ID W6QTY4_PENRF Unreviewed; 1855 AA.
AC W6QTY4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Actin-binding FH2/DRF autoregulatory {ECO:0000313|EMBL:CDM37604.1};
GN ORFNames=PROQFM164_S06g000566 {ECO:0000313|EMBL:CDM37604.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM37604.1};
RN [1] {ECO:0000313|EMBL:CDM37604.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM37604.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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; HG792020; CDM37604.1; -; Genomic_DNA.
DR STRING; 1365484.W6QTY4; -.
DR OMA; NHYWKAR; -.
DR OrthoDB; 1118745at2759; -.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProt.
DR Gene3D; 6.10.30.50; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR47102; PROTEIN BNI1; 1.
DR PANTHER; PTHR47102:SF2; PROTEIN BNI1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
FT DOMAIN 305..733
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1198..1621
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1637..1669
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1652..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1855 AA; 205578 MW; 02A2E6F76CE5CE20 CRC64;
MPTSSQADKP KQTSSGKSFF GRKLYKEKPT EERYDSYGAP YDGLAPPGSA GSRSSRHSKR
SSIQSVDMTQ DFDPSNIAHT SGVITSIPFE SLPTDTRTPI PIDNMSRPSS SRHEPSPNHL
GKAGNDYHQY PTVTSTSAPN GYVPYPGPRA HPHISNNTSY PGSNPGERGA RQQQQQQQQQ
QYQQQQQYQQ QQQQQQQQQQ QQQWGRPGSS SANNGPNHNS YSIDSSSNSR TSLDQASIYS
SVSSNTRGSS YFSSDNSSRT LTTSHSSDRP ALFPSSSSGR LSNAGSSHQI SVPAAIPRPQ
DNYLTRPRDD RIVDQLFLEL MQKRGWQNLP EQAKRQMLSY PASKKWTLVH QDRLTELQGE
QKRRQNARQT HGHDGMSGLL ERADEEGSPE WYVKKVMDDT ITSKQLASLS VSLRTQPISW
VKAFVEAQGQ IALTNVLLKI NRRKVSGPVP APPTGDKDLD REYDIAKCLK GLMNNKYGAD
DALEHQNVLV ALVSSLSSPR LNTRKLVSEV LTFLCHWGDG QGHLKVLQSM DKVKHDHNET
GRFDAWMRIV EVTIDGRGKM GSLVGASEEY RSGGIGMENL LMEYAVSTMI LINMLVDGAE
TDLQLRCHIR AQFTSCGIKR LLTKMEGFQY EVIDKQIERF RDNEAIDYED LLQREGSSMK
DSIEGEVKDM SDPMQIVDAI TSKINGSRSH DYFLSAMQHM LLIRENSGEE GLRMFQLVDA
MLSYVAMDRR LPDLDLRQGL TFTVQSLLDR LHTDAEARRV YDESLEARQI AEAAIAERDE
MRAQIELGAE GLVLKLQKQI DEQAGIIELQ QRQNESFKAE VAEIQRLRAQ ELQRNELETR
ELYLMLRDAQ DIAASNARKT NNHDMAEAAD PSQMPGIMDR ERLMERLERQ LERTKTQFKL
EGKVWGQHGP SDRLRELREK MEGEVDDSEY FAESTRRHLD PGALGSVYRK RSHIPTMDST
LEDEEDIPLD SNGEPMYERP RLVEMHRPRL NAAQTTGFLG ELASKVPRFE AEDPDVVEGE
QVPKLEDNEA ATKAMPPPPP PGGNIVPPPP PPPGVIALTP PPPPGGKILP PPPPPGGFSL
PPPPPPGGFT LPPPPPPGGK IGLPPPPPPG GMALPPPPPP GGAKGVPGLP PPPPPPGGRV
GVPPPPPPGG GGFALPPPPP VPGANGLMIP PPPPPSAALG TGWRPAYMVG DVSPSTIHMP
FIRPKKKLKA LHWDKVDTPQ VTVWATHAPT AEAKEEKYTE LAKKGVLDEV ERLFMAKETK
IFGASTGAKQ RTAKKQIISN DLSKNFQIAL SKFSQYPAEE VTRMIIHCDK EILDNSVVMD
FLQRDEMCSI PENVAKLMAP YSMDWTGPGA ATSDREQDPS EITREDQIYL YTAFELNHYW
KARNRALALT RTFEPEYEHI STRLKEVARV SESLRDSVSL MNVLGLILDI GNFMNDANKQ
AQGFKLSSLA RLGMVKDDKN ETTFADLVER IVRNQYPEWE GFLDEINGVI GLQKINVDQL
RTDAIKYISN IKNVQASLDA GNLSDPKRFH PQDRVSQVVQ RSMKDARRKA EQLQLYLDEM
AKAYDDIMVF YGEDNADENA RRDFFAKLSS FLIEWKKSRE KNTALEESRR RTEASLARKR
INVNLANSTP TAETVQSPAS SGAMDSLLEK LRAAAPQAKD QRDRRRRARL KERHNVRVTS
GTKPPPDSGE AEEGEDGVEK TTNGDNNDET GLLSPPSTAP EDGKQEAQVS EGEDVADRAA
SMLLGLRSNS DAGGGERQRR RRESADEERR NRRMRRRNPT GGSKDSADGS SGLATVQEPA
SPSQTDSMAT DDQQPPGSPN ESQPPPSIVV SEQGESSQDP SVAGSSPQKP TDLSD
//
