ID A0A081CHM8_PSEA2 Unreviewed; 1166 AA.
AC A0A081CHM8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Related to GTPase-activating protein beta-chimerin {ECO:0000313|EMBL:SPO46952.1};
DE SubName: Full=Signal transducer {ECO:0000313|EMBL:GAK66174.1};
GN ORFNames=PAN0_011c4396 {ECO:0000313|EMBL:GAK66174.1}, PSANT_04638
GN {ECO:0000313|EMBL:SPO46952.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK66174.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK66174.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK66174.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO46952.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO46952.1};
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF830078; GAK66174.1; -; Genomic_DNA.
DR EMBL; OOIQ01000011; SPO46952.1; -; Genomic_DNA.
DR RefSeq; XP_014655852.1; XM_014800366.1.
DR AlphaFoldDB; A0A081CHM8; -.
DR GeneID; 26305094; -.
DR HOGENOM; CLU_003874_0_0_1; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd09395; LIM2_Rga; 1.
DR CDD; cd00890; Prefoldin; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR23176:SF141; TRANSDUCER, PUTATIVE-RELATED; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053758};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 37..105
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 904..952
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 974..1165
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 544..651
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 698..760
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 180..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 127369 MW; 96141CE60FD40043 CRC64;
MAQDQLALRD RGAPLVPSSE LDDAPHNHDA DDELPEAYCG GCGRLIDEES VEEGVIQFAT
KLWHIECFRC AKCKNRVSTE RDDILLLSDG HPICGECNYS CNICNQPIME EAIMTGDESY
HASCFTCRSC HSKIEELVFA KTSQGIYCMK CHNERVARSR KHAEHKRAKA RREKQLQDAQ
NAEAKQQALS NTKAANNAPS PSSPPDQQPP SLPSKTPAAA STTPSASALP SPSPNAASLS
PWIHQGGSAA SAAASRPGSA GGKRPMHAPP PPNRDARSPA LGSLAKLEGR SLSANNASNT
SLASLATDDA SNPYETTAPL SPRKNAFHAT ISSPQGSPAA NKSRLPPFTD APYSSSSPTT
SPLKKSLPLQ ASPRTSSRPL QPPADRDALG VSLRSTTTAS TSPRNPLQAS ASSSRLSKVY
SFYDPDFLNL VESFGDFDSN DELRAQPPPV PELPASLPSA SAVTEPVNTK AAHDQTTTAP
LGTLLDEHDQ NNGADSPDSD QELLDEDRPR TQTPTGSLNE VSNKVRASMQ QARDGLVSMD
ISFVETILRD LEDTRQRMES LQTRYDRIRR ASQQAAHGFS MAKEEFEHEV NARHEAELEM
ARLRRQLAEQ ALKLATANSE KRQQEQLERR SQDVKASLKG MERDLAKLTV ERDLTVAEVA
ELMALQDGAA GPSSVLSSPN MARSSTSTSD AVITQNLATR LESVKNRYRK EIDELTMERD
SLLIEIEELK QSKELFLEEA QSLNAKNEEL NTVLGQLNRK IELAAQSRDQ LPPLPTIPRD
LASSATKSSG GFSFGSRHKQ LHKHTAHNAS ISSDAPPSSA GYDVSVDTAV QQVIQPGKIE
PAPVVKKFKW MKPKLSETTR NNVPPAGQVP PVPPKGGAGL AAPSASGSTT SMTRATSHDV
VVREHLFQPF NVLRPTRCFA CQKNMWGQSE MRCALCTQVC HSRCLQSLPV SCNQPYTRPD
ESVGDNAGPS MFGRSLVEQA AHEGRDVPLI VEKCIQAVEA FGMDYEGIYR KSGGTSQLKV
ITQLFERGNA FDLEDTDRFN DVSAITSVLK NYFRELPTPL LTFELYDELI RLVESKQGDA
GAKQEKMKEL VTRLPRQHFC TLQHLVLHLY RVQERSVDNR MNARNLGVVF GPTLMRSADP
SQEFAHMGGK AMTIEFFIDH APDLFT
//
