TC126_PHYPA
ID TC126_PHYPA Reviewed; 1149 AA.
AC A9SV60;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Translocase of chloroplast 126, chloroplastic {ECO:0000305};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=126 kDa chloroplast outer envelope protein {ECO:0000305};
GN Name=TOC126 {ECO:0000305};
GN ORFNames=PHYPADRAFT_188734 {ECO:0000312|EMBL:EDQ64903.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- FUNCTION: GTPase involved in protein precursor import into
CC chloroplasts. Seems to recognize chloroplast-destined precursor
CC proteins and regulate their presentation to the translocation channel
CC through GTP hydrolysis. Probably specialized in the import of nuclear
CC encoded non-photosynthetic preproteins from the cytoplasm to the
CC chloroplast. {ECO:0000250|UniProtKB:A9SY64}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O23680};
CC Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000250|UniProtKB:O23680};
CC -!- SUBUNIT: Part of the TOC core complex. {ECO:0000250|UniProtKB:A9SY64}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC159 subfamily. {ECO:0000305}.
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DR EMBL; DS545012; EDQ64903.1; -; Genomic_DNA.
DR RefSeq; XP_001770228.1; XM_001770176.1.
DR AlphaFoldDB; A9SV60; -.
DR SMR; A9SV60; -.
DR eggNOG; ENOG502QR60; Eukaryota.
DR InParanoid; A9SV60; -.
DR Proteomes; UP000006727; Unplaced.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045036; P:protein targeting to chloroplast; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR024283; TOC159_MAD.
DR InterPro; IPR005690; Toc86_159.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR Pfam; PF11886; TOC159_MAD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00993; 3a0901s04IAP86; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 3: Inferred from homology;
KW Chloroplast; Coiled coil; GTP-binding; Hydrolase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Plastid; Plastid outer membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1149
FT /note="Translocase of chloroplast 126, chloroplastic"
FT /id="PRO_0000451564"
FT TRANSMEM 1123..1144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 514..743
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..530
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 550..554
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 570..573
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 642..645
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 691..693
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 769..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..356
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 643
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
FT BINDING 691..692
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O23680"
SQ SEQUENCE 1149 AA; 125564 MW; 37D5205F605A8458 CRC64;
MDALRKLSSL GRNQDKILDT ASSSSYTEAS VAEIPKASVE TGGKDEASPS GLAPIKVRVS
NDVGAEIEEK RGGDEESVGS GESFDSALER LAASSVTSFE PPSPVGSVGE QSQFAGGVSE
DLEERGQEEY LYYDDYGDDG EVEKDGSEKD STSSSSSSSS SECSSSASNT EDEMDISEYG
ASSERAMPLA NPSGVTDEEE EDGKELKYNV ERAVTAEENM PNGLKLGSEA RGIASSSRGA
ELGNAFKDSR EDHEVQEELT ERSVKVAVEN YDQEGEDADS TEIKKEFPRE LTQSRTVIES
PAYRFTSEPV DPALLELKSE KAQPNTQSFA RIAEGESDAD ADADADDEDV ESGDEHEDGY
TEINIRQAAG KSESENESGN NPSLGPAGPS LISVLVRKTA RRPASTAATD TQSSNAASST
QVAGTTDVNP SIEVNEVNET REKLQNIRVK FLRLVHRLGQ SPQNVVVAQV LYRLGLAESL
RGGSTRNHTR AFDFDRANAI AEEQEADNQE EELDFACTIL VLGKTGVGKS ATINSIFDEH
KSVTNAYNPS TTNVYEVVGT MLGVKVRFVD TPGLLFSVAD QRHNERIMGR VKKYIKKASP
DIVLYFDRMD MQTREFGDVP LLRTITNVFG TAVWFNTIVV LTHASTAPPD GPNGTPMGYE
LFVAQRSHSV QQSIRQVAGD MRLQNPVSLV ENHPACRANR NGQRVLPNGQ IWKPHLMLLC
FASKILAEAN TLLKLQDTAA PGRPFGQRSR VPPLPFLLSS LLQSRAQLKL PDEQLDESDE
SDDDEEDEEE GDEYDDLPPF RSLSKEELEE LSKDQRQEYA EELAVRERLF QKKQHREQLQ
RRKEMKKRAT AMRKEGLSHP ADEADDEAGQ PAAVPVPMPD MALPPSFDSD NPTHRYRYLE
TANQWLVRPV LETHGWDHDA GYDGFNVEKM FVVKNKIPAS ISGQVTKDKK ESQVNFEAAA
SLKHGEGKVT LTGFDVQTIG KDLAYTLRAE TRFNNFKRNK TTAGVTATYL NDTIAAGVKL
EDRILIGKRV KMVVNGGVLT GKGDKAFGGS LEATLRGKEY PLSRTLSTLG LSVMDWHGDL
AIGGNLQSQF MVGKTMMVGR ANLNNRGSGQ VSIRASSSEQ LQMVLIGIVP ILRSLINCRF
GFGGGQSSQ
