ID A0A1Y2DPM7_9FUNG Unreviewed; 1522 AA.
AC A0A1Y2DPM7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=Rho GTPase activation protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LY90DRAFT_241571 {ECO:0000313|EMBL:ORY61129.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY61129.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY61129.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY61129.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) 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:ORY61129.1}.
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DR EMBL; MCOG01000060; ORY61129.1; -; Genomic_DNA.
DR STRING; 1754190.A0A1Y2DPM7; -.
DR OrthoDB; 1331137at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 1.
DR CDD; cd00030; C2; 1.
DR CDD; cd08368; LIM; 4.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 1..135
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 149..272
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 332..381
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 428..622
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1284..1344
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1346..1402
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1462..1522
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 758..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1522 AA; 174919 MW; 6406A62AC1578A37 CRC64;
MDRSLEQKYT IHRSLDIRIS EVKNVFSGEK QQNTYCTVHV NDNEIRRTPT VYNNTSPVFA
EHFEFNPLEP NFSQLKIMVW SDVTEKNDKN LNNDKDIDAL SRTLPTTICG DKALGQIIFP
LGFLKSGAFQ KEQWFVLQPT FENINKYNVS GDIRIEVSHT LNSNKTHRFE INIKQANDLL
RDSNGSLPDP YVACYLLPDL EGKTAQITTV KKNSINPVFN SKIVYDVDKV TENLEINVSI
WNWNKLSVNE FLGHCFVPLS DIPVNGSIDK RYTLLPKPAR IFHSSKNKGK GTLKSKRRFT
VVDGDTKISH RKFIQRLQRS DQKDNIPTTK RSHRLLDTKF YSLSFCGHCG GIIWVTKTHL
KCGNCNFCCH QQCAKYVSDN CGGVVTLLLK ITYNESFILP LEFYNSFLNV INENKYYLIE
LFGKLSSERE NAALSLIKIQ IKHDNFINCI KTLIEIEVSE SESSQTLFRA NSMVSKIIDV
YMKYTGLNYL SAVLKDIIHN IVENDLYIEV DPSKLDDKKK INESLYNLTK YLENILNAIF
SAEQAIPKDW RIIFSFIRNK VIEKYPTEYN VRFTSIAGFI FLRFFAPSIL GPKLFGLVKT
YVNERSTRTF KLLAKVIQTL ANLSDFNEKE LYMCPLNDYI NAKLPSMKKY LNDVCNEDVE
CNYSEELTKP LSDKLIGYEC SKLLKYYANI ESKLVESITS GNVLLLKKYI DVSTNLMEYV
NKLKKNEEML YEENLKKKKV SEIKISTLTI SSDKTYVNNG DENSIAEEEE DRSKKDVRSS
AISLMNDENI KYISEYYKND NFGEEDDSKF NKNLENRNTL YKSMNDVNLR NKANVDTIYH
STNDVNSRNN ANVNTIYYST DDVNSRNNAN VNTIYYSTDD VNSRKKADVN TIYYSSYNVN
TLKKKQEPSS AEIILSSEDS QIQAQVEAKS KAIEKKKLDR SRVLSMLSHI PQVGGVDFNY
LNTANGGNGG KIVPPPKDSQ NSPNHINNRE TLVAPSSPFD TTTTSRRTSK SPFDAPSSPF
DTTTTSKRTL KSPFDAPSSP FDTTATSKRI SKSPFDSPAS PFDARRISLS PYDDKRKAST
NPSSPFDVTN KRTSVKLMSP FDSPRKSISS NTTTTTTSPI KSPFDISVNP NSANSPSSPF
NESRRISTPN PISPFEKPTT NMRRSTISPF EMNKSTNKYN SPYSPIVDKE SYNRKLSNVS
ENENSSVTSS RKTSIQYEDL IPMIPRHMSA QDCNEFDQAQ GHIDPLNPLH VTQMNNPIDQ
EETIDIPESE INKEIYDKIS KNLKYCCMCR MQILSEYITF DNERYYHSEC FRCQRCDETL
TSNNCYKKDN WYYCRNCYLF EEGYCCNECE EIIEGPAINI NGKLYHQDCF VCNACGMKLN
KQYLAIDGRP YCKKDYLKFK GFLCGICGEF IEDEYITIFD RKYHINCKKC TLCGNTLNNK
SFFSLPQDPY IVYCEEHKKE LCTCHYCNLP IEDQMIRTIK KPTSYHTHCF KCLKCEKNLQ
NSDYFEKDEN IYCRNCYIEQ FL
//
