ID B6HMD1_PENRW Unreviewed; 1898 AA.
AC B6HMD1;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
GN ORFNames=Pc21g08730 {ECO:0000313|EMBL:CAP95770.1}, PCH_Pc21g08730
GN {ECO:0000313|EMBL:CAP95770.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP95770.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP95770.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Golgi apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
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DR EMBL; AM920436; CAP95770.1; -; Genomic_DNA.
DR RefSeq; XP_002567912.1; XM_002567866.1.
DR STRING; 500485.B6HMD1; -.
DR GeneID; 8317266; -.
DR KEGG; pcs:Pc21g08730; -.
DR VEuPathDB; FungiDB:PCH_Pc21g08730; -.
DR eggNOG; KOG3519; Eukaryota.
DR HOGENOM; CLU_001112_0_0_1; -.
DR OMA; DQVGWIW; -.
DR OrthoDB; 25601at2759; -.
DR BioCyc; PCHR:PC21G08730-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07589; BAR_DNMBP; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR PANTHER; PTHR22834:SF20; NUCLEAR FUSION PROTEIN FUS2; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT DOMAIN 1162..1386
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1421..1642
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1898 AA; 208309 MW; C03D2D41E05B7CF6 CRC64;
MSSGDEQGFD VRYRDPPFGR QSSAPAFGQS ANGHTTTSLD DSPTVSFSPQ AQSSTTYSPL
PSGFIRPHNP STSTNHLSSG DQLEDRSGRE SPDPADYYRQ RGSLPGTSNV REGYGDVRAG
MAAADYPIVG DKVSPLPTNV LESSRARRQP YRSTSDSPTL GAPSANVPPL YANPRSRQPS
FKDLVNKFNK TSDQILPLPS ASRPTSRAPS PCGSADGERN RVLPRRRQYR DSLPESITSN
PRAPVDSTPS SPEADKFGPP LDTKSAIPPP LFQRITESHP RRPLFGELLP INTQVNNGVL
SRLQQRRGSD GSIPSPNPAY LEHRDQYPAR SPLTPTAWYL GHTTSLEAVN PGINSTGKHR
RAQSDLDKIR KPLAEPWSPE MAVPAPLRQA KPGHGSPPGS PNSGIKSRIP VSSHRLVAAS
GPESLSPSSN PTFSTRSAAI TSPPKGSSRL PIPSPKQSPP RMPAEDPASF ATSSHGRRDL
TIGRTRNQLS ESSRRLQAYI AEPPPKKSPP LRSSRPRQPV SHGAAVSPRS KIGDRVLNLQ
KQATHSDSRS RPDRKLPELG KVDFDARRRH IQQAINRHSI NSGVQANQND RGPDGSTAAK
LRRRALVREQ ETHEDFKKSV DEPTITPTLP VTNSPSPDEM ATIVKESTGS VDCKENCVQA
VPKLHLNTAL PASDMAAPHT TMDSPTLGLP QGVNPTTSGE GQPINGDPTE SGATSDSDDT
HITTFDPEPQ SGLLQRNPSV SHRTILDQIM QIRECSPSDD SCDEPDCSLS ENDDRESIQI
MLGDTTYYNS SSSTNTQEIE RASTHPAQNG THLHNRWSMS SWSTGQNQHS TCDEHCSESG
DDSLLRGCET EPPTETCSAV STRPASIADD ESPPPIQDHG VMGPHTLQAS EQFRPNAFST
PPSLARLGRW DSKRVTQLYL EELTRGKGHH LGSAIYPSSE PRSHPSDTRT DGRPDSLTDD
PVVVPGYKAS NVSNRHSHTA SLVGRDDWEH ASPSIMDWMQ IAAEDDAMTP DTETDGRRTE
GVLTPRLVPS TTHDAGASNT NNGLGVSVDI QACNEQTESR AFPSSAFLPP SSTHQTDNEI
PGVQNPLKPS DHIGFDRSIQ VAPRPAGHSP GSSQDSSFQN LESIQSPAAP DSSATSLVPS
TEQTIRVERK DSPSPEQRRL KKRRHIIKEL VDTEHTFGHD MIIIEDIYKS TSLTVLDPDD
VKVLFANSDQ VAAFSDKFLR DLKQAAQSIY VMPKTLRWTS KRKRKNQPPE STTPSGDEVA
ELAGMSELEK DRATSVGQVF VGHMADMEKV YTEYLKNHDA ANKKLQVLQR NSKVGFWLSE
CQKGAMDLTT AWDLDSLLVK PVQRILKYPL ILRDLLDSTP NDHPDRAAIA NALEEVTNVS
HRINELKKRV DLVGQAVGRK RNQSDVRAGL SKAFGRRTEK FRQQVGLSDL FEDKTYDSLA
QKLSDGYFQL QVVMRDAESY SRDVQLYVNQ FNEYADSIEE VVGMSPSPYP QLESKWHQFK
MTVQELVTTA LPEHVAVVRK TVIDPMVELL GLYNAPQRVM RKRDKRLPEY ARYKAIKDRG
DKPDKKTTEQ GEQFLALNDT LKDELPKLYA LTTKLMTACL KNFVQIQTVW YSILQKKIGV
HVELFPNDLD RLISDFNSDH HLMEARMGEL GSCNGALMAH SLNLVPLSPS EQQNPMSPRR
PSTVNSSNAR PGSMTGDSPN VSRDFSVGSQ SFQSPQMESH SSRSSRYRAD SIMSGRVVPD
TPNQLLQQAI SSPAPARTSD VEPFPSLPRL SLDTPFLEDV INSSSHSSNA PTSPTDRYSG
FFSSAMPMSD VPSDTVVDGH FERSPPPVGP APLFCAASVY DFNIDSRTEG GYPYLTYASG
DIFDVIGEKG ELWLARNQDD AAGTVGWIWN KHFARLGS
//
