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Database: UniProt
Entry: A0A0V1P6J3_9BILA
LinkDB: A0A0V1P6J3_9BILA
Original site: A0A0V1P6J3_9BILA 
ID   A0A0V1P6J3_9BILA        Unreviewed;      1951 AA.
AC   A0A0V1P6J3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=MutS-like protein 5 {ECO:0000313|EMBL:KRZ91840.1};
GN   Name=ZFYVE9 {ECO:0000313|EMBL:KRZ91840.1};
GN   ORFNames=T08_15684 {ECO:0000313|EMBL:KRZ91840.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ91840.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ91840.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ91840.1};
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   -!- 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:KRZ91840.1}.
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DR   EMBL; JYDM01000040; KRZ91840.1; -; Genomic_DNA.
DR   STRING; 92180.A0A0V1P6J3; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   CDD; cd15729; FYVE_endofin; 1.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 1.10.1420.10; -; 1.
DR   Gene3D; 3.30.500.40; -; 1.
DR   Gene3D; 3.30.1360.220; Domain of unknown function (DUF3480), N-terminal subdomain; 1.
DR   Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022557; SARA-like_C.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46319; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46319:SF3; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF11979; SARA_C; 1.
DR   SMART; SM01421; DUF3480; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          137..196
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          202..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1951 AA;  222310 MW;  5ED2676F14F9314A CRC64;
     MVFNRRCAVE EHVQNDSLSS KGDGSEIDAE VERVLTFIVL QTCTLFDEKD SALIHQMEEN
     ADRLNSRSTS LLGFPDAGSS MPCSGKICES SLRVELTSDE LSSVNLLDRG DHSDSKWAIM
     AVFKERIGLV PPEWIPDEQW RICMSCSARF TLIKRRHHCR ACGRVLCCDC CHLRVKLQYL
     ENKKARVCQL CASLLDQSVE SDESEAHRRG RNDDSQQGSA EQISSDVLRA SCVLKKSGSI
     IFWKRTYPKA QSKNVTFEDG VCPGEVDSRR VNMFADSLSS SHTVQPKNDK RDRRSREKES
     LLPNTAALPP STFQKCSTEL QMTYTAVCRD EDLKVLLNEG KEVVFHIKRN LCVNVKLMQD
     SSLAKPFFWR FISNGFCNLG ISEKMFFLER TNDEILPPRD IDCSFVDVIP GCFPFGFLGN
     KENAAVLFFR PNRTIINQYK LPKTYYHIGL LVHRSEMIWA EILPLRLLLR FGFSDGVYPW
     SVVSSPMRCS FFGETGHTVM SLLNDMRNFT YTIPMVTNSM ITVDKKRFLP AVLSTCNEHV
     VAWASDFCDH AAAHFVCIQD IDSGTYVTKR FSKNRSSNPE VTGSAFIIFN ASLKSASLAV
     KNSIVEDGVM VQIHLDNLND LRECLRNKKD YFLKSNEEGG CSLEIRWDAH ITASSNFSIA
     SHIDSYNLDL KYRYLLPFRF VEAYRDGQLV RLTDVFTLPV DVNETLHSEP ESFAASCRRI
     ASATCKALLQ FAEDLLVENS SVVSLRLFMS ADVIDYKFSV KSQSLLRMMM AALDDAIVSV
     LHLEAINSIS SWKAEFIFRF LNQNFHSFTI EKRKLSFLFR TMVSAWNCST AHCMFSDEMS
     NCSKMSSEED DLDPKKTIRV ALNTCNTTKG LAVRKSKRRR MRRSVKQLDT SNRRGGPDAI
     PKLMMMRHGE RLDSCRFDIR RCFESGSYTP LQLNHPSFLQ TRGNGQLISC IEDWVEDTPL
     SNMGRAAAFL MGRAMAREDE VLDYVFASPA HRCVETADEV VRGYESVYNL LPEYKLKVKV
     EDGLFEFGFG KLNRVPPFLS LTALKEQYCV DENYVPFFPR EKLSIDESYV EFVRRTQAVV
     EHFARFSIAN KCSTLLVSHA PYMDALTSLY KGREPRDPND WIHLVQNTPY LYMRAVKWNG
     RKWQTTFFDM IIFLFRHVVY KYTVFIRSFK NIYIKMSAFN RNSTALEDFC FDSSSFSDEI
     ESHSGQIVLC IYLSNQKLGA AYYDTDSSKI FTLNDVAESM NEFSLLIDVL NQVRPTTILL
     SSKADERLCK LIDDFQNNKC QQNAEVEEAE NENDLIVVAA SEFELSRCKN TVERFISSIG
     SGHASVEDKI RASLFVDMES VCMIRALGVL INYCEIESIS TDHFGRPVAF CLRSFEVNDM
     LVMDDNAYES LQIFKKQFHP SVYKAGRDGF KEGFGLYSVC NRCCSSVGAA KLRRWFLRPT
     RNLNKLKQRL DSIEILSCDS NFHFIQAVQK PLKQIKSVTA IFNRLRVAKV NPSDWISLYK
     TINACIFVAE FLKNRKNLKV ILSEMYDISL EKLQKISSLI NELVDFKAMV EERQFTVKPG
     IDRLLDEKKE LLKRLPELLT EVIKSEIDNL PFPLAACTCV YIPTIGYLIA VPRSLSCSKD
     GDYEKPGLEF MFITNDRVHY KNETMRQLDA ELGDVKLDIK DLETREYNWV RPELVEENVI
     DITGSRHPLQ ELCTAPFVNN SVKSDETEFG KMHVLTGPNA CGKSVYLKQV GLLVYLAHIG
     SFVPASAARI GLVDRICTRL HSTGSINDGM STFAADVKQV AMATKYATKK SLIIIDEFGK
     GTLTDVGVAL LGACLTYWLE RDKCPHVFVS THLHRLFNIL PQSTLLRYNT MKVMRQGEDV
     LFLYSICEGQ ATESYAACAA SKAGLPERVC NRIRQVCQNQ KRGYQLFRPE STAEEIKEEF
     NRMKKLVSAF LNYNLNEHSV MELLTLIRQS N
//
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