ID A0A085NF58_9BILA Unreviewed; 1260 AA.
AC A0A085NF58;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=M514_03446 {ECO:0000313|EMBL:KFD68104.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD68104.1};
RN [1] {ECO:0000313|EMBL:KFD68104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD68104.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KL367508; KFD68104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085NF58; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR CDD; cd17755; MCM4; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 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; IPR008047; MCM_4.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
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; PS00847; MCM_1; 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 replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 839..1047
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 141549 MW; A367C6DE5F526B0B CRC64;
MALFSRRTVR EHLCELVFER FPAKAIQLFQ MWEAIKPKLS ENSSELDVPI PCTLSWTDVD
ILNSKGIIAC EQMLKTRENG VDVPDPVAEH AAKSEKTKLA DQISTEVRNY LADEFGKIPE
LDTLIAMNIE EAEKLLAEQL RRKLESGQFV PPLELSPIEY SPGQPPPFER TIYENATDLE
FVAENTPLSL TDCPKEQDCF IGNPIEMGVE SGGATDTKPL AEVLAQDSRD SRQDLSIRTS
PSKRKSLFES LIATHAPPTA KLLIEERENL DEKLSRMIKR FACLSSSSKD GSSAAEDPSA
TLDMADKGKK KNGKVLTKEM DPSLAVDGLE SEYFSHGEPV HPNMELQVIQ QVLRRELTAA
ANDCTNALLW IRLHLEQLED KTSEYYQQFL QVITILEGKR ADIVDKMSKM REFHEESMAS
SPSQNGVSAD EFLSPLSSPL RSRRSVASPS SGSRVGPSQD AERLSSFEHD IGSRVRSSQR
SYSAASDRLY LSYSNEALNI AQRTRTGSND ATGSRHVLAM VDEQTDEGEK RSYIWGTRIC
LSEVEKAFRR FIDNFRSGED ESDMLSEPSM EAGRASYRQK LYEVYHTQET VIELDLQHVK
SFDEVLYHQI VNYPNDIIAY LDYTLNEMFY EIYPESQRSI ELQIKPFNAE QVYGMRTLEP
DDINKLISIN GMVIRATGLI PEMREAFFEC NICKSSTTVF VEFGQIVEPT LCTNCNSKST
FVLVSNRSIF GDRQVVKLQE FPDEMPPGQA PLSVSVYLLD SMVDLVMPGD RITVTGIYRS
EPIRELPRQR AVKSVLRTFI DAIHILKLDK HKLNDKDDIS WLSEERINQI RSLAARPDVY
ERLAHALAPS IFEHDDIKKA VLFLLFGGTR KDFTSVASGY SRAEINILLC GDPGTAKSQL
LQYVHRLLPR GQYVSGKGTS AAGLTAHITR DPETKHFVLQ IGALALSDNG VCCIDEFDKM
NDYTRSVLQE VMEQQTLSVA KAGIVCQLNA RSSILAAANP VESQWNQQKT IVENVQLPHT
LMSRFDLIFL MVDPQDEYYD RRLAAHLVSL YFKGHEEEEA ELVDMSLLKD YISYAKAVCA
PVLSQAAADN LIHKYVEMRK GDSSRGHISA YPRQLESLIR LSEARAKIRL SGTVEELDVE
EAYSLYREAL KQVATDPLTG KVDVSILALG MSAATRRAAA DLRQLIKNSM LAKEDGAWVA
PKALLMEIRE SGSATVRRDL FEEVLNEMCK DEMLLRGRLG RVRLNRQNIA ADEPVVAAVE
//
