ID A0A1Q9F2E9_SYMMI Unreviewed; 1082 AA.
AC A0A1Q9F2E9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=DNA replication licensing factor MCM3 {ECO:0000313|EMBL:OLQ13866.1};
GN Name=MCM3 {ECO:0000313|EMBL:OLQ13866.1};
GN ORFNames=AK812_SmicGene2103 {ECO:0000313|EMBL:OLQ13866.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ13866.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ13866.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ13866.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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:OLQ13866.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSRX01000022; OLQ13866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9F2E9; -.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA-binding {ECO:0000256|RuleBase:RU004070};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 836..1042
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 423..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 118950 MW; 5AC15673BEC531BE CRC64;
MLFAFDWNVY FPPGCCGLLV CDRRVFLQLR KSWAELLHSG YDGDGRDEQL ILDERRQVQA
VVLQRCAPYM IVICLASFAC CFVALILMPE CWRLVIELDY LAMSSNVIGA IFLYRHLLPG
ARQKLHDWQL AGAFYLPWVC VTFLQIANFS CGDEARDGYY STRLVYFCYR ALLSVALMCP
FQCTVAELIC SGMVAADVQR SEARAVMMSI ELLFLLLIFA GTCFLGQRMI DWAFANARKA
EEALSALVDA RLGLIEKLCD AEVELSGDLK MLEASASWGS RMGIHLASFE GSFLDVVDEE
DEERVLTFLR AASSEGASSC IQASLRTFAN DRLDARLYHA AQSGRSDACQ HRLAVIFLGN
TEPPVATIVA KPTSEVSDDF SSDCEHLFHP LVSAERSLGP ASDTDGEMTD TLVCSESIAD
RSQGSRTTFT RNTFRPGSDR NVCRTHNKGT QTDAQPAKRR ADTSDAACQT AGIIRPPVLP
QTSQPSSRPQ SSDRKVRSHR QLAFAGDVVP NKRLIIARTC QLMLLEDARK MNVRGSGCCA
YHVIMSYLHK TVKSMTKSPC RQLEFHSDWQ CAICHALHSF EEDQESDADD GKFWCDVCGC
TDVPAEPETA PSSMDAEAMS DGPASSFEDA HSILGVSDSV KVAGSEERLK GRPQLRRYAS
SHVAGVEGLV TRCMVSQPKL VHSRHVHKDQ DDGYVESRDH RDTTMLGNQV NRSGGGFPKQ
DAEGRELKME VSFSEYKDTQ QFDLQESPEA APPGLIPRSI QVLCDGDLCD KAKPGDRVQV
IGVLKGFPPP MQDFTDGVFP IKLVATSITS VKDIVEGQFV ADDIENIKKI GSRQDTFALL
SRSFAPAICG HEKVKQGLLL QLLSGVEKNL SNGTHLRGDI NVLMVGDPSC GKSQMLRFVM
NTAPLAISTT GKGSSGVGLT AAMIRDPNSN DFHLEAGAMV LADRGVICID EFDKMNQADR
VAIHEAMEQQ VVTISKAGMH VTLNARCSVL AAANPIYGNF NSKLDLVKNI GLPDSLLSRF
DLIFIVRDNS TEELDRKIAE QVLAQHMTRF EGVEHKRGVE EVHSSCSPAL GVCPEVDEAS
KM
//
