ID A0A1Q9DVK3_SYMMI Unreviewed; 1263 AA.
AC A0A1Q9DVK3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Threonylcarbamoyladenosine tRNA methylthiotransferase {ECO:0000313|EMBL:OLP99190.1};
GN Name=cdkal1 {ECO:0000313|EMBL:OLP99190.1};
GN ORFNames=AK812_SmicGene18300 {ECO:0000313|EMBL:OLP99190.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP99190.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP99190.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP99190.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:OLP99190.1}.
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DR EMBL; LSRX01000371; OLP99190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9DVK3; -.
DR OrthoDB; 1122at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006466; MiaB-like_arc_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR NCBIfam; TIGR01578; MiaB-like-B; 1.
DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:OLP99190.1}.
FT DOMAIN 435..544
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 563..797
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 916..1247
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 869..916
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1003..1010
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1263 AA; 136794 MW; E377594A2A535483 CRC64;
MFAPRSLRRS TSAPGRAGSP SPASTSHASP RRSRAKPFLA LNEPSLAENA EKKVLNILAF
TGADRQTDMR TSTPAGDSKM DGSTAAGDDS VAASEKSSDV GGERPDETAV QVPLRKTLSC
SAKGILSSKL MESASGPVLP PGSPLSPCSQ YPPMATSASQ MLPRESTGPL LWRRTAFAAP
VATPQQCPRG GLVVPVVRRG RESSPPCQVM AACPPSSHQP VHVAPAWSQH SVVRLVHPAQ
HQVLHAAPQL GTRPSVLVQY PIQPQAVAVA PARFAQSTVP PAGTVECAEP ADAANAASAV
PHPLKDPAQI QAEEQIAKEA AASERRENAR CDICEAAQML STASAGLCLS HRRLRDQLLT
QFWQLASLFF GCQAAVGVSE PGSAPEPELE DLGAEGSRRP VEWGAGQVRR RRRLPQKAEV
SAEDETTRKR LPGKQRIFLK TYGCAHNNSD SEFMMGLLQD YGYTLTETVQ DADALVVNSC
TVKGPSQDNA VNLVRSAQDA GKAVVLAGCV PTADASLAKS LVGVSMIGVT QLDRVVEVVE
HALQGNTVSL LNHRSSMPSL DLPKVRRNSF VEIIPISGGC LGNCSYCKTK HARGSLSSYS
EEAIVSRALQ AVSEGVSEVW LTSEDTGAYG LDIGSNIASL LNRVADSLPE HVMLKLGMTN
PPYMLAHIDA VAKVFQRPNV FEHLHVPVQS GSDPVLRAMV REYTSGDFRR LVDGLRAQVP
GLFVATDVIC GFPAESEEDH QATLALVRDY RFPMLNISQF YPRPNTAAAR LKKLPGHIVK
ARSTEMTQLF ESYSTWDHLV GRRERVWFSD TDTKRQQTVG HTKGYAKVVV KRNDALLGRS
AFVQVNRATK WHVEAVVEAT QLDISTTDLA TLRQARTKLL NALASAQEVD LPRVERTVAE
QQRRRLHNAL QDLKGQLRVS CRIRPLSEEE KAQKGELGEP ALRPLDSSRV ELLSRDGPAQ
VFEFDSVFRP DVPQQVVEEI FEDCRDLVQS AVDGHNVTVM TYGQTGAGKT YTLFGNKDQQ
GLVQYMIREV FARLADQEDD EECTVSVSGS ALELYNNHFI DLLRPVDRTG RQSPGVKVCV
DAQGFVEVDG LVQDVAQTGD DLLEILQKGL AQRVVAEHAL NADSSRSHMI FTVRLQTEGG
SKKASTRKLT FCDLGGCERI KRTQVAGELQ KEAIEINKSL SALSGVIEAV AGRRRHVPYR
DHKLTRLLQD AVGGSAKVLM YVCCSPARSN IDETAAALKL ASRAAKVVNQ PKHAEIAEAS
SSL
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