ID A0A091D6H3_FUKDA Unreviewed; 790 AA.
AC A0A091D6H3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Dynamin-binding protein {ECO:0000313|EMBL:KFO25860.1};
GN ORFNames=H920_12778 {ECO:0000313|EMBL:KFO25860.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25860.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO25860.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO25860.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN123330; KFO25860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D6H3; -.
DR STRING; 885580.ENSFDAP00000007104; -.
DR eggNOG; KOG3519; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd07589; BAR_DNMBP; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd12141; SH3_DNMBP_C2; 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 Gene3D; 2.30.30.40; SH3 Domains; 2.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR PANTHER; PTHR22834:SF17; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 38; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 94..245
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 339..549
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 595..658
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 726..789
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 35..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 465..496
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 89611 MW; D29E9B62C1525030 CRC64;
MEPKDLPGKE NLGTKKKNLL FLRPRLYMLE RRKTDTAVEG AVSEDHAGVL RRSQSDRTEY
SQKLQEKMSP QAEGPAAASP TPEEELQMGS MMAKRAEVIK ELIQTERDYA NDLELCLREV
VRPLRDKEIE RLDVHSLFSN MESVHHLSAK LLSLLEEATA DVDPAMQVIG EVFLQIKGPL
EDIYKIYCYQ HDEAQSLLES YEKEEELKQH WGPCLQSLKG RPALLDMGSL LIKPVQRLLK
YPLLLWVAGR DGGLGLHPVS WVQEDGKHVH FVLSVDADLG NLEGSRALLC CVCSEMFSPS
SLSVLKYKKN DEDESLKDKL SKLNIHSISK KSKRVTNHLK ILTRGDSQVK DNTFNKEEKL
FRSLEKTVRQ CVKNISFCLQ DIQDALPFAL QRVTELQEMS QHPDQEELGS EETPRIAPDL
CHDFAVQLQR HVLNPLSALL SLFPGPQKLI QKRYDKLLDY NSYLQQSERA ESDLAKKEYE
ALNAQLVEEL QAFNQAAQTI LMNCLCSFVS LLRDLMLEAQ QGYATILPVP RLVSSLCEIQ
NQILVKVQNL NFVKENSATF IERKLSFEKK KSVQTQPEVP RQTDTHRSQL LSTYSAEGLY
QAKRKCNATQ EYDINLLEGE LVAVVEQKDP LGSTSRWLVD TGIVKGYVYS SFLRPYNPAK
AQKAETENRL CDEDFDNISF FVCSRPGSDS VTGTPEGSIS DSSSSLSGTC GKFETKGSDI
DSFQEVDEQI FYAVHAFQAR SNYELSLQEY QRVHILRFCD LSGNKEWWLA EAHGQQGYVP
ANYLGKMTYA
//