ID A0A2A9MEN6_9APIC Unreviewed; 1517 AA.
AC A0A2A9MEN6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Myosin H {ECO:0000313|EMBL:PFH36455.1};
GN ORFNames=BESB_046470 {ECO:0000313|EMBL:PFH36455.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH36455.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH36455.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH36455.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PFH36455.1}.
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DR EMBL; NWUJ01000003; PFH36455.1; -; Genomic_DNA.
DR STRING; 94643.A0A2A9MEN6; -.
DR VEuPathDB; ToxoDB:BESB_046470; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000224006; Chromosome iii.
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 Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 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; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
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 InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF13540; RCC1_2; 3.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 8.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 3.
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 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:UP000224006}.
FT DOMAIN 87..764
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 1152..1207
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1208..1269
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1324..1375
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 641..663
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 186..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1517 AA; 169574 MW; E2414755815AE0C8 CRC64;
MAAAAKKAGA GGGAAQKKVE RKYSAVELGD YLVGSPVFVR APEKEELYVK AIVKSISGTQ
LTVDDDGNAK TVDVSQCLNA NVGIDPATVV DLAKLPHANE ACALEVIRER YVRDQIYTYA
GRLLVATNPF KLIPGLYEPT TITKYQNADT SRGFPTDVPP HTYAVAQTAM DMLRVTKENQ
SCVVSGESGA GKTETARQLM QYFATSKSGA GGARIQEIIL GANPLLEAIG NAKTLRNNNS
SRFGRFVTLD VAPTGGIHGG IISNYMLELS RIEFQGQGER SYHIFYQMIK GLKPDELAKC
ALKAPTEYEF LNKSGCYEVE TVNDLKEFEE VRQQLKLLYA PEEELDYFKC LSAVLMAGNI
KYKNTQAMGT DKAGKVVNED DFKTIASLLG ADQNALNEAL TINVVEVQGN VIKSPLSAEQ
ATVMIRSMAK ELYSTLFDYI VKSVNKQIKF DAEAKAWIGI LDIYGFEFFQ KNSYEQFLIN
YANERLQQFF IQQVFQAEKV EYEAEGIDHS MVVYSDNATV LEVFDKPKAG VFAYLEEQCL
IQTGTSESFT AACHKNIKNP CFQIPKGDAR VTFLIVHTAA PVTYDTTEFV PKNKMRLPNE
LLMVFKSATN SCMKNAFEEI EIPDTKNMRG KFVGSKFQKS MTGLMTTLKS SHAHFGRCIK
PNQVKKPRVF ETETTLGQMI SLSVLEAVAI IHKGFAYRAS FHDFVEDNNV LMSVLGAKVE
GTDSKSACLT MLDRLGIPKE EYQLGNTKIF LRKTGWLMID KHFRTVMANL KPLILTLQNV
YRAYKARTLY TGFANRVIRV QALMRRYDLR RAAMKKGAAV RLFAGSIFFM MFCNLEERRQ
RAAVLIQKVY RGHSVRNRTR IAMRQAKARA LMKRAAVIGY AGVGGLRWKK FMVSKRQVRA
ATLIQANWRR CMAQKLRKQL KYEKIRNDAA TDIQRVWRGY LGRLRVQLMR LLTPYATTIQ
RFWRGYRVRK SPSYRAHAKI FGKIRQGFIE DRARIVIQSC MRRYIVLSRL QNVTQAAYSM
QKFAQAKLLR LYVSNVHAAT LTIQAWWRGN RVRRILQEEK LKLVLAGHLM RAEKQSLQEC
QEAVMLLRER ERRGMSEKGW QLIHVNVSVE RDDVYPQGWT AGIRAVENFN PSATLAHIEI
SAFHTVVATS SGYVYTYGLN DRGQLGLGKS SLAGLPVPRQ PIGGLALPIS VKQISCGVDH
TLLLDADGRV FAWGSNRYGQ CGCAPRQEVV PKATAVAFSA SRSGAGSLSR RRILTLSAGA
YHNAAVDETG RVYMWGRGEH IYIRGVFSDV PLPLWVSHES ITDLGPLRRV ECGLGFTYLL
TKEGSLYVFG QATTGQLGLG SKRRSSRVAV PVQNVEERVT AISCGVHSTL AVTADGTVYQ
WGVFLLWDPN AQVCVKAQSF VPMPVDLQRG NVTGIPVDVK VGWWEGVVLT SDGLLWAWSF
FDQPRENVLR PAVYQYILTE RQCVRAVQVV SSPLFSAVFS KLDVGRSSDK ARVSASAPSA
LRTKPAINPN WDPLTYN
//