ID A0A1Y3NUU4_PIRSE Unreviewed; 1440 AA.
AC A0A1Y3NUU4;
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=Ras-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PIROE2DRAFT_58155 {ECO:0000313|EMBL:OUM68274.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM68274.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM68274.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM68274.1,
RC ECO:0000313|Proteomes:UP000195826};
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.
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DR EMBL; KZ150774; OUM68274.1; -; Genomic_DNA.
DR STRING; 73868.A0A1Y3NUU4; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000195826}.
FT DOMAIN 1..268
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 279..346
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 620..740
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 797..991
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 460..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..161
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1245..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 165566 MW; A63D47C9AFEA9950 CRC64;
MSFENVYRYT NESINLCHDV LDFYKRKKDI EFQFSQSLSN LCQTYKNQYY NIINQQQNTP
ELQIKSHLLQ NTLWKTFINQ IEEFEQIARY HRTLAVSYED SVIHPLYNDI EDMEVNQKKI
VDNGLEKVKV LQNSYTELKK KKEIYKEAQE AAKEAAEAHN KGLNTYNIKD KELEKLTAKY
QNCLEKVNYA KDGVNICEKI CKKHQEQYYF SDLPVILENL KSKEEERSYN LKKLFIEANK
IEKLSIQYIV NINNTVAEGL KDIDVPGDID DFTQQYSVKP KEIIDLNDVS IHLLDDSYFN
ISNSFQIVVY NNITDKTRRK AFAYYFVAES AADRKEWFSY IRDVAYCCQT CNITKMILYE
YDMSIKGHNN GGGSRTPILM NRASEMSDSN YSKSNSHNLD CDCANKNLNC HRKTPIETSE
KNLKIDKSLM TFAEALGDPS IFLCSSENDE ETNDLLKKSI SISPNGSQTS LNKPMTKSPG
NSQLLSHEEP QNVFNKGSTI AQRFYEHNVK DKKLNRYSAS FLESPKPVFG SNLKRETSLE
VNGNNGSNLK KDTSFFKMIK NNQKNLNVYS IYNSASEGSI DNLSTSTSRQ NCRYSIISNI
SPTKMSQYSM SNTYANNNAS DDNMNSMFDY LNDKNKYRIN RSIKLCMLEA RNLYSNEKKK
NIETYAFIFF DDIVQAKTSK QVGTNPFWGE EFNFEHVLPC LNNIHIIICQ QHRVSNDSEI
GHIIIPINKL HSNKKVEEWI PIMPLNSNSN NFNASVRISV TLTDEHILPI EDYNEFLDYV
FQPSLEPVIR LGNVVQQREE FAKTLLYILI DKQKEVEGIK TLVSLEIKNT DDPNIIFRGN
SLTTKIIDQY MKLIGSRYLN NTLRRQVQNV YSLKESCEVD PSKMDKSEDI KKHWKKLLGH
VNSFWDAIRQ SIGKCPSKLK EIFNFTKMEV AKTFENENTV QYSSISGFIF LRFFCPAILS
PKLFGLAEQH PDPVTARTLT LIAKILQNLA NLTEFASKEP HMGESNHFIK NHINEMKYFI
DAISISPDKE EENAVVDYDV RSQCEKFYRF YRSNSKSCFS TKDPDDKKLL NIIQNISNIH
IKYREDLLNY QVSSEDKSIR KILNNSEISL YDLINEDEGE AETKSTTGGH IKKELSNFVI
DEYAKNEMDD SLKNIIFTIR RFSAQYNRKD NNPKRQYNTI TKMTGLNQFS PYMEEIFSPS
HRSSMIYGTP NNDAIKSDEY DSKSVYSTHS LNELNVNSTK IVGTSNNSLH SNSSNSIHSN
SSLVSGNRSR EMNHLAPEED ENELLSLEEG LNILNTTPPS TSNNNIQSSS YLDKKIKSSD
VSRSNSQRSS TTPHFIKIFT SREDNSSNNS SAVASPIMSP IDGPSYTLTS GNDGDAYQNA
LYSPNTKKRF PLATMKRKFS STVNSLTGGN SHMTNIHRDH VKRWMLVFQD EDLGIKMKIN
//
