ID A0A316YTQ6_9BASI Unreviewed; 2314 AA.
AC A0A316YTQ6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=FA10DRAFT_259679 {ECO:0000313|EMBL:PWN92512.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN92512.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN92512.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN92512.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KZ819635; PWN92512.1; -; Genomic_DNA.
DR STRING; 215250.A0A316YTQ6; -.
DR InParanoid; A0A316YTQ6; -.
DR OrthoDB; 2734911at2759; -.
DR Proteomes; UP000245768; 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 GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR003903; UIM_dom.
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 SMART; SM00027; EH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47473; EF-hand; 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; PS50330; UIM; 1.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 242..331
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 275..310
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1064..1081
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT DOMAIN 1293..1352
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1842..2040
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2250..2275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2013..2040
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..980
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1529
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2314 AA; 248758 MW; 36F5A65983498C0F CRC64;
MYGGGGPQQW GGQQPQQQPQ QQQQQQQGGY LQPGGYMQPQ ATGFMQQPQR PMMTGMPNQQ
AGGFLGPQQT GMGMGMGMGM GGMGGMGGMG GMGGMGMQPQ MTGMASMRQG YPGGPGGSGM
LGVPGGGQPQ GGRYLSPGPT GVAMRPQPTG YGGGGGGPMQ MQATGLMPQM TGMVMDPRLQ
LMSAQFLPAA QPFSGGPPMA SNMNFSSASM QPSNFQSSIQ QLSQQQQGSR EPKIPWALSK
EERKSYDSVF RGWDQQGTGF VSGDVAREVF GQSGLDQDKL MQIWHLSDTE NRGKLNLAEF
HVAMGLIYRA LNGNDIPNEL PAEMVPPSAR DLSDSVDFLK DLLKRDTNVR NTTGLNIPEA
GSNQGAQYGK SRSFHENPVV RQDATAYKHS DDSAGTGYRS SSRHLDRKTV RYGGESAAED
LSEMKRQLAN TQRMLDEQDD DKDDDDREVE KDMEELRFRI RRVQDDIDYY NRRGGREANE
NRRKAERELL HLMHERLPQL EKRLEAKDKK TKDKKAVESR ERDRRNDTYA RRGRYDDDGG
DYDYSDRNRD RDGDRDRDRD RRYRDEDSRG STPTPRSDDR RGDRSNDDAD RTRSPAPPPP
AAEPAARAAP APPAPPAVSA VAAPAPAPSS GPPKNMTPEE RQAWIRSEAQ RRIQERMRAL
GAAAPPSSSS SSTPASPVPD TTVESRLAAD RAEAEARAAQ ADAEAAAREE ARRARLEEQR
IEKERAAVST IKSELKAQEK SDAPPPAPVM QAAREEVDEQ EAMLKRREEV LQREKAEREA
RFKRLEEEEA EAKRQEEAFK ERQSMFQNQG KSAAGGLPAP SRKPKGGPPP PPPSRSRAPP
APAPAAAPAP PPPPPPAAPA APPAPAAPAA TEAGSAAPTT TTEGGSSTNP FHRMQGSATT
PSATTPGGTN PFFRGQPAPA SANPNLPAPQ RSTPPVSAVA SPAPAAAAAA TRAPPRAPTE
DDDDWGDDDR SHDDDDDDAD GPGSTTRATR QNLAQALFSG LVPSATPPPP PPPPPAPPAA
AAAAATAAPP AAPPAPAAPP APAAPPAPAA PPVVVAAPAP GPADRGALLG QIQGGLKLRK
AQTNDRSASS LAGAVIGDPS PPVQKYVPPP AAEEAPAAKA PAPAADDVQV NPNRQSVDWA
NNLAADQMNG KASVQPDEPS VVEEDSDDEN EGPEDVDGQS LARKEGVDGH VNGGIPTEPA
PTTDLASAAD AAGDKADAED GLADFDLSKT VRVRTLYQYA GQRDEDLSFE ENMVVLAHPA
KDGAPSDWWY GTLLTDAAGI KGTFPSAYVE DIEKPKQAKA LYDFVSSNPE EASFDEGATL
AVVDDSDPNW WKIEKTDKIL LAPATYMELA DRPAPAAPTR LEMGGTSHRS AAIAAPAEAA
GHKDKGFLTP STARTPVTPM YVHGDEVLKK KPSVLRQPSS SHLAAAPSVS VPGEGEGESI
GADGEEDVAM QEAIRASERD ERERSVARAR EDKDLKRALA LSRREGEEAE GEEEEDEEEV
SDEDGYSTTG WSSSEEEDEE DEQGGGGEEE DEEAREKRAA ERLRVLEAAG ILIRGDAPKG
KAAAAPAATS GGEEPAETLD ADPLAKEEAQ ETEEQLLQRK RTRRGPKPER PERKGSRRPK
KPQRAPPAVP PPVPASSTST SNIPVDGKHE VGPAVPAKDA PEVEMDDAYA RYVEFTQEVS
AKRPVETPTT PAASSSRHSG LFSSKRIPSL STTSPPSSPP PAASASGAGE SSRGSGFLST
IMSMSSRRGA ASPAERKATP TISGPMALGS PVPSPAPGEK PMPDRTSLIS NSSTSSSSQA
TTLATTTDSA AQQPSMTTTS WSSQLGGDNG DFLAQMPAKE RKRQEAIFEL IQTETTHVRD
LQVIVEVFYS SLIAPQLDGQ PPALTDKATT VIFANIEDVL LAAVSLLSDL ETRQRESHLI
VDRIGDVLQT HMERMAVYIP YCVNQSTAAQ ILEAERKRNK SLESQLALLR TTHPKARGLD
LASFLLIPMQ RLTRYPLLIS QIVKYTEAEE GEVAIFEQEV DSLKKSLREA QSLLDTTNET
IRLRQDHERL HDISRKLYIG SSEGKNGSVH LDLTQPTRFM GRRRILRDEV LTKQRSGRKI
SVLLCSDLLL LLVEGISSSK SANGGGPTTV TRLYRMPMPL EEIVVGDAPN VAKAFSANPR
DDAAFQVVHQ GREKTNLRCQ SARHAHLWMR DIDVARAACL AAARRNIERK KFSALANSAS
CQDRHLLRQE DGDDEIEESV RYFNGQACRE EGDNEEKVDK GSGESHFRRS KSEEKYHYGR
RRWDPLANWA RDQDRQDYLG WGGADEVEEL GPGI
//
