ID A0A195BAW1_9HYME Unreviewed; 1200 AA.
AC A0A195BAW1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
GN ORFNames=ALC53_07835 {ECO:0000313|EMBL:KYM81673.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM81673.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM81673.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM81673.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM81673.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-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}.
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; KQ976530; KYM81673.1; -; Genomic_DNA.
DR RefSeq; XP_018049800.1; XM_018194311.1.
DR AlphaFoldDB; A0A195BAW1; -.
DR STRING; 520822.A0A195BAW1; -.
DR GeneID; 108688164; -.
DR OrthoDB; 25601at2759; -.
DR Proteomes; UP000078540; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
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 CDD; cd00174; SH3; 3.
DR CDD; cd11800; SH3_DNMBP_C2_like; 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; 7.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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 Pfam; PF00018; SH3_1; 3.
DR Pfam; PF14604; SH3_9; 2.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 6.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 7.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 6.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 66..125
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 135..195
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 275..334
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 356..416
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 508..694
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 734..944
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1133..1197
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 136339 MW; 707E872A5305B54E CRC64;
MEPGTLARVL HDFFTTVDEE LSLPKGQYFV VHKIIDKHWC HGQSQDRIGK FPLNHLHKVE
IPPFYETERL FVSIATFPGQ EVGDLSFAEG ELIIGVRDIG SGWCMGRIDS KNGIFPLTHT
WELDTTLIKK TKNKSIKKRA KVKTTLKAQL DEELDLTAGE MVVVTEILDD GWCRGITEDG
REGIIPEGFI SYIEEDQDII DQEQITCTTE NNFTSFSTVH NSTIYKDFGE TSVNSYANLP
TEPTPNYFDL FPEMLPTTPN NTDSIQYNSH TNSVDIKPYA ITLYPFNAQF PNELSFGAGE
VVHLTRYIDS EWLEGLIDTT KGIFPLSYVN IIVDCAEAKQ YQIQSEVIPA KKDALEPNII
VKVLYTFDAQ MNGDLNVHEG ESVTVLEMTN EDWVKVKNKN GLIGLCPREY LSSESISEYS
LDSLQESNLE DFEDFVMIRH KEANIVVNEE PKRMSQPHRP APPAPAPGRV PLQKETIANG
EVSAKKEMWE NESAINNIVN MKQKNADQRQ NVISELVITE KEYVRDLKLT YETFNLHNPS
FLESKGIDVA TLFGNILEVI HVAEELLDMI LRAMKGCDEN LQTVGPCFVK MAEKLKSVYV
KYCGNHEAAL ALLKKYESNE EIMKVFNKGI ETLRRRIACF DMSSILIKPI QRIVKYPLML
YELIKCTEDN HPDKAAIMEA WETMTNVASY INEYKRRRDI VSKYLDNDNT LFSKMSKLSM
HSVAKMSTRL STRLSASLGL TNVASDTEFE ELEKQFRSIE KCTWQLVKDI EQCITYLSDE
AISGEAIAEL LVHYYQGSPT AEVKKLQDIR AIIWSQYIQD FKSYIEKTVS APLHFLATLL
EGPAMLVSKR HDKLLDYDAA ISKSEKYKES KIIQEELFTA KSNYEALNQQ LLEELPILLD
AAANILVNCI NAFAGARKLL SGKITKQYIS LCETTPHLSS QDVLESFLVN HNLIWNQITR
FAFAGTNTRI DEDQTQLSKQ TEEQRSSLRE KYTADKLYVV VEDISSTSTL EVDATRGTLV
GVIKKQDPMG NPARWYVDTG VTQGFLPSQK LRPVQRQSQH HDQITSDVAA AGRKSASPPN
LMSLDSPEKE IKKVFSSHLQ DLLSLDQEIK VYHNYSNVPE TPRVQVYQNI QNIHGEFYYA
MYDFAGNMPG TLPITNGQAL RLLRPHDEKG NDEWWLVENR NGKQGYVPRN YLSSPIKPKS
//
