ID Q4H1E6_TETTH Unreviewed; 1925 AA.
AC Q4H1E6;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Myosin 12 {ECO:0000313|EMBL:BAE16257.1};
GN Name=MYO12 {ECO:0000313|EMBL:BAE16257.1};
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911 {ECO:0000313|EMBL:BAE16257.1};
RN [1] {ECO:0000313|EMBL:BAE16257.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21338663; DOI=10.1016/j.gene.2011.02.006;
RA Sugita M., Iwataki Y., Nakano K., Numata O.;
RT "Unique sequences and predicted functions of myosins in Tetrahymena
RT thermophila.";
RL Gene 480:10-20(2011).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AB222078; BAE16257.1; -; mRNA.
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; cd14907; MYSc_Myo46; 1.
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; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00415; RCC1; 3.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50012; RCC1_3; 3.
PE 2: Evidence at transcript level;
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}.
FT DOMAIN 86..810
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 1171..1226
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1328..1381
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1382..1436
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 678..700
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1720..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1925 AA; 224524 MW; CF55105BAD39A7C3 CRC64;
MSQTNLPQKK TVLPPTLWIR PGQVCWVGNY DIQKKEVTNY FAAFIQTSNH SLQNARVKYL
DNIDAPTEVA MKFILMRSDD NKINFNSMDN LINLPILNEA ELIQCIKIRF QNNQIFSYVG
QTLIIVNPFK DIFDLFSNEI IENFKHCARK RGFILKQEQP HIYAVAALTY NQLFEYYKSQ
AIVISGESGT GKTVNTKLCM KLIVQMSSQK QNTNQQSHQL EQQIINCNPI LEAFGNAKTI
KNDNSSRFGK FVSIFIDMKL EKIMGARTQS YLLEKSRVIS QSKEERNYHI FYSLMYSNDS
ELLQSLGLKE KNQKVNLTKF NYLNKSDCYT VNTINDETSY FDVCQALSTL EIDTIDPKYI
WQILAAILHL GNLEFDDRYA DSNSDQPCQI IQSGSSTCEN ISSFLGVPLE KLKEALLKKI
IRVGNKEPTT SSKQKIDVIS HLHSLSKDLY DKLFFWLIKR MNDKLMQLSE KEIQIRTMQN
EMKQIGLLDI FGFEVLQNNS FEQLCINYAN EVLQQLYIEY TFKAEQVEFE EEGLQDELSQ
IPFSDNNEVI NLLDKPPFGL FHQIDENCSL ATAGDDGLYN KIKDQHKTNQ LLIVPTIKSD
KFTIQHTPRQ VQYSILGFRA KNKDEMNLQF IQLLSESKNP IINDIYYAEL QQLVQNQSNQ
KVTQAKDKFI GTKFRKQINQ LMSELRQSDV HFIRCVKPNE SKQPNQFNDD IILNQLRYLG
VLDTIKIRKE GFPVRKEYKD YFRKFGEIMD LNATFTELDK QKADFRKYVV NAELWKNSFQ
PKDNKKQVVF GKTKICFRSE AYDQLELIYQ EKIKKKTEAT IQIQRIARGF LARKQTKIVR
NKLLLINRWL KSRLIRIQFL KKKKAVDRIK KFYKQVLFKK IRKMAMVIQL YMKRQLHLRN
YQNSIKQIIT TQRYIKKQVQ VWKQRRYVNF KRTIVLNSLS QAWYKITNRN ATMIQKIIKG
YLVRNVFHAD KIKHTKIHMV RWHQNKAATK IQKIIRGVQG RKYAKHRMNC ILFIQRHYRI
KWLNEFKQKL ENAAISLQKI YRQKSENSKN QRSYFLNEDL ALQNIQISEQ TAMITSKMQL
LDQSRKDCTL ISNLDSKEAR INRDHLTPAD KKISFFLFVL DYEILTDTSE IYDPLWNKQF
SYLQKEMLQT SHDITHIQVG DTHSIASSTN GKIYGWGWND LCQIGIDSNE GYFCTKKPIP
IPWIEEITRP KAFSVGSNHT FVLDVDNNLY VQGKNNLGQL GLGHNDIVHD PERLDLNIKP
DDRIKIIKSR YEQSVVVTEK GVVFIWPFQL QNNNWINEPF ELAFPSSKVL ISQVSCGLKF
SIFLSNNGVL YSMGSNEQGE LGLGDCIDRN IPCQIESLKN SAEKIQQVEC GQKHTICKSG
LNKIYTWGFG AKGQLGHENK QNEYYPRQVN LSANYSKQKI MQVQAGQKSS LVLFDNKKIL
WWGTNNHLKY QSSPVEVDLS QIHKTMNSQD FYPVRIETTW SKSVSLTYIR MADTRTFDQG
IQFKQKLINT LIQKWQESYL NTMDVPFFDT ISKNISNRHV LKHFSAYKRV GPKYPKQKAE
KYYVLQNSSP IKKQDEFFEE NTQGSRFQNS SVITQSSPGK PFKDVFQNFI ENSAKKENKI
LKSQNQQEGG LDEFVSPVAK LQGKEEENLL DTMKVSPNSL FEKYKNENKN QQKVSQFEIN
IHKVPSMGPN QNMLQKMKTL QPTKLQPPMF GIVKQVSSNL PANRGSIDSE SSQITSSRSK
SKEKPKQNVK FSDNQFQKSS FSSNNRDGPN QDQNEQRQFA TKYNIPTSEQ GMLSSKVIYA
QNQYANNQES IAPQRDSSQN QNYRKENRVL EKTYSKQNMQ SIKELKFNNV TKDQVKYPFI
NDEKYENKTS ENDEFINSLH QKLAGIKSRM QTLTRIPKEE WTLDDHQFMS EVSNSKMIEF
FKSIS
//
