ID K1VNQ9_TRIAC Unreviewed; 2243 AA.
AC K1VNQ9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Myo2 {ECO:0000313|EMBL:EKC98312.1};
GN ORFNames=A1Q2_07326 {ECO:0000313|EMBL:EKC98312.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98312.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98312.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98312.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKC98312.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMBO01000391; EKC98312.1; -; Genomic_DNA.
DR STRING; 1220162.K1VNQ9; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG1980; Eukaryota.
DR HOGENOM; CLU_000192_9_0_1; -.
DR InParanoid; K1VNQ9; -.
DR OMA; QSSCYEV; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
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 CDD; cd15480; fMyo2p_CBD; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 2.
DR InterPro; IPR007034; BMS1_TSR1_C.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF04950; RIBIOP_C; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM01362; DUF663; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000006757}.
FT DOMAIN 96..776
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1236..1537
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 72..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..688
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1091..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1836..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 931..1066
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1562..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1885
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1919
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2243 AA; 250879 MW; 473B3443758062B1 CRC64;
MASVYTKGTR VWLPDKEAGW VPGTVTSVAI PGVPNPDSEV VITVSIDGRA SDEGGSKEFK
CSFATLQSAS ESNGNNLSLG SSQDVLPPLR NPPLLESSED LASLSNLNEP SVLHAIATRY
ATHQPYTYSG IVLADERDGN DILQAYAGKR KGDMEPHLFA IAEEALDLMR RGSGNGGVDP
TGAGDQTIVV SGESGAGKTV SAKYILRYFA SVINASKETP VERRRLDSSG DDEGMSEIER
QILASNPIME AFGNAKTTRN DNSSRFGKYI EVCLQFRGQG MADWQVLFDN ENEIVGARIR
TYLLERSRLV YQPDTERNYH IFYQLLAGAP AKERKDLSLP ADPQQFAYLA GGGPSSSFIA
GVDDAKEFRD TQEALSTVGI SVERQWHIFK VLAALLHLGN VKITQSRTDA VLADDDPALA
LATSLLGLPL SEFKKWTIKK QLTTRSEKIV TNLGSAQATV VRDSVAKFIY SCLFDYGFEH
FKKNSFEQFC INWANEKLQQ ELEQEEYMRE EINWTFIDFT DNQACIDVIE GKMGVLTLLD
EESRLPSGAD ASFANKLHQQ LGPKPEYKDV FKKPRFNQNA FTIAHYAHDV TYDADGFLEK
NRDTVPDEHL ALLQSSTNDF LREAITRSLD QAASSSAAPV VEAKPGPKRG GATRKPTLGS
IFKHSLISLM DTINHTNVHY IRCIKPNEAK KAWTFEPQQV LSQLRACAGE CTSMRRSNLS
YYVLVNSKEW EGNSDVKAFC QLLLQRTLKD ENKYQIGLSK IFFRAGMVAL LESLRTARLN
ALVTLVQKNV RRRIAYKHYQ DLRRRTITIQ SWWRGIQARR LVEQMRRDAA ATLLQRAARG
VLQRRAYANT RQAVVTIQAA RQRFREQRTE SAVLQLQSLF RGQIIVLQSQ WRRKLAVREL
KTLKAEAKSA DKLKEISYQL ENKVVELTKT LQKRTGENKS LKARISDLEK ELATWQLRHE
EAQARSASLE SKLAEPTVPR DKFDEVMASR NEHEERLRTA TRRMTELDEE ITRLSTQLER
ATVDANERQA AIDSAVAKHG EDESTIQSLR HEITSLKEQI SRASALQALT KGGRDAPPSP
TMDRGLRDFA NGLHGGEARN HPPARRRIRR HSTTGHGAVV PHSEEDALDL RKPGLNAPRA
VSVMFPQNNL LRPRDSNGLP TLNDSSADEV ARLLEDEEGL DDDVLHGLIA SLKIPAASLH
NPPLAKEVIF PAHLISLVSN EMWKLGMIPE SERFLANVMQ SIQSYVMQFK GEEVIVPGIF
WLSNVQEILS FICVAESDAQ QGIAPGMDEP GGRELDWEAY ERLVGIVKHD LDSLEYNIYH
TWMLEVKKKL GKMVIPALIE SQSLPGFITS DGSGRMFQRM IGMGGGNNQP TASMDDILNL
LNKVWKCLKS YYMEESVMQQ VVTELLKLIG TIAFNDLIMR RNFCSWKRGL LQLEHLMQAT
KLLQLKKIQK LISQYHNADY EAPISPDILK AVAARVRPED KNDQLLLQTE QDEVGPYQIP
PPRDIAGLET SMVLHSAFLQ STMAPQAHHH RSTLKQSKHA TKGSLKAAAK ASLGVSSHSR
SIEAGSKRDR IHQQAQKRDS KQRAARENAK FFSTSSNGGK VPRVISIIPL LPSISTEKFF
IQLLHSLALS AEEIEALSAQ YQPHCSIFVP APRFKTNLVV NIVPSLDLYA SLDVALVSDA
VLLLMSSTDE VQLEGEAILR SLQGQAGNVT VMPCVQRSLL SFTRYFFPNV HKVYSNDNAN
DASLLARAIC EVLPSNIEHQ EGRSWLVAEG RECATWEPSN AESGDLGTLP LQLRDQAVST
GELLSTQSES ADDLTSNNVP DLLANEQTWP TEEEINSAPA AQGGGRETQK PRIKRVPKGT
SAYQAAWIVD DDDDVDVDDD DESGSGMGSQ DGADVSEEEE MEEIELDSRE QEHDDMAPED
EEEQYAAYLR ERERAQKEDM AFPDEIDTPR HIAARTRFQR YRGLRSFRTS PWDPYENLPL
EYGEIFQFEN FKATKRRVEA EASEEGVEIG TRVTLVIGQV PKTILSRNPS APLIVHGLLR
HEHKQTVLHF VVQRNTEYSE TDPLVLCAGP RRYHINPLFS QHVRGGGKGV NNVHKSERFL
RHGAATVLTT FGPVCFGKAP CLLLRESDVP SLVATGSFMS SDPTRIIAKR IVLTGHPYKV
HKKTATIRYM FFNRDDVAYF QSVELHTKYG RTGHIKEALG THGYFKAHFD GPIQQMDTVC
MNLYKRQFPK SLREASKATA LWM
//
