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Database: UniProt
Entry: C3ZKJ5_BRAFL
LinkDB: C3ZKJ5_BRAFL
Original site: C3ZKJ5_BRAFL 
ID   C3ZKJ5_BRAFL            Unreviewed;      2860 AA.
AC   C3ZKJ5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN47094.1};
GN   ORFNames=BRAFLDRAFT_119067 {ECO:0000313|EMBL:EEN47094.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN47094.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN47094.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN47094.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   EMBL; GG666636; EEN47094.1; -; Genomic_DNA.
DR   RefSeq; XP_002591083.1; XM_002591037.1.
DR   STRING; 7739.C3ZKJ5; -.
DR   eggNOG; KOG1011; Eukaryota.
DR   eggNOG; KOG1090; Eukaryota.
DR   eggNOG; KOG4127; Eukaryota.
DR   InParanoid; C3ZKJ5; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd20827; C1_Sbf-like; 1.
DR   CDD; cd13208; PH-GRAM_MTMR5_MTMR13; 1.
DR   CDD; cd01235; PH_Sbf1_hMTMR5; 1.
DR   CDD; cd14534; PTP-MTMR5-like; 1.
DR   CDD; cd01301; rDP_like; 1.
DR   Gene3D; 3.30.450.200; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.11500; -; 2.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008257; Pept_M19.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR022096; SBF1/SBF2.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   InterPro; IPR005113; uDENN_dom.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF109; SET DOMAIN BINDING FACTOR, ISOFORM A; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 2.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF12335; SBF2; 2.
DR   Pfam; PF03456; uDENN; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00568; GRAM; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        2449..2471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..819
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   DOMAIN          1526..2152
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          2242..2292
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          2345..2396
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          92..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1135..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1676..1722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..112
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1676..1691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1708..1722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2860 AA;  318914 MW;  A3AEECD766BE6F7A CRC64;
     MARLADYFIV VGFDHNKERG IGTGRGKILQ RFPTTDWEDV TFHQGLELFC QPGGWNLSMQ
     RRPPAFFVAT LTDMDAERHY CACLSFMEPV EVQPNQPDEQ ESEEDEEEEG VENGEGPKQT
     LMFAPKSLVL VSRLQHFETF RHCLGILYTV YIENQSVQIE TLVGNHLGSV HVPPPXGPQV
     RFSIGAGDRQ ALQPPLSDSL PVTGTTVAML FRQLGIYNVI CLFCAALTDH KILFHSTSYS
     RMSDACQALC ALMFPIKYSY VYIPVLPAFL KEVLSTPTPF IIGVHASLKN EMADLLDVII
     ADLDGGCLTV PDCTSLSLYL TIVHVLFNVF CPQLDVIIAD LDGGCLTLDV IIADLDGGCL
     TVPDCIRLSL YLTVVHVLFN VFCPQLDVII ADLDGGCLTV PDCISLSLYL TIVHVLFNVF
     CPQLDVIIAD LDGGCLTVPY CTSLSLYQTI VHVLFNVFCP QLDVIIADLD GGCLTVPDFV
     SLSLCLTIVH VLFNVFCPQL DVIIADLDGG CLTVPDCISL SLYLTLVHVL FNVFCPQLDV
     TIADLDGGCL TVPDCISLSL YLTIVHVLFN VFCPQLDVII ADLDGGCLTL DVIIADLDGG
     CLAVPDCISL SLYQTVVHVL FNVFCPQLDV IIADLDGGCL TVPDCISVCL YLTIVHVLFN
     VFCPQLDVII ADLDGGCLTL DVIIADLDGG CLTVPDCISL SLLPEPLLSR TKLALSMVLH
     PDLHVSDHAF PPESTAPSPL PMLDKEIRAI FLRLIAELFF GYRGCLTLIR IHPEPVITFH
     KATFLSQRGL IDDDFLTKVL DGMSFRPFVH ERGPPYRPCD IFDELVSGIQ TVVRDEGVDN
     KRVMKNVHEL ARQLYLNENP SPQPYVEKIP KATEAAHSRL PQPQFPVLSE FLVQQVIEDA
     QAKRALTAPK MTSLRVQQPR IVPCGENRRD KFSGLNSSAR RLEVMRNCIN YIFDNKIQEA
     KKSFPAVLRG LKSKVTRLAL CDELSLHMQQ NRNKTFVNLQ KLAPGVMQFA YTLVQDHPVW
     ANLQFWEASF YTDVQKHIKE LYHQPDRNGS AKDTHELEVP SSPGMRRRVE VNRSLEKSAL
     DIAAEQLRLW PHRSKDDQQE LVNNEESTVY SQAIHYANRM VFMLVPLDTS KGIRVNMGND
     PESGSNSNVT SSIGGSDSFD AESAQYGEEE SDMTGSVCRF ITRFVDKVCT ESGVTPDHIK
     ALHAMVPGVT AMHVDSMEQV CRESKRLPPI QKPKILRPEL LPGEDIVMEG LRSYLIPDGR
     EEGTGGSMGG PALLPAEGAV FLTTYRTIFK GIPCDPLASE QIVVRSFPVA SLTREKKINV
     QYLSHINEWL SEGLQLRACT FQLVKLAFDE EVTSEDIETF RKLINRLRYP VSVQEMFALS
     RHHVGPRTMI QKHKEKNATL NLGSLNNSQT QQKMEPFRIS QANVKYSTCR RAVIYEDDYT
     GATAGSPMPR ASSERALSKT LGKGAKKAGK QIAKRTKYML PTDSIFMAKV DGDVRKAASL
     DELASDDAES RPSEKLSLER LKEQPAYRHY VKDWAWGRLT AARHSRRQNL SEYLKQTSST
     QPVGALIVVP QSVSDESVRK VARCYRQSRL PVVTWRHPRT RAVLMRSGGF HGKGVMGVLK
     SAQKSAQLVQ APQSGGSSDT SSSVEQEQYF SALVSATPAS RSGTLRQLDL SPSESLTSLF
     TVRTSDQSDP STPDSQRREA ANRKLPQPRQ GSGKSSNSSI SSIRSGFKHW NSLRSSGRAS
     SGSQIDTGLR LAFENGALSK DSGISNGSIQ NMHGSVLYAF GEKSQMKGVK ADQFPKCDFI
     PVDFVEVRHM KASFKKLMRA CVPSAPFTDP NLGLLKAVEE SEWLQQTPTW AVEESEWLQQ
     VPVYCGCLHC SNPSQTPTWA VEGSEWLQQV SHLLQLSGAA VDLLDMQGAS VLVSLEDGWD
     VTTQVVSLAQ VLLDPYYRTV DGFRYFCASV LISLEDGWDV TTQMVSLAQV LLDPYYRTVD
     GFRVLVEKEW LAFGHRFSHR CNHTQASQGS GFAPVFLQFL DAVHQVLHQF PLSFEFNSYY
     LKLLAFHSVS GRFKTLLMDS DRTIWDYISQ LHTSSPLLYN VNYQPQQESP VLRPYSCISS
     LRIWDYFLEE DLSSGQSYDR ELMAMAVQQH AEEVPEEQLS PVSNRIIISA CYDNIAQHQP
     NSLEWLLKES RDLEQDLGHL PLKWRFLWDK LEDNSCMPRP RKPSVSTQLV RAHGISTHKR
     ATIEVLIKGK LSTGAEKAFT HPHRFEMASF PTPTYCDFCS QMLWGIAKQG LRCADCGYSC
     HERCRELVPK HCRRVRALAD GGVGGSMVRL DSESDVSKAS STSMVIQGPS DGTLYDQFSS
     ASEEHSIHEG YLYKRGALLK GWKQRWFVLD SNKHQLRYYD AIHDQHCKGF IDLSEVVSVT
     LSTPLPGAPK KTEDRTFFDL LSKMADQTSG SSPASQESPA AASLSKNRVL LAVLAVLALA
     GLAAAIAVPL ANRARARRQE ETPMEQARRI LREVPMIDGH NNLPSRLRMD ARQLLQTVDL
     RQDLRVIYDV TENDIPRLRQ GLSSAHMWAA KMTCDSQYRD AVRRGFTQVD LIKRMVRMYP
     ADFMLVTEAD GIMEAFEQNK IGSIITLESG HAIDSSLALL RMFYDLGVRG MTLTWQCSTP
     WADYDGETNN PNPPHNGLTD FGKLVVREMN RLGMIVDLSH VSDKVMNDAL DISEAPLHFS
     HSGAYAICNT TRNVKDDVLI KMKEKDGILM IPFIDDFIGC RSNSDTDKVQ LSEVADHFDY
     VRNLIGADYL GIGSGFDCCT RDLFAEGLED ASTYPNLFAE LLRRGWTEDE LRKIAGQNLI
     RVWRRVEAVR DRLAAEGMTE IEELIPAEDT VDDTCRTWVD
//
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