GenomeNet

Database: UniProt
Entry: A0A452J657_9SAUR
LinkDB: A0A452J657_9SAUR
Original site: A0A452J657_9SAUR 
ID   A0A452J657_9SAUR        Unreviewed;      1954 AA.
AC   A0A452J657;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000035981.1};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000035981.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000035981.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   Ensembl; ENSGAGT00000040730.1; ENSGAGP00000035981.1; ENSGAGG00000025513.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd22729; FHA_KIF13A; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT   DOMAIN          1..310
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1841..1883
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1885..1932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          322..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          565..592
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1064..1091
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1892..1929
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1954 AA;  218391 MW;  5C4456AA896DDE1D CRC64;
     MTSVTALKPP KVFAFDYCFW SMDESNTTKY AGQEVVFKCL GEGILEKAFQ GYNACIFAYG
     QTGSGKSFSM MGNAEQLGLI PRLCGALFQR ISVEENDSQT FKVEVSYMEI YNEKVRDLLD
     PKGSRQSLKV REHKVLGPYV DGLSQLAVTN FEDIESLMSE GNKSRTVAAT NMNEESSRSH
     AVFNIVVTQT LYDLQSGNSG EKVSKVSLVD LAGSERVSKT GAAGDRLKEG SNINKSLSTL
     GLVISSLADQ AAGKGKNKFV PYRDSVLTWL LKDNLGGNSQ TAMIATISPS ADNYEETLST
     LRYADRAKRI VNHAVVNEDP NARVIRELRE EVEKLKEQLS QAEALKAPEL KEKLEESEKL
     IKELTVTWEE KLRKTEEIAQ ERQRQLESMG ISLESSGIKV GDDKCYLVNL NADPALNELL
     VYYLKDHTRV GADTSQDIQL FGIGIQPEHC EIHIELDGEV SLTPKENARS CVNGTLVCTA
     TQLWHGDRIL WGNNHFFRIN LPKRKRRDWL KDFEKETVLA EHDLDATSEA SSEPDYNYEF
     AQMEVIMKTL NSNDPVQNVV QILEKQYLEE KQSALEEQRL MYERELEQLR QQLSPERQHQ
     HGSDRLSYTA QTVQQKVNIW TEERDELFRQ SLAKLREQIV KANTLVREAN FLAEEMNKLT
     DYQVTLQIPA ANLSANRKRG AIVSEPAIQV RRKEKGTQVW TIEKLENKLI DMRDLYQEWK
     EKVPEIRKLI GKKGDPFYEA QENHILIGVA NVFLECLFYD VKLQYAVPII SQQGEVAGRL
     HVEVMRVTGV VPERVAEGDD SSENSSESGS LEIMDSNGEI IHRAKKLTCR VKIKEATGLP
     LNLSNFVFCQ YAFWDQCEST VAAPVVDPDV PSPQSKEAQF TVTFSHCKDY VVNVSEEFLE
     FISEGALAIE VWGHRCTGNG SSIWEVDSLH AKTRTLRDRW SEVTRRIEMW ISIQELNEMG
     EYTAVELHQA KDVNTGGIFQ LRQGHSRRVQ VTVKPVQHSG TLPLMVEAIL SVSIGCVTAR
     STKLQRGLDS YQRDDVDDGD MDSYQEEDLN CVRERWSDAL IKRREYLDEQ IKKISNKQEK
     TEDEIEREAR LLEQWMGLTE ERNAVLVPAP GSGIPGAPAD WTPPSGMETH IPVLFLDLNA
     DDLSANEQLV GPHASGVNSI LPKEHGSQFF YLPIIKHSDD EVSATAAWDS SVHDSVHLNR
     VTPQNERIYL IVKITVQLSH PAAMELVLRK RIAANIYNKQ SFTQSLKRRI SLKNIFYSCG
     VTYEIVSNIP KATEEIEDRE TLALMAARTE NEGTSDGETY IEKYTRGVLQ VENILSLERL
     RQAVTVKEAL STKARHIRRS ISTPNVHNVS SSRLDVFGCD EDDKGWSESH LDISDCSSSY
     QDVSCYGTLP RDSPRRNKDA GGCISETPHA LMASPFKAFS PQPPKFFKPL MPVKEEHKRK
     IPLETRPLLS QESMPSTQVH NAGCVVPSGS NASSMPVENN SIHEEKIDSD EEDSELEAIN
     KKLISSQGFH NFQPYVPEEF ADFSVYNASL ENTEWFSTKT DFMNSRVLEK EVSRSPTASS
     ITSGYISHSA SNATLSDMLV PCSDSTDQLA NQMKDLDSSD QSGPCLAYVL RSLNKEFPER
     GLAKDKIHVS PLKENSALAK EIPPSLNTTD KNSEMLHRAD SCSGLDSSTS KNMRDKIEFS
     SREATTEHTS DVLEDHSFTE FMGVEDGKDF DQSVDPKLCS TGSSKGRKEI PVAGVDSASD
     LSQNTYKEGI RLGQLDSVAV GYQLSNAIEN PLFSVLVKET SYCQTYPDSS LNDFITKNHL
     DVSDSEDGAS AEEAHTLPSW VAVGEQVCVG SNKTGTVRYI GPVDFSAGIW VGVELSVQLG
     KHDGTVKGRE YFHCRPRHGL FVRPGRLSKA PASTKRCSST SQSQASSSLE KRKSSVLQGS
     SSSSKAGEAP LCQSGDAVAS AFSRKQENRK SWIK
//
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