ID A0A1X2IMI4_9FUNG Unreviewed; 546 AA.
AC A0A1X2IMI4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Rho GTPase activation protein {ECO:0000313|EMBL:ORZ18989.1};
GN ORFNames=BCR42DRAFT_411993 {ECO:0000313|EMBL:ORZ18989.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ18989.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ18989.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ18989.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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:ORZ18989.1}.
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DR EMBL; MCGE01000008; ORZ18989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IMI4; -.
DR STRING; 90262.A0A1X2IMI4; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF134; ACTIVATING PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT DOMAIN 24..297
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 345..542
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
SQ SEQUENCE 546 AA; 61957 MW; 1EFF0FE394613594 CRC64;
MSVEEAQTRP SIAADTPSVN YHDDQNVISS LVDLDNGFQF LLDKVKLDMQ AAKDVSFFLK
KRAIIEEEYG KQMTKLTQSV TESFKSHPRS STFGSAWTSS LKVHENIGEQ RIKFASDITE
VADDLQLLVK DTEKARKHAK DIGSKQEKIL TDAELALDKS KQKYDMQNEE WERAILMKTN
DPYHVPKKGL FKSNKSQYQL NRSEEEAHNK AAASDHHYRQ QLQIVNSARQ DYFSTHLPEM
LAGLKTVGDE CCMALQYQLA RYAYIYERAL VADGYALDND SGLGLRSLAE KVDKDLDLMN
FIKSCSGQRN TGNVRVIQRG DVPYKEYIMS TAAHQILNPN PVFGIELSAL MKRDKQEVPL
IVQKCAEAVE KYGLQSMGIY RESGTGTQIQ KLKADFNRDC KQVNLDSDEN RSDINNVTGV
LKLWFRELPS PLFPQAAYDH FIAAAKIDDE RLRILGLHTV INDLPDAHYA TLKYLMGHLN
KVRQYEQYNK MGSSNLATIF GMTLMGDLSA GSLNSSGQHR LADTHLHVRV VQTILDHYRL
IFEQDE
//
