ID A0A177DV64_ALTAL Unreviewed; 942 AA.
AC A0A177DV64;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=CC77DRAFT_1048287 {ECO:0000313|EMBL:OAG23396.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG23396.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG23396.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG23396.1,
RC ECO:0000313|Proteomes:UP000077248};
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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DR EMBL; KV441473; OAG23396.1; -; Genomic_DNA.
DR RefSeq; XP_018388817.1; XM_018527524.1.
DR AlphaFoldDB; A0A177DV64; -.
DR STRING; 5599.A0A177DV64; -.
DR GeneID; 29113118; -.
DR KEGG; aalt:CC77DRAFT_1048287; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1048287; -.
DR OMA; HYHHITA; -.
DR OrthoDB; 1472at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; Dcp2p; 1.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 96..228
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 252..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 103663 MW; A7F8C1A2D3A16FC3 CRC64;
MTNTNRTLVD WLDDLCVRFI VNLPNEELQS VERICFQIEE AQWFYEDFIR PLDPNNLPSM
HLRKFSQLMF QHCPLFSAYS EELHQQAYEQ FLAYKTRVPV RGAIMLNEDM THAVLVKGWK
KGAKWSFPRG KINKEETDLD CAVREVWEET GYDLREADLV EPDEHMKKIT VTMREQSMML
YVFRGVPMDT YFEPRTRKEI SKIDWYKLTD LPTLRRKNQV QQQGTGNDLI KESSFYMVAP
FLGPLKQWIK QQHKLGRQRQ RNSAHMAPAP VAGTDDEHVQ PNLYETTADE AAPVADAQVA
NNFADMVARL GRGHRPSDSY PELSQAHQAP PPQQSQDPAE ALKRLLSVGM QSPPVEAPSQ
PPPQGNPLLA LFKQGNNQHA GNQQPRTPFE QMMSPPVQPS SPHGQHGPRP PQMGNMGPPP
PFFPPHQNMP FRGHPGHMNG MQPPPPHMSP HFMHQQQQQQ HIFPPQPPNM QQAFDQHNQR
PQFQEMGDSQ FAGGNGRPAI PPASKLPAPN LNAHAMGLLN SFKNDNQQPA FPPSPQTTIA
APLHRSQQTT PRIQHPMPQH RPHGLVSPQA QFAPSPPQFQ SPPISSSFEP EQPKPRNAHQ
DSLLSMFKST PPLASPQPPP AELSALPTTP AYVSAQPVAN PPKQHNAALL SVFHAPSSKT
NMTSATVSGP VNAPDFDTMK KNRQATNGSS RGPSPTTNMP FMPQQILKRT PQASPKPAPP
VEVSASPQTA FQPQILKRPQ QQIKVPGQAA SGETSHKQGL LDMFKSASPQ PPPVQLAVLP
SRSPVPPPLS DMDRRESVPA DQKNALLSLF GNKPSPSPKP QTHSPVPPAR SPFPPTPKTS
MSGVISPVSP LPTNSSVGAT SPEGNANRSR ISSIGDGTAP SIVIPPTSRP MDAGVSLTQN
EGVSVVGLST QQSRAGSTSE GKSPVDKSFL LGFLENVARG GR
//
