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Database: UniProt
Entry: A0A267FGX4_9PLAT
LinkDB: A0A267FGX4_9PLAT
Original site: A0A267FGX4_9PLAT 
ID   A0A267FGX4_9PLAT        Unreviewed;       912 AA.
AC   A0A267FGX4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=ANK_REP_REGION domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BOX15_Mlig027582g1 {ECO:0000313|EMBL:PAA72319.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA72319.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA72319.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA72319.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA72319.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC       {ECO:0000256|ARBA:ARBA00005430}.
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:PAA72319.1}.
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DR   EMBL; NIVC01001098; PAA72319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267FGX4; -.
DR   STRING; 282301.A0A267FGX4; -.
DR   Proteomes; UP000215902; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08204; ArfGap; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   PANTHER; PTHR45819:SF5; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          568..682
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          699..819
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          290..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  97767 MW;  7D7FBCC6FEFAE9AB CRC64;
     MTASGKDSDS FELLESAIKE EIQRFESVHP CIYAIYDLIE TISNRELKDA IHNNLVTIED
     AFVNSQEWTL NRNVKELKLG LLGSADSGKS ALVHRFLTGS FLQDASPEGG RFKCRVGLSG
     APHLALIRDE AEPPSPQFAV WCDACLLVFA AGRPGSLVAA ADLRRRLADV RRPPDLPLIV
     VGVLDSASES RAQAEAVSRR QAAAAAELGL RQEDMVYFEA SVATGYNVER VFTEACQAAL
     AARRNRGLAE LPAAGDATPV AFAARRETPQ PPAPPARFPQ PAPELDFARS TEKVAHSRNG
     SAVSLQQQQQ SAAAPRVSRD SRFPTVTSAV AHWLMLGSML AWAGGVSKYL HKYQASPRYV
     SKLLTTQPKT PICIGIMTAL EPTPIPKPIC MENNKTHCVQ SAEPAASVKL RPKPAVPQRL
     SRQRPSSQLL QTPPSAAAAV SGDVTEPHVT LRPKRPSTRR ASSVAAESRK NLTATRPQQQ
     QAATLAANPL PVEVEIRTRN AVNQAAQDRR QPAAPAAPPP QIPLRDKRSS QLHPESAAPQ
     SQPQRRSHLF GSSPDAAPAV SVGPGRAIPV KQGVLAKRCT GGISSEWRRK FVTLGEDGRL
     TYYASLHEYM ENGRGRCVDL GQATVRLQEH PHHHHKRGKS GGSGSEAAGF ELVTLDGRVR
     QFEAPNRDVR DAWVTALRAA TLGRLRAGRD GDVDGNDAAA LLDAARRLPG NERCADCGAP
     QPDWASVSLG LLICLRCSGA HRQLGTHLSR VRSLHLDSWT TGHALPLSVV GNALGNGVWE
     ARLPPGARPS PGADSAEWEA FARAKYERGD FLPEAARPSD LADAAASGDT RRLLAALARA
     SPADLDAVPA DPSRLPPLHA CAAAGSRAHL QLLLWRGASP GARDRRGRTA SDCARAAGHA
     DCEKLLRLAC SS
//
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