ID J4H2C3_9APHY Unreviewed; 666 AA.
AC J4H2C3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=BCS1 N-terminal domain-containing protein {ECO:0000259|SMART:SM01024};
GN ORFNames=FIBRA_03323 {ECO:0000313|EMBL:CCM01274.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM01274.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM01274.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM01274.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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DR EMBL; HE797025; CCM01274.1; -; Genomic_DNA.
DR RefSeq; XP_012180557.1; XM_012325167.1.
DR AlphaFoldDB; J4H2C3; -.
DR STRING; 599839.J4H2C3; -.
DR GeneID; 24096185; -.
DR HOGENOM; CLU_010189_3_1_1; -.
DR InParanoid; J4H2C3; -.
DR OrthoDB; 404208at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR014851; BCS1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070:SF87; ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14760)-RELATED; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08740; BCS1_N; 1.
DR SMART; SM01024; BCS1_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT DOMAIN 26..214
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 73101 MW; AB0DB2024403AB8C CRC64;
MNTIKSLLSP LTGSNANPIQ DTLKLVVIGG TVETARRASV SAWNGFIDSF FLTAHFSQED
YPYDWLMHWL SKQPAWGRSR EFDITTRTAS RHGLTQSTTG DLEDQEEDED ALVGGQRKRK
VAIIPSLDTT HTIYYRGHWL RITRTKRFQD YGSYAELKIS VVARNNDILK RLVLEAKREY
EKDAEHRVHI FMADTTYGCW RWNGARQKRP MSSIVLEPGV KDMILADCKD FLCSEDWYAE
RGRPSHVLLS DMGTDDPRKA SHSAAGICCT VCLEVDSGKT SLIHSLAGEL GLDIYVVSLS
SKGMSDNTLS NLMGNVPSRC ILLLEDLDAA FTRGVSRDDT STGAPTSTTS SSSALSAKNK
DDSNDGSTLS LSGLLNSLDG VAAAEGRLLF ATTNHIERLD PALSRPGRMD VWINFKHATK
WQAEGIFKCF FPVKSATPAG SSSSASAPST GADPTSQEGL PVSKRKQATH AIPLLTEEEI
STLAKRFADA IPEDELSVAS LQGYLLRNKT RPQECVDEVA DWVIQERETR AKLKKEKEER
EAKEKKEAEE KAKKEKESES KEKAAADSAE KSSKKESRTK TKKSSRSESK SASTTDASQA
SDAASSDSTS TSESESSSGG AEADTEESVT SEEEAEQPEK SDKAVETTDR QEKWVAVKGH
PPDPCV
//
