ID A0A0V1A369_9BILA Unreviewed; 1404 AA.
AC A0A0V1A369;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=DNA replication licensing factor mcm7 {ECO:0000313|EMBL:KRY18825.1};
DE Flags: Fragment;
GN Name=unc-1 {ECO:0000313|EMBL:KRY18825.1};
GN ORFNames=T12_6997 {ECO:0000313|EMBL:KRY18825.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18825.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY18825.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18825.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KRY18825.1}.
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DR EMBL; JYDQ01000042; KRY18825.1; -; Genomic_DNA.
DR Proteomes; UP000054783; 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:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0051130; P:positive regulation of cellular component organization; IEA:UniProt.
DR CDD; cd01874; Cdc42; 1.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR037874; Cdc42.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 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 Pfam; PF00071; Ras; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01663; MCMPROTEIN7.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 351..547
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT DOMAIN 747..846
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 883..1202
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY18825.1"
SQ SEQUENCE 1404 AA; 159660 MW; 542297231987A5C5 CRC64;
LLLIICRNYH FKNMVVRRDY ESEKTKIRDF INNFYVQDND GRGKIYVYLQ KITSLANRQT
VAFVVDLNDL LEYDPDLVES VVNNTRRYTE LFSVVVEDLI FKALQGRAPP IKDCYDEFVN
YRINFELQKQ RDRGETISNP SAAYPPDLLR RFEVYFKALS NEKTYSVRQV GAEQIGKLVT
IRGVAVRVTE VRPLITIVTY LCTECGCEIY QPVTGPNYTP AECCPSKECK ENKTRGRLIF
QIRGSKLVKF QEVRIQEHSD QVPVGHIPRS LTVHLRGENT RLINPGDHVH ITGVFLPKLK
TGFRQLIQGL ISETFMEAHH IVCLSKTNDE INEDHLRLSE DDIKLMAEDD FYDKLTYSIA
PEIYGHEDVK KALLLMLVGG VDRSINVCLM GDPGVAKSQL LSYVDRLALR SQYTTGRGSS
GVGLTAAVIH DQLTGEFTLE GGALVLADQG ICCIDEFDKM MDTDRTAIHE VMEQQTVSIA
KAGIIATLNA RTSILAAANP AYGRYNPRRS IEQNIQLPAA LLSRFDLIWL IQDKPDREND
LKLAKHITFV HAHSKEPPSQ FKPLSMRLMR AYIALCKRKH PTVPESLTEN LVSTYVEMRK
DAKSDKDAMF TSPRSLLAIL RLSTALARLR LADEVVEDDV MEACRLIEVS KESLRPQREG
RGRVIQPVDQ VFAILRELLV QQPDKSGEIS MQDAINKCIR KGIDTHLLED CLETYEEQGI
FESKDEKCCH WEEVKEKDPI LFKKFRKICS LIIYPCNRRN LHVQAMFMSC QVCEIRDSFI
FACIDCATVG CLKNNHFEEH SKEKEHVFGV NIITGHVFCF RCQSIISDAK LNSIICKVNC
RYRQIYGLNP VSYEKVTDDP PAELVPYLRA KRLVNPPSLL GVRGLLNLGN TCFFNTVLQV
FLHTARVQEY FLSDCHPPCG KPLCLICEIG TVMQERLFVE RPPIAPARLL ASLWKAAPEI
AYAEQQDAHE VYLALMNGIH QSSDGKDFGE VCSCIAHKVF SARHKCDVFC ICCHRVTSKV
EPCFNISVDI LDSAEGVSLM KCLDRFTDAE KLILHAYCCY CGCECAIWKQ VTFLDFPNVV
CFHVKRTEKS RHRFQKVKTW MHFPEILDLM PYYRNRLKEI DPTVDLPLIE ECPWLKLLAT
VENQYVLYAV INHAGQTETG HFTCFLRPND GQWYHCDDNV ITPATDSEVY DSEAYIWHDQ
AAGYSILEHK LAAMQTIKCV VVGDGAVGKT CLLISYTTNK FPSEYVPTVF DNYAVTVMIG
GEPYTLGLFD TAGQEDYDRL RPLSYPQTDV FLVCFSVVSP SSYENVKEKW VPEITHHCAK
TPFLLAGTQI DLREDSSVLD KLSKNKQKPI TVEQGEKLAK ELKAVKYVEC SALTQKGLKN
VFDEAILAAL EPPQPEKRKR CFII
//
