ID A0A0P9EYU8_RHOGW Unreviewed; 1799 AA.
AC A0A0P9EYU8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1 {ECO:0000256|ARBA:ARBA00015110};
DE AltName: Full=Actin cytoskeleton-regulatory complex protein pan1 {ECO:0000256|ARBA:ARBA00020728};
GN ORFNames=RHOBADRAFT_55867 {ECO:0000313|EMBL:KPV72399.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV72399.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV72399.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV72399.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KQ474087; KPV72399.1; -; Genomic_DNA.
DR RefSeq; XP_018268448.1; XM_018418059.1.
DR STRING; 578459.A0A0P9EYU8; -.
DR GeneID; 28978507; -.
DR OMA; DATVYKY; -.
DR OrthoDB; 2734911at2759; -.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00052; EH; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR46006:SF5; DH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF12763; EF-hand_4; 1.
DR Pfam; PF16652; PH_13; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF02205; WH2; 1.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00027; EH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 183..272
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 216..251
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1022..1039
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT DOMAIN 1179..1238
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1483..1662
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 14..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..932
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1799 AA; 195446 MW; 326B555435F0C03E CRC64;
MSWMNQPYAG GYGQQQYPQP TGYMPQQLQQ QRTGFAPQPQ FQQPQPTGFA GQGAMGGMRP
PVPMQPQPTG FMGAPMQQRP MQTGYGGPGA PAPLVPQATG FNSSGLGAGV QNQFLQTFLP
AAQSHPSAYM QPGQMQFAAQ QQLQAQPTGV APAPSLQQQF QQSNQQQMGQ ASVPIPWKLT
PEEKKRYDQI FRAWDQQGSG FLPGSMAKEV FGQAGLQTDD LMAIWNLADV SDRGKLNIDE
FHVAMGLIYR RLNGNPIPQT LPAEMAPPSA RDLEDSANFL TSLLKNDTNR RATNQTDVDG
PQSRAKLRSL HESGPSGSSR KDATVYRNDD DATPVYKSSS RHLNRDDVRS RSTDSPTSEL
DEAKRRLREA QREAERSREE DDDEEDLKEE LRRLTRKIQR VQDDLDDNRR SGRRTAAKDE
ERRMLERELL RLEHDDLPRL EKRLEDKERE KRLDRKKLAI ERDGRNGPAS RRYEDKYDRE
RYGSSSRYDD DERSYSSSRR RGDDGDDGED RGYNRGTYDR DDRGRYAPSL PRRQSPSARS
RTPPPPPPPA PSTAKIDAPP PPPPTAPPTT AAAPAAPDTR SMTPEQRQAF IRSEAQRRIQ
ERLRALGVAA PSAANGVDTS VQDRLEADKL EAARKAAEAD EQLKAKELER QAKLDRERAK
GVAVEQALQD TQRESHAVQQ VRDEVERDAR ALPGQSNGAE PRQAVAAAED QLDAEEKALR
EREAQLERER DERRRRIEDL EREAKEAEDN FARSKAAFQQ ASTKPKTAPP PPASRKPAPP
PSRKAAPAPA PARPQQDDDD DFGAPPPRAS APVASPPPAP PAPPIPPVAP PAPSASATTL
SPPPSIASPQ AKSPSTNPFF RLQGAGGGAS PAAATAQAGK PNPFFAAGGA PAAAPPAPVA
PPAPKARAPP ADDDDWDAPA GLERDVDESD SDDEPIGGAR AQRAALAQNL FSGLGMGGGR
SSPAQNTTPP TRSAVATPAP AAAGGAPPPP PPPPPAAPSA PSAPPAPKAP AVALGGAAGP
ADRGALLGAI QGGLRLRKAQ TVDKSGPVGA GAVIGDASPP VQTYAPPPRE PTPPPREPTP
EPAAPEVEPE QYGANGDGAE TLPAIVSEDP LANVDLSKTI RVRSLYDYDA QRPEDLGFVE
NRVLLAHPSR DGAGDWWYGA TEVDGNTFGW FPKAYVEEIN AQPARALYAY EATSADELSF
EEDAMLAVVD SSDASWWKAE KDGVVGLVPA TYFDLSKELV VASSAVPVLL DAPLSPVPPT
SPSSPTSPTD ADLSDDDADS DDEGAVAARE AERLRVLAAA GLLVKPAARP GSPKRRRRPP
PARPQRRPGS MAVAIEEQAR ASDEQKDEQG EREPELEEEK MEDAYDLYQR AMREQRTASL
APTVDSPAVP QPSPPGSPTL STAPSTTAAV KDAFQSSVSG FFNRRGRSAT VGSEKARPII
SAPLAPQGDN TSRDSRASGA FGSTWASLVD EAALVDLPDS ERKRQEACYE LIATEQSYVQ
SLQLVIEVFL TALQPILPEK ALQVIFANID DILLFDTVFV SELEERQRQA RLYIDTIGDV
LKEHMRGVAR HYRLFCVNQS NAMRTLDDLK LSNAPVRETL DHLRVKNLEL DHFLLEPMQR
VTRYPLLINQ ILRYTPPDHP DHPALSRALE LAEAALNDIN EAVRAHENQE KLVWLSDNIE
FPGIPGGHLD LSAPTRLLGP RRILREGKVE KAKSRRQLNA FLFNDLLIFT ESRPGAGEVV
YRYPIPLEES SIRGADSEFS VTHRGEAIRV RAGTPRQAQL WVREVGAARR ACLEAVMRL
//
