ID A0A0D2FDM6_9EURO Unreviewed; 1917 AA.
AC A0A0D2FDM6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
GN ORFNames=Z518_10325 {ECO:0000313|EMBL:KIX00187.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX00187.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX00187.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX00187.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Golgi apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
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DR EMBL; KN847483; KIX00187.1; -; Genomic_DNA.
DR RefSeq; XP_013267323.1; XM_013411869.1.
DR STRING; 1442369.A0A0D2FDM6; -.
DR GeneID; 25298396; -.
DR VEuPathDB; FungiDB:Z518_10325; -.
DR HOGENOM; CLU_001112_0_0_1; -.
DR OrthoDB; 25601at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
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; 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; PF03114; BAR; 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; 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:UP000053617}.
FT DOMAIN 1149..1367
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1799..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1082
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1917 AA; 211843 MW; 46852F28515744EA CRC64;
MPSAVSSQNN YYAAHHRRQS SQSQTNLPDQ IRNSPSQAQS PNRSLVFLPS TAYSPSQPVT
QRSRNSSFTT ASKSNPRLDT APSEDVTNDP HEFYRQYQDP FTNSSPVALH QEAIRTTALD
NEDEHPIAAR KSSFASAQSD EDKASRAARN SVGAHKLSVN TQRISNGNWD NGQTKPSTTM
PNVLRSRKTS FKDLVARFDA SPGDVPSLPT QQISRPASRT ASPMPYAPMD TSHSYGSSLP
QPKQPASRLS ESSRRMPTTS ARTGIRAPSN DKSSRPRGSS STAGPSPGAS NPEAPEPGRK
LLFGEVLLST SNVPAAGYGI YNARRRRGSE GSPMHSPNPM FPSNDGISQS QREATTRRPQ
SPSQSQSGRK HRRANSDFTG PQSKTFLRQS QSPSLMGMAT TSKHQAEPLA KSSAQSRIPV
STRHHRMASD SATISSANHP AIVSQLPLRV PDRGQSSSGP SPSGDRKPPS PRRRPHSPMQ
IKSPGRRTRV TGSATGEKSP SLRANIIAPP PKISPPLRSS RPRLPVSSAT TAASRAKMAE
KFQTMAKQQS EQKTYRRQRP PELSDIDLKA RRLKITQALS RSREGQELRG GGIETRSTSR
TNSVTPSLEG PDRPDQGVQE HTEIPAVVVN EAVMDTPDER SFYSPIQGQA GDQRAFTQNA
LKVVEDIDSP TLGHAEAAFN SIPLTLDTHL LPRRDEQEPY SAVTEGTMAT EATEATMIDA
EPQTDATRLQ TPGQSLLSQI NTLRSQSSNS PLSSTSPVSG ENSDHADEVS VHLMLRETTY
LDDDEAVEKG YRPFAPTAGP ELALSRSNEG SSWSSSIEDQ RESETREQTS SGPEVTPRQD
EEVANNIHSD SLSESSHSGI QDDAHGENYA SDAYTIVNLV LQQQTPSGVV DQQLVDDIYH
RIIQASPDLA DAENVDEEKV VRLCLQELDE YHSQWDRSEP LRPRSAQYFH PGPGRDAAGE
KAGISHASAD FPSSDHVVHP PPQSYRSHKY KSSLDSAEDW AETSPSVGDW MQFALKSPTD
AQRQHQQSSL THETFLHDGL EPPGQGHTDH TNQMSEPTPL AADPNIPRPP SHSPPPPPVA
KRPSIDQTWS APAGIKSVMA HPPPPARPLT AVSQISARSS LDQQVVPSSS STTRPSVEDQ
SPEHRRLKQR RHVLKELVDT EYTYERDMRV LCDIYKQTAE TVISDEDIKI IFGNVELVQQ
FSRDFLGYLK QVVYPAYVME KSDRRKNGDR ASTAQSSNAS IDLIEMTDAQ KDEKTTVGEA
FEAGMPEMEK VYTDYIRTRH AANKRLEALQ SSSTVRQWLK ECSENSTDIT NAWSLDALLV
KPIQRITKYP LLLHQLLEAT PDTHPDINPL RRAAAEISEV NVRINEVKKH TELVDQVLNR
KRKESDVRNG LTKAFGRRAE KLRQHVGINE MYEDGEYAKL KINYDNNIAH LFLVNKDCQG
YIEAIKEWVT RMCELAAAAE AWVDVGHTNY AQAESKLRQF AIVVRGINSI ALPDHIDQVT
KRVLQPMEKT TPLLEKFKSD SKGLIQKREK RLLDYNQFKN KKDKGEKIDK KMTERMEQWE
ALNLEAKERM KRLLRATADL VHSCQANLLE LHLNWLAMCK QKFSAAMEIP LDKLDKADIV
KDWQEDFDYQ EASALSLSIC NGSLLADAVN MLSFLTPGST LTGDDSPRQA SWNSGMNRSV
SMSNDGTQGL MTEQYRRHSG GPLSSQNEDP TDWSSATHVN GRIRAPSAMS GRMPETSSRT
VAASIHTVNS ANVSRPGTSL GQSEDHTRPA PRLSLETPSP SIGPLLTESP AAVKHTSMST
FYSASPGPSQ SQSHLPTSGG SIFSSAMPME DGIEPEREPE QREPRREPGV LFTAASVYEF
NIDRSRQQGG FRYLTYVTGE IFDVIAEHGE LWLAINQDDA TREIGWIWNK HFAKLAE
//
