ID A0A165EFY0_9BASI Unreviewed; 1145 AA.
AC A0A165EFY0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Myosin-1 {ECO:0000313|EMBL:KZT54789.1};
GN ORFNames=CALCODRAFT_510525 {ECO:0000313|EMBL:KZT54789.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT54789.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT54789.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT54789.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex. {ECO:0000256|ARBA:ARBA00025586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KV424007; KZT54789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EFY0; -.
DR STRING; 1353952.A0A165EFY0; -.
DR InParanoid; A0A165EFY0; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 41..724
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 782..969
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1061..1119
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 597..619
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 946..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1145 AA; 128009 MW; 5CF5C49EA0846BB6 CRC64;
MAISKKSGKK GAVAVAKPVK KSAGQQFVKA DWKEGFKKKQ TGVSDMTLLT TISNESVNEN
LQKRWLNGEI YTYIGAVLIS VNPFRDLGIY TRDVLDSYKG KNRLEMPPHV FAIAESAYYN
MKAYKDNQCV IITGESGAGK TEAAKQIMQY IAAVSGTGAD TEGSRIGEIK EMVLATNPLL
ESFGCAKTLR NNNSSRHGKY LEIMFNERGE PIGAQITNYL LEKNRVVGQI DNERDFHIFY
QFTKGATDAQ REMFGLQGPE AYVYTSRSNC LDVQGINDVN DFADTLKAMG VIGLSAAEQT
DILRVLAMIL WLGNVQFQEM DDGNSKVSDT GVTDFIGYLM EVEGAAVEKV LVSKIVETQR
GGRRGSVYEV PLNPAQASSG RDALAKALYN NLFEWIVKRV NVSLAPQTSY TQLIGVLDIY
GFEIFEDNSF EQLCINYVNE KLQQIFIELT LKTEQEEYVR EQIKWTPIKY FNNKIVCDLI
EERRPPGIFA ALNDACATAH ADPAAADQSF VQRLSSLSSN PHFETRGEKF LIRHYAGDVM
YNVQGMTDKN KDQLVKDILD LIDKSSNKFL HTLFPDRPDP NSKKRPPTAG DRIKASAGAL
VENLMRAQPS YIRTIKPNQN RSSSEYDVKA VLHQIKYLGL QENIRVRRAG FAYRNTFEKV
VERFYLLSKA TSYAGDYIWQ GDAKSGCEKI LTDTGIAKDE WQMGTTKAFI KNPETLFALE
TMRDRYWHNM AARIQRAWRN YWRYKNECAR RIQRFWRNNK EAIVYAQARD YANQVLAGRK
ERRRMSILGS RKFLGDYLGA ESGDSLGLKQ PAGIAPGETV VFSCRAEVLI SKFGRTSKLS
PRFIVLTGKA VYLLMAVARD GQAVVAVDRK LPIVTLRSIS MSNLRDDWFA LNGPISEEGD
PLMTCVFKTE FAADLVKISN GSINVLIGPT IEYNQKKDKK RVIKFVKDEN SRGDPYKSQT
VSVTSGEPPN SVARPMPKRK PGQVRPITSG KLLRAGGPST KSSSAPKPKP QALPGQSAPP
ATVKPVIPAA VKSTAGTAAS KRHSMAPPPP PPPPVSAPAA PEVPMYKALF DFSGQEGEMS
MKKGDLVQVE EKDDNGWWLV KLNGKEGWAP SNYLELLRLY RSQPRFQPHR SPRLPLLRQL
MEVRR
//
