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Database: UniProt
Entry: A0A1Y1W7N0_9FUNG
LinkDB: A0A1Y1W7N0_9FUNG
Original site: A0A1Y1W7N0_9FUNG 
ID   A0A1Y1W7N0_9FUNG        Unreviewed;      2013 AA.
AC   A0A1Y1W7N0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   31-JUL-2019, entry version 15.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN   ORFNames=DL89DRAFT_293183 {ECO:0000313|EMBL:ORX69550.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Kickxellomycotina; Kickxellomycetes; Kickxellales; Kickxellaceae;
OC   Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX69550.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX69550.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX69550.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A.,
RA   Culley D., Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E.,
RA   Spatafora J.W., Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ORX69550.1}.
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DR   EMBL; MCFD01000007; ORX69550.1; -; Genomic_DNA.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000193922; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-KW.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   Gene3D; 3.10.120.10; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01117; Cyt-b5; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01194079};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00875240};
KW   Complete proteome {ECO:0000313|Proteomes:UP000193922};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|SAAS:SAAS00874053};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01033784};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00874078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193922};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    896    913       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    934    956       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1205   1224       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1593   1617       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1629   1647       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1654   1677       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        8    775       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   REGION      475    495       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      650    672       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION      778    809       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    475    492       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   2013 AA;  226611 MW;  4C8B4B1A50DCFF4B CRC64;
     MSQVLEDDDL SRLSEAANMD SEDIVNILVK RFERRPHGQP YTNIGSRVLI AMNPFEVQET
     SSDDGAMRYA DDYRDMSPER PELPPHVFKT AEQAYLHMRQ TGLNQSLIFI GESGSGTTEQ
     RRLAFRFFSL LRSHSKKDVK LFARLQQADQ VLEAFSSART MAHGNASRVG IYSELQFDQR
     GRAVGAKTLT YLLEKARVTD VPADERNFHV LYYLANGASA EERVSFGIPQ DIAAFEYLSR
     AAGGHQRAAH VGDIEQFSDL CSAMKHVGLH KRYQRHVFAV LGAILCLGNL MFVYESQNGF
     DSAVVRNTDL LQQVSKVLGV DPISLETALT NKTQSVANES CTVYLDAVGA AQRRDELARA
     LYSLLFNWVA EFINARFCRD DSERESFIGM LDFPGWHTQR RNGYEQLCTN YANERIQHFM
     FHQVFEVGND EYKAERIAAS IPSVEFPDRT LCLDLFMKPK TGLFSIMDRQ AAELMGRKPQ
     KKRNRRDSAS SVAPEFDPEA TGRVATFQLL SAFNKHHSGK ASERNPHYQS IESKNEMNSF
     TVSHFWGHAT YDIEGFVDKN LDQLSSDFVA VFRGDGTAEN AGTRNGFVSG LFTDKSIATE
     VHPRNEKTIV QAQALNVPMR APSMMRAKSK LPASRLKKIG CLATQFSRAM SELMATLDDT
     LPWFVVCIKS NDQGKPKWAD ARKVLGTVKG FALDDAVRRK RVEYAAAMLP TDFCDRYGAV
     ISEHVPTAAG KHGDPREKCQ ALKLAMGLDD ASMMVGASKV FLDFATWRRI DDPVRAHERG
     ARNLQDTGDL SDWAEQRGPD DAKEGNVGVS FNVDPKDDAY ARALKDRVDN DTRSFYSDDE
     AYQDLLGKDG FSDILSEGGF QAGFSDVLSN GDADEQKESF EDQEDNAHSM TLVRRVWLGV
     VAFMTWMVPN KCIATCAGRK RKDEQVAWRE KLTLCLLIFW SCAFVIFWIC GLGLLLCPHQ
     NVYSIEELAD HSTEKDALIA IRGEVFDIKN FNHMNIANKY IVDHNYLGRD QSDIFPLQLS
     FVCPFENMDP RLSTQPKPVL YSEAYFHDQR WWRHPTDKGF NYYQYRLMRI MREQYAKGHI
     AVDPKLIRDQ AAGNAKGQND GKNLIRCIIN EEVFDLTDYI SANGAPYVVV PDGMSNSSSF
     NRQFLDSNVV TMFEENKGKD ITDKWNAYFS RDPNMRNLHY QCLRGAFYVG KVDFRKSARC
     YAANYLLLAG SIALVSVIFF KFIAALQLGS RREPEPGDKF VLMNVPCYTE GEESLKNTID
     SLARTKYDDK RKLLFIVCDG MIMGSGNDRP TPRIVLDILG VDRDQDTEAL SYIALGEGSK
     QHNMAKVYSG LYEIAGHVVP YLVVAKCGTP QERTRPGNRG KRDSQIMLMG FFNKVHFDLP
     MTPLELEMYH QIKNVIGVAP SLYEYVLMID ADTVVLPDSL NRMIRTMLHD VKVMGLCGET
     RLANAKSSWI TMMQVYEYFI SHHLTKAFES LFGSVTCLPG CFCMYRIRSA DGRPLLISKE
     VIHDYSENIV DTLHKKNLLH LGEDRYLTTL MLKHFPYFKN KFNAEAQCLT NAPDSWSVLM
     SQRRRWINST VHNLFELVFL PQMCGFCCFS MRFVVFIDLI STIIMPATLV YLAYLVYQLT
     NPDSTTSYIS LYLLAGIYGM QALIFILKRQ WQHIGWMIVY IIAIPFFTFI LPVYSFWHFD
     DFSWGNTRVV VGESGRKHVY MVDNEKFDTT TIPQRKWTDY EQELMWEAGT PSQQGGSEMG
     SRLDHVMSGR PGSAIGNFPK SMSGVYNSAT MPGAYAASKT GSVYMDAGYG YNSNSAANMT
     IRSNMPLVDN MANSGRMTPG GTSPPAHMYS GDTYDVMSYA AASSPPLDYS AAFASQHQPM
     QQSLMQVQPQ QFMQQMPPGY DPRVSQLMTS QSSPMPQQQP AQRMPSPIVG GMPGDSAMYA
     GTVYGQNAGT MMPGDVQQFN TVASARSAGP VTDEMIALQV AHVFSMADLQ TSTKKQVREQ
     VARDLGMTAD ELKARKEFIN SCISSELVKR GGA
//
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