GenomeNet

Database: UniProt
Entry: G3XPW4_ASPNA
LinkDB: G3XPW4_ASPNA
Original site: G3XPW4_ASPNA 
ID   G3XPW4_ASPNA            Unreviewed;      2245 AA.
AC   G3XPW4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   03-MAY-2023, entry version 54.
DE   RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE   AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
GN   ORFNames=ASPNIDRAFT_128721 {ECO:0000313|EMBL:EHA27313.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA27313.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA27313.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Golgi apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
CC   -!- SIMILARITY: Belongs to the peptidase C48 family.
CC       {ECO:0000256|ARBA:ARBA00005234}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA27313.1}.
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DR   EMBL; ACJE01000003; EHA27313.1; -; Genomic_DNA.
DR   STRING; 380704.G3XPW4; -.
DR   HOGENOM; CLU_001112_0_0_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0019783; F:ubiquitin-like protein peptidase activity; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; 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   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR   PANTHER; PTHR22834:SF20; NUCLEAR FUSION PROTEIN FUS2; 1.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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.
DR   PROSITE; PS50600; ULP_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949}.
FT   DOMAIN          1191..1413
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1448..1665
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   DOMAIN          2019..2188
FT                   /note="Ubiquitin-like protease family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50600"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1078..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1133..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1702..1802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1817..1864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1092
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1135..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1702..1757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1773..1802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2245 AA;  248506 MW;  1EFE7AE6763B83C1 CRC64;
     MSEGDVEHVS GLFDGSPRQF QRLSSQSTTD YFYDALSNGA REDHLAALSS TPVPLSGKAY
     PTQPGLTNLQ PFPPPTSIPP EGHPNSYDRS SPDPDDYYRP HLPTVAANDE EDLDLSAGHP
     MLEVGSDAAA DNRPKPFQRV SSVPIHLLES TSAGLSQYRS ASDSSYKSVG HEPTWGSSVR
     ASAARSGQTS FKDLINKFNN NVDQVLPVPS TSTVRSRVTS RAASPTSPTQ SSQSRALPRL
     RETHHLSSRP QSGHWQPRSV FDTESPSDLL AASLTTAGVD DNHSSTLASS DAIPRRPTLG
     EPLRIDTSPQ ISGYGNSSRI RRRGSDGIIP SPNPAFLDPF DPSAGVTPLT PTAWYLGRTP
     FLESVSTGSN TNPHRRTKSD IPGNWSIEVA ASPPDSHMAV PAPLQANSQA CPDNSPHTPK
     SRIPISSHRL NSPSVSDESP PPSRAGTHSG NRATVQVHLP PKGTSRLPKP SPKSPRDMPK
     NDQLPGYAAS PRAKREMAHS RSRQQLPERN ALLEAYIAAP PPKKSPPLRS SRPRQPIAHT
     QSSRSKVVET VSNFQRQINR DREYRTSRAR ERRLPELGHV DFATRRQKIQ QAFNRTVEEN
     ERKEEKAAEL RRQTKAQEDK PELAQASTAE PSQPTESEVQ PSLHADDNET VIEETVAAPI
     EESNQVPETK DPRPRPELHV DTDVHTTLEN VDGASDTHLM TMDSPTLGHA AIIERDLAYE
     PKSHGPPASD VTSESNETHV TAFDTEPQVE LSRKDLHTSH RTLLSQIMNI RESSPSSSSC
     DEQECSFSDN DERDPLPTRL RNAFAFDDQA DSSDNPESCD IYMRHGVMNG ETSNRWSMSS
     WSSSLRNQHS ADEQCDNSGD DFSHLQQCTE DSEVATQSCS ASSSTPSITD HKLLSSSSPK
     NGNAKEGRQE AVAHPNGFAF SNASSLARLG GWDSKRVGQL YLQELANGRG HGLPLPAIRA
     SPEPSQTYAD KETDQGSEGL TDDPVVVSRL RDPPALERPG HTASLVLRDD WEHASPSIMD
     WMQVAAAEDE SVLQAQNGNT GPVPDSATTP RLVTPNPQSS CSEEADEGLG LAIKVHQPQE
     LDSREKQLPS VPEPPEEDIP TQNIAPQQRT QPPSNVNATE QRLSTIISGI FAPLDPVQST
     GSSEDSSLRR LDPIPSPQTF DSSSTSLVPS TSEPSRLKAQ SPSPEQRRLK KRRHVIKELV
     DTEYTFGRDM KVVDDIYKGT SSSCLDLSSE DVKILFANSD QVVQFSMAFQ DALKEAAKSV
     YVMPKSQRWS SKRSARHHAS RTDSENSSTA GISDLDKDRM TYIGQAFMNQ MGYMEKVYAD
     YLKNHDAANK KLQTLQRNPK VAIWLKECRD WASDLTTAWD LDSLLVKPVQ RILKYPLLLA
     ELLDSTPDDH PDHPALVSAL EEVTNISVRI NEMKKRADLV GQVVGRKRKE SDVRAGLSKA
     FGRRTEKLKQ QVGLSDMVED KEYDTLAQKF GDNFFQLQLV MRDAEMYTRE VQTSMDGFNE
     FVEAIQGFVN VSPSNYAELE GRWRELKTTV AEIMTVALPE HIAVVRKSVI DPMVTLLKLH
     DGPQRVMRKR DKRLMDYARF KAAKERGDKP DKKTTEQGEQ FVALNETLKD ELPKLYALTA
     KLMEACLKNF VHIQTTWFRQ LQHKLGSLFE AFPEDIQKIV EDWSCNFNFS ESQVLSLGIC
     NGSLLADTVN LVNFNTPSTG ATINSPRRPS TVNSVSTRVG STMEDSPKVS QEFGNGSHSF
     HSPSFETQSQ VSHGRHRADS TFSGRTGHET AEIPRSQMLQ QITSTSTASV PASTSTTEAF
     PSLPRLSLDS PFLVDVIGPS SDGNGGAKVE EPPTSPDGRY SGFFSSAMPM SDNPQENAPA
     HSERPHEPAV LFLAASIYEF NIDRARREAG YPYLTYVVGE IFDVIAEKGE LWLAKNQDDP
     THQWLRMADD RRPTTNLQLR SSAIVSISPR FVNCWSLHHH LPYSPSFPSQ LAPDVLPYVI
     RAPQPGITNT NIPCLGVLNT MRDGGLGKLQ RRMRRFGDTL NPDDAYLSLT RGDMQSLKND
     WLTDNVISFW EEYLEHEFLV QYRSSNIVLL RPSMSFMILQ TPNPHSLREA LPDFSRTTHV
     FLPINDCRNV TEAEGGTHWS LLLISIVDGI AFHYDSLPPG NFWEARTVTM KFAALLGRPI
     NYVHLEDSPV QENGSDCGVF VCLSMRHLLL KRLLTANANE KVSMSLGGRK VDARSGRKEM
     AKIIEGFRKE GERRRSYVIE PPANN
//
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