P78621

SS
Gene name
Sden_0378
Protein name
Cytokinesis protein sepA
Names
Forced expression inhibition of growth A, Protein FH1/2
Species
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
KEGG Pathway
ani:AN6523.2
EC number
Protein Class

Descriptions

(Annotation from UniProt)
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments.

Autoinhibitory domains (AIDs)

1581-1613 (DAD domain) SS

Target domain

274-702 (GBD/FH3 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P78621

Entry ID Method Resolution Chain Position Source
AF-P78621-F1 Predicted AlphaFoldDB

No variants for P78621

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P78621

No associated diseases with P78621

5 regional properties for P78621

Type Name Position InterPro Accession
domain Formin, FH3 domain 490 - 718 IPR010472
domain Formin, GTPase-binding domain 273 - 485 IPR010473
domain Diaphanous autoregulatory (DAD) domain 1581 - 1613 IPR014767
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 274 - 702 IPR014768
domain Formin, FH2 domain 1141 - 1658 IPR015425

Functions

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

2 GO annotations of cellular component

Name Definition
cell division site The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
mating projection tip The apex of the mating projection in unicellular fungi exposed to mating pheromone; site of polarized growth.

2 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
small GTPase binding Binding to a small monomeric GTPase.

3 GO annotations of biological process

Name Definition
actin filament bundle assembly The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
barbed-end actin filament capping The binding of a protein or protein complex to the barbed (or plus) end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
mitotic actomyosin contractile ring assembly Any actomyosin contractile ring assembly that is involved in mitotic cytokinesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPTSDKSRQT SAGKSFFGRK LHKERPVEDR WDAHGSWESL APPSSAAGSR SSRYSKRSSI
70 80 90 100 110 120
QSVDFGADID PSLLSTSAGP ITSIPFESLS TDTQSPIPVD YLSKAETSPR KEPSPGHLAK
130 140 150 160 170 180
GVGDFHQYPA WDPSAMRNHQ QFSHPTGPRP PPHAAGVAMS SSATGDKGAR YQQWGRPGSS
190 200 210 220 230 240
AGNAGLSHHS SSTVDSSTNS RMSIDQASIH SSLSSNTRGS SYISTDGSSR TTLPSHSNDR
250 260 270 280 290 300
SNYYAAMNSG RGSSAQGAIP PAQPRVQNTE QYLTRPRDDR VVDQLFLELM QKRGWQNLPE
310 320 330 340 350 360
QARRQMMAYP ASKKWTLVHQ DRLTELQGEQ KRKQKARETH GYDGPSGILE RADEEGSPEW
370 380 390 400 410 420
YVKKVMDDTI TSKQLASLSV SLRTQPISWV KAFVEAQGQI ALTNVLVKIN RKKVTGPVPA
430 440 450 460 470 480
PPSGDKDLDR EYDIVKCLKA LMNNKYGADD ALAHQQIIVA LISSLLSPRL NTRKLVSEVL
490 500 510 520 530 540
TFLCHWAEGQ GHERVLQAMD HVKNHQGETG RFDAWMRIVE VTIDGRGKMG SLVGASEEYR
550 560 570 580 590 600
SGGIGMENLL MEYAVSTMIL INMLVDAPEN DLQLRCHIRA QFISCGIKRL LSKMEGFQYE
610 620 630 640 650 660
VIDKQIEHFR ENEAIDYEDL LQRESSSTKD SIEGEVKDMT DPLQITDAIA SRLNGTRAHD
670 680 690 700 710 720
YFLSALQHLL LIRENSGEDG LRMYQLVDAM LSYVAMDRRL PDLDLRQGLT FTVQSLLDRL
730 740 750 760 770 780
HTDAEARRAY DESLEARQIA EAALAERDEM KAQVELGADG LVRKLQKQIE EQTGIIELQS
790 800 810 820 830 840
RQNEMLKAEL ADVQRLRAQE LQRNELETRE LYLMLRDAQD IAASNAKKSN MGEAETDPAH
850 860 870 880 890 900
MRGILDREKL LTRLEKQLER TKTQFKLEGK VWGQHDPSDR LRELREQMDG DAGPREAFEE
910 920 930 940 950 960
QARLNLSLNP VGSVYRKKTY IQGMEDTATE ELGQTDDEVV YAKARLVDLH RPRMDPEQAT
970 980 990 1000 1010 1020
GLLGEIAAKV PKIDADDAKD EGKPTESEQP AEGAATKGDE QGVDDTVAVD KATAAPPPPP
1030 1040 1050 1060 1070 1080
PPPPAHPGLS GAAPPPPPPP PPPPPGAGAA PPPPPPPPPP PPGGLGGPPP PPPPPPPGGF
1090 1100 1110 1120 1130 1140
GGPPPPPPPP GGFGGPPPPP PPPPGGAFGV PPPPPPPGTV IGGWRANYLA SQGAPSHAIP
1150 1160 1170 1180 1190 1200
VMSSIRPKKK LKALHWDKVD TPQVTVWATH GTTPQEKEEK YVELAKRGVL DEVERLFMAK
1210 1220 1230 1240 1250 1260
ETRIFGGGVA AKQRKDKKQI ISNDLSKNFQ IALSKFSQFP AEEVVRRIIH CDAEILDNMV
1270 1280 1290 1300 1310 1320
VMEFLQRDEM CTVPENVSKL MAPYSKDWTG PDAANTEREQ DPSELTREDQ IYLYTAFELN
1330 1340 1350 1360 1370 1380
HYWKARMRAL ALTRSFEPDY EHISAKLREV VRVSESLRDS VSLMNVLGLI LDIGNFMNDA
1390 1400 1410 1420 1430 1440
NKQAQGFKLS SLARLGMVKD DKNETTFADL VERIVRNQYP EWEDFTEQIS GVIGLQKLNV
1450 1460 1470 1480 1490 1500
DQLRTDAKKY IDNIKNVQAS LDAGNLSDPK KFHPQDRVSQ ITQRSMKDAR RKAEQMQLYL
1510 1520 1530 1540 1550 1560
EEMVKTYDDI MVFYGEDNTD DGARRDFFAK LAAFLQEWKK SKEKNIALEE ARRRTEASLA
1570 1580 1590 1600 1610 1620
RKRINVGLAN GAGAAGDAPV SPATSGAMDS LLEKLRAAAP QAKDQRDRRR RARLKERHQV
1630 1640 1650 1660 1670 1680
RVASGQKIPD LEGAEAPGSG GQNSGATDTN ATDSSLLSPT IQEPEGGSSP IASQSEDVAD
1690 1700 1710 1720 1730 1740
RAASMLQDML RNSPDPERTR RRRESAEEER RKRRLRRRNG ATSGSKDSND TTPLSPVTEP
1750 1760 1770 1780
TSTQGESAEP ENLSLSSPPN GEDPTLNPPT IVLSSDASDT PDDEHRPSTS