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
//