ID A0A0V1DF96_TRIBR Unreviewed; 1941 AA.
AC A0A0V1DF96;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=DNA replication licensing factor mcm7 {ECO:0000313|EMBL:KRY60159.1};
DE Flags: Fragment;
GN Name=mcm7 {ECO:0000313|EMBL:KRY60159.1};
GN ORFNames=T03_16192 {ECO:0000313|EMBL:KRY60159.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY60159.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY60159.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY60159.1};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC {ECO:0000256|ARBA:ARBA00008164}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000256|ARBA:ARBA00006824}.
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:KRY60159.1}.
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DR EMBL; JYDI01000007; KRY60159.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 6.10.250.2090; -; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 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; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
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; IPR007248; Mpv17_PMP22.
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; IPR001972; Stomatin_HflK_fam.
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; PF01145; Band_7; 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; PF04117; Mpv17_PMP22; 1.
DR Pfam; PF00071; Ras; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00350; MCM; 1.
DR SMART; SM00244; PHB; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 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; PS01270; BAND_7; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
DR PROSITE; PS51419; RAB; 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};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT TRANSMEM 1405..1423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1686..1714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 REGION 1591..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY60159.1"
SQ SEQUENCE 1941 AA; 220072 MW; EA3BE34ED653FB96 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 LTIHLRGENT RLINPGDHVH ITGVFLPKLK
TGFRQLIQGL ISETFMEAHH IVCLSKTNDE INEDHLRLSE DDIKLMAEDD FYDKLTYSIA
PEIYGHEDVK KALLLMLVGG VDRSINVCLM GDPGVAKSQL LSYVDRLALR SQYTTGRGSS
GVGLTAAVIH DQLTGEITLE 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 NIVTGHVFCF 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 DSEAYISHDQ
AAGYSILEHE LAAMQTIKCV VVGDGAVGKT CLLISYTTNK FPSEYVPTVF DNYAVTVMIG
GEPYTLGLFD TAGQEDYDRL RPLSYPQTDW VPEITHHCAK TPFLLAGTQI DLREDSSVLD
KLSKNKQKPI TVEQGEKLAK ELKAVKYVEC SALTQAIFVK LFSKEYILKC SCMIVSLLMG
TGDVISQTVL EGHRSYNFFE FDRTFRFVFL GTFYTGPLIW AWFVKLDKIF VGHSLLSVIK
RVALDQEFRQ VYLTNLQLWP AVQLFNFYFI PIQHRLFVTK CVGIFWNTYL AWQTNQISRP
RSFKEKSNIC ELFNGVDGVD MLTWNTIEGL VSQVSVRRLS SSLSLRLCNF ISTPPADSQS
WRGRRPTPAV SYLLRRPVLP PLLRPFAAFF PRSHRPRQPP PPPVDNSMSI ERRRKASPII
GQRCGQRRPP LEIPSTAHRA STASNAASSA ETEMSSPGMH KETKQQWASP SVQSDSPADF
EIIGIWFGYI LTGLSWFIVA ITFPFSMCFC LKVVKEYERV VIFRLGRLMP GVARGPGLVF
IMPCIDTYRK IDLRVVSYAV PPQEILSKDS VTVSVDAVVY FRTSDPIAAV NNVDDAIYST
KLLAQTTLRN ALGMKTLTEM LCEREAIAQL TETILDEGTE HWGIKVERVE VKDIRLPQQL
TRAMAAEAEA AREARAKVVA AEGEMKASRA LKEAADVLAD SPVAIQLRHL QALSSIAAEH
NSTIVFPIPI DLFGSFMRKD K
//
