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Database: UniProt
Entry: A0A0B7MX32_9FUNG
LinkDB: A0A0B7MX32_9FUNG
Original site: A0A0B7MX32_9FUNG 
ID   A0A0B7MX32_9FUNG        Unreviewed;       836 AA.
AC   A0A0B7MX32;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=PARPA_03228.1 scaffold 7241 {ECO:0000313|EMBL:CEP09677.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP09677.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP09677.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP09677.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LN722188; CEP09677.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7MX32; -.
DR   STRING; 35722.A0A0B7MX32; -.
DR   OrthoDB; 5482027at2759; -.
DR   Proteomes; UP000054107; 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; cd00159; RhoGAP; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR046349; C1-like_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:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
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:UP000054107};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          9..73
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          540..588
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          639..828
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          76..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          216..264
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        85..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   836 AA;  92391 MW;  7E0B9AFDA97AA545 CRC64;
     MVVNEIIVPT CQGCCELIEE GAVVAFGDSL FHVKCFICAK CGECVDNKIN LLLLDDGRPG
     IYCTVCNKTR KADRQTKKSK ASDASQSSKE SLCQDQQLPQ PSCQQNQARP ISISPKLPTP
     DRSRSNSPVQ KAIMEVNSSC NSVLLEDFTF SFFENDSNEL NNLSNTLGAN LTLSDDKYTP
     QYRIKRASEI LQTSLRTSSL SKTSNEPSPS AQNDELIETR SRLKELEANY KVLQDASQQA
     LNEITQLKDD LEQESAIKKQ QELTIVSLMS KSNTLLSRKE VDKLAYVRIE LERACKELIH
     YRDKIATTLD EQVSNTTVFP NYQKSLKMQI KSLIQERNLL KSQTKDLATS RDEVIHEMVL
     LNTKIAELAT MNNDLSRRVI AKEEATLTAS PAMPLSNSPP LSPSRSSDAL SRIPPASAQH
     LRKPSNASST VLNASSKKSF ISDQTPTLFR LKKKGSTMFG KLGTVSATPK PSKLDIPSSG
     LLSSSSSSIF RATSKTIYNN PSYSSSLQSI NYQDSSALGK SSSKSFTNTS ISLSRAVHES
     HSFQPTFFLK PVKCGSCGDK IWSRSEYRCD GCGLSSHSRC LSKVSQQCTV ANTSSSLDLG
     SSSSFENASS PKTSSSDIEG KTLPQQLTKS TTDCSIFGSC LSEHVKTENR TVPLIVEECI
     KEVEKRGLDC EGIYRKSGGA AQIRAIQLAF EKGEDINLSD EVQYNDVCAI TSVLKQFFRE
     LSNPLLTFEL YDQFIQASAM DHGEEKTKAF SNVLQQLPMA HIDTLEMLLR HLVDVYKQSD
     VNRMSVKNLA MVFAPTLMRH SDTSKDFLDI SYKNATIEYL LLHKSELFSA PSPSTS
//
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