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Database: UniProt
Entry: A0A163KJ82_ABSGL
LinkDB: A0A163KJ82_ABSGL
Original site: A0A163KJ82_ABSGL 
ID   A0A163KJ82_ABSGL        Unreviewed;      2070 AA.
AC   A0A163KJ82;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   31-JUL-2019, entry version 24.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN   Name=ABSGL_14146.1 scaffold 14385 {ECO:0000313|EMBL:SAM08483.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM08483.1, ECO:0000313|Proteomes:UP000078561};
RN   [1] {ECO:0000313|EMBL:SAM08483.1, ECO:0000313|Proteomes:UP000078561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM08483.1,
RC   ECO:0000313|Proteomes:UP000078561};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-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}.
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DR   EMBL; LT554895; SAM08483.1; -; Genomic_DNA.
DR   EnsemblFungi; SAM08483; SAM08483; SAM08483.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000078561; 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-UniRule.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   CDD; cd14879; MYSc_Myo17; 1.
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; IPR036037; MYSc_Myo17.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 2.
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|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078561};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874053};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01033784};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    986   1003       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1024   1043       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1290   1309       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1685   1706       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1712   1733       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1740   1763       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       11    829       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   NP_BIND     112    119       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      592    683       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      704    726       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION     1945   1972       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    622    675       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   2070 AA;  232123 MW;  59052AA41286E0FF CRC64;
     MQDDRRTDLT CLLTAGSSSQ PPSEDNVTSL LQSRYKRNQP YTQIGHFNFI VVNPYQPLDL
     LNDATLQTYA DYGYRNIGGS KPFMQPHIYD LAARVYFHMR RTGEDQTIVL SGTTGSGKST
     THTHLLNQLL LLSTHSKKET KLQFQIKNAL VILESFGHAR TCQNNSASKF GLFQELQFSE
     RGRIQGAKTL TYSFDKIRVT TVPKDERSFN VFYQLLGGTS PDEQAALHIN FDPDYFHYLG
     QSKCVQVPGV NDAIGFGALK SALKICGFKA KTVTQIFQLL AAILHLGNLQ FGENRDGGMA
     TQEACSVRNM DELELVSAML GVSPSKLETA LTYKLRLIRK ELCTMFLNPQ GAVEQRDALA
     RALYHVLFLW IVESINTKIC YNDVDEPANF IGVLDQFGFQ NFKTNGFEEF CANFANERIH
     QFMMQRQFND AEGLNAVMVK DGLSLPKVVT MDNTACLELL IGKDNCNIYD INSSNSSKLI
     LKSAALGLGG IVGVMDRDCA KLQTGATDAT DANFLANVQR QYGNHPSFAK SGYAYAFGVN
     HFSGTVHYTV DAFLEKNLDD LSPDFVNLLR DSSTNMFVST LFQSTVMATE SHPKDDRTIV
     KAQLPSKPTR APSMKRSNKR RMAGMTATTT TANTISALGS TPMDLTAGSS DANAGGDSSN
     NNDANATNGG DSDSRQQKLT SKDAEDAYQN MQVTTVTDQL FITLRDLFYT VSDTKIYNII
     HIRPNDTMTP DNFDLKRVKA QVRAFLLPDL ALRCSRQEYL NYYTFAEFLT RYHTLVQSLL
     PDDTSKMPAR EKLETTMTMM NWTNDQATLG NEMIWLSHDT WRELENGLRL AEKEDRERSR
     TEATTTGHLL QQQLDPEIGN STATLTVDPH GDGKLEPTNH HTAVASDAMY YDGKPRQHFM
     GYNSDATNND PHLPRSSFFE DNASYAETED GVKREGSQWG DESEWGMKGL SEGFGPNMDM
     SKMVEDYQTP QHELVEEMPI SPVRIWWVRF VWLMTWWIPS PFLRWFGKMK REDVQMAWRE
     KVTLCIVIFF FSSLVIFVIV GLGEVVCPGT KSMYSPANIK AHGTPDDIYM SVRGVAYDVT
     SFAIAGHGTT AHNANKDAMS ELAGLDVSYT VPPPLTVACQ GLVTNPSVQV IPNQTIDIGP
     FKHLSGDQLV ETTLADMKDP MWYWNTFVPN MKLYKKGTVV IQLSQLQQDF QGWGRKAMAI
     NKKVYDITDY LETAKNFDSG AGGGDYHFLS PAVEEIFNKF SGGDATTQWN KYKGAMSAAD
     QATNLNCLNN FFYIGDVDER ETPRCTFTNY LLLSFACIMC LVILVKFLAA LQFGGAPTPE
     DHDKFVICQV PCYTEDEESL RKTFDSLTVL NYDDKRKLLL IIADGMIMGS GNDRPTPRIV
     LDVLGYDTKN DPEPLMFKSI GEGSKQLNYG KVYAGLYECD GHVVPYVVVV KVGKASERAK
     PGNRGKRDSQ MICMNFLNKV HFDGEMTPLE LEMYHQIKNV IGVNPSFYEY ILMVDSDTEV
     LPDALNHMIS CMLHDGRIIG LCGETKLVNE DRSWTTMIQV YEYYISHHLA KAFESLFGSV
     TCLPGCFCMY RIRTPVKNEP LIISPKVILD YSDNHVDTLH KKNLLHLGED RYLTTLMMKH
     FPSHKMKFTS HAQCKTVAPD RWQILLSQRR RWINSTIHNL FEVVLLPDLC GFCCFSMRFV
     VLIDLIGTLT LPVSVVYLGY LIYVIASGTG PIPILAMCML AGIYGLQAVL FILKRQWQHI
     GWMFFYILAI PVFSFFLPIY SFWHFDDFSW GNTRVVVGDN KQKKIIVADD EKFDEKMIPL
     KKWSVYEQEL WELGSTGSKE TGVTGQSYPS YYTHGGGGIG FGGNTNGSVG MYDAKSQYGS
     QVDAGGEYDY YRDTNLGVNR SRSPMPAMMG APGSMVGMDL SPPLHRGSRT MSLNSFGPDL
     GQFANTMMND RGSVMGYTQQ QPQLLLQQQQ QQQQQQQQQQ QQPGAYSNFM GSRSSLLHGQ
     PTDFDLPMRP MSQFSVPLSQ GGLAPIIFPA GFPTDEDILC EIRNILATAN LMSVTKKQVR
     EQLGAFFGFD MTPKKEFINS SIAYILQGGL
//
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