ID A0A0V0WHF0_9BILA Unreviewed; 1497 AA.
AC A0A0V0WHF0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Minichromosome maintenance 8 {ECO:0000256|ARBA:ARBA00042306};
GN Name=Mcm8 {ECO:0000313|EMBL:KRX75022.1};
GN ORFNames=T06_8706 {ECO:0000313|EMBL:KRX75022.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75022.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75022.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75022.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRX75022.1}.
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DR EMBL; JYDK01000132; KRX75022.1; -; Genomic_DNA.
DR Proteomes; UP000054673; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd22247; MCM8_WHD; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 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; IPR000742; EGF-like_dom.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630:SF47; DNA HELICASE MCM8; 1.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Helicase {ECO:0000313|EMBL:KRX75022.1};
KW Hydrolase {ECO:0000313|EMBL:KRX75022.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 543..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 463..500
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1083..1286
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT COILED 602..645
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 490..499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1497 AA; 167129 MW; 623FDB340519A984 CRC64;
MSSYDMTMMC FSGTPCSSKT FWNFCSSIKK YLMSVIVPTI RAGHQNCPDF SVFLHRAPQP
SYNLARIKKQ LLPEECMMKL FSIVVLLVLI FKVDGISYTC PFESFPNDIK GGKTSSDKCI
SIITHEYVKK YFGTKGLSTD TGGLACQHLF KNGAQMVFKN ESDLAYNRYV KMLENEYFLV
HAGMEQIATS YYYTKDIYSS KLGYTILFYC YDYKMRKFGP GNFFMLTRCY TYKHVAFTGY
VYDGMQHPWL DVCYIHSKEC LDADTGCTYF ACMHDAYRNC EEDRVRNCSV VPGKKECREY
TYISHSHQEK PYGKPCQKRD YGNTCKCPCS NRPWSSWSQS SHTCGKGYRQ KSKPRVLYEN
ENVDCNRQPE KCCIKTESIQ LSNCLDKFVH SGLPLEKGSF ICMQNGGVPI QTDEGYICKC
EDPLKHGYMC EYEYNICEKY QGICQNGGTC KGKGRSYYCI CPTVKGCAQE NMCQNGGTCV
ENENGLSCNC RYPYTGEFCE TQMLVCPPRL CKNGGTCTAF QELKGFLCTC AEVIMDGEPP
ENLMNMIGLG IVGALVLIAI VIYVVHRIKE RERVMFFIYI LNYLLINSGG ETLETFGAYH
FYLLLLHKAK ELARKKKEAK EKALKQKKEA KLKALKEKEA KAKDKCATIW LCGINLQRMK
RGNSANVVNS TRGTFQLKKR TFHNFRPYYW RRRHFKQQSS VNIPLNGHLS LPSTTNAVDG
QQADEISTTL LYAVSVEKSE TYCSQYPAWL LYFPWAKFEQ NSELHVLVNA CSTVLEQSDR
FCYSLNDVLR SRRFMVDFSK FSSALTAEHR TLISSTWTDH QADSLICAIG LAMHTAVVDR
LRSRLCEKLA DRAEQLLHGD AVQFVQMVPK INARLYNLEK LTNIRELDFT DCGRLVSVVG
VVIKAATVEP KCTACGFQCQ SCGFRFQALL VDGLFSTPTR CPSVSGECRG RVFEPVVDTV
ETLTETVDCQ LIRLQELLPP GGNSATGTAS LIPKTIDCEL TDDLVFTCSP GSVITLTGVV
RVRKNEEARR RGQCQYFLYL HANSVIQKED LFGVAAASIS FSSSEARLAA MSAVGELMGD
RNLFSRLVAS LCPTIYGHEA VKAGLVLALF GGATPSQQHS TIRSNIHALL VGDPGLGKTH
LLQACADLSS RGVYVCASTT TAAGLTVTMG RGVDGDATVE AGALVLANDG CCCIDEFDKL
HSHQQCLLEA MEQQELSVCK AGARCQFSAR VSVVAACNPA KGHYEPRLSL TANVNVGPAL
LSRFDLIFLL VDKPDQQADR RLSEHVLAIR RPHSARLTDR LAAPDPIGAV PAPLFRQYVA
FARQTVPAPK LSRAACRLLL AFFRRQFDQT VQVRTPVGVR QMESLIRLTQ ARAKCQLRSE
ATEQDAADVL EIVGHCPLLF VGTDRQSGNA ELKAGSEQRL SFAGRFLQAL KRKAAQTPSS
KGPFTRAELK AIASEVNNNS TTPTSQSFDQ LIDKLNNAGL LLLEKPNCFR LQLDGID
//