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Database: UniProt
Entry: A0A2X0PQ12_9BASI
LinkDB: A0A2X0PQ12_9BASI
Original site: A0A2X0PQ12_9BASI 
ID   A0A2X0PQ12_9BASI        Unreviewed;      1902 AA.
AC   A0A2X0PQ12;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Name=BQ5605_C042g12048 {ECO:0000313|EMBL:SGZ31933.1};
GN   ORFNames=BQ5605_C042G12048 {ECO:0000313|EMBL:SGZ31933.1};
OS   Microbotryum silenes-dioicae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=796604 {ECO:0000313|EMBL:SGZ31933.1, ECO:0000313|Proteomes:UP000249464};
RN   [1] {ECO:0000313|EMBL:SGZ31933.1, ECO:0000313|Proteomes:UP000249464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; FQNC01000116; SGZ31933.1; -; Genomic_DNA.
DR   STRING; 796604.A0A2X0PQ12; -.
DR   Proteomes; UP000249464; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00052; EH; 1.
DR   CDD; cd00160; RhoGEF; 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; IPR013182; DUF1720.
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; PF08226; DUF1720; 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; PF14604; SH3_9; 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; 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; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249464};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          204..293
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   DOMAIN          237..272
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1018..1035
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   DOMAIN          1218..1277
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1581..1759
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1793..1890
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1449..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1541..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          638..681
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          709..761
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..586
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..787
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..893
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1002
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1072
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1339..1367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1902 AA;  207995 MW;  5C2C46FC7FB05672 CRC64;
     MSWLNQPYAG GYPGQQPQPG YLQSQPTGYM GQPMQQQPLQ GQRTGYAPQG GFQVSRVWPG
     VRAGPTGFIG QRPPMQQMQV QPTGYAPSML QPQPTGYPAP MQQRPMATGY PFQQQQPPPP
     QQQQPLMSQP TGMPGMGGGM QSQFLSTFMP APSLQPTSFI DPSQMQFAHS GHNGASLAQT
     FQQRNQAQTG HADVPIPWAL TKDEKKRYDQ IFRAWDQQGT GFIEGRVSKE VFGQAGLDQN
     DLMSIWNLAD VQDRGKLNID EFHVAMGLIY RRLNGNPIPQ TLPPEMAPPS ARDLDDSVGF
     LTNLLKNDNN QRSTNQDFDG GRGSMAKARS LHDTAPRRDR KDATVFRNDD DEARAVYKSS
     ARHLNRDQIR SRSETDSPSS DLDDIRNRLR TTRSTLDRSR DQDDEDEDLK DQLRNMKRRI
     QRVQDDIDHN LGSGRRTTAK EDERRKLERE LLRLEYEELP ELERRIKEKE RDKKRDQRKY
     ALERDSRNND SDRYGDRDRY STRKDPYESR SSSRRESPER GYNRGTYDNG DGREKRSRDR
     DDDHYTSPSR GITSPSRART EPPPPPPAPG SERATPPPPP PAPVAALKSP AVDTRSMTPT
     ERQAHIRAQA QARIQERLRA LGVAAPASGE NAVDTSVADR LEKDKAEAAA KAAKADEDLK
     AKELERQAKL EREKLRGVAI EQSINSQNEA AVEQVREEVN AAAPESMIAK AANEQLDVEE
     DALARREAQL KREKEERMAR IKQLEQEAHE AEENYARSKA MFAPKIAKVA PPPPAPRARP
     AAPPFRTAPA PASATKPAVD DDETAPPAPR AADPAPAVIS SFLSPPVARS DVGAVGASPS
     SESKNPFYRL QQGGASPAAT SAAPAASPSG KPNPFFASSS PPAGPPAPSA PLLAPVSPAQ
     TALRQPGLVV KPEYRSPPVD DDDWDAKEKD VDESDSDDEI GGLRAAQANL AAKLFQGLGL
     GPARPASAQG NTPTRSTAAS PDLGAPAAPP GPPAPSAPAA SPTPKAAPAF VVPTEAPPRS
     ALLGAIQGGL TLRKTETKDK SGPAVTGSVI DDPSPPVRTH RAPSPPPAFA GPAAQVAPAA
     NGGGSFGESH YNANRQSIAW LGSMAAVEGS SQNAQTFSNI ATVAEDEEPA EEAKSSTLPA
     IVAASNEDDP LAPFDMTTTH RMKSLFAFQG EGPNDLSFKE NLVLNVHPSK DPAGDWLYGT
     VESSGEQGWV PKSYVEAFTP QSAKALYAYD AASEEEMSFL EKDIISIVDS ADASWWQAEN
     NGLIKLVPAS YIELGSPISF SPRLYTPYRI RLPSRTSEAH LASALASPRL ETAMTRPHDK
     DQRLPMPSEN SRIFKVSGSR VADDSDSEIE TPDGGDPKER EAERLRVLEA AGLLVRGGPS
     ADRRKRRQAP ARPPTKPTTG SVSGGGEGNE ILAEESVNAD SAPEEDVDQE GRVKDAYDIY
     QRVMRELPPV PTTTSNRLSM VSDSTTPSTT AGSMLYPTSP PASPAPSSST VASSLATGAS
     IKDQWQATTS GLRAKLGRPR ESSSAALDHA RLHISGPIIG EATGSAQSKS QESATPSNFG
     ASWASMIDSG ALEIMPDRER KRQESMFELI TTEQAYVQSL QLTIEVFFNR LQPVIPAKAL
     QVIFANIEDI LLFDTIFLSE LEDRQRTARL YIDTIGDIVK KHVRGYECYR GYCVNQANAA
     RTLADLKRSD PQLRSFLEGS RIKGLELEHF LLEPMQRVTR LPLLLRQILR YTEQDHSDRA
     LLTQSLEIAE GILGVINEAV RAHENEERLV YLSDVIEFSH SIEARLDLTA PTRLMGLRRL
     LKEDRVTKAR SGRKLNVYLF NDLLIFTETK AGGNEVVYRW PIALEECIIR DQSRDDLTFA
     VAHRGDTINV RTSSARQCLL WTQEIEQARK ACLAAVQKRR GM
//
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