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Database: UniProt
Entry: A0A452I1G0_9SAUR
LinkDB: A0A452I1G0_9SAUR
Original site: A0A452I1G0_9SAUR 
ID   A0A452I1G0_9SAUR        Unreviewed;      1700 AA.
AC   A0A452I1G0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000021299.1};
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:ENSGAGP00000021299.1, 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:ENSGAGP00000021299.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}.
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; ENSGAGT00000024255.1; ENSGAGP00000021299.1; ENSGAGG00000015625.1.
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; cd22726; FHA_KIF1A; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR049779; FHA_KIF1A.
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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          5..354
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          525..581
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1585..1683
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1415..1459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1538..1571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          439..466
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          637..686
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1415..1453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1547..1571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1700 AA;  192332 MW;  2BC552EB0F50B956 CRC64;
     MAGASVKVAV RVRPFNSREM SRDSKCIIQM TGSTTTIVNP KQPKETPKSF SFDFSYWSHT
     TPEDINYASQ KQVYQDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGR QEKDQQGIIP
     QLCEDLFSRI NDATNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
     LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETDITTEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
     TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAVI
     NEDPNNKLIR ELKDEVARLR DLLYSQGLGD IIDTNTAPGR PKLTNALVGM SPSSSLSALS
     SRAASVSSLH ERIMFAPGSE EAIERLKETE KIIAELNETW EEKLRRTEAI RMEREALLAE
     MGVAMREDGG TLGVFSPKKT PHLVNLNEDP LMSECLLYYI KDGITRVGRE DAERRQDIVL
     SGHFIKEEHC IFRSNTKASG EVVVTLEPCE GADTYVNGKK VMEPSVLRSG NRIIMGKSHV
     FRFNHPEQAR QERERTPCAE TPAEPVDWAF AQRELLEKQG IDMKQEMEQR LQELEDQYRK
     EREEANYLLE QQRLDYESKL EALQKQMDSR YYPEANEEEE EPEDEVQWTE REFELALWAF
     RKWKWYQFTS LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPNA
     AKDREKRPFP RTIVAVEVQD QKNGATHYWT LEKLRQRLDL MREMYDRAAE VPSSILEDCD
     NVVTGGDPFY DRFPWFRLVG RAFVYLSNLL YPVPLVHRVA IVSEKGEVKG FLRVAVQAIS
     ADEEAPDYGS GVRQSGTAKI SFDDQHFEKF QSEACPMAGM SRSGTSQEEL RIVEGQGQIT
     DIGPSADEVN NNTCGVTPDD LLLDSPEKVA LDDPLEAVLD HLTLGSIFTF RVTVLQASSI
     SAEYADIFCQ FNFIHRHDEA FSTEPLKNTG RGPPLGFYHV QNIAVEVTKS FIEYIKSQPI
     VFEVFGHYQQ HPFPPLCKDV LSSLRPSRRH FPRVVPLSKP VPATKLSTLA RPSAGPCQCK
     YDLMVFFEIC ELEANGDYIP AIVDHRGGMP CLGTFLLHQG IQRRITVTLV HENSSLVRWK
     EVRELVVGRI RNTPEGDESL IDPNILSLNI LSSGYVNPSQ DDRTFYQFEA AWDSSMHNSL
     LLNRVTPYRE KIFITLSAYI EMENCTQPAV ITKDFCMVFY SRDAKLPASR SIRNLFGSGS
     LRASESNRVT GVYELSLCRV ADAGSPGMQR RRRRVLDTSV AYVRGEENLA GWRPRSDSLI
     LDHQWELEKL SLLQEVEKTR HYLLLREKLE TTQRSGLESL SPCSSEDSES HSTSCVSSPL
     SADGASEGRS SPLETPSERQ KELAVKCLRL LTHTFNREYS HSHVCISASE SKLSEMSVTL
     QRDPSMTALG VTTLTPSSTC PSLLEGRYNA TEVRTLHLSS RAESPEPEPI AEGEQKKSPT
     HGPEDEKETQ RLLVPDIQEI RVSPIVSKKG YLHFLEPHTN GWVKRYVVVR RPYVYIYNTD
     KDSVERAILN LSSAQVEYSE DQQAMLKTPN TFAVCTEHRG ILLQASSDKD MHDWLYAFNP
     LLAGSIRSKL SRRRTAQMRI
//
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