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Database: UniProt
Entry: Q1RQ06_CIOIN
LinkDB: Q1RQ06_CIOIN
Original site: Q1RQ06_CIOIN 
ID   Q1RQ06_CIOIN            Unreviewed;       817 AA.
AC   Q1RQ06;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   08-NOV-2023, entry version 69.
DE   SubName: Full=Zinc finger protein {ECO:0000313|EMBL:BAE93279.1};
DE   Flags: Fragment;
GN   Name=Ci-ArfGAP-5 {ECO:0000313|EMBL:BAE93279.1};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|EMBL:BAE93279.1};
RN   [1] {ECO:0000313|EMBL:BAE93279.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16519883; DOI=10.1016/j.ydbio.2006.01.024;
RA   Miwata K., Chiba T., Horii R., Yamada L., Kubo A., Miyamura D., Satoh N.,
RA   Satou Y.;
RT   "Systematic analysis of embryonic expression profiles of zinc finger genes
RT   in Ciona intestinalis.";
RL   Dev. Biol. 292:546-554(2006).
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DR   EMBL; AK222397; BAE93279.1; -; mRNA.
DR   AlphaFoldDB; Q1RQ06; -.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IEA:InterPro.
DR   CDD; cd13252; PH1_ADAP; 1.
DR   CDD; cd01251; PH2_ADAP; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR037849; PH1_ADAP.
DR   InterPro; IPR037851; PH2_ADAP.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR46021; ARF-GAP WITH DUAL PH DOMAIN-CONTAINING PROTEIN 1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR46021:SF2; ARF-GAP WITH DUAL PH DOMAIN-CONTAINING PROTEIN 1-LIKE PROTEIN; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 2.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          1..123
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   DOMAIN          125..227
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          246..348
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          374..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAE93279.1"
SQ   SEQUENCE   817 AA;  92817 MW;  39CC723F60E26C40 CRC64;
     TVGINTEAAK PGNKTCAECY ARDPQFASLT FGVFICGECS RFHRELSNGP NKVVEISKHQ
     WSNDEVTFFN AQGNGNVNSE FEKELPIFYH RPDKDDPTVI REQWIRAKYE REEFKLTSQQ
     SSYNQGSKTG ALFKRGKDNG RYHRRKFILK EPEGVLKYFI RYSDKTPKDV IPIKDLVSIY
     VVPGKMGNEN GMQLTYEKNG TRRNIYVYGE DGKTTSDWYH AIRASMVKHK YENFPVNEAQ
     RYLNIKMIKE GWMSKTGPKA KEKFRQRWFS LVGTLIWYYN EPLDPHPIGF IPLGSKTFGY
     GIMKGLPLRI TVEGCGITVH TPDRVYALIC SDIKSRDEWY TAIDQVLESC TNMWVQPGIG
     RLGSEKTLLE PAAQKPNENE NAASENLQSR TSPISKEVDS SPDMKESKTK KSKIKREGSI
     PSSPEVTIKH ESPKRVLRTH DSKLYSDDSG DDTAIRCKFQ LQSISDNDSE EDVVVVVQHR
     IEPKTTPKKP PRKHLKQNTS NEFLATISNQ TSSQENLTLE VSSDDQSGSY SFQPEPDSLS
     PLANKDWRKK TFSSFRRVAG NERKSVKQRQ GSVARRSSLT SIASTSTSME SKEICKPVDI
     TLVNQMDESL WFMVFQSEVD HEHLDSYVTP WIGAQIAEAP ASVGPIRIPC DFEIAIIDTA
     PGGFNLQRTT GPFYAEPGDV WEVEIPNDDG SAPEMFFHEG METEDGSVMV YSNIDNVKRF
     DVAVFKSKRK LFTRTGVKPG DSVPIKIQPA LHFMAVDSET YYNLENQELR SVDYIPKASI
     VKFNYRTTKL KVVAKKRGKT VYFTCEKPKS LRNQNIK
//
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