ID A0A409Y6N5_9AGAR Unreviewed; 875 AA.
AC A0A409Y6N5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=CVT24_003410 {ECO:0000313|EMBL:PPQ98702.1};
OS Panaeolus cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ98702.1, ECO:0000313|Proteomes:UP000284842};
RN [1] {ECO:0000313|EMBL:PPQ98702.1, ECO:0000313|Proteomes:UP000284842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2629 {ECO:0000313|EMBL:PPQ98702.1,
RC ECO:0000313|Proteomes:UP000284842};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent, however specific
CC DNA sequences that define origins of replication have not been
CC identified so far. ORC is required to assemble the pre-replication
CC complex necessary to initiate DNA replication.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBUNIT: ORC is composed of six subunits.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365058}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000256|ARBA:ARBA00008398,
CC ECO:0000256|RuleBase:RU365058}.
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:PPQ98702.1}.
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DR EMBL; NHTK01001378; PPQ98702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409Y6N5; -.
DR STRING; 181874.A0A409Y6N5; -.
DR InParanoid; A0A409Y6N5; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000284842; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10763:SF23; ORIGIN RECOGNITION COMPLEX SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51038; BAH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365058};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU365058};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365058};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000284842}.
FT DOMAIN 108..237
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..381
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 97968 MW; 805FA10761BCE572 CRC64;
MPPALPQTPT RRSQRFQPLA TPTTKSHDRN ILECGWQGPP IYRRTIIPEL DLLPEELDDL
NSKEKEEEEG EGVPDERETV FYNSFRMKRK GVPYRGARRI QAAKTESQLY SVGDTIMVET
DTLYNFKRPP SIGVIVAMWD TCHPSERQDS IPFTSMRVRI HWFLRPFELA AIRASRTHKE
NEIYFSLSTK AVITPAVILS RCVVNGQVAR PIKEVKEKPY VYIPVTPSKT RPSSPLKKST
KFAMGDSDDS SSDEEADVPD FAQDPDRNFC CQSAIDSRRG LYYNLNWEQH RRKALSANQP
PTDEPGTSSQ AEAASAFWEG LAWDVSIKPS KPKTASKPKD AEISESEGGS SDEFEAGEDS
EDDDDMEIDG DEEDEDEDGL ADPSAEPRTP RKRKRSGKSG FRKDKRGRTH ALATPHSKAA
LERREKGSAP SSPRKRGAKA TFAVRFPEQS LEFKSSMAHL PEDLWLRSMH ALHVGSRPDT
LPCRDEEFTK VLRSIGDLLE EGSGGCVYIS GVPGTGKTAT VHAVVRELKR MAESNEINPF
TYVEINGLKI PEPAAAYNVL WEGISGHDVA KDGHLRMGSK ESLKALMRYF TNSNRGPGGH
ACVVLMDELD QLVTPKQDVV YNFFNWPTLV GSKLVVIAVA NTMDLPERVM TGRVRSRLGM
IRINFQPYTR EQLEKIVEAR LNAAKDGLDE EKIKGQVVIA PDAIKLASMT VSRITGDARR
ILDICRRAVE TVQHTKNTVK AMQVREVVQS MQNSPTAAFL RDLSLHERLM LASLIKVVKR
EGVEEVKWGE VKYQHQIYTK TLTAADDPKT PPTHNEMLMI LDSLVASRAI VVEDGPAVAR
KHEGERRMFL NIEQGEVERV LGDLGGQAWK NVLSN
//
