A6ZZJ1

PR
Gene name
MYO3 (SCY_3251)
Protein name
Myosin-3
Names
Actin-dependent myosin-I MYO3, Class I unconventional myosin MYO3, Type I myosin MYO3
Species
Saccharomyces cerevisiae (strain YJM789) (Baker's yeast)
KEGG Pathway
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

893-1270 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A6ZZJ1

Entry ID Method Resolution Chain Position Source
AF-A6ZZJ1-F1 Predicted AlphaFoldDB

No variants for A6ZZJ1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6ZZJ1

No associated diseases with A6ZZJ1

5 regional properties for A6ZZJ1

Type Name Position InterPro Accession
domain SH3 domain 1118 - 1180 IPR001452
domain Myosin head, motor domain 30 - 716 IPR001609
domain Class I myosin tail homology domain 760 - 961 IPR010926
domain Fungal myosin-I, SH3 domain 1123 - 1177 IPR035535
domain Class I myosin, motor domain 50 - 702 IPR036072

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton, actin patch
  • Localizes to cortical patch-like protein structures that assemble actin patches
  • Enriched at sites of polarized growth (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
actin cortical patch An endocytic patch that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.
myosin complex A protein complex, formed of one or more myosin heavy chains plus associated light chains and other proteins, that functions as a molecular motor; uses the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments; has magnesium-ATPase activity and binds actin. Myosin classes are distinguished based on sequence features of the motor, or head, domain, but also have distinct tail regions that are believed to bind specific cargoes.

4 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cytoskeletal motor activity Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force).
hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

1 GO annotations of biological process

Name Definition
cellular localization A cellular localization process whereby a substance or cellular entity, such as a protein complex or organelle, is transported to, and/or maintained in, a specific location within a cell including the localization of substances or cellular entities to the cell membrane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGVSD LTLLSKISDE SINENLKKRF
70 80 90 100 110 120
KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKSYN
130 140 150 160 170 180
ENQCVIISGE SGAGKTEAAK RIMQYIAAAS NSHSESIGKI KDMVLATNPL LESFGCAKTL
190 200 210 220 230 240
RNNNSSRHGK YLEIKFNSQF EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDT
250 260 270 280 290 300
YRQMFGVQMP EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI
310 320 330 340 350 360
LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS HGMKRGSVYH
370 380 390 400 410 420
VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG ADKSIGILDI YGFEIFEHNS
430 440 450 460 470 480
FEQICINYVN EKLQQIFIQL TLKAEQETYE REKIKWTPIK YFDNKVVCDL IEAKNPPGIL
490 500 510 520 530 540
AAMNDSIATA HADSNAADQA FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK
550 560 570 580 590 600
NKDQLQKDLI ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP
610 620 630 640 650 660
SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK FVERFYLLSP
670 680 690 700 710 720
DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF IKTPESLFAL EDMRDKYWYN
730 740 750 760 770 780
MAARIQRAWR RFLQRRIDAA IKIQRTIREK KGGNKYVKLR DYGTKLLAGK KERRSMSLLG
790 800 810 820 830 840
YRAFMGDYLS CNESKTKGSY IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK
850 860 870 880 890 900
TFYIIGQTRE QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQP DPLINTPFKT
910 920 930 940 950 960
ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS STIYVRRGHP
970 980 990 1000 1010 1020
ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH RDAAKKQPLP SQKPVNPLSL
1030 1040 1050 1060 1070 1080
AATAAQAAYN PKPDKTVPIK SSAIPAAKVS SKHSSKPSSK EKVAVKKASS SHKSSSAKQN
1090 1100 1110 1120 1130 1140
QVSMPPSKGV EKNKEPLKET TATANIPIPP PPPPMGQPKD PKFEAAYDFP GSGSSSELPL
1150 1160 1170 1180 1190 1200
KKGDIVFISR DEPSGWSLAK LLDGSKEGWV PTAYMTPYKD TRNTVPVAAT GAVNDVTNQK
1210 1220 1230 1240 1250 1260
SSQIDNTISS AQEGVQFGSA TVGPTSDNQS NPVGTFSDGL ASALAARANK MRAESADDDD
NDDGDDDDDW