB; FungiDB:SMAC_05091; -.
DR eggNOG; ENOG502S8GB; Eukaryota.
DR HOGENOM; CLU_030515_2_0_1; -.
DR InParanoid; F7W2M9; -.
DR OMA; YHWSQQK; -.
DR OrthoDB; 2358302at2759; -.
DR Proteomes; UP000001881; 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 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:UP000001881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..503
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003363942"
FT DOMAIN 152..297
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 336..477
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT REGION 45..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 441
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 381
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 383
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 388
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 427
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ SEQUENCE 503 AA; 53867 MW; 9EACF99B51BB6BBA CRC64;
MTVLAVLLAL ATAVSQSTGL ALPAPAPAPA PQMVYGENSG PVAGVSPPIP TASGRTGSLR
GSTNLLGANS PQPDLDTANS AIVPNPQSVN GQDANADLGL YLDFNSANPP QPNRGGRGGT
DPGPRTYDYE KLNPDLYAPP GTDAGSTPQF MFNMGLAHNR AGVGNHSGWA RQQNQDVLPV
AKAMAGVDMR LEPNAYRELH WHTAAEWSLV LKGCTRVAAL DTDGRTYIDD VCAGDVWFFP
AGVPHSLQAL EMGTEFLLVF DSGAFNEEAT FLVTEMMLRN PVEVLSKDLK ANTSAFDNLP
KDQLYIFNGT PAPKNIAEQN LTGPAGARTG NESFTYHWSR QQPMEVEGGS VKIIDPLTFP
IASNFSASQV VIHPGAMREI HWHTTSDEYA FFIQGSGRIT VYVAPSASRT YDFTAGGVGY
IPQGSSHYIE NTGTEDLVYL EVLQASKFTD ISVAQWLALT PRQVIKDHLH LPDELLDRLP
TEKPYVVAGN KNLTAMAGGG QAY
//