Q5TJ55

SS
Gene name
forD
Protein name
Formin-D
Names
Diaphanous-related formin dia4
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0282245
EC number
Protein Class

Descriptions

Formins are conserved actin nucleators responsible for the assembly of diverse actin structures. In a study with Formin-3, the autoinhibition mechanism involves the intramolecular interaction between N-terminal DID domain and C-terminal DAD domain. This interaction is disrupted by Rho GTPase that is able to bind to the DID domain.

Autoinhibitory domains (AIDs)

245-296 (DID domain) SS

Target domain

562-1130 (FH2 domain)

Relief mechanism

Partner binding

Assay

1065-1095 (DAD domain) SS

Target domain

562-1130 (FH2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5TJ55

Entry ID Method Resolution Chain Position Source
AF-Q5TJ55-F1 Predicted AlphaFoldDB

No variants for Q5TJ55

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5TJ55

No associated diseases with Q5TJ55

4 regional properties for Q5TJ55

Type Name Position InterPro Accession
domain Formin, FH3 domain 201 - 434 IPR010472
domain Formin, GTPase-binding domain 8 - 197 IPR010473
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 10 - 379 IPR014768
domain Formin, FH2 domain 562 - 1130 IPR015425

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.

3 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
profilin binding Binding to profilin, an actin-binding protein that forms a complex with G-actin and prevents it from polymerizing to form F-actin.
small GTPase binding Binding to a small monomeric GTPase.

2 GO annotations of biological process

Name Definition
'de novo' actin filament nucleation The actin nucleation process in which actin monomers combine in the absence of any existing actin filaments; elongation of the actin oligomer formed by nucleation leads to the formation of an unbranched filament.
actin filament polymerization Assembly of actin filaments by the addition of actin monomers to a filament.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVKLFGKSKK KEESPQSIDI AFQSILDEIG VVETEKKHLM ATMDTVRKQQ LIQSYSSKKF
70 80 90 100 110 120
SKNEFGNKSK KKSIITQSPH YFVDCLKNDP SKEVLTSLRV RLGNQPLKWL KEFLSLDGVS
130 140 150 160 170 180
LLIKVLILNE IKQVKNQEDI YKIAQCLHSL KLIMNTKFGL ESVIKQPTNI HSISLVMDTP
190 200 210 220 230 240
HLKTRIMVIE LLAALCVVNS KGLPLVLSAM DNYREVKREK KPFIHLFQGL KNPSGSLQAT
250 260 270 280 290 300
TFALINTLIS SSQSVEERQK IRNQFKKLGI TKVIEELEPE YANNPDLATQ KDLYEQECRW
310 320 330 340 350 360
DEQEQIENAR GDISDENPEA LVKAILDRTA GGPLYSSFTS ILRLLANSIT DQTKDQSLSN
370 380 390 400 410 420
YLFVEKVIGK MNNGESYLDD IGTFFGGGGG GDGSLDIAHV SGEKAVLIQK EIEDLKKQKK
430 440 450 460 470 480
RDQDKLAEKD KLLTKLAKRM RKMEEAIKLG KGLEYLNNQI EIESPPDSST STPQETTPGG
490 500 510 520 530 540
TKVPLKTSPV TKADLKHKLS TFTTAKAPNG VSDFLSGLDT TNQQGSTDAS QTEAGSGDGI
550 560 570 580 590 600
PLPPGAPPPP PPPGGKLAPS TPQLCSRPPS IKMKSYQWTR YRTRNVTNTF WKNVNLTKYN
610 620 630 640 650 660
DCLPHEQIEG LFGAAIFEKK EKELKKGSEV TVIDTKRAQN IGILLSRFKN VTHDAIYDAI
670 680 690 700 710 720
YSLDESILDL ETINQFIKYI PSKEEIDCII AFKQQQEQLP EEERMKLGKS EIFIDKISTI
730 740 750 760 770 780
PRLEQRIQAL HFKLNFPDKL YHAKPDIRKF NEAFVQLQNN NIFAIMELIL SIGNFINFGT
790 800 810 820 830 840
NRGNASGFKI DSINKMADTK SNIREKYTLV HYLIELLEST QPELLKVFDE IPSVVDAATL
850 860 870 880 890 900
SFNQSSSEIK LLRAGLIKLE KEIFVRQPKS VEPKPDDETI NNNGEDDINN TSSDEKTEGQ
910 920 930 940 950 960
QQRQGEEEEN DESESTGNSF ADSLKKKKSQ VNTNSTSDSK QSLEPLKDDD PLKLKLSEFL
970 980 990 1000 1010 1020
LASKTELDDT ETLIAETEVL FKSICKFFGE DSTKIQPEEF LAIFKKFNDK FIMSKKDLEI
1030 1040 1050 1060 1070 1080
EKSIKDKSTQ RKNEKERKEM EIKKSKLEMI HSKLKKIGSP SSSNRILASN ESSPTSSTSS
1090 1100 1110 1120 1130 1140
VVHQHDDEDE ETIKEYINNP SPSQQSNSSE EEGMMDDLLN LIRDGNFREL RRMNLQQKKP
1150 1160 1170 1180 1190 1200
VRTKRVIAKQ PTRPQALDTP SSTYSSISSI YDAEPLDMSD QEDEDEEEEE DEEEEEEEEE
1210
GDDDNDNDEE EGEN