ID V5I3C9_IXORI Unreviewed; 1972 AA.
AC V5I3C9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative myosin class v heavy chain {ECO:0000313|EMBL:JAB84247.1};
DE Flags: Fragment;
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB84247.1};
RN [1] {ECO:0000313|EMBL:JAB84247.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB84247.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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; GANP01000221; JAB84247.1; -; mRNA.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14911; MYSc_Myh2_insects_mollusks; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 6.10.250.2420; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF71; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 663..685
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1657..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1918..1972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB84247.1"
SQ SEQUENCE 1972 AA; 227623 MW; C91EF061D9C8A674 CRC64;
ADIDTFNSPE LKYLVVDKND VYDPAKQAEW TAKKLIWVPH ETQGFVSASV KGERGDELDV
EVLETGKRYF VSKDDVQKMN PPKFNKVEDM AELTCLNEAC VLHNIKDRYY SGLIYTYSGL
FCVVVNPYKK LPIYTEKVIE LFKGKKRHEV PPHIFAVTDG SYRSMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAYVAS SKPRSSTSGI HSTYTPPVFN MGELEQQLLQ ANPILEAFGN
AKTVKNDNSS RFGKFIRINF DASGFIAGAN IETYLLEKSR AIRQARDERC FHIFYQLLHG
ATPEQKKEYL LEDVKNYTFL THGHVPVPGV DDAQEFRNTV KSMSIMGLNQ EDLNCIFRVV
SATLLFGNME FRQERNSDQA TLPDNTVAQK VSHLLGLNVT EMTKAFLRPR LKVGRDHVTK
AQTKEQVEFA VEAISKACYE RMFRWLVNRI NRSLDRTKRQ GASFIGILDI AGFEIFELNS
FEQLCINYTN EKLQQLFNNT MFVLEQEEYR REGIEWKFID FGLDLQPTID LIEKPMGILA
LLDEECMFPK ATDKTFTEKL VTSHNQHPKF IKTDFRGTAD FSILHYAGKV DYLANQWLMK
NMDPLNENVV SLLQNAQDPF IVQIWKDAEI VGMGTATMGD TQFGARTRKG MFRTVSQLYK
DQLAKLMVTL RNTNPNFVRC IIPNHEKKAG KIDAPLVLDQ LRCNGVLEGI RICRQGFPNR
IPFQEFRQRY ELLTPNTIPK GFMDGKLACE KMIAALDLDP NLFRVGQSKI FFRAGVLAHL
EEERDMKISD LIIQFQAYCR GNLARRNYQK RMQQLNAMRI IQRNCASYLK LRNWAWWRLY
TKVKPLLQVT KQEEKLNAKE DELKAMRDRM EKTQMDLKEL ERSLQQATDE KVTLQEQLQA
ETELCAEAEE MRMRLATRKQ ELEEILHDLE GRVEEEEERC QALMQDKKKL QVTIQDLEEQ
LEEEEGARQK LQIEKYTLEG KLKKIEEAYA VMEDGSSKLA KERKALEERQ AELAQALAEE
EEKAKHLGKL KAKQEAGISD LEERLRREQQ MRQELERAKR RLETELNDAR EQLAEKKLQV
EELQTQLAKR DEDVAQALLR CDEEAAAKGQ AQKAFRELEA QLAELQEDLD AEKLARAKSE
KQKRDLNEEL EALKNELLDS LDTTATQREL QKQREQEVVG LKRALEEEAQ SHELQVAELR
QKHAQAIEEV NDNLDNVKKA KATLEKQKGN LEAENVDMAN EIKALSSARQ ESDRRRKALE
FQLQELSVKL AELERSRSDA VERCTRLQGE YDQASTALEE LESRASLSIK SSQTLESQLA
EVQDLLQEET KQKLALSSRL RQLEGERTSL QEQLDEEEEA KRNMEKQIVA LTQQVADAKK
KADEEGEQLA LAEDARKKSQ KDAEALQRQL QELQGLADKL DKSKRKLQAE VEDVNVELES
QRTKVVELEK KQRKFDQLLA EEKAVSERLA AERDNAERES REKETRILSL VRELEERQDS
LEELERSRKQ LQMELDDLMN SQGTADRNVH DLEKAKRSLE NQLAAQKTRL EELEDELQLA
EDAKLRLDVT LQALKAQHER DLQARDEQSE EKRRALAKQV RDLEAELDEE RKQRSAALTL
RKKLESDLQE ADRQMDSLGK AKEEALRQLK RLQVQAKDWQ REAEEARSSR EELQAQTKEA
EKRAKGLEAE LVQLQEDLAS SERARRTAEG ERDELQDEIG STASKGSLLL EDKRKLEAKM
HAMEEELEEE QSNAEILHEK YRKMQAQVDQ LTADLTAERG TSQRLENNAL VQERQMKELR
AKLQEVESAH KSKLRGAQAQ LESRLAQVEE QLDQAEQEKQ AAMRTVRKME KRLKESLIQV
EDERRHADQF KEQVEKTNNR MKNLKRQLDE VDEECSREKA QRRKLQRELE EVQEFNEKLQ
SDLNAARSKL RRTGASSGAT SRMFKRGSVP TASGDESPIS MPEESLTEDG QP
//
