Q6FN18
Gene name |
MYO5 (CAGL0K03487g) |
Protein name |
Myosin-5 |
Names |
Class I unconventional myosin MYO5, Type I myosin MYO5 |
Species |
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
KEGG Pathway |
cgr:CAGL0K03487g |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q6FN18
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6FN18-F1 | Predicted | AlphaFoldDB |
No variants for Q6FN18
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6FN18 | |||||
No associated diseases with Q6FN18
5 regional properties for Q6FN18
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | SH3 domain | 1083 - 1145 | IPR001452 |
| domain | Myosin head, motor domain | 31 - 717 | IPR001609 |
| domain | Class I myosin tail homology domain | 761 - 962 | IPR010926 |
| domain | Fungal myosin-I, SH3 domain | 1087 - 1141 | IPR035535 |
| domain | Class I myosin, motor domain | 51 - 703 | IPR036072 |
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 |
| MAILKRGARN | KTHQEPAKRG | GNNIKKAAFE | TSKKKEVGVS | DLTLLTSISD | ESINDNLKKR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FLNGTIYTYI | GHVLISVNPF | RDLGIYTDAI | MKSYQGKNRL | EVPPHVYAIS | EAMYYNLKAY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NENQCVIISG | ESGAGKTEAA | KKIMEYIAAT | SSTHSESIGK | IKDMVLATNP | LLESFGCAKT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LRNNNSSRHG | KYLEIRFNSQ | FEPCAGNITN | YLLEKQRVVG | QITNERNFHI | FYQFTKGASD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NYRQTFGVQL | PEQYVYTSAS | KCTSVDTIDD | VKDFEATIKA | MQVIGLAQEE | QDQIFRMLAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ILWIGNISFI | ENEEGNAQVR | DTSVTDFVAY | LLQVDSQSLI | KALVERIVET | NHGSRRGSVY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HVPLNIVQAT | AVRDALAKAI | YNNLFEWIVD | RVNKSLHAYP | GADKSIGILD | IYGFEIFEHN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SFEQICINYV | NEKLQQIFIQ | LTLKSEQDTY | AREKIQWTPI | KYFDNKVVCD | LIEAKRPPGI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FAAMNDSVAT | AHADSSAADQ | AFAQRLSLFS | SNPHFEQRQN | KFVIKHYAGD | VTYDVLGMTD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KNKDQLQKDL | VELVGTTTNA | FLTTLFPNQV | DKDNKRRPPT | AGDKIIKSAN | ELVETLSKAQ |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PSYIRTIKPN | QTKSPNDYDD | HQVLHQVKYL | GLQENVRIRR | AGFAYRQGFE | KFVERFYLLS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PRCSYAGDYT | WTGDILEAVR | LILQDALIPE | KEYQLGVTQV | FIKTPETLFA | LENMRDKFWH |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NMAARIQRAW | RRYLQRRIDA | AVKIQRTIKE | RKEGNKFEKL | RDYGTSLLGN | KKERRSMSLL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GYRAFMGDYL | SCNESKSNGS | YIKRQAGISE | KVVFSFHGEA | LHSKFGRSAQ | RLKKTFILSP |
| 850 | 860 | 870 | 880 | 890 | 900 |
| TTLYIIGQVR | VQNAMQYTAD | YKINVNSILQ | LNMTNLQDDW | VGIVLANSSM | PDPLINLSFK |
| 910 | 920 | 930 | 940 | 950 | 960 |
| TELITHLKTL | NSKIQVKVGP | TLEYQKKPGK | MHSVKCQVSD | TAPKYGDVYK | SSTIFVRRGN |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| PANSKSKKKP | RKKSSGMSAP | TTQSSKTLAP | PRMSSNNQNT | TVSQSLNGGM | NVKPQTPASR |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| SAKKPAPPPP | GSKKPAPQPM | AKKPAPHPTP | QAQMQTQTQI | PASQSSATQS | SIPPPPPPPP |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| SKTSEPQFEA | AYDFPGSGNP | SELPLMKGDI | VYITKEEPSG | WSLAKTLDGS | KSGWVPTAYM |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| VKHEGAKAPP | PAPAVTASQP | AIQNQSQPAS | AQTVAATSQV | PASFGDGLVS | ALAARANKMR |
| 1210 | |||||
| VESDEEAAAS | SDNDDDW |