ID A3LZZ6_PICST Unreviewed; 1325 AA. AC A3LZZ6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 2. DT 27-MAR-2024, entry version 110. DE SubName: Full=Cell division control protein 25 {ECO:0000313|EMBL:ABN68625.2}; GN ORFNames=PICST_73961 {ECO:0000313|EMBL:ABN68625.2}; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL OS Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces. OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68625.2, ECO:0000313|Proteomes:UP000002258}; RN [1] {ECO:0000313|EMBL:ABN68625.2, ECO:0000313|Proteomes:UP000002258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545 RC {ECO:0000313|Proteomes:UP000002258}; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting RT yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000502; ABN68625.2; -; Genomic_DNA. DR RefSeq; XP_001386654.2; XM_001386617.1. DR STRING; 322104.A3LZZ6; -. DR GeneID; 4841059; -. DR KEGG; pic:PICST_73961; -. DR eggNOG; KOG3417; Eukaryota. DR HOGENOM; CLU_002171_1_0_1; -. DR InParanoid; A3LZZ6; -. DR OMA; LEISANC; -. DR OrthoDB; 68574at2759; -. DR Proteomes; UP000002258; Chromosome 8. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR CDD; cd00155; RasGEF; 1. DR CDD; cd06224; REM; 1. DR CDD; cd11883; SH3_Sdc25; 1. DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1. DR InterPro; IPR008937; Ras-like_GEF. DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N. DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS. DR InterPro; IPR023578; Ras_GEF_dom_sf. DR InterPro; IPR001895; RASGEF_cat_dom. DR InterPro; IPR036964; RASGEF_cat_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1. DR PANTHER; PTHR23113:SF99; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; 1. DR Pfam; PF00617; RasGEF; 1. DR Pfam; PF00618; RasGEF_N; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00147; RasGEF; 1. DR SMART; SM00229; RasGEFN; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF48366; Ras GEF; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00720; RASGEF; 1. DR PROSITE; PS50009; RASGEF_CAT; 1. DR PROSITE; PS50212; RASGEF_NTER; 1. DR PROSITE; PS50002; SH3; 1. PE 4: Predicted; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:ABN68625.2}; KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658, KW ECO:0000256|PROSITE-ProRule:PRU00168}; KW Reference proteome {ECO:0000313|Proteomes:UP000002258}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 27..91 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 883..1017 FT /note="N-terminal Ras-GEF" FT /evidence="ECO:0000259|PROSITE:PS50212" FT DOMAIN 1050..1287 FT /note="Ras-GEF" FT /evidence="ECO:0000259|PROSITE:PS50009" FT REGION 135..190 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 283..317 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 672..699 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1286..1325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 299..317 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 680..694 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1325 AA; 151628 MW; 1E1635C9B63A7C4B CRC64; MSHYMDEIAP DVISPHDTKP TVDQPLKHLD TVIALYDFPG TQPSHLPLNL GDTIYVLSKS DTGWWDGVLV GQTGELQRGW FPHHYVRSVN YVQPVLNKLK SNKELDSITA SNTAANVLIP SFTNLLQKNL IDSEKNTPAN STRKNSVVSF ASSETSIPSD SKGSSLPKHH SEASTQFSQH QPTSISHTLT SADFNNDNII FTDVEEAEQM ILEYKEKNKK NLTWIPRNTT SGDFVFYCEQ LNIYCQTMPM VPFELTDVTA EVEMPSKEAL TDKFDVQVYG TRSSSGDIGS RANSAGTFDP LKRDSNASSV TQSSGASSYH HFTKPFFSMD NLFYKHPSDL TRWSELREQY NYLLDLSSKS LKDHNKQLFS THFSRLNKVM SIILATSRLN QDDFFGTKYE RSIRRKLKRI AGAFAQLYIN GILHLSVMHH SQSTSEAQLF SFDIFKLNKS TSKAGSEAFS AHSSVSTIRQ NSNESTVPAS TGVNHDQQEM SYLSQLENDI ETLRSNVNSL VKIFMKLSED KVVKRSDYDS SDASEDDGQD RYDILPQTYP RFIVDEFNGG NWCNPFFTTN NPVLNVSGDD LKNRYHSKVI IDHSTYESVY QLSEEMIKLS KETLEYLKPQ AQKLYYNDVL KNERNTQILR LIYKYLYHGS SMVDLIESFD FTVFCLINRS SSGEEADPEG VRNQLNDENN QKDESRSTNT SNLTFDYPVV LDFFQLKQEF HNLILRIIMS TQSLTLDDPE VFKALRDEDP LFYNRDILKL QTEKAALLLT NILADQVNPN KGDSISLNPD TLMSTYLTEG IKFFDVLLGT IQQLIDERET ILNYATRVMH DDFNVQLLVI ERNNTLLSEK SEDHSYYSGG HKKSSDLPWY LEGDEEFDLL LDLKGNIKGG TKEALIAHLT HHDLFDSNFN AAFLLMFASI MPLSEFVGLL IHRFNLEAPE GLSYEEYNTW ITKKQNPIRL RVMNIMKLLV EKHWSKSYYN ESLLKRWIAF AQSPAVQSYS IGKQLTGYLI RILNGELIYI EREPVIPNTK PPASLTKGSS LKKLKLLDID YIELARQLTL REFRLYSKIT KFTCLAKVWG KKSGLNERFE NITAFIKASN QLTNYVAYMI LRKTDAKKRI QVIRYFVQVA EKCRQYNNFS SMTAIISALY SSSIHRLKKT WKYVSADTLS HLQSMNKLMN SSRNFNEYRD VLKFIGSEPC VPFFGVFLTD LTFVYHGNPD YLMNRTRMIN FAKRAKTCEI VTGIDRFKTT GYNFQTVPEI QKYLDSWFDK CPTIEEQYQL SLNLEPREGQ PSQHSQSTSS AVSGRDLPSF RNSKMSSTIT NLALK //