ID A0A165TX10_9APHY Unreviewed; 1955 AA.
AC A0A165TX10;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=DAEQUDRAFT_720946 {ECO:0000313|EMBL:KZT74078.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT74078.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT74078.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT74078.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KV429034; KZT74078.1; -; Genomic_DNA.
DR STRING; 1314783.A0A165TX10; -.
DR OrthoDB; 2734911at2759; -.
DR Proteomes; UP000076727; 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 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; 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; 2.
DR Pfam; PF02205; WH2; 1.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00054; EFh; 2.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 224..313
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 257..292
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1097..1114
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT DOMAIN 1297..1356
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1631..1812
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1849..1943
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1005
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1955 AA; 214511 MW; CC16D83EB06F2FF2 CRC64;
MAQWGQPGYQ YPMQTGYNPQ QFQQGFQPSG GIAPQPTGFP GQRPPGFQQA QPTGFPGASG
FQQPQPTGFP GQQGPLLPQQ TGFPGASGFQ QRAPPPPPPV PPIPSQFQQN AGPQNSGFLG
LQSQPTGRFQ LTSPLQAQPT GFPGAGGLRP LVPQMTGFVD PRLQMMSSTF MPINTSMPYN
PAGAPQLPSA QLGGMSLQQN FQQHNQAQRG NAAPKVPWAL SKAEKKQYDQ IFRAWDAQGT
GFISGQTALE VFGQSGLDKN DLAKIWALAD VDNRGKLNLA EFHVAMGLIY RRLNGNEIPD
ELPQEMVPPS HRDLDASVTL LKDILKNDTR ARSPSNIDTP VSRLKERSFN SAGAAGAGGR
QDATVYKYTD DSPPGGFYQP RSRHIDRSTV RTTSDLENPV SDLDEMKRQL ENTAKMLDRT
TEENASRTAE DEALDREMED LRYRVNRVKD DLDYVSRGPR SQGKDEERRR LERELLKLMH
ERIPEVERKM KDREERRARE KREWARDRDR RNERFGRYDD RDDRYSSRYD DDRDRPYSRN
RDRDYDRDRD YDSRPYSRNR DRDYDRDRDY DRDRLRDYDR PRSPPAAARS PPPAPPSAPP
PSAIAKPPPP APTPTKSPAP NLKNMSDEER KAFIRAEAQR RMQERMAALG VAPAGSTSPK
LDTSVEDRLA LEKKEAEEKA RAAEKEAEER ERIRRERLDN EKALKGTPSP APPTPSPSAP
APPAPSVRTA TAQTPTPKPT PPPVKSRAPA PPPPRKAPAP KPPPPRAAAV APTPPVAFPV
PPAPAIPQED PEEAALRARE EAVRKQRERL ERLRQLEREE EEARRAEEEY QDRRRAFKAK
AAAPSPSVSS PPAPAPPPLA PPAPVPEISA AISSPPPPAP PAPPIPAATP STDRSATNPF
SRIMKEGPSP GSAGVSGTPA ANSGTNPFFK SQAASPPAEA PTLAPLPPPA PPTAPAPPRA
PSVPPPSKSP APPAVRTSYH TAPAGDDEDW DDLKENEDDN SSDDEIDSSR DTRNKLAQQL
FGSILPPSRP QSAGPPVSSP KTAASPQTSP PAPPPAPPPS APPALVAEDV PAAPPPPPMA
PAAPPPPAVA APAPSGDRSA LLSAIQSGAR LRKTQTNDRS ASGLAGKVVG DTAPPLHISS
APRAPSPPSS PELPEAAVPP SRYELPAGLP ELPSVSARSS NRDSVDWYAG LAADAGSTPP
EMSRLPSMAE EEEPTTPVPA IQVDAAENDA MADVDKSIDY HVRSLYPYEG QRPEDLSFAE
NLVIKANPSK SGGDWWYGTL LRDSKAGFFP KTYVEKIESV KAHALYSYEG SSPEELPFSE
GDELTIVDRS DADWWKAERD GVVFIVPAGY LEVNEASSFV LVPMADKQLP RLRMEAEDRK
QENTTGVGRE IPSFEPAQEE LTVESHEEGS SDDESEYASS SESDADDSEE DQTEEARAAE
RKARTLEHQR VLEAAGFIIK EDVKPPPRPP KKDRKRRPPP AVPDRQSASA HSRDTSADLD
VSGETDSSLR LDDAFERYEA FRNANPNMNR LSMASMDGSI SGPNASPTSP SFITRSSSTE
PESRIGLHLL SIFGRKTPGN DGEARTMPII SAPISRDNSS AGAEVDSAFG STWASLVDKS
VLEDIPTKER RRQEAIFELI LTEAAYVRDL QLIVEHFYAN LISVLEDKAV KVIFANVEDI
LIVNTTLLSV LEERQKECRL YVDKIGDILC SNMSEMGLYV EYCVNQAFAA KVLQSERDSK
PELAQLLQRL RDDSTARNLD LSSYLLVPMQ RITRYPLLIR QVLHYTEAAD DRRQIKQALD
IAERILSHIN ETIREQEGQE RLRTISKDLW IGQGRLDLTA PTRHMGPRKL LKEGVLMKAK
SGRRLRAFLC SDILVLTQEP AKQLYRTPIP LSQVRVQEVP GRRDDLVFQI SIAYPRGGDA
IALRTSSARD CQVWMQAIEK ASASCRDAEH RARGR
//
