ID A0A371CM67_9APHY Unreviewed; 890 AA.
AC A0A371CM67;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=NACHT domain-containing protein {ECO:0000259|Pfam:PF05729};
GN ORFNames=OH76DRAFT_1412176 {ECO:0000313|EMBL:RDX41386.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX41386.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX41386.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX41386.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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DR EMBL; KZ857514; RDX41386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371CM67; -.
DR STRING; 139420.A0A371CM67; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd21037; MLKL_NTD; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10039; AMELOGENIN; 1.
DR PANTHER; PTHR10039:SF17; NACHT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05729; NACHT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 281..431
FT /note="NACHT"
FT /evidence="ECO:0000259|Pfam:PF05729"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 99537 MW; 1717532C1F37ACC9 CRC64;
MPVPVRRERD TLGSATKPIQ KPAKDARTVT DALNNLQTVL DKSRDLLTFA PVPGLSAALG
ALLAIGEQIK KMKSNGETVK AISEQIRKLN DVVGKVVRQV ESRAERLQIL PEQRGDMLDC
MQAPGGWRER VNQLAEELSE LLQKAEPCAE GPWYRRLFRT IRDEETLKTI HEDLTAVIQH
FLLAGGLSIE ALTEQSLALV ETMHGDIKML AAAQKADTVT RTQQRTRQQA ESERMAIETI
PHATNAGFNS AGNADKSSYL VGTRNAVFDR LDEWVSSELS VCFLVGAAGM GKSTIASEFC
RRHQRELGAS FFFRRGDARV GSTTAFFSTL AYQLAKSSKE LRPHIVHAAE RHMQAGNSQQ
MQYVVDDLLH TPLRAAKIAG VHFRVYVVVD ALDECMESAS QPDLVPECLR LLVSCALQHP
FIRLLITSRP EPDYVGQALR RRPELKDSSV SISLYNVEDR LAIDRDIGEI IRTRLCAVQE
GAEWYRRDES VVSRLTNQSQ GVFVYARTAV DFIVRAAGIA QMEHRLALLL TPGNTYGLDN
LDVLYRTVLE TAFPPADLDP VTRERVGLML AWIALCQYRY GVTPHRVQMV SGISCRESVP
ILTKLRSVIV FNLEAKDVRE ARFRAMHVTF RDFLVDRARC GELYHVDPQR MHARLAVDCL
TFMRNNPRRE LVFSSKSGGV IYPVFNWMDH VVQASPTREL VGLLFEMYTS TLTGRTSLPV
FFCRERFSEY GGGSSLLRWV DMHIGRDLAK TMGEQMCLEN QDLTVHFGEE ITVSKRSPGS
QEGLTVHEDR QRRDIWSSYI RPEVTSTPSP APSPPAVHPA RVRRPDRRGS PASRSRPVQD
HSTLQESKSH ASPGSLGYPK SRSRYSGGVA HGASSASRRQ GGTMTRPPSR
//
