B0Y9Q4

PR
Gene name
myoA (AFUB_081890)
Protein name
Myosin-1
Names
Class I unconventional myosin, Type I myosin
Species
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
KEGG Pathway
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

923-1249 (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 B0Y9Q4

Entry ID Method Resolution Chain Position Source
AF-B0Y9Q4-F1 Predicted AlphaFoldDB

No variants for B0Y9Q4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0Y9Q4

No associated diseases with B0Y9Q4

5 regional properties for B0Y9Q4

Type Name Position InterPro Accession
domain SH3 domain 1076 - 1137 IPR001452
domain Myosin head, motor domain 45 - 731 IPR001609
domain Class I myosin tail homology domain 775 - 978 IPR010926
domain Fungal myosin-I, SH3 domain 1083 - 1134 IPR035535
domain Class I myosin, motor domain 65 - 717 IPR036072

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton, actin patch
  • Localizes to cortical patch-like structures
  • Enriched at sites of polarized growth, like the growing hyphal tips and sites of septum formation (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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGHSRRPAGG EKKSRGFGRS KAVADVGDGR QTGGKPQVKK ATFESTKKKE IGVSDLTLLS
70 80 90 100 110 120
KISNEAINDN LKLRFEHDEI YTYIGHVLVS VNPFRDLGIY TDNVLQSYRG KNRLEVPPHV
130 140 150 160 170 180
FAVAESAYYN MKSYKDNQCV IISGESGAGK TEAAKRIMQY IASVSGGTDS SIQHTKDMVL
190 200 210 220 230 240
ATNPLLESFG NAKTLRNNNS SRFGKYLELE FNTNGEPVGA NITNYLLEKS RVVGQITNER
250 260 270 280 290 300
NFHIFYQFTK AAPQKYRDLF GIQQPQSYLY TSRSKCFDVP GVDDSAEFRD TLNAMNVIGM
310 320 330 340 350 360
TEGEQDEVFR MLAAILWIGN VQFAEDDSGN AVITDQSVVD YVAYLLEVDA AQVNKAFTIR
370 380 390 400 410 420
VMETARGGRR GSVYEVPLNT VQALAVRDAL AKAIYFNLFD WIVQRVNASL TARGEVANSI
430 440 450 460 470 480
GILDIYGFEI FEKNSFEQLC INYVNEKLQQ IFIQLTLKAE QDEYAREQIQ WTPIKYFDNK
490 500 510 520 530 540
VVCSLIEDKR PPGVFAALND ACATAHADSS AADNTFVGRL NFLSQNPNFE NRQGQFIIKH
550 560 570 580 590 600
YAGDVSYAVA GMTDKNKDQL LKDLLNLVGT SGNQFVHTLF PEQVNQDDKR RPPTASDKIK
610 620 630 640 650 660
ASANDLVATL MKAQPSYIRT IKPNDNKAPR EYNVGNVLHQ IKYLGLQENV RIRRAGFAYR
670 680 690 700 710 720
QTFDKFVERF YLLSPKTSYA GDYTWTGDAE SGARQILKDT SIPAEEYQMG ITKVFVKTPE
730 740 750 760 770 780
TLFALEAMRD RYWHNMAIRI QRAWRNYLRY RTECAIRIQR FWRRTTGGLE FIKLRDQGHQ
790 800 810 820 830 840
LLNGRKERRR MSLLGSRRFL GDYIGVGNKG GPGEMVRNGA GISGSEEILF SCRGEVLVSK
850 860 870 880 890 900
FGRSSKPAPR ILALTNRHVY IIAQNLVNNQ LVISSERTIP IGAIKAVGAS NLKDDWFSIV
910 920 930 940 950 960
VGSPQEPDPL VNCVFKTEFF THLNNALRGQ LNLKIADHIE YNKKPGKLAT VKVVKDPAVA
970 980 990 1000 1010 1020
RDDSYKSGTI HTGPGEPANS VSKPTPRPKQ VSARPVTKGK LLRPGGPGGG PSKLAARPTP
1030 1040 1050 1060 1070 1080
AAQPLPRATP QPAEPQPAAR AVPQPVAAVA ASHTRTGSTA SVRAPPPPPP AAAPAPKKPT
1090 1100 1110 1120 1130 1140
AKVLYDFNSQ QSNELSIKAG EIVQIVSKEG NGWWLCMNMT TSAQGWTPEA YLEEQVAPTP
1150 1160 1170 1180 1190 1200
KPAPPPPPAA PRSTPAPATN GAAAAAKAKP APPAPPAKRP NMAARKAVPT PPPAPRDSAV
1210 1220 1230 1240
SMNSHDSSGG SGRGTPNSMS NASLAGGLAE ALRARQHAMQ GKQDDDDDW